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EBI DbfetchID AM270320; SV 1; linear; genomic DNA; STD; FUN; 306261 BP. XX AC AM270320; XX DT 28-JAN-2007 (Rel. 90, Created) DT 24-MAR-2007 (Rel. 91, Last updated, Version 3) XX DE Aspergillus niger contig An14c0130, complete genome. XX KW . XX OS Aspergillus niger OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Trichocomaceae; mitosporic Trichocomaceae; OC Aspergillus. XX RN [1] RP 1-306261 RA Pel H.J.; RT ; RL Submitted (01-MAY-2006) to the EMBL/GenBank/DDBJ databases. RL Pel H.J., DSM, 624-0295, P.O. Box 1, 2600 MA Delft, THE NETHERLANDS. XX RN [2] RP 1-306261 RX DOI; 10.1038/nbt1282 RX PUBMED; 17259976. RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M., RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., RA Ussery D., Varga J., Vervecken W., van der Vondervoort P.J.J., Wedler H., RA Wosten H.A.B., Zeng A.P., van Ooyen A.J.J., Visser J., Stam H.; RT "Genome sequencing and analysis of the versatile cell factory Aspergillus RT niger CBS 513.88"; RL Nature Biotech 25(2):221-231(2007). XX RN [3] RP 214576-218998 RX PUBMED; 1324406. RA Johnson R.E., Henderson S.T., Petes T.D., Prakash S., Bankmann M., RA Prakash L.; RT "Saccharomyces cerevisiae RAD5-encoded DNA repair protein contains DNA RT helicase and zinc-binding sequence motifs and affects the stability of RT simple repetitive sequences in the genome"; RL Mol. Cell. Biol. 12(9):3807-3818(1992). XX RN [4] RP 235537-237514 RX DOI; 10.1073/pnas.89.15.6813 RX PUBMED; 1379722. RA Stepien P.P., Margossian S.P., Landsman D., Butow R.A.; RT "The yeast nuclear gene suv3 affecting mitochondrial post-transcriptional RT processes encodes a putative ATP-dependent RNA helicase"; RL Proc. Natl. Acad. Sci. U.S.A. 89(15):6813-6817(1992). XX RN [5] RP 274363-276854 RX DOI; 10.1016/0378-1119(92)90042-N RX PUBMED; 1452021. RA Wang X.W., Hynes M.J., Davis M.A.; RT "Structural and functional analysis of the amdR regulatory gene of RT Aspergillus oryzae"; RL Gene 122(1):147-154(1992). XX RN [6] RP 183669-184457 RX DOI; 10.1016/0092-8674(92)90539-O RX PUBMED; 1623516. RA Meier U.T., Blobel G.; RT "Nopp140 shuttles on tracks between nucleolus and cytoplasm"; RL Cell 70(1):127-138(1992). XX RN [7] RP 129678-131246 RX DOI; 10.1002/yea.320070903 RX PUBMED; 1803816. RA Buckholz R.G., Cooper T.G.; RT "The allantoinase (DAL1) gene of Saccharomyces cerevisiae"; RL Yeast 7(9):913-923(1991). XX RN [8] RP 102131-102970 RX PUBMED; 1918059. RA Takahashi K., Inoue H., Sakai K., Kohama T., Kitahara S., Takishima K., RA Tanji M., Athauda S.B., Takahashi T., Akanuma H., et a.l.; RT "The primary structure of Aspergillus niger acid proteinase A"; RL J. Biol. Chem. 266(29):19480-19483(1991). XX RN [9] RP 102131-102970 RX PUBMED; 1918060. RA Inoue H., Kimura T., Makabe O., Takahashi K.; RT "The gene and deduced protein sequences of the zymogen of Aspergillus niger RT acid proteinase A"; RL J. Biol. Chem. 266(29):19484-19489(1991). XX RN [10] RP 41386-41959 RX PUBMED; 1985966. RA Casero Jr R.A., Celano P., Ervin S.J., Applegren N.B., Wiest L., Pegg A.E.; RT "Isolation and characterization of a cDNA clone that codes for human RT spermidine/spermine N1-acetyltransferase"; RL J. Biol. Chem. 266(2):810-814(1991). XX RN [11] RP 274363-276854 RX PUBMED; 2188110. RA Andrianopoulos A., Hynes M.J.; RT "Sequence and functional analysis of the positively acting regulatory gene RT amdR from Aspergillus nidulans"; RL Mol. Cell. Biol. 10(6):3194-3203(1990). XX RN [12] RP 42489-46331 RX DOI; 10.1016/0014-5793(88)81416-9 RX PUBMED; 2828113. RA Wagle G., Noegel A., Scheel J., Gerisch G.; RT "Phosphorylation of threonine residues on cloned fragments of the RT Dictyostelium myosin heavy chain"; RL FEBS Lett. 227(1):71-75(1988). XX RN [13] RP 219472-224463 RX PUBMED; 2839509. RA Ann D.K., Smith M.K., Carlson D.M.; RT "Molecular evolution of the mouse proline-rich protein multigene family. RT Insertion of a long interspersed repeated DNA element"; RL J. Biol. Chem. 263(22):10887-10893(1988). XX RN [14] RP 1-1767 RX PUBMED; 3275614. RA Rai R., Genbauffe F.S., Cooper T.G.; RT "Structure and transcription of the allantoate permease gene (DAL5) from RT Saccharomyces cerevisiae"; RL J. Bacteriol. 170(1):266-271(1988). XX RN [15] RX PUBMED; 3294799. RA Turoscy V., Cooper T.G.; RT "Ureidosuccinate is transported by the allantoate transport system in RT Saccharomyces cerevisiae"; RL J. Bacteriol. 169(6):2598-2600(1987). XX RN [16] RX PUBMED; 3301804. RA Rai R., Genbauffe F., Lea H.Z., Cooper T.G.; RT "Transcriptional regulation of the DAL5 gene in Saccharomyces cerevisiae"; RL J. Bacteriol. 169(8):3521-3524(1987). XX RN [17] RP 137763-138878 RX DOI; 10.1016/0378-1119(87)90234-4 RX PUBMED; 3443301. RA Buxton F.P., Gwynne D.I., Garven S., Sibley S., Davies R.W.; RT "Cloning and molecular analysis of the ornithine carbamoyl transferase gene RT of Aspergillus niger"; RL Gene 60(2-3):255-265(1987). XX RN [18] RP 42489-46331 RX DOI; 10.1073/pnas.83.24.9433 RX PUBMED; 3540939. RA Warrick H.M., De Lozanne A., Leinwand L.A., Spudich J.A.; RT "Conserved protein domains in a myosin heavy chain gene from Dictyostelium RT discoideum"; RL Proc. Natl. Acad. Sci. U.S.A. 83(24):9433-9437(1986). XX RN [19] RP 171354-173095 RX PUBMED; 3549700. RA Chisholm V.T., Lea H.Z., Rai R., Cooper T.G.; RT "Regulation of allantoate transport in wild-type and mutant strains of RT Saccharomyces cerevisiae"; RL J. Bacteriol. 169(4):1684-1690(1987). XX RN [20] RP 42489-46331 RX DOI; 10.1073/pnas.82.20.6807 RX PUBMED; 3901008. RA DeLozanne A., Lewis M., Spudich J.A., Leinwand L.A.; RT "Cloning and characterization of a nonmuscle myosin heavy chain cDNA"; RL Proc. Natl. Acad. Sci. U.S.A. 82(20):6807-6810(1985). XX RN [21] RP 304137-304904 RX PUBMED; 4055781. RA Yonezawa N., Nishida E., Sakai H.; RT "pH control of actin polymerization by cofilin"; RL J. Biol. Chem. 260(27):14410-14412(1985). XX RN [22] RP 244025-245366 RX PUBMED; 7601342. RA Lohr D., Venkov P., Zlatanova J.; RT "Transcriptional regulation in the yeast GAL gene family: a complex genetic RT network"; RL FASEB J. 9(9):777-787(1995). XX RN [23] RP 126254-128389 RX DOI; 10.1073/pnas.92.14.6299 RX PUBMED; 7603986. RA Kauh E.A., Bjornsti M.A.; RT "SCT1 mutants suppress the camptothecin sensitivity of yeast cells RT expressing wild-type DNA topoisomerase I"; RL Proc. Natl. Acad. Sci. U.S.A. 92(14):6299-6303(1995). XX RN [24] RP 126254-128389 RX PUBMED; 7608137. RA Matsushita M., Nikawa J.; RT "Isolation and characterization of a SCT1 gene which can suppress a RT choline-transport mutant of Saccharomyces cerevisiae"; RL J. Biochem. 117(2):447-451(1995). XX RN [25] RP 271389-273164 RX DOI; 10.1111/j.1365-2958.1995.tb02400.x RX PUBMED; 7651133. RA Reifenberger E., Freidel K., Ciriacy M.; RT "Identification of novel HXT genes in Saccharomyces cerevisiae reveals the RT impact of individual hexose transporters on glycolytic flux"; RL Mol. Microbiol. 16(1):157-167(1995). XX RN [26] RX DOI; 10.1007/BF02456618 RX PUBMED; 7651333. RA Hohn T.M., Desjardins A.E., McCormick S.P.; RT "The Tri4 gene of Fusarium sporotrichioides encodes a cytochrome P450 RT monooxygenase involved in trichothecene biosynthesis"; RL Mol. Gen. Genet. 248(1):95-102(1995). XX RN [27] RP 287775-290673 RX DOI; 10.1006/geno.1995.1015 RX PUBMED; 7665160. RA Borsani G., Rugarli E.I., Taglialatela M., Wong C., Ballabio A.; RT "Characterization of a human and murine gene (CLCN3) sharing similarities RT to voltage-gated chloride channels and to a yeast integral membrane RT protein"; RL Genomics 27(1):131-141(1995). XX RN [28] RP 250523-252136 RX PUBMED; 7793957. RA Yu J., Chang P.K., Cary J.W., Wright M., Bhatnagar D., Cleveland T.E., RA Payne G.A., Linz J.E.; RT "Comparative mapping of aflatoxin pathway gene clusters in Aspergillus RT parasiticus and Aspergillus flavus"; RL Appl. Environ. Microbiol. 61(6):2365-2371(1995). XX RN [29] RP 210596-213665 RX PUBMED; 7865880. RA Takahashi K., Yamada H., Yanagida M.; RT "Fission yeast minichromosome loss mutants mis cause lethal aneuploidy and RT replication abnormality"; RL Mol. Biol. Cell 5(10):1145-1158(1994). XX RN [30] RP 290705-291989 RX DOI; 10.1073/pnas.92.5.1624 RX PUBMED; 7878029. RA Sinha S., Maity S.N., Lu J., de Crombrugghe B.; RT "Recombinant rat CBF-C, the third subunit of CBF/NFY, allows formation of a RT protein-DNA complex with CBF-A and CBF-B and with yeast HAP2 and HAP3"; RL Proc. Natl. Acad. Sci. U.S.A. 92(5):1624-1628(1995). XX RN [31] RP 134719-137446 RX PUBMED; 7926755. RA Lee B.N., Adams T.H.; RT "The Aspergillus nidulans fluG gene is required for production of an RT extracellular developmental signal and is related to prokaryotic glutamine RT synthetase I"; RL Genes Dev. 8(6):641-651(1994). XX RN [32] RP 231387-235082 RX PUBMED; 7935475. RA Ono Y., Ohno M., Shimura Y.; RT "Identification of a putative RNA helicase (HRH1), a human homolog of yeast RT Prp22"; RL Mol. Cell. Biol. 14(11):7611-7620(1994). XX RN [33] RP 139361-140487 RX DOI; 10.1016/0014-5793(94)01105-2 RX PUBMED; 7957893. RA Machray G.C., Burch L., Hedley P.E., Davies H.V., Waugh R.; RT "Characterisation of a complementary DNA encoding a novel plant enzyme with RT sucrolytic activity"; RL FEBS Lett. 354(1):123-127(1994). XX RN [34] RP 160178-161564 RX DOI; 10.1111/j.1432-1033.1993.tb18221.x RX PUBMED; 8223590. RA Wen Y., Bekhor I.; RT "Sorbitol dehydrogenase. Full-length cDNA sequencing reveals a mRNA coding RT for a protein containing an additional 42 amino acids at the N-terminal RT end"; RL Eur. J. Biochem. 217(1):83-87(1993). XX RN [35] RP 214576-218998 RX DOI; 10.1093/nar/21.25.5964 RX PUBMED; 8290359. RA Doe C.L., Murray J.M., Shayeghi M., Hoskins M., Lehmann A.R., Carr A.M., RA Watts F.Z.; RT "Cloning and characterisation of the Schizosaccharomyces pombe rad8 gene, a RT member of the SNF2 helicase family"; RL Nucleic Acids Res. 21(25):5964-5971(1993). XX RN [36] RP 106306-108402 RX DOI; 10.1016/0378-1119(93)90004-M RX PUBMED; 8299945. RA Velasco J.A., Cansado J., Pena M.C., Kawakami T., Laborda J., Notario V.; RT "Cloning of the dihydroxyacid dehydratase-encoding gene (ILV3) from RT Saccharomyces cerevisiae"; RL Gene 137(2):179-185(1993). XX RN [37] RP 300696-302422 RX PUBMED; 8380406. RA Najjar S.M., Accili D., Philippe N., Jernberg J., Margolis R., Taylor S.I.; RT "pp120/ecto-ATPase, an endogenous substrate of the insulin receptor RT tyrosine kinase, is expressed as two variably spliced isoforms"; RL J. Biol. Chem. 268(2):1201-1206(1993). XX RN [38] RP 300696-302422 RX PUBMED; 8420979. RA Sippel C.J., Suchy F.J., Ananthanarayanan M., Perlmutter D.H.; RT "The rat liver ecto-ATPase is also a canalicular bile acid transport RT protein"; RL J. Biol. Chem. 268(3):2083-2091(1993). XX RN [39] RP 235537-237514 RX DOI; 10.1016/S0092-8674(00)80975-7 RX PUBMED; 8565066. RA Margossian S.P., Li H., Zassenhaus H.P., Butow R.A.; RT "The DExH box protein Suv3p is a component of a yeast mitochondrial RT 3'-to-5' exoribonuclease that suppresses group I intron toxicity"; RL Cell 84(2):199-209(1996). XX RN [40] RP 134719-137446 RX PUBMED; 8617205. RA Lee B.N., Adams T.H.; RT "FluG and flbA function interdependently to initiate conidiophore RT development in Aspergillus nidulans through brlA beta activation"; RL EMBO J. 15(2):299-309(1996). XX RN [41] RP 160178-161564 RX PUBMED; 8761460. RA Hoshi A., Takahashi M., Fujii J., Myint T., Kaneto H., Suzuki K., RA Yamasaki Y., Kamada T., Taniguchi N.; RT "Glycation and inactivation of sorbitol dehydrogenase in normal and RT diabetic rats"; RL Biochem. J. 318(Pt1):119-123(1996). XX RN [42] RP 253990-256648 RX PUBMED; 8816497. RA Hatfield L., Beelman C.A., Stevens A., Parker R.; RT "Mutations in trans-acting factors affecting mRNA decapping in RT Saccharomyces cerevisiae"; RL Mol. Cell. Biol. 16(10):5830-5838(1996). XX RN [43] RP 122449-124650 RX DOI; 10.1016/0378-1119(96)00043-1 RX PUBMED; 8890750. RA Koiv V., Marits R., Heinaru A.; RT "Sequence analysis of the 2,4-dichlorophenol hydroxylase gene tfdB and RT 3,5-dichlorocatechol 1,2-dioxygenase gene tfdC of 2,4-dichlorophenoxyacetic RT acid degrading plasmid pEST4011"; RL Gene 174(2):293-297(1996). XX RN [44] RP 183669-184457 RX PUBMED; 8972203. RA Miau L.H., Chang C.J., Tsai W.H., Lee S.C.; RT "Identification and characterization of a nucleolar phosphoprotein, RT Nopp140, as a transcription factor"; RL Mol. Cell. Biol. 17(1):230-239(1997). XX RN [45] RP 253990-256648 RX DOI; 10.1093/nar/24.23.4791 RX PUBMED; 8972867. RA Wang X., Watt P.M., Louis E.J., Borts R.H., Hickson I.D.; RT "Pat1: a topoisomerase II-associated protein required for faithful RT chromosome transmission in Saccharomyces cerevisiae"; RL Nucleic Acids Res. 24(23):4791-4797(1996). XX RN [46] RP 214576-218998 RX DOI; 10.1093/nar/25.4.743 RX PUBMED; 9016623. RA Ahne F., Jha B., Eckardt-Schupp F.; RT "The RAD5 gene product is involved in the avoidance of non-homologous RT end-joining of DNA double strand breaks in the yeast Saccharomyces RT cerevisiae"; RL Nucleic Acids Res. 25(4):743-749(1997). XX RN [47] RP 109464-114248 RX DOI; 10.1038/ng0297-137 RX PUBMED; 9020838. RA Decottignies A., Goffeau A.; RT "Complete inventory of the yeast ABC proteins"; RL Nat. Genet. 15(2):137-145(1997). XX RN [48] RP 6766-8598 RX PUBMED; 9023923. RA Saito Y., Ishii Y., Hayashi H., Imao Y., Akashi T., Yoshikawa K., RA Noguchi Y., Soeda S., Yoshida M., Niwa M., Hosoda J., Shimomura K.; RT "Cloning of genes coding for L-sorbose and L-sorbosone dehydrogenases from RT Gluconobacter oxydans and microbial production of 2-keto-L-gulonate, a RT precursor of L-ascorbic acid, in a recombinant G. oxydans strain"; RL Appl. Environ. Microbiol. 63(2):454-460(1997). XX RN [49] RP 163695-165405 RX PUBMED; 9055077. RA Mosch H.U., Fink G.R.; RT "Dissection of filamentous growth by transposon mutagenesis in RT Saccharomyces cerevisiae"; RL Genetics 145(3):671-684(1997). XX RN [50] RP 253990-256648 RX DOI; 10.1046/j.1365-2443.1996.d01-215.x RX PUBMED; 9077451. RA Lin R., Allis C.D., Elledge S.J.; RT "PAT1, an evolutionarily conserved acetyltransferase homologue, is required RT for multiple steps in the cell cycle"; RL Genes Cells 1(10):923-942(1996). XX RN [51] RP 304137-304904 RX DOI; 10.1046/j.1365-2443.1996.05005.x RX PUBMED; 9078368. RA Moriyama K., Iida K., Yahara I.; RT "Phosphorylation of Ser-3 of cofilin regulates its essential function on RT actin"; RL Genes Cells 1(1):73-86(1996). XX RN [52] RP 250523-252136 RX PUBMED; 9097431. RA Yu J., Chang P.K., Cary J.W., Bhatnagar D., Cleveland T.E.; RT "avnA, a gene encoding a cytochrome P-450 monooxygenase, is involved in the RT conversion of averantin to averufin in aflatoxin biosynthesis in RT Aspergillus parasiticus"; RL Appl. Environ. Microbiol. 63(4):1349-1356(1997). XX RN [53] RP 86934-92909 RX DOI; 10.1002/(SICI)1097-0061(19970330)13:4<391::AID-YEA92>3.0.CO;2-Q RX PUBMED; 9133744. RA Martegani E., Vanoni M., Mauri I., Rudoni S., Saliola M., Alberghina L.; RT "Identification of gene encoding a putative RNA-helicase, homologous to RT SKI2, in chromosome VII of Saccharomyces cerevisiae"; RL Yeast 13(4):391-397(1997). XX RN [54] RP 63282-64976 RX PUBMED; 9168605. RA Essenberg R.C., Candler C., Nida S.K.; RT "Brucella abortus strain 2308 putative glucose and galactose transporter RT gene: cloning and characterization"; RL Microbiology 143(Pt5):1549-1555(1997). XX RN [55] RP 176709-181113 RX DOI; 10.1007/s004380050434 RX PUBMED; 9180695. RA Del Sorbo G., Andrade A.C., Van Nistelrooy J.G., Van Kan J.A., Balzi E., RA De WaardM.A.; RT "Multidrug resistance in Aspergillus nidulans involves novel ATP-binding RT cassette transporters"; RL Mol. Gen. Genet. 254(4):417-426(1997). XX RN [56] RP 109464-114248 RX DOI; 10.1074/jbc.272.24.15358 RX PUBMED; 9182565. RA Ortiz D.F., St Pierre M.V., Abdulmessih A., Arias I.M.; RT "A yeast ATP-binding cassette-type protein mediating ATP-dependent bile RT acid transport"; RL J. Biol. Chem. 272(24):15358-15365(1997). XX RN [57] RP 116581-117775 RX DOI; 10.1002/(SICI)1097-0061(199712)13:15<1399::AID-YEA187>3.3.CO;2-Z RX PUBMED; 9434346. RA Gonzalez F.J., Montes J., Martin F., Lopez M.C., Ferminan E., Catalan J., RA Galan M.A., Dominguez A.; RT "Molecular cloning of TvDAO1, a gene encoding a D-amino acid oxidase from RT Trigonopsis variabilis and its expression in Saccharomyces cerevisiae and RT Kluyveromyces lactis"; RL Yeast 13(15):1399-1408(1997). XX RN [58] RP 187512-189364 RX PUBMED; 9435078. RA Alexander N.J., Hohn T.M., McCormick S.P.; RT "The TRI11 gene of Fusarium sporotrichioides encodes a cytochrome P-450 RT monooxygenase required for C-15 hydroxylation in trichothecene RT biosynthesis"; RL Appl. Environ. Microbiol. 64(1):221-225(1998). XX RN [59] RP 17794-21678 RX DOI; 10.1562/0031-8655(1998)067<0263:FAPORP>2.3.CO;2 RX PUBMED; 9487803. RA Sineshchekov V., Hughes J., Hartmann E., Lamparter T.; RT "Fluorescence and photochemistry of recombinant phytochrome from the RT cyanobacterium Synechocystis"; RL Photochem. Photobiol. 67(2):263-267(1998). XX RN [60] RP 261013-261697 RX DOI; 10.1016/S0092-8674(00)80942-3 RX PUBMED; 9491890. RA Ramos P.C., Hockendorff J., Johnson E.S., Varshavsky A., Dohmen R.J.; RT "Ump1p is required for proper maturation of the 20S proteasome and becomes RT its substrate upon completion of the assembly"; RL Cell 92(4):489-499(1998). XX RN [61] RP 238632-241078 RX PUBMED; 9526009. RA Dresbach T., Burns M.E., O'Connor V., DeBello W.M., Betz H., RA Augustine G.J.; RT "A neuronal Sec1 homolog regulates neurotransmitter release at the squid RT giant synapse"; RL J. Neurosci. 18(8):2923-2932(1998). XX RN [62] RP 67917-69622 RX DOI; 10.1007/s004380050666 RX PUBMED; 9529523. RA Trapp S.C., Hohn T.M., McCormick S., Jarvis B.B.; RT "Characterization of the gene cluster for biosynthesis of macrocyclic RT trichothecenes in Myrothecium roridum"; RL Mol. Gen. Genet. 257(4):421-432(1998). XX RN [63] RP 100433-101832 RX DOI; 10.1006/bbrc.1998.8354 RX PUBMED; 9535763. RA Mahadevan U., Padmanaban G.; RT "Cloning and expression of an acyl-CoA dehydrogenase from Mycobacterium RT tuberculosis"; RL Biochem. Biophys. Res. Commun. 244(3):893-897(1998). XX RN [64] RP 214576-218998 RX DOI; 10.1016/S0921-8777(97)00070-0 RX PUBMED; 9637242. RA Liefshitz B., Steinlauf R., Friedl A., Eckardt-Schupp F., Kupiec M.; RT "Genetic interactions between mutants of the 'error-prone' repair group of RT Saccharomyces cerevisiae and their effect on recombination and RT mutagenesis"; RL Mutat. Res. 407(2):135-145(1998). XX RN [65] RP 152306-154163 RX DOI; 10.1083/jcb.141.7.1563 RX PUBMED; 9647649. RA Fry A.M., Mayor T., Meraldi P., Stierhof Y.D., Tanaka K., Nigg E.A.; RT "C-Nap1, a novel centrosomal coiled-coil protein and candidate substrate of RT the cell cycle-regulated protein kinase Nek2"; RL J. Cell Biol. 141(7):1563-1574(1998). XX RN [66] RP 134719-137446 RX PUBMED; 9691036. RA Yager L.N., Lee H.O., Nagle D.L., Zimmerman J.E.; RT "Analysis of fluG mutations that affect light-dependent conidiation in RT Aspergillus nidulans"; RL Genetics 149(4):1777-1786(1998). XX RN [67] RP 157408-159653 RX PUBMED; 9811645. RA Sakai Y., Nakagawa T., Shimase M., Kato N.; RT "Regulation and physiological role of the DAS1 gene, encoding RT dihydroxyacetone synthase, in the methylotrophic yeast Candida boidinii"; RL J. Bacteriol. 180(22):5885-5890(1998). XX RN [68] RP 173682-174944 RX DOI; 10.1016/S0167-4838(98)00256-8 RX PUBMED; 9989239. RA Kabashima T., Fujii M., Hamasaki Y., Ito K., Yoshimoto T.; RT "Cloning of a novel prolidase gene from Aureobacterium esteraromaticum"; RL Biochim. Biophys. Acta 1429(2):516-520(1999). XX RN [69] RP 141333-142531 RX DOI; 10.1074/jbc.274.13.8379 RX PUBMED; 10085068. RA Otto J.C., Kim E., Young S.G., Casey P.J.; RT "Cloning and characterization of a mammalian prenyl protein-specific RT protease"; RL J. Biol. Chem. 274(13):8379-8382(1999). XX RN [70] RP 6766-8598 RX DOI; 10.1002/(SICI)1097-0290(19980420)58:2/3<309::AID-BIT30>3.3.CO;2-Q RX PUBMED; 10191408. RA Saito Y., Ishii Y., Hayashi H., Yoshikawa K., Noguchi Y., Yoshida S., RA Soeda S., Yoshida M.; RT "Direct fermentation of 2-keto-L-gulonic acid in recombinant Gluconobacter RT oxydans"; RL Biotechnol. Bioeng. 58(2-3):309-315(1998). XX RN [71] RP 304137-304904 RX DOI; 10.1046/j.1365-2443.1999.00235.x RX PUBMED; 10231390. RA Iida K., Yahara I.; RT "Cooperation of two actin-binding proteins, cofilin and Aip1, in RT Saccharomyces cerevisiae"; RL Genes Cells 4(1):21-32(1999). XX RN [72] RP 253990-256648 RX DOI; 10.1007/s004380050027 RX PUBMED; 10394921. RA Wang X., Watt P.M., Borts R.H., Louis E.J., Hickson I.D.; RT "The topoisomerase II-associated protein, Pat1p, is required for RT maintenance of rDNA locus stability in Saccharomyces cerevisiae"; RL Mol. Gen. Genet. 261(4-5):831-840(1999). XX RN [73] RP 214576-218998 RX PUBMED; 10430580. RA Lewis L.K., Westmoreland J.W., Resnick M.A.; RT "Repair of endonuclease-induced double-strand breaks in Saccharomyces RT cerevisiae: essential role for genes associated with nonhomologous RT end-joining"; RL Genetics 152(4):1513-1529(1999). XX RN [74] RP 305851-306260 RX DOI; 10.1007/s004380051056 RX PUBMED; 10503533. RA Shuster J.R., Bindel Connelley M.; RT "Promoter-tagged restriction enzyme-mediated insertion (PT-REMI) RT mutagenesis in Aspergillus niger"; RL Mol. Gen. Genet. 262(1):27-34(1999). XX RN [75] RP 145840-147599 RX DOI; 10.1007/s004380051097 RX PUBMED; 10517336. RA Chung K.R., Jenns A.E., Ehrenshaft M., Daub M.E.; RT "A novel gene required for cercosporin toxin resistance in the fungus RT Cercospora nicotianae"; RL Mol. Gen. Genet. 262(2):382-389(1999). XX RN [76] RP 166831-168258 RX DOI; 10.1105/tpc.11.10.2013 RX PUBMED; 10521529. RA DeZwaan T.M., Carroll A.M., Valent B., Sweigard J.A.; RT "Magnaporthe grisea pth11p is a novel plasma membrane protein that mediates RT appressorium differentiation in response to inductive substrate cues"; RL Plant Cell 11(10):2013-2030(1999). XX RN [77] RP 29503-34050 RX PUBMED; 10556049. RA Jacobsen S.E., Running M.P., Meyerowitz E.M.; RT "Disruption of an RNA helicase/RNAse III gene in Arabidopsis causes RT unregulated cell division in floral meristems"; RL Development 126(23):5231-5243(1999). XX RN [78] RP 195969-197381 RX DOI; 10.1128/JB.182.7.2018-2025.2000 RX PUBMED; 10715011. RA Jones R.M., Pagmantidis V., Williams P.A.; RT "sal genes determining the catabolism of salicylate esters are part of a RT supraoperonic cluster of catabolic genes in Acinetobacter sp. strain ADP1"; RL J. Bacteriol. 182(7):2018-2025(2000). XX RN [79] RP 261013-261697 RX PUBMED; 10757750. RA Lutz M.S., Ellis S.R., Martin N.C.; RT "Proteasome mutants, pre4-2 and ump1-2, suppress the essential function but RT not the mitochondrial RNase P function of the Saccharomyces cerevisiae gene RT RPM2"; RL Genetics 154(3):1013-1023(2000). XX RN [80] RP 143709-145722 RX DOI; 10.1007/s002530051660 RX PUBMED; 10855719. RA Yu J., Chang P.K., Bhatnagar D., Cleveland T.E.; RT "Genes encoding cytochrome P450 and monooxygenase enzymes define one end of RT the aflatoxin pathway gene cluster in Aspergillus parasiticus"; RL Appl. Microbiol. Biotechnol. 53(5):583-590(2000). XX RN [81] RP 253990-256648 RX DOI; 10.1128/MCB.20.16.5939-5946.2000 RX PUBMED; 10913177. RA Bonnerot C., Boeck R., Lapeyre B.; RT "The two proteins Pat1p (Mrt1p) and Spb8p interact in vivo, are required RT for mRNA decay, and are functionally linked to Pab1p"; RL Mol. Cell. Biol. 20(16):5939-5946(2000). XX RN [82] RP 74646-77136 RX DOI; 10.1002/1097-0061(200008)16:11<1025::AID-YEA602>3.0.CO;2-1 RX PUBMED; 10923024. RA Grava S., Dumoulin P., Madania A., Tarassov I., Winsor B.; RT "Functional analysis of six genes from chromosomes XIV and XV of RT Saccharomyces cerevisiae reveals YOR145c as an essential gene and RT YNL059c/ARP5 as a strain-dependent essential gene encoding nuclear RT proteins"; RL Yeast 16(11):1025-1033(2000). XX RN [83] RP 176709-181113 RX PUBMED; 10931903. RA Andrade A.C., Del Sorbo G., Van Nistelrooy J.G., Waard M.A.; RT "The ABC transporter AtrB from Aspergillus nidulans mediates resistance to RT all major classes of fungicides and some natural toxic compounds"; RL Microbiology 146(Pt8):1987-1997(2000). XX RN [84] RP 65757-67143 RX DOI; 10.1074/jbc.M005860200 RX PUBMED; 10962001. RA Sakamoto Y., Taguchi T., Honke K., Korekane H., Watanabe H., Tano Y., RA Dohmae N., Takio K., Horii A., Taniguchi N.; RT "Molecular cloning and expression of cDNA encoding chicken RT UDP-N-acetyl-D-glucosamine (GlcNAc): GlcNAcbeta 1-6(GlcNAcbeta 1-2)- RT manalpha 1-R[GlcNAc to man]beta 1,4N-acetylglucosaminyltransferase VI"; RL J. Biol. Chem. 275(46):36029-36034(2000). XX RN [85] RP 261013-261697 RX DOI; 10.1073/pnas.190268597 RX PUBMED; 10973495. RA Burri L., Hockendorff J., Boehm U., Klamp T., Dohmen R.J., Levy F.; RT "Identification and characterization of a mammalian protein interacting RT with 20S proteasome precursors"; RL Proc. Natl. Acad. Sci. U.S.A. 97(19):10348-10353(2000). XX RN [86] RP 152306-154163 RX DOI; 10.1083/jcb.151.4.837 RX PUBMED; 11076968. RA Mayor T., Stierhof Y.D., Tanaka K., Fry A.M., Nigg E.A.; RT "The centrosomal protein C-Nap1 is required for cell cycle-regulated RT centrosome cohesion"; RL J. Cell Biol. 151(4):837-846(2000). XX RN [87] RP 305851-306260 RX DOI; 10.1016/S0005-2728(00)00251-6 RX PUBMED; 11245784. RA Joseph-Horne T., Hollomon D.W., Wood P.M.; RT "Fungal respiration: a fusion of standard and alternative components"; RL Biochim. Biophys. Acta 1504(2-3):179-195(2001). XX RN [88] RP 259799-260608 RX DOI; 10.1074/jbc.M100727200 RX PUBMED; 11279123. RA Cavdar Koc E., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.; RT "The small subunit of the mammalian mitochondrial ribosome. Identification RT of the full complement of ribosomal proteins present"; RL J. Biol. Chem. 276(22):19363-19374(2001). XX RN [89] RP 134719-137446 RX PUBMED; 11454752. RA D'Souza C.A., Lee B.N., Adams T.H.; RT "Characterization of the role of the FluG protein in asexual development of RT Aspergillus nidulans"; RL Genetics 158(3):1027-1036(2001). XX DR EMBL-CON; AM270993. DR RFAM; RF00005; tRNA. XX FH Key Location/Qualifiers FH FT source 1..306261 FT /organism="Aspergillus niger" FT /mol_type="genomic DNA" FT /clone="An14c0130" FT /db_xref="taxon:5061" FT CDS complement(join(<1..188,242..459,511..1029,1080..1357, FT 1405..1767)) FT /locus_tag="An14g02910" FT /note="Function: Dal5p of S. cerevisiae is a component of FT the allantoate transport system." FT /note="Remark: C-terminally truncated ORF due to contig FT border." FT /note="Title: strong similarity to allantoate permease Dal5 FT - Saccharomyces cerevisiae [truncated ORF]" FT /db_xref="InterPro:IPR011701" FT /db_xref="UniProtKB/TrEMBL:A2R336" FT /citation=[14] FT /citation=[15] FT /citation=[16] FT /inference="profile:COGS:COG0477" FT /protein_id="CAK46528.1" FT /translation="MSMENISSTPAGGPDSKGASTAVEDHKPPQDVSHVERVLSPSDKL FT KAPIDANRVDNEVLEYAARGQIEVDEAESRRLRRMIDRRVLVIMIVTYFLQALDKGTMS FT FASIMGIRDDAHLVGQQYSWLTTCIYIAVLIVEYPTNWIIQRVRIAKYLGFNIICWGTI FT LALHSACHNFAGLVTVRTLLGIFEAACQPSFVVLSGMWYKREEQAATVTFWYMMNGGQQ FT IVGGLLAYCFSLIGSDRALKSWQALFLTYGCISVLWGLFVVWWMPDSPMRAKCFTEEDK FT HKMVERVRANQTGLQNKKFRAYQMWEAFRDPQMYCYCAIQIFTTLPTSGLGAFANIIIS FT GFNFTELQTQLLAMVLGFYIIIVLLTSAWLVKKFEQNLLVMLGFIIPCRSFVGTIVLMT FT VQNHSLSTKVGLLISYYITLSFWSAQNLGLSMVTRNIAGATKKSTVVAATFVSWAVGNA FT IGPQVFLDRDAPRYFIAFGVHLGCYSAMTLAVIFLRFYLIRENKKKDKAMAEMGIALDG FT EDHLA" FT mRNA complement(join(<1..188,242..459,511..1029,1080..1357, FT 1405..>1767)) FT /locus_tag="An14g02910" FT exon complement(<1..188) FT /locus_tag="An14g02910" FT /number=1 FT intron complement(189..241) FT /locus_tag="An14g02910" FT /number=1 FT exon complement(242..459) FT /locus_tag="An14g02910" FT /number=2 FT intron complement(460..510) FT /locus_tag="An14g02910" FT /number=2 FT exon complement(511..1029) FT /locus_tag="An14g02910" FT /number=3 FT intron complement(1030..1079) FT /locus_tag="An14g02910" FT /number=3 FT exon complement(1080..1357) FT /locus_tag="An14g02910" FT /number=4 FT intron complement(1358..1404) FT /locus_tag="An14g02910" FT /number=4 FT exon complement(1405..1767) FT /locus_tag="An14g02910" FT /number=5 FT exon 2289..3386 FT /locus_tag="An14g02920" FT /number=1 FT CDS 2289..3386 FT /locus_tag="An14g02920" FT /note="Title: strong similarity to hypothetical conserved FT protein yesR - Bacillus subtilis" FT /db_xref="GOA:A2R337" FT /db_xref="InterPro:IPR010905" FT /db_xref="UniProtKB/TrEMBL:A2R337" FT /inference="profile:COGS:COG4225" FT /inference="similar to AA sequence:PIR:A69797" FT /protein_id="CAK46529.1" FT /translation="MASTSPPAVRSKIDLLITNLVNIQDKTGQFLLPLADGRIIDTKSW FT HGWEWTHGIGLYGIWKYYEMTGSPHLLQIIEDWFAARFAEGGTTKNINTMAVFLTLAYV FT YEKTQNPVYLPWLDAWAEWAMHELPRTKQGGMQHATYLTENYQQLWDDTLMMTVMPLAK FT IGKLLNRPDYVEEAKRQTLVHVKYLVDTSTGLWFHGWTFEDGGHNFARARWARGNSWVT FT MVIPEFIELLDLKEGDPIRLFLLDTLEAQCEALMGLQEESGFWHTLLDHPDSYVEASAT FT AGFAYGILKAVRKRYLPKKYRVVAEKAIQAVLSAVDETGELQQTSFGTGMGDSLDFYKK FT IPLTAMPYGQAMAIMALGEYLRGHL" FT mRNA <2289..>3386 FT /locus_tag="An14g02920" FT CDS complement(join(5453..6303,6616..6676)) FT /locus_tag="An14g02930" FT /note="Title: similarity to hypothetical protein encoded by FT An12g07270 - Aspergillus niger" FT /db_xref="UniProtKB/TrEMBL:A2R338" FT /protein_id="CAK46530.1" FT /translation="MSTITSCSYLWSWDSVYMNEILHHQAETMDSPHQIFLIPEVLEPV FT LLNLDTTTLLFSQRVCHVWNSLIKTSPSLQTALFFRPQKDSSTSTPALKPKRTVNPLMN FT KLLKHFVSNHGSSFHRDISSYLSRFGPQKSSDPSTTELERQHPYLRPEASWREMLLHQP FT PAPTLAVSDDLIPLSIGGVPSNESNAVLRLKHLEKLVQVCFSFPVEKVLIFYPMHNPPW FT GRAPVSILRRFLDTCDTYIVPRYFVLTGLSTAVDAPVECGWPAGLPWLTEVGRWLKEWE FT AIRESWRLECLTHFMYLYFYGS" FT mRNA complement(join(<5453..6303,6616..>6676)) FT /locus_tag="An14g02930" FT exon complement(5453..6303) FT /locus_tag="An14g02930" FT /number=1 FT intron complement(6304..6615) FT /locus_tag="An14g02930" FT /number=1 FT exon complement(6616..6676) FT /locus_tag="An14g02930" FT /number=2 FT CDS complement(join(6766..7727,7789..8502,8556..8598)) FT /locus_tag="An14g02940" FT /note="Function: L-sorbose dehydrogenase (SDH) and FT L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans FT T-100 show an ability to convert D-sorbitol to FT 2-keto-L-gulonate (2-KLGA)." FT /note="Function: chemical mutation of the host strain to FT suppress the L-idonate pathway and replacement of the FT original promoter with that of E. coli tufB resulted in FT improving the production of 2-KLGA." FT /note="Function: consequently, high-level production from FT D-sorbitol to 2-KLGA (130 mg/ml) was achieved by simple FT fermentation of the recombinant Gluconobacter." FT /note="Title: strong similarity to FAD dependent L-sorbose FT dehydrogenase - Gluconobacter oxydans" FT /db_xref="GOA:A2R339" FT /db_xref="InterPro:IPR012132" FT /db_xref="UniProtKB/TrEMBL:A2R339" FT /citation=[48] FT /citation=[70] FT /inference="profile:COGS:COG2303" FT /inference="profile:PFAM:PF00732" FT /inference="profile:PFAM:PF05199" FT /inference="similar to AA sequence:UniProtKB:GOD622.2" FT /protein_id="CAK46531.1" FT /translation="MASTDQTWEFVVVGGGPAGCALASRLARSARRPQVLLLEAGPRND FT DPSLRVDGQRWQTFMNGNLNWGYKTTPQEHCNGRQIDYSRGKVLGGSSAINFGVYTVGA FT RDDYNQWAGLVGDDLFRWERMQARFRQLETFNGAIVDPKNSKYAAPRTSDHGSQGSLKV FT GYAAEWEQDLPLMMDVFEQAGLARNPDHNSGDPIGMALVINSSHQGRRVTATDLLDEAP FT SNLTIITETPALRLVLQGTKTVGVETKGAKYFASKEVILTTGSLDTPKILMHSGLGPAG FT QLQQFGIPVVKDMPAVGQGLRDHFFAPLCFQRNPTTNDRDAFFGNPAAMESALEQWSKD FT GTGPWARHSCQIGAGWLKSDRLVASEEFKALPPTVQEFLQRDTVPHYEFMTHFPLHLIS FT PEPFKDYSYVCMLVFLMNEQSSGEVRLQSANPEDPLLFDPKFLSHPFDRRACIEIYRHA FT LEVTKHESFQKDTVSALIAPPSESDEDILEFWKNTLGSSWHMTGTTKMGKSGDADAVVD FT SRFRVFGVENLRIADMGVVPVLTNNHTQATAYVTGLTCGDALAEEYGLDTSEARL" FT mRNA complement(join(<6766..7727,7789..8502,8556..>8598)) FT /locus_tag="An14g02940" FT exon complement(6766..7727) FT /locus_tag="An14g02940" FT /number=1 FT intron complement(7728..7788) FT /locus_tag="An14g02940" FT /number=1 FT exon complement(7789..8502) FT /locus_tag="An14g02940" FT /number=2 FT intron complement(8503..8555) FT /locus_tag="An14g02940" FT /number=2 FT exon complement(8556..8598) FT /locus_tag="An14g02940" FT /number=3 FT CDS join(10475..10580,10674..10895,10964..11505,11552..12514) FT /locus_tag="An14g02950" FT /EC_number="1.1.3.-" FT /note="Similarity: show strong similarity to several FT oxidoreductases of different organims." FT /note="Title: strong similarity to hypothetical isoamyl FT alcohol oxidase mreA - Aspergillus oryzae" FT /db_xref="GOA:A2R340" FT /db_xref="InterPro:IPR016166" FT /db_xref="UniProtKB/TrEMBL:A2R340" FT /inference="profile:COGS:COG0277" FT /inference="profile:PFAM:PF01565" FT /inference="similar to AA sequence:UniProtKB:AB048606.1" FT /protein_id="CAK46532.1" FT /translation="MRRALPWQSTTSSSSNTGRTFRPRRAVPRYAQCFGVSPVVRASSQ FT CRCQPGDACWPSRDGWKHLNESISGHLVRVYPIGHVCHEPFFDQASCNQLVHLQYDSNW FT RAEQPGALQSFNWENWPRENENCTIEANPSSVCGQGRIPLYSAVIQSVDEICAVVKFAK FT QRNIRLVIKNTGHDSTGRSGAPHSLQILTNRLKDITFHDDFVPSQGDLGMDNPNASGVP FT AVTIGAGVMVGELYAAAAARGLIVVAGECSTVGVAGGYLQGGGVSTVLSPMYGLAVDHV FT LELEVVTAQGEIVTANGYQHDDLFWALRGGGGGTYGVVTKATMRAFPDIPAVIPTVHFI FT YPRANDVFWQAVAQVVRLTQSMSVNGNSGQYIVGHLPNYHWYVNWTMFVWDDTESELVE FT EQIPPFLRFLDWFGIEYQYELAEYSKISAFLTIPKQVDIGGIGYLQSSVVISESFMNST FT AGASRLTASFSKLMLDPGALITVNVLGGQINLNAKDEDASVNPLWRSSSLLVVLMQSFP FT PTPEAQSAAHQTLSQTNTPILASIDPEGGGVYFNEADPDQSDFQNAFWGHHYGRLRRIK FT SRWDPAGLFVVRNGVGSEDWDVESMCRKETMVPA" FT mRNA join(<10475..10580,10674..10895,10964..11505,11552..>12514) FT /locus_tag="An14g02950" FT exon 10475..10580 FT /locus_tag="An14g02950" FT /number=1 FT intron 10581..10673 FT /locus_tag="An14g02950" FT /number=1 FT exon 10674..10895 FT /locus_tag="An14g02950" FT /number=2 FT intron 10896..10963 FT /locus_tag="An14g02950" FT /number=2 FT exon 10964..11505 FT /locus_tag="An14g02950" FT /number=3 FT intron 11506..11551 FT /locus_tag="An14g02950" FT /number=3 FT exon 11552..12514 FT /locus_tag="An14g02950" FT /number=4 FT CDS join(14534..15185,15282..15497,15577..15590,15686..15837, FT 16275..16569,16830..17312) FT /locus_tag="An14g02960" FT /note="Title: similarity to hypothetical protein encoded by FT An01g14870 - Aspergillus niger" FT /db_xref="UniProtKB/TrEMBL:A2R341" FT /protein_id="CAK46533.1" FT /translation="MVPGQSIVLYSRLHLVVQSQTLLRRVLYLIIFDTIVLLIPTTVLT FT YCTIYVRTTPVIRGFNVMERMQLAWFCAQEILISLIYIAETLKLLRLRPEKDAERHKTM FT YELIAINLVIILLDIALLVLEYVGLYTLQTTLKAAVYSVKLKLEFGVLRKLVSLVHARP FT AESSSSDQDTYPTFVDPNQITGDVTRAAPAYSRRQSQYPWTAISMDSLVLSDRRSCDIS FT HTRATPILISGTSPQRTASALVKGPPPKQVSRALYSKWPGMREMWLQRWLGSPIHGCPD FT QSLVTPIPYDHSCIPVDSHRACPQGPERARPKEKIASGGSELVRRPGKLELSSPAALAK FT QPGDSIVPDSWESDAMVRGAVTASATELSDQDEFIVVIVVERLLKATQLFGMNMTNWPV FT TLEDCDDVINRSTSISGTRRSRRGCLKVSSHSKLLSGSISLGGVSGGTSSGGITRAADW FT SLPTFGHQRLAANPKEGIRPSLTRSIWQSNPWGTTESPSLMKLILFPPPLTAPSACFFA FT RNPRLRGVWIPEYLTSRSVTGLHLTVRALRQTKSPFAAATIYIVVVYYSLLSARLPPHP FT SAPRVSASPSSPTVSMCFGLSSPSGRV" FT mRNA join(<14534..15185,15282..15497,15577..15590,15686..15837, FT 16275..16569,16830..>17312) FT /locus_tag="An14g02960" FT exon 14534..15185 FT /locus_tag="An14g02960" FT /number=1 FT intron 15186..15281 FT /locus_tag="An14g02960" FT /number=1 FT exon 15282..15497 FT /locus_tag="An14g02960" FT /number=2 FT intron 15498..15576 FT /locus_tag="An14g02960" FT /number=2 FT exon 15577..15590 FT /locus_tag="An14g02960" FT /number=3 FT intron 15591..15685 FT /locus_tag="An14g02960" FT /number=3 FT exon 15686..15837 FT /locus_tag="An14g02960" FT /number=4 FT intron 15838..16274 FT /locus_tag="An14g02960" FT /number=4 FT exon 16275..16569 FT /locus_tag="An14g02960" FT /number=5 FT intron 16570..16829 FT /locus_tag="An14g02960" FT /number=5 FT exon 16830..17312 FT /locus_tag="An14g02960" FT /number=6 FT CDS join(17794..20487,20545..21300,21352..21678) FT /locus_tag="An14g02970" FT /note="Similarity: shows strong similarity to sensory FT transduction histidine kinases and phytochrome-like FT proteins." FT /note="Title: similarity to phytochrome phy - Synechocystis FT sp." FT /db_xref="GOA:A2R342" FT /db_xref="InterPro:IPR016132" FT /db_xref="UniProtKB/TrEMBL:A2R342" FT /citation=[59] FT /inference="profile:COGS:COG4251" FT /inference="profile:PFAM:PF00072" FT /inference="profile:PFAM:PF00512" FT /inference="profile:PFAM:PF02518" FT /inference="similar to AA sequence:PIR:S74389" FT /protein_id="CAK46534.1" FT /translation="MDGATVGGTDRVYPIRSIISFNPAATDPNQQGIPNEIRSPRSGAR FT SYSIIDADTWDQLSSQPTSSPHTNPSPNAPVHTPESTDRLSQQQSPNVFSPASSAAERD FT APPDESSTYRKVAPEEGHASLVTSRFQHVVTAAGHAVITGNTPDSFRACEDEPIHIPGA FT VQTFGVMLVLRETPEGSLAVHVASENSEAILGHSPSNLFALESFTDLLQDDQTDILLDH FT IDFIRDDGYDPVSDGPEVFILAVKDRFGRPRRFWCAIHVNTAHRDVIICEFELEDDRIN FT PLNVAGRTTPTSPTVTLGFEPTPDQLASSTVNISQPLRVLRNARRRRGEAAAMEVFSIV FT SQIQDQLGDAQNMDALLNITIGIVKELTGFHRVMIYQFDSEANGDVVAELVDTRMTKDL FT YKGLHFPSTDIPKQARDLYRLNKVRILYDRDQMSSRLVCRGIEDLKTPLDMTHAYLRAM FT SPIHIKYLANMGVRASMSISINNTHDLWGLISCHSYGDTGMRVPFPIRKMCRLIGDTLS FT RNIERLSYASRLQARKLLNTIPTDANPSGYIIASSDDLLKLFDADYGALSIRGETKILG FT KSTESQEMLALLEFLKIRQLNSVVASHHVKKDFPDLRYPPGFKEISGMLYVPLSADGKD FT FIVFFRKGELTQIKWGGNPYTKLLQNGHLEPRASFQVWTETVMDRAREWSESEVETAAV FT LCLVYGKFIKVWRQQEAALEGSQLTKLLLANSAHEVRTPLNAIVNYLEIALEGALDTET FT RDNLTKSYSASKSLIYVINDLLDLTNTEKGHNLIKDEPFDLPLCFKEATAMFSGEAHRK FT GIEYTVHAHPGLPKTVLGDERRVRQAISNLISNAIQHTSTGGVTVEMWRAPGNPEPGFA FT TIHMTVLDTGTGMSDAMLETMFQELEQHTEVERGKGVLGLGLALVSRIVRNTHGQLTVR FT SEEGKGSRFQISLQFSTPDDTGSDQPETPQPSTQEGDATPFEAKEEFILVDSSSSAPSD FT GWRRSGSHRGTISPSADELDAKLVAEDSIDRTKDEAAGLLPSSDRRKLVTLPSTPERLD FT DVTRALQQNVQNLAISDKPAITSAGPAGPAPTSAPPAESDAKAPPGKYRVLVAEDDPIN FT GKIVQKRLGKLGHTVQLTVNGEECAAAYRADSAQFDVVLMDIQMPIVDGINSTKMIREF FT ETSSDSTALSSVAKLNNRIPIFAVSASLLEKDMSLYVDAGFDGWVMKPINFNRLNVLLE FT GLQTGDTRNSATYHPGCDWEQGGWFTPIPEEKQ" FT mRNA join(<17794..20487,20545..21300,21352..>21678) FT /locus_tag="An14g02970" FT exon 17794..20487 FT /locus_tag="An14g02970" FT /number=1 FT intron 20488..20544 FT /locus_tag="An14g02970" FT /number=1 FT exon 20545..21300 FT /locus_tag="An14g02970" FT /number=2 FT intron 21301..21351 FT /locus_tag="An14g02970" FT /number=2 FT exon 21352..21678 FT /locus_tag="An14g02970" FT /number=3 FT CDS complement(join(22505..23794,23922..24248,24339..24561, FT 24785..25146)) FT /locus_tag="An14g02980" FT /note="Similarity: similarity results from repetitive FT sequences." FT /note="Title: weak similarity to mucin-like glycoprotein FT 900 GP900 - Cryptosporidium parvum" FT /db_xref="UniProtKB/TrEMBL:A2R343" FT /protein_id="CAK46535.1" FT /translation="MKSISAVLIALLAASVSAGPVVTTVTIALANDQTGAQGSAAIPAD FT GSEQSISALYGGTGVGSGGVIKASSAQLTNFQANTNCVITKYGSVLATLNSRNTYVDLD FT GNPSAAQPVDLSAASVKCHHNAVEVTLIALPRRQSIAEYIEVVLQEMTAGPQETLSGGP FT SHPRAMTFLSVSGSESPDISSVAQPRVTLFKFHQGTSMPPTVSTKQASVHSVMHKQLLV FT RLTSPDQNIPPCDQLINKWMNCSQLSPTFVAANQHDDLPWASRILALFVALQLRSGGSR FT PLQVPLSTKDPTMNISELYLRLRHRPHIKPIPYILPITSLHGTLPLILEPRNDQTTAMN FT TTTTTTAIASYYTLPRADSYTAISLISISTFTCLLLYYLIFDLSFFTTTSTSTSTKPRP FT LTVPTTTLLTTTTTTLLSSTFCILLLFHHTHTPTRIASAILFVLTTTAASITNTLLLYF FT SLPLITIHQRPQAHFQLRIQRILLSTIIATILLFQLPHVIVAPAAATLYKDGHWTHAVT FT ILSRISVTAYCTREILLLAVYTWGVIKYLRPVIHHFHYESTHQDRQRICSTLLVAGCIS FT LILNIANIVAVYTVHNAAAMAFFPFVVSTKVLVEGVAVGRLVGFVGASRQPRCVYSIHG FT GGGGGDSRRGSAQPLITSTYSSASTMSGGLGAVETKDCGSDRDESPVGVQGRDKEWYTR FT NRIGSVDTIVSVAEPPLAHSVGHLVQEMPDLEGGSGVWC" FT mRNA complement(join(<22505..23794,23922..24248,24339..24561, FT 24785..>25146)) FT /locus_tag="An14g02980" FT exon complement(22505..23794) FT /locus_tag="An14g02980" FT /number=1 FT mat_peptide complement(join(22508..23794,23922..24248,24339..24561, FT 24785..25092)) FT /locus_tag="An14g02980" FT intron complement(23795..23921) FT /locus_tag="An14g02980" FT /number=1 FT exon complement(23922..24248) FT /locus_tag="An14g02980" FT /number=2 FT intron complement(24249..24338) FT /locus_tag="An14g02980" FT /number=2 FT exon complement(24339..24561) FT /locus_tag="An14g02980" FT /number=3 FT intron complement(24562..24784) FT /locus_tag="An14g02980" FT /number=3 FT exon complement(24785..25146) FT /locus_tag="An14g02980" FT /number=4 FT sig_peptide complement(25093..25146) FT /locus_tag="An14g02980" FT /inference="protein motif:SignalP:2.0" FT CDS join(27731..27754,27815..28050,28167..29199) FT /locus_tag="An14g02990" FT /note="Title: similarity to hypothetical protein KIAA1715 FT -Homo sapiens" FT /db_xref="InterPro:IPR019273" FT /db_xref="UniProtKB/TrEMBL:A2R344" FT /inference="profile:COGS:COG5415" FT /inference="similar to AA sequence:UniProtKB:AB051502.1" FT /protein_id="CAK46536.1" FT /translation="MVSLWPFRAEDTSPASFEKALAALSTKITRATTRLDLHRQHARRF FT KALWTLYTTFAYLLYSIIIALVLGWQNWGITEYGAIIGGPILIYLIRTISTRYYDYRIT FT KTQAYLDDLHKQREKTIEDLKTATRWNSTQQLLEKYGGESPKPARSNSVKSGDAKRNKS FT EGAKRKQPSQQQQQHVQRTGIPPPPTANIRRPAPQQFPSSPQPPSTPPVAFQHHQQSPH FT VFPGQQQLQQQQQSAPSMNVGLEEPGFAPNAFSSTSTQYVEQSHWYDRLLDVLLGEDET FT QPKNRLALICSTCRLVNGQAPPGIKTLEELGRWRCGNCGAWNGEESEAKKVLAGIRKEQ FT QQQSSNISSGSVDGTETRSSVGGDVTDDGVMVAATGSEDDQLESQSEGAETSEEQVEQV FT AESENEEEEEPEPQPSKRVTRSRAKGGKRKG" FT mRNA join(<27731..27754,27815..28050,28167..>29199) FT /locus_tag="An14g02990" FT exon 27731..27754 FT /locus_tag="An14g02990" FT /number=1 FT intron 27755..27814 FT /locus_tag="An14g02990" FT /number=1 FT exon 27815..28050 FT /locus_tag="An14g02990" FT /number=2 FT intron 28051..28166 FT /locus_tag="An14g02990" FT /number=2 FT exon 28167..29199 FT /locus_tag="An14g02990" FT /number=3 FT CDS complement(join(29503..31996,32053..32945,33003..33132, FT 33181..33328,33435..33687,33747..33770,33861..33889, FT 33963..34050)) FT /locus_tag="An14g03000" FT /note="Function: CAF of A. thaliana appears to suppress FT cell division in floral meristems." FT /note="Title: similarity to RNA helicase/RNAseIII carpel FT factory CAF - Arabidopsis thaliana" FT /db_xref="GOA:A2R345" FT /db_xref="InterPro:IPR000999" FT /db_xref="UniProtKB/Swiss-Prot:A2R345" FT /citation=[77] FT /inference="profile:COGS:COG0571" FT /inference="profile:PFAM:PF00271" FT /inference="profile:PFAM:PF00636" FT /protein_id="CAK46537.1" FT /translation="MTVAATVLPAGEDAPAYRPRSYQVEMFEANGNWQWENSHELESNP FT HKLIWFLTPTVALCLQQFKFLSDNIPAVRARTLTSLDKVELWTEQPVWDAILKEMQVVV FT STHAVLADAMSHGFVKITQLGLMIFDEAHHCMRRHPANKIMQDFYHPALERHGAEAVPK FT ILGLTASPVVRSNRQELLKIESNLDAVCKTPRTHRSELMTHTHRPHLQQILFTPVLLDD FT LQDDPYIKKLRKSPLDGRALQKVLESGKTYCNDQLKRFATRSLHIFEELGEWAADYFIH FT ASIEQLKARAGNSADTMGWTDEEKAYLLDIVSKLPIPNIDLTHSDPDRIPISSKFRSLL FT EFLDTKGEPNFSGLIFAKQRATVSVMEKLLSIHPVTKHRFRCASFVGWSGGGSKDVLGE FT LLDARMQRDTLSEFRTGQKNLIIATDVLEEGIDISACSVVVCFDKPPNLKSFVQRRGRA FT RHRQSTYAIMFATDDESSALSKWEDLEQAMIEAYEDDERRLREAWALEAINEEVVERLE FT VQSTGAVLTADTAVAHLNHFCAVLPRQPYASNEPEFSYEKDDADLLRGTVTLPSCVHPG FT VRRIQGQRWWQTERAARKEAAFQAYKRLYEFGLLSDHLLPFKRNLELKETDLTNLPALV FT EVSEQYDPWVDWACSWSSPDVHQTRIAIKHNGDSRMCIRLTSPTSLPPVEPMTLFWDSE FT TIYTLDFDKPKRMKEIAAESIENMRLATALYLQAASSRQMRPEQDFVTLFGPDLTDLEL FT AEWLNKHAGDEPALEVYSRKDFPTVMGIVRDRSRYNEPMLFKRWVVSGQDDTPIVELEC FT DAVPKRRNLLHRQTLAAKQPDSETPAISSKIRLILAENCTIDKLPYAETIFGRFISVIL FT DRLEATLVATRLCETILRDLEFSSIRHIITAITAPSAQSLTNYQRYEFFGDSVLKFTVS FT CQLFFQHPNWHEGYLSEGRDEIVQNSRLARAALDAGLDAFIMNKMFTPRKWSAPLISEK FT ISLTPKQRTMSTKVLADVVEALIGASYIDGGFAAAHACIHRFLPEVNLENIDRTTAPMP FT KDGVTNHTLNDDHLMAHIGYTFTNKSLLVESLTHPSCQFDTTTQSYQRLEFLGDAVLDM FT AIMSTLLSHPREIPQGLMTKIKHAVVNANLLAFFCMEFALTEKRTNVQVTPTGTVTLNP FT STEHIELWRFMRYQGAHLQTARDLALSRHSSLRGSIIHGLKHSPSYPWKSLSQLNADKF FT FSDIIESILGAIFIDSHGNLAECEKFLERLGLLRYLRRILKDEVDVMHPRNIAQQMAKG FT EIRFEVLRVPNEGGGGGEDDGATYRCTVKMAGVDGVAVVVEGCLTSEEAEITAAERAVE FT ILVGRGCSL" FT mRNA complement(join(<29503..31996,32053..32945,33003..33132, FT 33181..33328,33435..33687,33747..33770,33861..33889, FT 33963..>34050)) FT /locus_tag="An14g03000" FT exon complement(29503..31996) FT /locus_tag="An14g03000" FT /number=1 FT intron complement(31997..32052) FT /locus_tag="An14g03000" FT /number=1 FT exon complement(32053..32945) FT /locus_tag="An14g03000" FT /number=2 FT intron complement(32946..33002) FT /locus_tag="An14g03000" FT /number=2 FT exon complement(33003..33132) FT /locus_tag="An14g03000" FT /number=3 FT intron complement(33133..33180) FT /locus_tag="An14g03000" FT /number=3 FT exon complement(33181..33328) FT /locus_tag="An14g03000" FT /number=4 FT intron complement(33329..33434) FT /locus_tag="An14g03000" FT /number=4 FT exon complement(33435..33687) FT /locus_tag="An14g03000" FT /number=5 FT intron complement(33688..33746) FT /locus_tag="An14g03000" FT /number=5 FT exon complement(33747..33770) FT /locus_tag="An14g03000" FT /number=6 FT intron complement(33771..33860) FT /locus_tag="An14g03000" FT /number=6 FT exon complement(33861..33889) FT /locus_tag="An14g03000" FT /number=7 FT intron complement(33890..33962) FT /locus_tag="An14g03000" FT /number=7 FT exon complement(33963..34050) FT /locus_tag="An14g03000" FT /number=8 FT CDS complement(join(35102..35605,35659..35915,36113..36128, FT 36407..36460)) FT /locus_tag="An14g03010" FT /note="Function: might be involved in transcriptional FT regulation." FT /note="Similarity: shows similarity to proteins containing FT bZIP transcription factor domains." FT /note="Title: weak similarity to transcription activator FT Cin5 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R346" FT /db_xref="InterPro:IPR004827" FT /db_xref="UniProtKB/Swiss-Prot:A2R346" FT /inference="profile:PFAM:PF00170" FT /inference="similar to AA sequence:PIR:S50316" FT /protein_id="CAK46538.1" FT /translation="MQPTLAPAPHPSMQTSAQDHADQAAHQHLSHPQQARPQGPTAQPP FT HMQPNTTSPRDQNNIDPAISGAAMLSGPPQTPPQPEPTGQESPKTYGKRPLSTSKRAAQ FT NRAAQRAFRQRKESYIRKLEEQVKEFDNTNETMKQLQAENYQLREYIINLQSRLLDSQG FT EVPELPGNIDLNQPRNDISVPPPGAPAATGPAPGPGGAPQQMQVPNPGAATNEDMNSLN FT RIAVAGLGMRKHPNEEANFLGNNFQARRPRNDDGQPDGSEATKTEPGHGLPVVS" FT mRNA complement(join(<35102..35605,35659..35915,36113..36128, FT 36407..>36460)) FT /locus_tag="An14g03010" FT exon complement(35102..35605) FT /locus_tag="An14g03010" FT /number=1 FT intron complement(35606..35658) FT /locus_tag="An14g03010" FT /number=1 FT exon complement(35659..35915) FT /locus_tag="An14g03010" FT /number=2 FT intron complement(35916..36112) FT /locus_tag="An14g03010" FT /number=2 FT exon complement(36113..36128) FT /locus_tag="An14g03010" FT /number=3 FT intron complement(36129..36406) FT /locus_tag="An14g03010" FT /number=3 FT exon complement(36407..36460) FT /locus_tag="An14g03010" FT /number=4 FT CDS complement(join(38295..39545,39595..40026,40092..40380, FT 40451..40607,40677..40761)) FT /locus_tag="An14g03020" FT /note="Function: suggested activities include nutritional FT activity, cytokine and cell proliferation/differentiation FT activity, immune stimulating (e. g. as vaccines) or FT suppressing activity, haematopoiesis regulating FT activity,tissue growth activity, activin/inhibin FT activity,chemotactic/chemokinetic activity, haemostatic and FT thrombolytic activity, receptor/ligand FT activity,anti-inflammatory activity, cadherin/tumour FT invasion suppressor activity, and tumour inhibition FT activity." FT /note="Function: the human secreted proteins, and the FT polynucleotides encoding them, are predicted to have FT biological activities which would make them suitable for FT treating, preventing or ameliorating medical conditions in FT humans and animals." FT /note="Remark: blast hit against protein of patent FT database." FT /note="Title: similarity to secreted protein SEQ ID NO:58 FT from patent WO9957132-A1 - Homo sapiens" FT /db_xref="InterPro:IPR007632" FT /db_xref="UniProtKB/TrEMBL:A2R347" FT /inference="profile:PFAM:PF04547" FT /protein_id="CAK46539.1" FT /translation="MASTIPRDPVHSNHYVDYVIRYNFGGETDAAYATEQLDRLLRKLF FT EVGLQTEVRQGDESSLLIFVRASRKKSLKRAIYQSRIRDWLYGVRNNEPESESSAEAQS FT ESERLRVIYHMITVPKEAGGAGITPKHGEWKCVDAIFPLHDEAMNKQCIKDWSQKTFLS FT ADDLDQIRNTFGENVGFYFAFLQSYFRFLIFPAVFGFSCWLLLGSFSIIYAVVNSLWCI FT IFIEYWKRQEEDLSCRWQTKGVSAVRPKRREFQPEREVQDESTGEVRGVFPATRRMYRQ FT LLIVPFALLSAVALGVIIATCFAIEIFISEIYNGPLKTYLVFIPTILLSALIPTMSSVL FT VSIATKLNDYENYETQPAYDVALTQKIFIINFITSYLPIFLTAFVYVPFASRIVPYLDV FT FHLTVRPFVSKEDANSRRTEFSIDPDRLRKQVIYFTVTAQAVNFAMETIVPMLKQRLSR FT EYKEYNRRKQGKIETEDGSEAKKEALFDDHPDETKFLTRVRNEADMEDYDVTEDLREMC FT IQFGYLALFSPVWPLVPVSFLVNNWVELRSDFFKICMECKRPWPQRADTIGPWLESLGF FT LSWVGSITSSALLYMFSNGHEGPNGEPTAIRGWALLLTIFFSEHIYLMVRYAIRAAMAK FT LEPPNAKKERTERYLMRKRYLESTIAARSSDDEGDGNEQDHSMKVPDITRKSLEEDARE FT WSTHDTDPAERFWMRQKGWKESAHVGATIIKTLATEPQAKKEQ" FT mRNA complement(join(<38295..39545,39595..40026,40092..40380, FT 40451..40607,40677..>40761)) FT /locus_tag="An14g03020" FT exon complement(38295..39545) FT /locus_tag="An14g03020" FT /number=1 FT intron complement(39546..39594) FT /locus_tag="An14g03020" FT /number=1 FT exon complement(39595..40026) FT /locus_tag="An14g03020" FT /number=2 FT intron complement(40027..40091) FT /locus_tag="An14g03020" FT /number=2 FT exon complement(40092..40380) FT /locus_tag="An14g03020" FT /number=3 FT intron complement(40381..40450) FT /locus_tag="An14g03020" FT /number=3 FT exon complement(40451..40607) FT /locus_tag="An14g03020" FT /number=4 FT intron complement(40608..40676) FT /locus_tag="An14g03020" FT /number=4 FT exon complement(40677..40761) FT /locus_tag="An14g03020" FT /number=5 FT exon complement(41386..41959) FT /locus_tag="An14g03030" FT /number=1 FT CDS complement(41386..41959) FT /exception="reasons given in citation" FT /locus_tag="An14g03030" FT /EC_number="2.3.1.-" FT /note="Catalytic activity: it catalyzes the FT N(1)-acetylation of spermidine and spermine and, by the FT successive activity of polyamine oxidase, spermine can be FT converted to spermidine and spermidine to putrescine." FT /note="Function: human SPD/SPM acetyltransferase is a FT rate-limiting enzyme in the catabolic pathway of polyamine FT metabolism." FT /note="Remark: contains putative sequencing error that FT caused a wrong geneprediction (wrong start codon)." FT /note="Similarity: shows similarity to several FT acetyltransferases of different species." FT /note="Title: similarity to spermidine/spermine FT N(1)-acetyltransferase SAT - Homo sapiens [putative FT frameshift]" FT /note="putative frameshift" FT /db_xref="GOA:A2R348" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:A2R348" FT /citation=[10] FT /inference="profile:COGS:COG0454" FT /inference="profile:PFAM:PF00583" FT /protein_id="CAK46540.1" FT /translation="MPLCITCVGPIRPLAIPPLLTNHVLATIADVPIIHQFICELADYE FT KALHEVEATHESLLETLSFPDSPPKRGSVYTALITPPATAENPTPKPVGMALFFYNYST FT WRAAPGIYLEDLYVQPSARGNGYGFKLLKYLAAKVLEIKGRRLEWSVLKWNEPSIKFYE FT QVGAKAMDEWTKMMMEGPALNKLAEGL" FT mRNA complement(<41386..>41959) FT /locus_tag="An14g03030" FT CDS complement(join(42489..43965,44048..45389,45628..46066, FT 46200..46331)) FT /locus_tag="An14g03040" FT /EC_number="3.6.4.1" FT /note="Similarity: shows similarity to myosin heavy chain FT of different species." FT /note="Title: similarity to myosin heavy chain FT -Dictyostelium discoideum" FT /db_xref="GOA:A2R349" FT /db_xref="InterPro:IPR000237" FT /db_xref="UniProtKB/TrEMBL:A2R349" FT /citation=[12] FT /citation=[18] FT /citation=[20] FT /inference="profile:COGS:COG1196" FT /inference="similar to AA sequence:PIR:A26655" FT /protein_id="CAK46541.1" FT /translation="MLPFFPAYRLLLLVLTFCRLLYFCLSFISLAVALAHRPATVMFQR FT LRDAIDSRIAEEQARQRSAQTSLSRSNSARHPTGRNLSPTRRTSRPRRNTGTPVRGPDP FT NEFEPEFAIGDDEGSSRSATPRLESAGGSEAAPEENTGEGKTSSEESATKKPEAQPVTE FT TNQSPSELPPEIRVKLRRLGKLESRYQAERDDYKKKLEESQKSTKAAWDEVTKLKEDSK FT SQAKKDEGPTSESSATDKSTPDSAAKSGKASTSGAKVTAEASQKESDAQGDSEEFFSYD FT SEIPRLESELKEKQEEIETLKSQTESLKRDLSVARESTEGMVHNLESATRELVELRDTK FT DKQDAELEKLKTSKQEEVSELKAKLEKSEAAVSKTSSEIESLKSELKQKADEIEQLQAQ FT TAHAKSADQQAEIESKLEQLNREKEANDKRLGVLQGLVDSLRSQLKETEETFTSLKKEM FT GQKNEDMGKLQNVVNFLDANLKDNEKWQQTKDQIANGKEAAFDELRESLAPPPQTTAVK FT EDPAGPTAPAANPAGGAGGGKKKNKKKKKGGKANEEASKVIEAAAPEEKQEPAEQDDQA FT ALKLTELEQNIESLKTQLAEKDATIDRLCSKLKGEEDLKEEIETLRDDLLNIGQDHVKP FT RISSESSKVDTEKAHNDLKDEYESLKIKSTTLETELSAAQQLAATRFKDMTELRETLQK FT LQPEVKKLRAESAELKSTKESLNSKTADLRNLEGQHDELRAELKSLKSTISERDAEVKS FT LNQKIRQETDSRLKSEEKLTVAQSDLRYSESKKQEAVEAKEKLASDLSKAQDELKAARA FT RLREAESQAAQLNKDLGGLREEIQLKTAQHASAQSLMNSMRDQAGELGMQMKEARERCE FT SLEEELADAHRLLSERTREGETMRRLLNDIDGRAEAKVRDFKERMEAAIEERDRAEDEA FT SAQSRRRARELEDLKGKLREAERALRTVEEDKEELEHTQKDWKRRRDQLEAESEKTTQE FT LSDLRQAMARLRDALDESEKQVRDLEKEKAELRRSVEETNARLEKVRKSNKMLPDESRF FT GTNPQSSRSSIDSGSRKALASPVSKDRSPSTRRSETPTGPSTSSIDYIYLKNVLLQFLE FT QKDKNYQKQLVPVLGMLLHFDR" FT mRNA complement(join(<42489..43965,44048..45389,45628..46066, FT 46200..>46331)) FT /locus_tag="An14g03040" FT exon complement(42489..43965) FT /locus_tag="An14g03040" FT /number=1 FT mat_peptide complement(join(42492..43965,44048..45389,45628..46066, FT 46200..46226)) FT /locus_tag="An14g03040" FT intron complement(43966..44047) FT /locus_tag="An14g03040" FT /number=1 FT exon complement(44048..45389) FT /locus_tag="An14g03040" FT /number=2 FT intron complement(45390..45627) FT /locus_tag="An14g03040" FT /number=2 FT exon complement(45628..46066) FT /locus_tag="An14g03040" FT /number=3 FT intron complement(46067..46199) FT /locus_tag="An14g03040" FT /number=3 FT exon complement(46200..46331) FT /locus_tag="An14g03040" FT /number=4 FT sig_peptide complement(46227..46331) FT /locus_tag="An14g03040" FT /inference="protein motif:SignalP:2.0" FT CDS join(47674..48035,48143..48792,48940..52376) FT /locus_tag="An14g03050" FT /note="Similarity: shows weak similarities to neuropathy FT target esterases." FT /note="Title: strong similarity to hypothetical protein of FT the UPF0028 family - Schizosaccharomyces pombe" FT /db_xref="GOA:A2R350" FT /db_xref="InterPro:IPR002641" FT /db_xref="UniProtKB/Swiss-Prot:A2R350" FT /inference="profile:COGS:COG0664" FT /inference="profile:COGS:COG1752" FT /inference="profile:PFAM:PF00027" FT /inference="profile:PFAM:PF01734" FT /inference="similar to AA sequence:PIR:T50444" FT /protein_id="CAK46542.1" FT /translation="MATGDGIIAAPPSLESSSLDPLHVLPASSSTAARSLATSIPALTA FT SFSVVSGFSSHLPPPPVTPPAPSTMVGWIGWIFSFIFQVIPSVLYWIVTFTTITLPTWL FT FTLFSMSLTFTMNFTTLLLIALAVVSTISWFIRYRFLNMYSRLPPEPQRKEPQLDLFPD FT VPDSDTKPGLANYLDEFLSAIKVFGYLERPVFHELTRTMQTRKLIAGETLLLEEEKGFC FT LVVDGLVQIFVKSMRDRKSGSDEELNRMAGESSDEDDHRPDGRQGYQLLTEVKNGASMS FT SLFSILSLFTEDVQLRYADSSASSASSIGPGLAIGPDSFPASPREMDDSPHVYQGDLHP FT DIVARAMVDTTIAIIPASAFRRLTRVYPKATAHIVQVILTRLQRVTFATAHSYLGLNNE FT VLGIEKQMTKFTTYDLPNELRGSALDRLKDKFIKERDRLGQEEVTKGIALHNPYGGRRP FT RSSSFRRKEAALQAKMVASKRPVSMVAQDSALSDRENSGVSPGDLLSTIQLSRFGPRYE FT HLAPRLLSPLTEKEHSPLRSPSPMIPGRASPFHRKESLDEDALFRESILECIMKGIGLT FT GSTNDFLRKSSHPSGDVSPKLLSYDSRRQKAVFSNNAFGFIDPYEGSADGESESMMSMS FT VTSAGGTSPIVNLREELRNDIEIVYFPQGSVLVEQGERHPGLYYVVDGFLDVGIPVDDK FT EEDLVGSSRPAHEELFPMLRRTNTSSSRVSGSAAAANDPRRKKQSRRSLYLIKPGGIQG FT YVGAVASYRSYTDVVAKTDVYVGFLPRASLERIAERYPLALLTLAKRLTSLLPRLLLHI FT DFALEWVQVSAGQVIYHQGDESDAIYLALNGRLRSVHEGPNGKMTVVGEYGQGESVGEL FT EVMTESTRPATLHAIRDTELAKFPRTLFNSLAQEHPGITIQVSKLIAQRMRDLVETPLA FT EKGGEPGVSGTVKTAKSTLNLRTVGILPVTAGVPVVEFGNRLLQALHQIGVTNGATSLN FT QAAILNHLGRHAFSKMGKLKLSQYLADLEEKYGMVLYIADTSVNSPWTQTCITQADCIL FT LVGLAESTPSIGEYERFLLGMKTTARKELVLLHGERYCPPGLTRQWLKNRVWINGGHHH FT VQMAFRLTAEPSHPQTKRFGTVLKQRVQVIQAEIQKYTSRRIRQSPLYSAQTPFKGDFH FT RLARRLCGRSVGLVLGGGGARGIAQVGVIKALEEAGIPIDVIGGTSIGSFIGALYARDA FT DVVPMYGRAKKFAGRMGSIWRFALDLTYPTVSYTTGHEFNRGIFKTFGDSQIEDFWLEF FT YCNTTNISRSRAEYHSSGYTWRYVRASMSLAGLIPPICDEGSMLLDGGYIDNLTVDHMK FT GLGADVIFAVDVGSIDDNTPQVYGDSLSGFWAVVNRWNPFSSCPNPPTLSEIQARLAYV FT SSIENLERAKNTPGCLYMRPPIDPYGTLDFAKFDEIYQLGYAYGKNYLEKLKREGSLPL FT PEETEEKKKLQRTLAPRRASI" FT mRNA join(<47674..48035,48143..48792,48940..>52376) FT /locus_tag="An14g03050" FT exon 47674..48035 FT /locus_tag="An14g03050" FT /number=1 FT intron 48036..48142 FT /locus_tag="An14g03050" FT /number=1 FT exon 48143..48792 FT /locus_tag="An14g03050" FT /number=2 FT intron 48793..48939 FT /locus_tag="An14g03050" FT /number=2 FT exon 48940..52376 FT /locus_tag="An14g03050" FT /number=3 FT CDS join(53477..53546,53606..53705,53773..54339,54403..54472) FT /locus_tag="An14g03060" FT /note="Title: strong similarity to hypothetical protein FT encoded by An16g01890 - Aspergillus niger" FT /db_xref="UniProtKB/TrEMBL:A2R351" FT /protein_id="CAK46543.1" FT /translation="MFCLGLLALLYVRLLRDDLILVLGRVEKPPARRKHNALVLAKTSS FT EDVTWAYALKPHWKPYIYTSDKEPGYRPIPANKAREGMAYLTHIIEHYDYLADVTAFMH FT ASATQWHNDVGDTASSSLLQNLSLDAVNKAGYANLRCEHRPGCPVAVRPFDPAMESNHN FT VVYRNFTSIYMDMFSVPREQVPTEIGGVCCGQFVLTRDRIRERPRDDYVRMRDWALATD FT MDTFAAGSVFEMLWHIIFLEQPVSCPDVQQCYCELYNICPEIDSGS" FT mRNA join(<53477..53546,53606..53705,53773..54339,54403..>54472) FT /locus_tag="An14g03060" FT exon 53477..53546 FT /locus_tag="An14g03060" FT /number=1 FT sig_peptide 53477..53524 FT /locus_tag="An14g03060" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(53525..53546,53606..53705,53773..54339,54403..54469) FT /locus_tag="An14g03060" FT intron 53547..53605 FT /locus_tag="An14g03060" FT /number=1 FT exon 53606..53705 FT /locus_tag="An14g03060" FT /number=2 FT intron 53706..53772 FT /locus_tag="An14g03060" FT /number=2 FT exon 53773..54339 FT /locus_tag="An14g03060" FT /number=3 FT intron 54340..54402 FT /locus_tag="An14g03060" FT /number=3 FT exon 54403..54472 FT /locus_tag="An14g03060" FT /number=4 FT CDS join(55400..55991,56050..57059) FT /locus_tag="An14g03070" FT /EC_number="1.5.3.-" FT /note="Catalytic activity: CHO has oligosaccharide FT oxidation activity." FT /note="Function: it can oxidize the reducing end of an FT oligosaccharide more efficiently than the corresponding FT monosaccharide, e. g. preferentially oxidizing FT maltodextrins or cellodextrins over glucose." FT /note="Similarity: shows strong similarity to several FT oxidases with unknown function and to M. nivale FT carbohydrate oxidase (CHO) i. e. protein Y24919 of patent FT WO9931990-A1." FT /note="Title: strong similarity to carbohydrate oxidase CHO FT from patent WO9931990-A1 - Microdochium nivale" FT /db_xref="GOA:A2R352" FT /db_xref="InterPro:IPR016166" FT /db_xref="UniProtKB/TrEMBL:A2R352" FT /inference="profile:COGS:COG0277" FT /inference="profile:PFAM:PF01565" FT /protein_id="CAK46544.1" FT /translation="MAPPVIFTAAVLFMLPNQLAALPQNPGNISTPATANHGVLPRSLE FT SCLGATGVSVVYATDAGYSNLTVADNSNYHPHPQAVVIPNSTEQVAATVRCVAAEQGRV FT TLTTRGGGHGYAAYSLSGQVVIDSSQMTDIVLDESTQEVTVQMGQKLGPLALAMGRAGY FT ALPHGTCPGVGVAGHSLGGGWGFTSREWGWLVDRLVSLELVDVTGRIRTISPKATNPNT FT TSTDDTNDGDLWWALRGAGSNNFGIVTSFTYRMQPAPTAIVNYNIGFASQSDCVQVLLT FT LQEIGSHPATSSAGFPTSLGGELIIDGGYQPPKAYCSFTGQYLGDSAAYNETIQRLLSP FT LARQSIQPLTTTSSFYTNWVSALTNLMGDLDSPSVPQPYYAKSLFDDGHPNYTSASISR FT IFSAIQPAGPDAFISFDLNGPDAATTLPPDDSVGPMAFNHRNNLFMSQIYAWDFPGFTN FT ASARETAVDRLSDVADAVRQAAPKGGWQAYQNYIDPYLQNWAERYYGDALDRLKEIKKK FT WDPLNILDFPQGLGRA" FT mRNA join(<55400..55991,56050..>57059) FT /locus_tag="An14g03070" FT exon 55400..55991 FT /locus_tag="An14g03070" FT /number=1 FT sig_peptide 55400..55462 FT /locus_tag="An14g03070" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(55463..55991,56050..57056) FT /locus_tag="An14g03070" FT intron 55992..56049 FT /locus_tag="An14g03070" FT /number=1 FT exon 56050..57059 FT /locus_tag="An14g03070" FT /number=2 FT CDS complement(join(58536..58794,58858..58961,59023..59166)) FT /locus_tag="An14g03080" FT /note="Localization: might be a transmembrane protein." FT /note="Similarity: seems to be the aminoterminus of the FT predicted protein." FT /note="Similarity: shows strong similarity to pos. 121 to FT 553 of cDNA clone 2960 of A. niger." FT /note="Similarity: the ORF shows strong similarity to cDNA FT clone 2960 - Aspergillus niger." FT /note="Title: similarity to hypothetical membrane protein FT YDL218w - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R353" FT /db_xref="InterPro:IPR019640" FT /db_xref="UniProtKB/TrEMBL:A2R353" FT /inference="similar to AA sequence:PIR:S67781" FT /protein_id="CAK46545.1" FT /translation="MFSSTVARPLQLVTRFMQWASAVIVMGITSYFIHKGPRGQHTIYW FT EVISTMSVVFFLPAFISPFMPNALSKFVLIIDVIFSYLWLTAFIFAAQDYNWHNCGANS FT PPGLSCSKKKANEAFIFLTFIFTFFAIFLEVGALWAYRRESTPVREKNTGGAHGGPADA FT PVATA" FT mRNA complement(join(<58536..58794,58858..58961,59023..>59166)) FT /locus_tag="An14g03080" FT exon complement(58536..58794) FT /locus_tag="An14g03080" FT /number=1 FT mat_peptide complement(join(58539..58794,58858..58961,59023..59100)) FT /locus_tag="An14g03080" FT intron complement(58795..58857) FT /locus_tag="An14g03080" FT /number=1 FT exon complement(58858..58961) FT /locus_tag="An14g03080" FT /number=2 FT intron complement(58962..59022) FT /locus_tag="An14g03080" FT /number=2 FT exon complement(59023..59166) FT /locus_tag="An14g03080" FT /number=3 FT sig_peptide complement(59101..59166) FT /locus_tag="An14g03080" FT /inference="protein motif:SignalP:2.0" FT CDS complement(join(63282..63420,63503..63731,63790..63930, FT 63990..64252,64312..64634,64697..64711,64779..64976)) FT /locus_tag="An14g03090" FT /note="Title: strong similarity to glucose/galactose FT transporter gluP - Brucella abortus" FT /db_xref="InterPro:IPR011701" FT /db_xref="UniProtKB/TrEMBL:A2R354" FT /citation=[54] FT /inference="profile:COGS:COG2271" FT /protein_id="CAK46546.1" FT /translation="MSTTTIELAPQGLQESQSPVQPFGPSTEEAIVQQKQKWNDPPINR FT WRLLATFISFTVVGANDGVYGALVPYLREDYKLSTTVVSLIFVTPFAGYTIATLIVNKI FT HMTLGQRGIAIIGPLCHIIPYVIMAIHPPWPAMLAVYVIVGLGNGLIDAAWNSWIADMA FT NANAMMGVLQAFYGLGATISPLVGTQVIKSGLRWNYFYYTLLGGSVLELMVSSTLFWKA FT NAVSYRATNHRNSDSGDGSRTTEAMKSPITWLIAVWLFVYMGVEVSVGGWVVDFMVQVR FT HGAPYQSGLIPTGFWAGVTVGRLVLGFVNDWLGERIAISIYLVISIALELIFWLVPQFV FT VSAVAVSLLGFFTGPLFPAAIVVAAKLLPKHLHTPGIGLASALAGGGGAILPFVAGAIS FT GARGVQSLQPFVLALLVALIAIWVLLPRNKHHAHGV" FT mRNA complement(join(<63282..63420,63503..63731,63790..63930, FT 63990..64252,64312..64634,64697..64711,64779..>64976)) FT /locus_tag="An14g03090" FT exon complement(63282..63420) FT /locus_tag="An14g03090" FT /number=1 FT intron complement(63421..63502) FT /locus_tag="An14g03090" FT /number=1 FT exon complement(63503..63731) FT /locus_tag="An14g03090" FT /number=2 FT intron complement(63732..63789) FT /locus_tag="An14g03090" FT /number=2 FT exon complement(63790..63930) FT /locus_tag="An14g03090" FT /number=3 FT intron complement(63931..63989) FT /locus_tag="An14g03090" FT /number=3 FT exon complement(63990..64252) FT /locus_tag="An14g03090" FT /number=4 FT intron complement(64253..64311) FT /locus_tag="An14g03090" FT /number=4 FT exon complement(64312..64634) FT /locus_tag="An14g03090" FT /number=5 FT intron complement(64635..64696) FT /locus_tag="An14g03090" FT /number=5 FT exon complement(64697..64711) FT /locus_tag="An14g03090" FT /number=6 FT intron complement(64712..64778) FT /locus_tag="An14g03090" FT /number=6 FT exon complement(64779..64976) FT /locus_tag="An14g03090" FT /number=7 FT CDS complement(join(65757..66501,66575..67143)) FT /locus_tag="An14g03100" FT /note="Function: chicken enzyme is responsible for the FT formation of pentaantennary asparagine-linked FT oligosaccharides (N-glycans)." FT /note="Similarity: shows only similarity to aminoterminal FT part of chicken enzyme and similiar enzymes of other FT species." FT /note="Title: weak similarity to FT N-acetylglucosaminyltransferase VI GnT-VI - Gallus gallus" FT /db_xref="UniProtKB/TrEMBL:A2R355" FT /citation=[84] FT /inference="similar to AA sequence:UniProtKB:AB040608.1" FT /protein_id="CAK46547.1" FT /translation="MLPIPPTRVAKQFFTHFPYYLQLRASKILISSLFVWLLIFFYCRV FT TLWRDPHSAYFEDRHVYELDYSLHREREAWHFISQHNSGIDPPDYVKSGSTPSVCIAMV FT TVRRDSDHYFEASVGSLLEGLDERERQALYLSILFADTDPRVHPSWDQKWVGRLVDSAD FT SYNVTEGQLQHLQDLEKEKNFYEKGVFDYIYALRACQEVNAPYTIIFEDDIILATGWFS FT KTLKALSDISQRSQQPRDPWIYLRLFYTETSLGWSDSDMAYRNMPLIFGLLMLSTFSSL FT SMLRHTRFQRLHLDTLSIVVISMVCVPAFTALVYMAGKYNVMPLHGVVEMNQYGCCTQG FT LVFPRENVDGLIEFLSARGHGQTDSMIEEYADQSQLTRYALAPPQLQHVGLKSSRNNLD FT INTQSTWAFWFETNDPAKLRREHATLLEDYDVERMLNV" FT mRNA complement(join(<65757..66501,66575..>67143)) FT /locus_tag="An14g03100" FT exon complement(65757..66501) FT /locus_tag="An14g03100" FT /number=1 FT intron complement(66502..66574) FT /locus_tag="An14g03100" FT /number=1 FT exon complement(66575..67143) FT /locus_tag="An14g03100" FT /number=2 FT CDS complement(join(67917..68729,68779..68992,69038..69368, FT 69415..69622)) FT /locus_tag="An14g03110" FT /EC_number="1.14.-.-" FT /note="Function: initial oxygenation step in trichothecene FT toxin biosynthesis." FT /note="Remark: trichothecenes are sesquiterpenoid FT mycotoxins and act as protein synthesis inhibitors for FT eukaryotic organisms." FT /note="Title: strong similarity to cytochrome P450 FT monooxygenase TRI4 - Myrothecium roridum" FT /db_xref="GOA:A2R356" FT /db_xref="InterPro:IPR017972" FT /db_xref="UniProtKB/TrEMBL:A2R356" FT /citation=[26] FT /citation=[62] FT /inference="profile:COGS:COG2124" FT /inference="profile:PFAM:PF00067" FT /inference="similar to AA sequence:UniProtKB:MRAF9417.1" FT /protein_id="CAK46548.1" FT /translation="MSLLWNVGVAALLAVLWTASEAVRRLYFHPLAHIPGPRLAALTWW FT YEFYFDVIRPGQYVFKIQELHTRYGPIIRITPDEVHVNDVGFLDTIYAPSMIRRDKYGY FT QLRSLRVPGGLGTTTDHDLHKVRRESLTPFFSKKNIQYMEGLITDKVDQLKQLISTHAA FT RDTPVNLSDVFLAFSNDVVNNFLFAHRTDVLASEPKAATLRQNSKELLMGININKHFPQ FT IPDLLESLPMSISRPVMPPGLIDLLALFDRVREEIFMIKKDKESSVTHKKNIGPTGKAS FT VFDSLVDNPNLPASEKTLLRLQQEGALLVLAGTESPAQTLNIIFYHLLANPALLEKLRR FT ELRAVPVPSSWTQLEQLPYLSAVIEEGNRLSFGVTARSARIAYEPLTYKPSAHVSSTCP FT PSTRSKSYIIPAGTPVCTTTLSAHTADTVFPDPFVFDPERWIGDAGKERRRFQMAFNKG FT GRRCLGIELARAELYHVVAALVREFDMALFETDADDVAFMYDYQVAMPKMGSKGVRIMA FT KLAH" FT mRNA complement(join(<67917..68729,68779..68992,69038..69368, FT 69415..>69622)) FT /locus_tag="An14g03110" FT exon complement(67917..68729) FT /locus_tag="An14g03110" FT /number=1 FT mat_peptide complement(join(67920..68729,68779..68992,69038..69368, FT 69415..69556)) FT /locus_tag="An14g03110" FT intron complement(68730..68778) FT /locus_tag="An14g03110" FT /number=1 FT exon complement(68779..68992) FT /locus_tag="An14g03110" FT /number=2 FT intron complement(68993..69037) FT /locus_tag="An14g03110" FT /number=2 FT exon complement(69038..69368) FT /locus_tag="An14g03110" FT /number=3 FT intron complement(69369..69414) FT /locus_tag="An14g03110" FT /number=3 FT exon complement(69415..69622) FT /locus_tag="An14g03110" FT /number=4 FT sig_peptide complement(69557..69622) FT /locus_tag="An14g03110" FT /inference="protein motif:SignalP:2.0" FT CDS join(69984..70136,70189..70329,70378..70707,70759..70826, FT 70876..70955,71036..71364) FT /locus_tag="An14g03120" FT /note="Similarity: shows only similarity to the central FT part of pth11." FT /note="Title: weak similarity to integral membrane protein FT PTH11 from patent WO9913094-A2 - Magnaporthe grisea" FT /db_xref="UniProtKB/TrEMBL:A2R357" FT /protein_id="CAK46549.1" FT /translation="MSRTYATPAAIITISILFPVLGTLTVILRFYTRRKTKSVLWIDDW FT LTLPALGLEYVLAALLLWGTTTGSLGGLLPQPDDPRPDAYIFSNSDQQIRLLQIQYVAD FT IVTVWAFGFTKLSILYFYRSIFCSRRTIRTAFHSVTMCMTVLVSVWTVAFGVGTIFICG FT AHPVNAWGTIAVVTTECTVQVPIVEGYAISDFIMDVIIWLLPLPRIWLLNISVRQKMAL FT GLVFLVGLLAIAASATRMAIYIAHHINPFAQSDGEKCGLGVIVICLPSLRPMYKKRELN FT SLINSFKRYLYRIPTSTTSSALRNNSLNGLTNSNSSNVNLVRPWHPGPTTSPAVGHNAS FT MAQHPSNTEQRIQVTREIELIRLDSS" FT mRNA join(<69984..70136,70189..70329,70378..70707,70759..70826, FT 70876..70955,71036..>71364) FT /locus_tag="An14g03120" FT exon 69984..70136 FT /locus_tag="An14g03120" FT /number=1 FT intron 70137..70188 FT /locus_tag="An14g03120" FT /number=1 FT exon 70189..70329 FT /locus_tag="An14g03120" FT /number=2 FT intron 70330..70377 FT /locus_tag="An14g03120" FT /number=2 FT exon 70378..70707 FT /locus_tag="An14g03120" FT /number=3 FT intron 70708..70758 FT /locus_tag="An14g03120" FT /number=3 FT exon 70759..70826 FT /locus_tag="An14g03120" FT /number=4 FT intron 70827..70875 FT /locus_tag="An14g03120" FT /number=4 FT exon 70876..70955 FT /locus_tag="An14g03120" FT /number=5 FT intron 70956..71035 FT /locus_tag="An14g03120" FT /number=5 FT exon 71036..71364 FT /locus_tag="An14g03120" FT /number=6 FT CDS complement(join(72909..73063,73119..73182)) FT /locus_tag="An14g03130" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R358" FT /protein_id="CAK46550.1" FT /translation="MKISLIWAVSLLLNVHAAVIPRAAESATSIEAGVRAAEFGAGGIH FT ERAALSYGEGDSKVDNKEDNTVIGEGW" FT mRNA complement(join(<72909..73063,73119..>73182)) FT /locus_tag="An14g03130" FT exon complement(72909..73063) FT /locus_tag="An14g03130" FT /number=1 FT mat_peptide complement(join(72912..73063,73119..73131)) FT /locus_tag="An14g03130" FT /product="hypothetical protein" FT intron complement(73064..73118) FT /locus_tag="An14g03130" FT /number=1 FT exon complement(73119..73182) FT /locus_tag="An14g03130" FT /number=2 FT sig_peptide complement(73132..73182) FT /locus_tag="An14g03130" FT /inference="protein motif:SignalP:2.0" FT CDS complement(join(74646..74678,74742..75518,75572..76512, FT 76565..76885,76953..77136)) FT /locus_tag="An14g03140" FT /note="Function: sporulation and tetrad analysis revealed FT that deletion of YNL059c/ARP5 was lethal for vegetative FT growth in strain W303 and caused severe growth defects in FT strain FY1679." FT /note="Title: strong similarity to nuclear protein YNL059c FT - Saccharomyces cerevisiae" FT /note="nucleus" FT /db_xref="GOA:A2R359" FT /db_xref="InterPro:IPR004000" FT /db_xref="UniProtKB/TrEMBL:A2R359" FT /citation=[82] FT /inference="profile:COGS:COG5277" FT /inference="profile:PFAM:PF00022" FT /inference="similar to AA sequence:PIR:S58718" FT /protein_id="CAK46551.1" FT /translation="MAITSIQPVLPTRFTINSEKGATKPPPEPYNVQDHPFKGYHPPQP FT EGYEKSKSTSAIVIDNGSNLVKAGWSFDKSPRFVLPPVMSRYRDRKLNKACQFIGYDSY FT VDATTRGQLRYAFDPGTSVVGNWDVMEGVLDYLFIKLGVDGANGGVDRPIVMTEPIANL FT AYPRRMMNEILFECYSAPSVAYGIDSLFSYRYNRGKDGLIISSSHTSTHVIPVLNNKAL FT LSNCSRLNWGGLHASEYLLKLMRLKYPTFPARMTESQMEDIVHKHCYVSKDYDQELSHY FT LDWTGLEERDCIVQYPYTEHVVPEKTEEELARIAERKKESGRRLQEQAAKMRLEKLMKK FT EQELEYYKDLQHGLASETKKEARRILEAEDLKDEAHLDRLIRDLERSIKRSRNRDLGIE FT ETEEPQEEMSFPLLDVPDEELDEAGLKEKRHQRLMKSNVEARQRAKAEKEREKARREEE FT ERLDREKRENDFENWLAERRANRQNIMQKIKERDRMKADLGNRKSLASQMRMKTLANLA FT ADGPKKRRRGGDDDTFGANDEDWGVYRTVATGEQSDEEEEEDLGGMLDAVEKELLEYDP FT EFTENHTLAAQSDWTKSLVHVFLRGPWPFDPESQREAHQLHLNVERIRVPEVVFKPSIA FT GIDQAGLLEIAADIVNQRFPNPEEQSKLLRDVFLTGGNTMFQNFDERLRNDFRAYLPVD FT AQLNVRRANDPVLDAWKGAAQWASGSELAKSSITRQEYLEKGSEYLKEHDMGNATTW" FT mRNA complement(join(<74646..74678,74742..75518,75572..76512, FT 76565..76885,76953..>77136)) FT /locus_tag="An14g03140" FT exon complement(74646..74678) FT /locus_tag="An14g03140" FT /number=1 FT intron complement(74679..74741) FT /locus_tag="An14g03140" FT /number=1 FT exon complement(74742..75518) FT /locus_tag="An14g03140" FT /number=2 FT intron complement(75519..75571) FT /locus_tag="An14g03140" FT /number=2 FT exon complement(75572..76512) FT /locus_tag="An14g03140" FT /number=3 FT intron complement(76513..76564) FT /locus_tag="An14g03140" FT /number=3 FT exon complement(76565..76885) FT /locus_tag="An14g03140" FT /number=4 FT intron complement(76886..76952) FT /locus_tag="An14g03140" FT /number=4 FT exon complement(76953..77136) FT /locus_tag="An14g03140" FT /number=5 FT CDS complement(join(77600..77646,77694..77778,77833..77856)) FT /locus_tag="An14g03150" FT /product="hypothetical protein" FT /db_xref="InterPro:IPR013959" FT /db_xref="UniProtKB/TrEMBL:A2R360" FT /protein_id="CAK46552.1" FT /translation="MVMNRSLQEVNIQNMNVELVAQMFKNYQSNVLFHLEATENLKDPS FT SSSSSS" FT mRNA complement(join(<77600..77646,77694..77778,77833..>77856)) FT /locus_tag="An14g03150" FT exon complement(77600..77646) FT /locus_tag="An14g03150" FT /number=1 FT intron complement(77647..77693) FT /locus_tag="An14g03150" FT /number=1 FT exon complement(77694..77778) FT /locus_tag="An14g03150" FT /number=2 FT intron complement(77779..77832) FT /locus_tag="An14g03150" FT /number=2 FT exon complement(77833..77856) FT /locus_tag="An14g03150" FT /number=3 FT CDS join(78484..78970,79121..79161) FT /locus_tag="An14g03160" FT /note="Title: weak similarity to hypothetical protein FT CAE02259.1 - Oryza sativa" FT /db_xref="InterPro:IPR013272" FT /db_xref="UniProtKB/TrEMBL:A2R361" FT /inference="profile:COGS:COG5195" FT /protein_id="CAK46553.1" FT /translation="MAPLTPVEQENHQALLDRLDIAAVPRPFRNPNWKPSQRRNKNVKQ FT LISESSRKEASVMATQSNSGATTPLAATSASTDGSQTPADGTPRTNIAQAAQNLSTLVL FT EKNARAAFTSGPAVTYTNIESAPSLHPSQQTRYCDITGLPAPYTDPKTRLRYHDKEIFE FT IMHSDSNEGPAR" FT mRNA join(<78484..78970,79121..>79161) FT /locus_tag="An14g03160" FT exon 78484..78970 FT /locus_tag="An14g03160" FT /number=1 FT intron 78971..79120 FT /locus_tag="An14g03160" FT /number=1 FT exon 79121..79161 FT /locus_tag="An14g03160" FT /number=2 FT CDS join(80139..80274,80469..80581) FT /locus_tag="An14g03170" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R362" FT /protein_id="CAK46554.1" FT /translation="MPTMWLSDNQSKKRLLCTLRTKAFPGHWLTHVLSTTEIGVIFCSA FT AWRWEMYAILNYPTPMRYVETPTNPLHRRSSSSSASP" FT mRNA join(<80139..80274,80469..>80581) FT /locus_tag="An14g03170" FT exon 80139..80274 FT /locus_tag="An14g03170" FT /number=1 FT intron 80275..80468 FT /locus_tag="An14g03170" FT /number=1 FT exon 80469..80581 FT /locus_tag="An14g03170" FT /number=2 FT CDS complement(join(81666..81797,81871..82005,82104..82188, FT 82277..82292,82393..82420)) FT /locus_tag="An14g03180" FT /note="Function: Cdc3-profilin may play an essential role FT in cytokinesis by catalyzing the formation of the F-actin FT contractile ring." FT /note="Function: in S. pombe, cdc3-124 mutant is defective FT for cytokinesis, but not for DNA replication, mitosis, or FT septum synthesis." FT /note="Function: profilin is an actin-monomer-binding FT protein." FT /note="Title: strong similarity to profilin cdc3p FT -Schizosaccharomyces pombe" FT /note="cytoskeleton" FT /db_xref="GOA:A2R363" FT /db_xref="InterPro:IPR005455" FT /db_xref="UniProtKB/TrEMBL:A2R363" FT /inference="profile:PFAM:PF00235" FT /inference="similar to AA sequence:PIR:A53952" FT /protein_id="CAK46555.1" FT /translation="MGQHSAIWQGYVDSSLMGSGQFDKAGILSHDISGVEASSPGFTIS FT PQELQGLAAAFKDPNAAWGNGITVGGEKFVTIKADDRSLYGKKGKEGIVVVKAVSCVMV FT AHHAENVQTPNAATVVENLVDYINNPR" FT mRNA complement(join(<81666..81797,81871..82005,82104..82188, FT 82277..82292,82393..>82420)) FT /locus_tag="An14g03180" FT exon complement(81666..81797) FT /locus_tag="An14g03180" FT /number=1 FT intron complement(81798..81870) FT /locus_tag="An14g03180" FT /number=1 FT exon complement(81871..82005) FT /locus_tag="An14g03180" FT /number=2 FT intron complement(82006..82103) FT /locus_tag="An14g03180" FT /number=2 FT exon complement(82104..82188) FT /locus_tag="An14g03180" FT /number=3 FT intron complement(82189..82276) FT /locus_tag="An14g03180" FT /number=3 FT exon complement(82277..82292) FT /locus_tag="An14g03180" FT /number=4 FT intron complement(82293..82392) FT /locus_tag="An14g03180" FT /number=4 FT exon complement(82393..82420) FT /locus_tag="An14g03180" FT /number=5 FT CDS join(84711..85583,85644..86471) FT /locus_tag="An14g03190" FT /note="Remark: only repetitive elements are matching." FT /note="Title: weak similarity to hypothetical protein FT EG:56G7.1 - Drosophila melanogaster" FT /db_xref="UniProtKB/TrEMBL:A2R364" FT /protein_id="CAK46556.1" FT /translation="MARGTFLGRSRTIRQAEAGSSPTSKHPDMLPRKDQKCIEDGANKG FT RPAPHVNRSFHRPGVSEGHQQKKMQAMSPINTEAPPLLSSPVSSPVSTDNDMNGSLIGV FT ALGSPRMIDPQVPTSQMQETVPVKPAEPQTRPSLQRKPSKWKKIGGLFKAKAAMTTPPN FT QPFYQVRLENEWPMQGSTYSFDQQPKTQSSGHENPASPTSGTDAWPSLVPEIQTSTQEP FT QQSHADATSGSPPEKEQSLGSGPLLQVDIPDIQLERYSVMFGGVLKKNRLSAMSRRSKN FT LEDSNSPTEQDTHHSPTPTRSKSPSPSFSLFPATRTSKASKVLGSQNVPRGPSPIHKSQ FT TSLGESNQENLSEKNSVVLMVHSTQPSHKQQNSVSSFLSSTTIGSEDERLLLQKLGPVR FT SYFDAREPEWEIINKKPTAKEPVRESPPPLRIDTQMDSPRTASYASSTLSESSDTPVDA FT PRQRNEVPSPASRRTSPTSPRPKPSGVAQKDSNPSDPENPVPTVEISIARSVSVSKGRR FT QVLVPIRPRPDRLDPNERVGDKKGKAPQVMEADRSHLPGRSQEVLVDTI" FT mRNA join(<84711..85583,85644..>86471) FT /locus_tag="An14g03190" FT exon 84711..85583 FT /locus_tag="An14g03190" FT /number=1 FT intron 85584..85643 FT /locus_tag="An14g03190" FT /number=1 FT exon 85644..86471 FT /locus_tag="An14g03190" FT /number=2 FT exon complement(86934..92909) FT /locus_tag="An14g03200" FT /number=1 FT CDS complement(86934..92909) FT /locus_tag="An14g03200" FT /note="Remark: the ORF is transcribed in vegetative cells FT but it is not essential for viability as demonstrated by FT gene disruption." FT /note="Similarity: homologous to RNA-helicase SKI2 S. FT cerevisiae." FT /note="Title: strong similarity to hypothetical FT RNA-helicase G9365 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R365" FT /db_xref="InterPro:IPR014001" FT /db_xref="UniProtKB/TrEMBL:A2R365" FT /citation=[53] FT /inference="profile:COGS:COG1204" FT /inference="profile:PFAM:PF00270" FT /inference="profile:PFAM:PF02889" FT /inference="similar to AA sequence:UniProtKB:SC35242.1" FT /protein_id="CAK46557.1" FT /translation="MAVNGSVETQWLAQLAAMRQAIADLKLPQDPAKDTSYGSDLDLDF FT DEDYSSPGTADDDIWDIISSDEEASDDFDDYDELPSPPTSSAYDQLWLEQKCMSLAANK FT PGMDAGELAQQITAALATDSGDDELQMSLAEIVGFDDLDFVIDLIAHRADIVASSHTGP FT EAQTDGLMAGKLMTRAEREQALRQADYEHKHASLMPAQTRSEPHYPHVFKLHESRNVLA FT LGGKRYGLPMGSKQIDEKKYTEVEVPASKVGTLRPGHKLVEIASLDGLCQGTFKGYKTL FT NRMQSLLYEVAYKTNENMLICAPTGAGKTDAAMLTILNAIGKNTVPNPIEEPQATEFAV FT QVEDFKIIYVAPMKALAAEVTEKLGKRLAWLGIKVRELTGDMQLTKREIVETQIIVTTP FT EKWDVVTRKSTGDTELVQKVRLLIIDEVHMLHDERGAVIESLVARTQRQVESTQSLIRI FT VGLSATLPNYVDVADFLKVNKMAGLFFFDQSFRPVPLEQHFIGVKGKPGTKQSRENLDV FT VAFEKVRDMLERGHQVMVFVHSRKDTVMTARMLKQMASEDGCENLFSCQEHEGYSNGLG FT DVKRSRARELRELFASGLGTHHAGMSRSDRNLMERLFSEGLIKVLCCTATLAWGVNLPA FT AAVVIKGTQLYNPQEGKFVDLGILDVLQIFGRAGRPQFQDTGIGFICTTHDKLHHYISA FT VTSQQPIESRFSSRLVDNLNAEISLGTVTSVPEAVQWLGYSYLFVRMKREPRNYGIDFA FT ELRDDPMLVQRRRQLVIQAAIVLQKSQMIIYNEKTEELRAKDVGRIASQYYVLQTSVEI FT FNNLMRPRASEADVLRMISMSGEFDNIQARESESKELNRLRDEAIQTEVEGGNDSPHAK FT TNILLQSYISRARVEDFALVSDTGYVAQNAARICRSLFMIALNRRWGYQCQVLLSLCKA FT IEKQMWPFDHPFHQFDLPQPILRNLDDKLPTSSIESMRDMETAEIGQLVHNQKMGKTLA FT KLLDNFPTLGVEAEIAPLNRDVLRIRLSLYPEFIWNDRHHGASESYWIWVENSETSEIY FT HHEYFILSRKKLNDEHELNFTIPLSDPLPSQIYVRAISDRWLGAETVHPVSFQHLIRPD FT TESVYTDLLNLQPLPISALKNPILEELYGQRFQFFNPMQTQIFHMLYHTPANVLLGSPT FT GSGKTVAAELAMWWAFREKPGSKVVYIAPMKALVRERVQDWKKRLTAPMGLKLVELTGD FT NTPDTRTIRDADIIITTPEKWDGISRSWQTRDYVRKVSLVIIDEIHLLGGDRGPILEII FT VSRMNYIASQSKGSVRLMGMSTACANATDLANWLGVKEGLYNFRHSVRPVPLEIYIDGF FT PEQRGFCPLMQSMNRPTFLAIKNHSPEKPVIVFVASRRQTRLTAKDLINYCGMEDNPRR FT FVRMSEEDLQLNLARVKDEALREALSFGIGLHHAGLVESDRQLAEELFGNNKIQILVAT FT STLAWGVNLPAHLVVVKGTQFFDAKIEGYRDMDLTDVLQMLGRAGRPQFDTSGIARIFT FT QDAKKAFYKHFLHTGFPVESTLHKVLDNHLGAEVSAGTITTKQDALDYLTWTFFFRRLH FT KNPSYYGLEISAEEHNTMAAQAIAQDFMIELVDKSLGELAESSCVVLDSATGDVDPTPF FT GKIMSYYYLSHKTIRYLMSHAKPNPTFHDVLSWMCSATEFDELPVRHNEDLINAELARN FT LPLSVESMCDLPLWDPHVKAFLLLQAYMSRIDLPISDYVGDQTSVLDQGIRIIQASIDV FT MAELGYLHACHMFMSLLQCIKSARWPEDAPLSILPGIDPVEKKSALPTSLTALVSLPFK FT ATEALTKKLSLPAQFAKAASNLPNISLSIPTISPNGLTVTLTRKNAPRDRDYRIYAPRF FT PKPQTEGFFMLVYSGASSDGKNGELLALKRVSWPSSSNQRNGSGPSRKPNDNRNGPLVV FT RSSVKFPENVRGLSMRVTIKVISDSYPGMEWTLSDVEVDAGVPEKQTLPESSTFPEKS" FT mRNA complement(<86934..>92909) FT /locus_tag="An14g03200" FT exon complement(94149..95153) FT /locus_tag="An14g03210" FT /number=1 FT CDS complement(94149..95153) FT /locus_tag="An14g03210" FT /note="Remark: strong similarity to human transcriptional FT regulator protein #28 patent WO200078954-A2." FT /note="Title: strong similarity to transcriptional FT regulator protein #28 TXREG from patent WO200078954-A2 FT -Homo sapiens" FT /db_xref="InterPro:IPR000253" FT /db_xref="UniProtKB/TrEMBL:A2R366" FT /inference="profile:COGS:COG0744" FT /inference="profile:COGS:COG1716" FT /inference="profile:PFAM:PF00498" FT /protein_id="CAK46558.1" FT /translation="MPDSRDDYSRRRHRSPSGSPAPDRDQRQRRRDEDRGSDSGHRESH FT QSSRRDSSRRRSSRSPADRRSHRRDYDSRRSERRDKEDVSEDDRRRRRHTSDRESSYRR FT HRDRDSYDRKEKSSRRRRDYSRSRSPTRRSPGPDSRAPVRSKAPLPPQQDAYTSSEVAR FT TGESEGPPPEKEKPNFAQTGRLAAESKTVNVNGSSVVLKYHEPPEARKPPAKEPWRFYV FT FKGQDLLEMVELGIRSCWLIGKEQLVVDFPLEHPSCSKQHAALQFRFVEKRNEFGDRIG FT RVKPYLIDLESANGTTVNGDAIPAGRYVELRDKDVVQFGLSSREYVLMLPPPE" FT mRNA complement(<94149..>95153) FT /locus_tag="An14g03210" FT exon 95399..96325 FT /locus_tag="An14g03220" FT /number=1 FT CDS 95399..96325 FT /locus_tag="An14g03220" FT /note="Similarity: the ORF shows similarity to some FT putative DNA-J-like chaperones/heat shock proteins." FT /note="Title: similarity to hypothetical DNA-J-like protein FT SPAC4G9.19 - Schizosaccharomyces pombe" FT /db_xref="GOA:A2R367" FT /db_xref="InterPro:IPR001623" FT /db_xref="UniProtKB/TrEMBL:A2R367" FT /inference="profile:COGS:COG0484" FT /inference="profile:COGS:COG2214" FT /inference="profile:PFAM:PF00226" FT /inference="similar to AA sequence:PIR:T38878" FT /protein_id="CAK46559.1" FT /translation="MFKKPNILCCGGGLQLLNSPCLSSPPRYRSFPSQSRYSARRYATA FT SHNPETDLSWPSSPTFTPYELFKQDRTAPYSKARYYEMVKIYHPDRPCSGHPLCRDLTP FT EVRLQRYHILVAAHEILSDPSRRAAYDFSGAGWNLHPYETPIPSWARTGSSNYGPIYAN FT ATWEDWERWNNRHQGKQQTLVDHRTFATFVILLTLMGGALQASWISKLSSGYEDRLWEL FT NEESSRLLKGRRENTQHQMQSVDARVQHFLIRRDPSGCGLKEEEQPVYKQVLHSQKSSN FT DPPAEILGSERQDGRVSGDSVQTGTSS" FT mRNA <95399..>96325 FT /locus_tag="An14g03220" FT sig_peptide 95399..95467 FT /locus_tag="An14g03220" FT /inference="protein motif:SignalP:2.0" FT mat_peptide 95468..96322 FT /locus_tag="An14g03220" FT CDS join(96881..97450,97599..97652,97687..97994,98061..99035, FT 99074..99185,99239..99307,99341..99442) FT /locus_tag="An14g03230" FT /note="Title: weak similarity to hypothetical protein FT encoded by An13g03440 - Aspergillus niger" FT /db_xref="UniProtKB/TrEMBL:A2R368" FT /protein_id="CAK46560.1" FT /translation="MRGPMVMLFPLVRHQWYETGNWKSGAHDFFRLSKCDIRQRPGSNP FT GELIGHGHINSGSVLISRPVLVSSGHQRQWKELNNALVSAITDIVERWWTNSVSRFPER FT MPLKPAEEDLLRVCYVPPPTVHPAAGSGTFSQQHDISDPIEEFPRHRDCSYEEAPPRYF FT ALQVLREDRCRGGVLSGMDVGKLSSPAILQSIWWTNVQRPIDKLLDVGSEHAEHFPILT FT QDLEITSSSPINTNCLIDARAIDVTMSAEELLANVEGGVVPVTCHEDVLRIAFIYLDEG FT LWTGNGVFDVVDKLHSHGLSFGEGVLRFNRSLDIFYLAQLAAAIYRYISQLKDDFPSFS FT DFPAFYIAYHAFLHSSAWRSYYSYPFLTQRTTACFYRLPNLQDLPDSSSPLCQPRHSPA FT SLHILKIPRWAYTVGCTRRRQPFLPSETLTALALSTLEATMTRLHTAYPSAPPYSEAHP FT RFWLDYFTPDPSPSRVAEVTPWQAWRPHSFGILVAQGKYDIHRLEAEYLTRIAGGEIIE FT GDSQPEQVIWYGWPDGGIEGQAWWRGWEEEVGSEEEVDFLAAVAVEETVGLGLQGIDMD FT ELDLSIRSHILLAVMQAAVKDKQEKERFLDEMKRRMVQKGRIVNERAGKWTREALETME FT PGEREDAAADSGGKCAALCTLEVVAYFEAVHFRAEAEGYPNQLKKIRIPASQRNATPYL FT NLCMQEALGSTCLPILSFKGNQAELRKSLDAKRHY" FT mRNA join(<96881..97450,97599..97652,97687..97994,98061..99035, FT 99074..99185,99239..99307,99341..>99442) FT /locus_tag="An14g03230" FT exon 96881..97450 FT /locus_tag="An14g03230" FT /number=1 FT intron 97451..97598 FT /locus_tag="An14g03230" FT /number=1 FT exon 97599..97652 FT /locus_tag="An14g03230" FT /number=2 FT intron 97653..97686 FT /locus_tag="An14g03230" FT /number=2 FT exon 97687..97994 FT /locus_tag="An14g03230" FT /number=3 FT intron 97995..98060 FT /locus_tag="An14g03230" FT /number=3 FT exon 98061..99035 FT /locus_tag="An14g03230" FT /number=4 FT intron 99036..99073 FT /locus_tag="An14g03230" FT /number=4 FT exon 99074..99185 FT /locus_tag="An14g03230" FT /number=5 FT intron 99186..99238 FT /locus_tag="An14g03230" FT /number=5 FT exon 99239..99307 FT /locus_tag="An14g03230" FT /number=6 FT intron 99308..99340 FT /locus_tag="An14g03230" FT /number=6 FT exon 99341..99442 FT /locus_tag="An14g03230" FT /number=7 FT CDS complement(join(100433..101448,101511..101832)) FT /locus_tag="An14g03240" FT /EC_number="1.3.1.8" FT /note="Catalytic activity: acyl-CoA + NADP+ = FT 2,3-dehydroacyl-CoA + NADPH." FT /note="Remark: is a medium chain acyl-CoA dehydrogenase FT (MCADH). the active site glutamic acid of the protein does FT not lie in the same position as other well characterized FT MCADH, but in a position present in long chain and FT isovaleryl acyl-CoA dehydrogenases (LCADH and IVDH)." FT /note="Similarity: belongs to the acyl-CoA dehydrogenase FT family." FT /note="Title: strong similarity to acyl-CoA dehydrogenase FT (NADP+) ACDH - Mycobacterium tuberculosis" FT /db_xref="GOA:A2R369" FT /db_xref="InterPro:IPR006092" FT /db_xref="UniProtKB/TrEMBL:A2R369" FT /citation=[63] FT /inference="profile:COGS:COG1960" FT /inference="profile:PFAM:PF00441" FT /protein_id="CAK46561.1" FT /translation="MSRIYQLSRAFQRSQVGALRPRSLLPARSSRCGFSTSATRPLMEL FT TGFTEEQLTVRDAVSAICAKFPNTYWQDCDQNERDPNEFHAALARDGWLGIALPEELGG FT AGLGISEATMMMQTITQSGAGMAGAQAIHANVYATQPLARFGTREQLEETIPKIINGTW FT RTCFGVTEPNTGLETLKLKTLATKKSRGDSDIYSISGQKIWITCAQVASKMILLARTTP FT LEEVTKSTQGLSMFCIDLDRTQPGLDMRKIKKMGGRAVDANEVFFDGYEVPANTLIGQE FT NEGFRIILHGMNAERCLLAGEALGLGYAALERAADYAKERVVFGRPIGQNQGIAHPLAD FT AYMRLEAAKLATYHAARLYDASKKDEGIPLHSVGVACNSAKYLAAEAAFTACERAVLSH FT GGMGYAMEYDVERYLRECLVPRIAPVSREMILNYVSEKVLQLPRSY" FT mRNA complement(join(<100433..101448,101511..>101832)) FT /locus_tag="An14g03240" FT exon complement(100433..101448) FT /locus_tag="An14g03240" FT /number=1 FT intron complement(101449..101510) FT /locus_tag="An14g03240" FT /number=1 FT exon complement(101511..101832) FT /locus_tag="An14g03240" FT /number=2 FT exon complement(102131..102970) FT /locus_tag="An14g03250" FT /number=1 FT CDS complement(102131..102970) FT /locus_tag="An14g03250" FT /EC_number="3.4.23.19" FT /note="Catalytic activity: preverential cleavage in B chain FT of insulin: Asn3-|-Gln,Gly13-|-Ala, Tyr26-|-Thr." FT /note="Remark: alternate name is proteinase A." FT /note="Remark: proteinase A obtained from the culture FT medium of Aspergillus niger var. macrosporus is a unique FT acid endopeptidase that is insensitive (or less sensitive) FT to specific inhibitors of ordinary acid or aspartic FT proteinases, such as pepstatin, diazoacetyl-DL-norleucine FT methyl ester, and 1,2-epoxy-3-(p-nitrophenoxy)-propane." FT /note="Similarity: belongs to peptidase family a4." FT /note="Title: strong similarity to aspergillopepsin II FT -Aspergillus niger" FT /note="extracellular/secretion proteins" FT /db_xref="GOA:A2R370" FT /db_xref="InterPro:IPR000250" FT /db_xref="UniProtKB/TrEMBL:A2R370" FT /citation=[8] FT /citation=[9] FT /inference="profile:PFAM:PF01828" FT /inference="similar to AA sequence:PIR:A41025" FT /protein_id="CAK46562.1" FT /translation="MKFTNYLLTTATLASSVLAAPAPRTGLEDRLRARSLQRQSHPLAP FT IPLDTSTKENSRLLEADENTTHVTYSSNWAGAVREQPPPQGTYSAVSATFRVPEPTAQG FT GSGTQAGSAWVGIDGDTYSNAILQTGVDFYVENGQTYNDAWYEWYPDYAYDFDLDVSTG FT DTIVAKVEAISPSQGVATIENISTGKKATQTIRAPAATATLAGQNADWIVEDFQSGDSM FT VDLAGFGEISFWGVQAQGGGSTWGVDDATIVELKQGNEVLTDVEVQSDSAFTVKYTS" FT mRNA complement(<102131..>102970) FT /locus_tag="An14g03250" FT mat_peptide complement(102134..102913) FT /locus_tag="An14g03250" FT sig_peptide complement(102914..102970) FT /locus_tag="An14g03250" FT /inference="protein motif:SignalP:2.0" FT CDS complement(join(103370..103566,103674..103911)) FT /locus_tag="An14g03260" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R371" FT /protein_id="CAK46563.1" FT /translation="MSRNRRLKLPCFRPRDIWPYPGTQDKQGSNKLRADVFSDHADMPQ FT NRKGSCVDWYVRFLIPALVTLPFATRPQTATAEPSPLWQVIRSAEVPSLAQTPASASAV FT VDPALFRRSFALPIASEGPVGVLHLSGKTCALHPLVPAGV" FT mRNA complement(join(<103370..103566,103674..>103911)) FT /locus_tag="An14g03260" FT exon complement(103370..103566) FT /locus_tag="An14g03260" FT /number=1 FT intron complement(103567..103673) FT /locus_tag="An14g03260" FT /number=1 FT exon complement(103674..103911) FT /locus_tag="An14g03260" FT /number=2 FT CDS complement(join(104666..104862,104932..105799)) FT /locus_tag="An14g03270" FT /note="Title: strong similarity to hypothetical FT SAM-dependent methyltransferase YOR240w - Saccharomyces FT cerevisiae" FT /db_xref="GOA:A2R372" FT /db_xref="InterPro:IPR017280" FT /db_xref="UniProtKB/TrEMBL:A2R372" FT /inference="profile:COGS:COG0500" FT /inference="profile:COGS:COG2230" FT /inference="similar to AA sequence:PIR:S67133" FT /protein_id="CAK46564.1" FT /translation="MAPAPIASSSDDIATVLQLVTPPQIAPHRSHDPSNNQKRSDPFQF FT GSRYLEEGDDVFEFNAWDHVEPDDEFKAFAEVQYSKQRETPVSDFDRNRFNADPAKWWN FT LFYKNNTSNFFKNRKWLRQEFPVLADVTQPTAGKKVVLEVGAGAGNTAFPLLENNENEE FT LMVHACDFSKTAVKVMRESPHYNPKHITADVWDVTAEPDENSNGLPPGLTEESVDVVVL FT IFIFSALAPEQWNQALRNVYRVLKPGGHVLFRDYGRGDLAQVRFKKNRYMGENFYVRGD FT GTRVYFFDREETEVEEEQNPTDTKGVFDIEKLGVDYRLIVNRQRKLKMYRCWIQGHFLK FT RDTTAAVDISKIES" FT mRNA complement(join(<104666..104862,104932..>105799)) FT /locus_tag="An14g03270" FT exon complement(104666..104862) FT /locus_tag="An14g03270" FT /number=1 FT intron complement(104863..104931) FT /locus_tag="An14g03270" FT /number=1 FT exon complement(104932..105799) FT /locus_tag="An14g03270" FT /number=2 FT CDS complement(join(106306..106354,106447..106765, FT 106842..108247,108329..108402)) FT /locus_tag="An14g03280" FT /note="Catalytic activity: 2,3-dihydroxy-3-methylbutanoate FT = 3-methyl-2-oxobutanoate + H2O." FT /note="Pathway: fourth step in valine and isoleucine FT biosynthesis. valine, leucine and isoleucine biosynthesis; FT pantothenate and CoA biosynthesis." FT /note="Remark: the biosynthesis of branched-chain amino FT acids (aa) involves three shared pathways through which FT pyruvate or alpha-ketobutyrate are converted into FT alpha-keto acids, precursors of valine, leucine or FT isoleucine." FT /note="Similarity: belongs to the dihydroxyacid FT dehydratase/phosphogluconate dehydratases." FT /note="Title: strong similarity to dihydroxy-acid FT dehydratase Ilv3 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R373" FT /db_xref="InterPro:IPR000581" FT /db_xref="UniProtKB/TrEMBL:A2R373" FT /citation=[36] FT /inference="profile:COGS:COG0129" FT /inference="profile:PFAM:PF00920" FT /inference="similar to AA sequence:PIR:S55205" FT /protein_id="CAK46565.1" FT /translation="MLLSQTRGRMPSALRSIAKRSLLNSRPLSTTLPKQQNGNDDEYTG FT LNKVSRHITQPISQGASQAMLYAAGLTEADMNKAQVGISSVWYNGNPCNMHLLDLNNRV FT REGVQKAGLVGFQFNTVGVSDAISMGTKGMRFSLQSRDLIADSIETVMGGQWYDANISI FT PGCDKNMPGVLMAMGRVNRPSLMVYGGTIKPGCASMQGNADIDIVSAFQAYGQFISKEI FT TEPQRFDIIRNACPGGGACGGMYTANTMATAIEVMGMTLPGSSSNPAESDAKYLECLAA FT GEAIKTLLKEDIRPSDILTRQAFENAMVLVNITGGSTNAVLHLIAIADSVGIKLDIEDF FT QSVSDRIPFLADLKPSGKYVMADLHKIGGTPSLLKFLLKEGLIDGSGMTVTGQTLAKNL FT ENVPDFPEDQKIIRPLSNPIKETGHIQILRGSLAPGGSVGKITGKEGTVFTGKARVFDD FT EDDFIAALERNEIKKEEKTVVVIRYTGPKGGPGMPEMLKPSSALMGAGLGQSCALITDG FT RFSGGSHGFLIGHIVPEAAVGGPIGLVKDGDVITIDAEKRVLDLDVEETELAQRRKQWE FT ADRAAGKLPPTGLTLRGTLGKYARTVKDASHGCITDSLE" FT mRNA complement(join(<106306..106354,106447..106765, FT 106842..108247,108329..>108402)) FT /locus_tag="An14g03280" FT exon complement(106306..106354) FT /locus_tag="An14g03280" FT /number=1 FT intron complement(106355..106446) FT /locus_tag="An14g03280" FT /number=1 FT exon complement(106447..106765) FT /locus_tag="An14g03280" FT /number=2 FT intron complement(106766..106841) FT /locus_tag="An14g03280" FT /number=2 FT exon complement(106842..108247) FT /locus_tag="An14g03280" FT /number=3 FT intron complement(108248..108328) FT /locus_tag="An14g03280" FT /number=3 FT exon complement(108329..108402) FT /locus_tag="An14g03280" FT /number=4 FT CDS join(109464..109799,109860..112373,112422..114248) FT /locus_tag="An14g03290" FT /note="Remark: ATP-dependent bile acid transport was FT abolished when the BAT1 coding region was deleted from the FT genome and restored upon reintroduction of the gene." FT /note="Remark: ATP-dependent transport of bile acids is a FT key determinant of bile flow in mammalian liver and is FT associated with cholesterol excretion, gallstone FT formation,and numerous inherited and acquired hepatobiliary FT diseases. Secretory vesicles and a vacuole enriched FT fraction purified from S. cerevisiae also exhibit FT ATP-dependent bile acid transport." FT /note="Remark: alternative names are YLL048c, BAT1." FT /note="Similarity: to ABC-type multidrug/protein/lipid FT transport system, ATPase component." FT /note="Title: strong similarity to bile acid transporter FT Ybt1 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R374" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A2R374" FT /citation=[47] FT /citation=[56] FT /inference="profile:COGS:COG1132" FT /inference="profile:PFAM:PF00005" FT /inference="profile:PFAM:PF00664" FT /inference="similar to AA sequence:PIR:S64800" FT /protein_id="CAK46566.1" FT /translation="MASIATGALGILLISGCTVPALLGIIRRFLHVKETPPIHLPGAHA FT FDRPGYEDKDGEASDEALKGFSDLWQRLGIIILSITGLGISLTQVVISITKGQHLMIVP FT FGLQMGSWGILCVQATGFFIEPAPTKRYMLGVYGFGASLLAAIIPCLEIGLVWNTGYRL FT DTVSVGLTISQFGISCFRATLCLLLPRRPDVYHDGQIVDRERTVSAMERFTFSWVDNLL FT NHAVANEGLEIDDLPKMPFNTRSETLHTHLDRMRGSRALWRSLVVAHQNSLILQSSLSM FT IICVLSFGPQAAMYGILTSLENRYSNPDLNPKDANEAWAWVFGLGTVLILSSSIESWLW FT WIIYAKLWIPIYEGLSALVFAKSMRCKDIKQLVSLEEKEGDDHDADKMQQDVVSQSPIN FT LASVDSKRIADFVMFSYLIPSSVIRLLIGGVFLVHLIGWPSLLAGVATALLVAPMNAYL FT TKNYSTAQEEYMKASDKRMGAVGEVLHGIRQIKFAALEQQWQDRIKEKRRAELGLLWQT FT SLYTIGMVSVWIMGPLMLSAVSLTVYTLTRGELSASVAFTTLSIFGSLESAMASLPDLL FT SKGMEAKISADRIERYLDSSEKSLHTSAVDKISFHNATIAWPGEEGVEFDQRFLLRDLT FT LQFPPKGLSVISGKTGSGKSLLLASILGECDVLSGTVAVPHAPSINKTYDQRATRHNWI FT IDSAIAYVAQNPWLENATIKDNILFGLPYDRYRYRKVIYAAGLKKDIAMFPDSDRTDIG FT ANGINLSGGQRWRISFARALYSRAGILVMDDIFSALDAETGRHVYEHALIGKLGQGRTR FT ILVTHHLGLCLSRTDYCVILSDGLTIHAGTVDELAATQNLIDLLGESAKSSNGRKFDVV FT DEEPVSPMTPMKRVSTESGFSVATSVAEPPRKFTEDEKREKGAVSMQVYTTYITKGKCL FT RWWMMTFLAYVAFMVLLVGRSWWISVWTDSSTSSSQPTHSYDASQSRTIVAKRHYVDKD FT SMFYLSIYVCFSVAACIIGTLRTLALALASLESSQRLFDDLLAAVLRSPLRWLDTVPLG FT RILNRFTSDMYILDWRLGYDIGHFVFKALELTSILAAGVLVSPILLVLACILLVLCFRL FT SKIYLTGMREIKRLESTAKSPVLERFGSSLSGLTTIRAFNKAEIYMKDMYDRIDRHAQA FT AWYLWLLDRWLSFRMSIAGAVLAGMTAALVVYVPSISPALAGFAMTFALQYNYAVSMGL FT RFYANVETDMNATERVLEYCNIELEEQGGHNPPAAWPTRGKVEVEDLAVGYAPDLPPVI FT DGLSFTMENNQRVGVVGRTGAGKSSLTLALFRFLEARQGRVLIDGLDISQIKLEALRSR FT LAIIPQDPVLFSGTLRSNLDPFNEYSDLELYNALERVHLVSFEDTLTLASHSSSEPLSD FT SGTLPSSANSSTEPVKTSNFFASLSSVVSQGGLNLSQGQRQLLCLARAIVSQPKIMILD FT EATSAVDMETEALIQRSIREEFGRNATSLLVIAHRLSTVADFDRILVMDAGKAVEFGTP FT QELLEIEGGVFRNLVENSGERAHLERVIRGEETGSRSS" FT mRNA join(<109464..109799,109860..112373,112422..>114248) FT /locus_tag="An14g03290" FT exon 109464..109799 FT /locus_tag="An14g03290" FT /number=1 FT sig_peptide 109464..109535 FT /locus_tag="An14g03290" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(109536..109799,109860..112373,112422..114245) FT /locus_tag="An14g03290" FT intron 109800..109859 FT /locus_tag="An14g03290" FT /number=1 FT exon 109860..112373 FT /locus_tag="An14g03290" FT /number=2 FT intron 112374..112421 FT /locus_tag="An14g03290" FT /number=2 FT exon 112422..114248 FT /locus_tag="An14g03290" FT /number=3 FT CDS join(114395..114504,114557..114927,114991..115775) FT /locus_tag="An14g03300" FT /note="Title: weak similarity to hypothetical protein FT BAB32722.1 - Oryza sativa" FT /db_xref="UniProtKB/TrEMBL:A2R375" FT /protein_id="CAK46567.1" FT /translation="MYYFCELIGEDFQECIVFRVFTKPYPTYDEQPLLPFRSGGPALLT FT GFRLAFSYSVIAAFPLRPSLPVVTIIISCFSIQESIQFRHTHMGSDLLRSPTNQDISTE FT KATRSSSPPPLPVVTPAVTAAAAASTAQVDPEDDWAGLCDRQERRRRQNRLNQRAYRKR FT KQAERSGNNALAIRSSSSHPPPPSLGTNIKIEQGSSSSPPSSSSSPSSDSNPSQTLTRR FT TLTREASKPENIRRIFEHFARVAYESYFRGSPSADHLLTLSKLNVFRAFMTNMTVLGFG FT NQTTWCDDDDALSLFNTLPPEAIEEKKLPVSLRPTKIQMQVPHHPWLDFFPLPRLRDNL FT CLMIDRFDDDELCHDVMGFWDNASDTCSLLVWGEPSDPANWEVTEQFLRKWPWVLRGCP FT ELLKSTNRWRQKRGEKMIIRYL" FT mRNA join(<114395..114504,114557..114927,114991..>115775) FT /locus_tag="An14g03300" FT exon 114395..114504 FT /locus_tag="An14g03300" FT /number=1 FT intron 114505..114556 FT /locus_tag="An14g03300" FT /number=1 FT exon 114557..114927 FT /locus_tag="An14g03300" FT /number=2 FT intron 114928..114990 FT /locus_tag="An14g03300" FT /number=2 FT exon 114991..115775 FT /locus_tag="An14g03300" FT /number=3 FT CDS complement(join(116581..116863,116936..117333, FT 117392..117775)) FT /locus_tag="An14g03310" FT /EC_number="1.4.3.3" FT /note="Catalytic activity: D-amino acid + H2O + O2 = 2-oxo FT acid + NH3 + H2O2." FT /note="Pathway: glycine, serine and threonine metabolism; FT arginine and proline metabolism; D-arginine and D-ornithine FT metabolism." FT /note="Remark: strong similarity to D-amino acid oxidase FT DAO1 patent EP0969088-A/2 from Trigonopsis variabilis." FT /note="Remark: the patent is the dao gene with an addition FT in 5 of a nucleotide coding for a polyhistidine of 6 FT (hisDAO" FT /note="Remark: the three C-terminal amino acids of the DAO1 FT gene of Trigonopsis variabilis encoding a D-amino acid FT oxidase suggest that the enzyme may be located in FT peroxisomes." FT /note="Similarity: belongs to the DAMOX/DASOX family." FT /note="Title: strong similarity to D-amino acid oxidase FT DAO1 from patent EP0969088-A - Trigonopsis variabilis" FT /db_xref="GOA:A2R376" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2R376" FT /citation=[57] FT /inference="profile:COGS:COG0665" FT /inference="profile:PFAM:PF01266" FT /protein_id="CAK46568.1" FT /translation="MGELQHYPADTPNVPFAQRPIIILGAGIIGCAAARQLLQNGFPVI FT LVAEYLPGDQDFRYASAWAGAAWHPAGGISPEWRYLQAISHRQLLKMAQEEPESGVSIV FT DALEYVERPPAENSSAWGRTLAAKWRDLQPGEYPSEFSCGWSYETLVTDPTLHMPYLAK FT KITALGGQFIRKRVESLEDLYGMFPESSIFINASGIGSQTLKDVQDDLCFPERGQNVFY FT KTENCRTMYFRNGQEYTYVIPRPMSHGVILGGVKQADNLSSEPDMEIARDEIARAHRLA FT PEIVPEHPPEDTLSYIVGIRPSRKGGFRLDSEQQGSRYILSAYGFGGGGYAFSYGVADA FT LCKMVEKAERENVI" FT mRNA complement(join(<116581..116863,116936..117333, FT 117392..>117775)) FT /locus_tag="An14g03310" FT exon complement(116581..116863) FT /locus_tag="An14g03310" FT /number=1 FT intron complement(116864..116935) FT /locus_tag="An14g03310" FT /number=1 FT exon complement(116936..117333) FT /locus_tag="An14g03310" FT /number=2 FT intron complement(117334..117391) FT /locus_tag="An14g03310" FT /number=2 FT exon complement(117392..117775) FT /locus_tag="An14g03310" FT /number=3 FT CDS join(117861..117940,118052..118165,118260..118452, FT 118503..118583,118716..118931,119021..119178, FT 119238..119465,119705..119747) FT /locus_tag="An14g03320" FT /note="Title: weak similarity to hypothetical protein FT 68B2.60 - Neurospora crassa" FT /db_xref="UniProtKB/TrEMBL:A2R377" FT /protein_id="CAK46569.1" FT /translation="MVQEGKKDGTVVWEANDARAHRERDDNHESDHEPLARKKCSGMGE FT LFGSKRPEARSARRLEPTSGEVNPSRTRQLPVSPAALIGPGWMAPCPTRLDGAALSDRQ FT ILLYSQTDPRKSIWCFMSTCHVIESDDNVRKPSSSQMKSRKKSAYRLPRPIMSGTSAGH FT SNPVCSAIAFVLPSRMLRGLDSHRNNESSLVNEVDLSGDAAYTRPLNSQPPHPCRSPAG FT VCRVFEDNCVQGTSSGECCKRSSLSMTTVSGRPELTGIVSGALSQENRCVSEPPGLPDW FT VSHYMVQLGTERSDACLPACLHFSKKIRFKEDLRFSGHDKARCRFRELALVTLRDILAT FT SALMPDIIDVVSRCRKRQQKNKQLAIPELL" FT mRNA join(<117861..117940,118052..118165,118260..118452, FT 118503..118583,118716..118931,119021..119178, FT 119238..119465,119705..>119747) FT /locus_tag="An14g03320" FT exon 117861..117940 FT /locus_tag="An14g03320" FT /number=1 FT intron 117941..118051 FT /locus_tag="An14g03320" FT /number=1 FT exon 118052..118165 FT /locus_tag="An14g03320" FT /number=2 FT intron 118166..118259 FT /locus_tag="An14g03320" FT /number=2 FT exon 118260..118452 FT /locus_tag="An14g03320" FT /number=3 FT intron 118453..118502 FT /locus_tag="An14g03320" FT /number=3 FT exon 118503..118583 FT /locus_tag="An14g03320" FT /number=4 FT intron 118584..118715 FT /locus_tag="An14g03320" FT /number=4 FT exon 118716..118931 FT /locus_tag="An14g03320" FT /number=5 FT intron 118932..119020 FT /locus_tag="An14g03320" FT /number=5 FT exon 119021..119178 FT /locus_tag="An14g03320" FT /number=6 FT intron 119179..119237 FT /locus_tag="An14g03320" FT /number=6 FT exon 119238..119465 FT /locus_tag="An14g03320" FT /number=7 FT intron 119466..119704 FT /locus_tag="An14g03320" FT /number=7 FT exon 119705..119747 FT /locus_tag="An14g03320" FT /number=8 FT CDS complement(join(120552..121642,121715..121931)) FT /locus_tag="An14g03330" FT /note="Title: similarity to hypothetical protein SCF12.05 FT -Streptomyces coelicolor" FT /db_xref="UniProtKB/TrEMBL:A2R378" FT /inference="similar to AA sequence:UniProtKB:SCO939105.22" FT /protein_id="CAK46570.1" FT /translation="MSHSAAELQKPTGEYRQYLPDLSLKRFQVMRNQDAHEYAHDFKTL FT KNPPWLHALYMHWVDLLQEPFKGVTTDGNVRPGLFTLQDEGVPVGDIVDSVQNVLSLAD FT DKQRQALSYHIDSPEWRTWSNPEFLLAHKGLRLDEIDNKLRDAIMNVLKTSLSPEGYDK FT AVKAMRINHFLGELVESPKVMNEFSYNFVLFGRPSTTRPWGWSFYGHHLCLNIFLYKNQ FT IVASPWFTGAEPNEIDDGPYSGTRIMQVEEELGLRLMQSLTPDLQQKARVFAEMHDPAM FT PPGRWNRDDQRHLCGAYRDNRVVPNEGITVDGFTEEQKKYMYGIFEQYLLYLPARARQM FT KLDQIRQYESETYFCWIGGYGDSDPFYYRLQSPVVLIEFDHHSGVFLNNEEPKKFHIHT FT LLRTPNAGDYGQALRAQIPAVEGLNGKEIVWEKSAL" FT mRNA complement(join(<120552..121642,121715..>121931)) FT /locus_tag="An14g03330" FT exon complement(120552..121642) FT /locus_tag="An14g03330" FT /number=1 FT intron complement(121643..121714) FT /locus_tag="An14g03330" FT /number=1 FT exon complement(121715..121931) FT /locus_tag="An14g03330" FT /number=2 FT CDS complement(join(122449..123337,123394..123551, FT 123634..123788,123840..123984,124041..124151, FT 124209..124450,124542..124650)) FT /locus_tag="An14g03340" FT /note="Remark: expression analysis of tfdB FT (1,2-dichlorophenol hydroxylase (DCPH))and tfdC in FT Escherichia coli suggested that these genes form one FT operon, tfdCB." FT /note="Title: strong similarity to 1,2-dichlorophenol FT hydroxylase tfdB - Pseudomonas putida" FT /db_xref="GOA:A2R379" FT /db_xref="InterPro:IPR003042" FT /db_xref="UniProtKB/TrEMBL:A2R379" FT /citation=[43] FT /inference="profile:COGS:COG0654" FT /inference="profile:PFAM:PF01360" FT /inference="profile:PFAM:PF01494" FT /inference="similar to AA sequence:PIR:JC5013" FT /protein_id="CAK46571.1" FT /translation="MSPTKDEIPFDDDVPILIVGAGPCGLLLAYLLAQLGVRSLLCERY FT PTRLQAPKAHALSPRTLELCRQYGLDVNEIRSIGTKRGEAFWVNFITSLSGRHVGRLPY FT ERMDPAVLESTPTMIHNIPQPEFEELVAKRLSKNNLVEIRKNHSFVRLVDRGDHVLATI FT EDRATKQEYTVKCCHLVACDGAKSAVRRCLGIESEGEDSYETMMTIHINANLHPVVKER FT VGMLHWVMDPEVSGFIIGYDLGGNQVLICNFDAEKHPVETWDEALCRKVVDAAIGTKIP FT YDVLSYRPWILSRKVALSYRANRVLLAGDAAHSFPPTGGLGLNSGLGDVHNLAYKLAAV FT HHGWGGDRLLDSYEADRRPVACDNAEQSVKNGKQIFGLLKALGTTDPDVRVARQNLYRN FT IEDSHMMKEINKGIEGQREHFDNLGLHVGYVYGNHRRPDCASTYEPVCTPGARLPHAWI FT NLLTPEQIRLPPIDCSYVSEFLPEELKLKQFSTLDLCAFDAFTLIVDIRSADHWGKILE FT EVKRQLSGKCDGLKIEMMTRGANFDLQPGGGDKWMALTRVAEGQAILVRPDQHVLARFE FT YPGESSGVLGELRAHLAWDEGAGGSG" FT mRNA complement(join(<122449..123337,123394..123551, FT 123634..123788,123840..123984,124041..124151, FT 124209..124450,124542..>124650)) FT /locus_tag="An14g03340" FT exon complement(122449..123337) FT /locus_tag="An14g03340" FT /number=1 FT intron complement(123338..123393) FT /locus_tag="An14g03340" FT /number=1 FT exon complement(123394..123551) FT /locus_tag="An14g03340" FT /number=2 FT intron complement(123552..123633) FT /locus_tag="An14g03340" FT /number=2 FT exon complement(123634..123788) FT /locus_tag="An14g03340" FT /number=3 FT intron complement(123789..123839) FT /locus_tag="An14g03340" FT /number=3 FT exon complement(123840..123984) FT /locus_tag="An14g03340" FT /number=4 FT intron complement(123985..124040) FT /locus_tag="An14g03340" FT /number=4 FT exon complement(124041..124151) FT /locus_tag="An14g03340" FT /number=5 FT intron complement(124152..124208) FT /locus_tag="An14g03340" FT /number=5 FT exon complement(124209..124450) FT /locus_tag="An14g03340" FT /number=6 FT intron complement(124451..124541) FT /locus_tag="An14g03340" FT /number=6 FT exon complement(124542..124650) FT /locus_tag="An14g03340" FT /number=7 FT CDS join(125104..125161,125406..125681,125861..125919) FT /locus_tag="An14g03350" FT /note="Remark: weak similarity to fragment of human FT secreted protein encoded by gene 92 patent WO9947540-A1." FT /note="Title: weak similarity to fragment of secreted FT protein encoded by gene 92 from patent WO9947540-A1 - Homo FT sapiens" FT /db_xref="UniProtKB/TrEMBL:A2R380" FT /protein_id="CAK46572.1" FT /translation="MATDPPGVPRVPIGSEARCVELPYRKNMGQRHARPSPVTRNGDIP FT RDRHAHPRTPRASHDSSTSKPDALIGTPLWQSSRILHILVNQCLSRQLYSLTISFPTVL FT GAVEIPTASLPVKLDNCCDILSGKLR" FT mRNA join(<125104..125161,125406..125681,125861..>125919) FT /locus_tag="An14g03350" FT exon 125104..125161 FT /locus_tag="An14g03350" FT /number=1 FT intron 125162..125405 FT /locus_tag="An14g03350" FT /number=1 FT exon 125406..125681 FT /locus_tag="An14g03350" FT /number=2 FT intron 125682..125860 FT /locus_tag="An14g03350" FT /number=2 FT exon 125861..125919 FT /locus_tag="An14g03350" FT /number=3 FT exon 126254..128389 FT /locus_tag="An14g03360" FT /number=1 FT CDS 126254..128389 FT /locus_tag="An14g03360" FT /note="Remark: gene disruption experiments showed that SCT1 FT is not an essential gene under the standard culture FT conditions. SCT1 did not suppress a null mutant of FT ctr1,indicating that a mutant form of choline transporter FT is necessary for the suppression caused by SCT1." FT /note="Title: strong similarity to choline-transport mutant FT SCT1 supressor protein - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R381" FT /db_xref="InterPro:IPR002123" FT /db_xref="UniProtKB/TrEMBL:A2R381" FT /citation=[23] FT /citation=[24] FT /inference="profile:COGS:COG0204" FT /inference="profile:PFAM:PF01553" FT /inference="similar to AA sequence:SWISSPROT:SCT1.YEAST" FT /protein_id="CAK46573.1" FT /translation="MARRFMIPWLYDLGVWIFTLCLDIFFREVYSRGAWRIPKRGPVII FT VAAPHANQFVDSILLMRILKHYAGRRTSFLIAEKSMREPYIGTMAGCMGALPVVRSMDH FT VKPAKGEIYLPDPDNDPTLVRGRGTDFTSDQFMVGGAIILPRVGKTSPEQQAIEEILSP FT EEIRLRKPFKKFEKDHPLYEPLRKGTPFKAAPHIDQSKMFASVYSELVAGGCIGIFPEG FT GSHDRPSLLPLKAGVAIIALGTLAQDPNCGLSIIPCGMNYFHPNKFRSRAVVEFGNPVQ FT VHPDQIEAFKAGGNSKRNAVGSLLETITEALTAVTQQAPDHETLMVIQATRRLYKPLRM FT KLPLPVVIELNRRLLKGYTQFKDEPKVLQLKKAISDYNRRLRALGIRDHQVEWGDVTHR FT PWWLVFGTLLYRVGELLTLAIGTLPSVALFWPVFVTAKVVSVKKQRKALAGSVVKLEGR FT DVVGTWKILVAMGLAPALYTWYTVIVTIWLHYCRHDGHYASVVPWWLNARTYISDSIPL FT ALFSIFFFGLMISVSFAGLRIGEIGIDVLKSLPPLLRALDPRSANSLAKLRAERQALSA FT RVVDVIDTFAPEIFPDFESEKLIPHEHPEDDTYQSRLKSMPPSEPESRNRSKDRTSRSR FT SRSAGFHLYDTLLKPLSIKSKDDLGEVNRRIHVSMQERGRQRARNEIDPDEDVVSLDGS FT VSAQSGDIAVEEVKKTK" FT mRNA <126254..>128389 FT /locus_tag="An14g03360" FT sig_peptide 126254..126346 FT /locus_tag="An14g03360" FT /inference="protein motif:SignalP:2.0" FT mat_peptide 126347..128386 FT /locus_tag="An14g03360" FT CDS complement(join(129678..130003,130028..130103, FT 130155..130691,130749..131246)) FT /locus_tag="An14g03370" FT /EC_number="3.5.2.5" FT /note="Catalytic activity: allantoin + H2O = allantoate." FT /note="Function: utilization of purines as secondary FT nitrogen sources, when primary sources are limiting." FT /note="Pathway: first step in the degradation of allantoin FT (purine catabolism)." FT /note="Remark: DAL1 is expressed in an inducer-independent FT manner in strain M970 (sigma 1278b genetic background) and FT modestly responds to mutation of the dal80 locus. FT Expression was also sensitive to nitrogen catabolite FT repression (NCR)." FT /note="Similarity: belongs to the DHOASE family." FT /note="Title: strong similarity to allantoinase Dal1 FT -Saccharomyces cerevisiae" FT /db_xref="GOA:A2R382" FT /db_xref="InterPro:IPR001969" FT /db_xref="UniProtKB/TrEMBL:A2R382" FT /citation=[7] FT /inference="profile:COGS:COG0044" FT /inference="profile:PFAM:PF01979" FT /inference="similar to AA sequence:UniProtKB:SCDAL1A.1" FT /protein_id="CAK46574.1" FT /translation="MEASQIPSIAVIASSRAVISGRLTSATIVISRTTGKITAVFDSVI FT PASDFPAGTPYTDYSPHVLLPGLVDAHVHLNEPGRTEWEGFYTGTQAAAFGGVTTVIDM FT PLNAIPPTTTVANFKEKLRAAQGKCWVDVGFYGGIIPGNAGDLKALVQEGVRGFKGFLI FT DSGVDEFPAVSSEDIRKAMAELADEPTTLMFHAEMLPPSTAAEEKDQALEGPAEAYSTF FT LASRPSAFETCAVEEIITLSQVAPKLPLHIVHLSAMEAIPLLRKARADGVPITAETCFH FT YLSLAAEEIRDGDTRHKCCPPIRSQSNQDALWDELERHAEDGVIQTVVSDHSPCTPDLK FT LLPSHGSFLSAWGGISSVGLGLPILWTELSHETTTQQALQDVVRLCCTNTAVQVGLQHQ FT KGDLVPGHDADICVFDDTAEWIVEPSTMLFRNKCSPYQGRKLRGMVRETWLRGEKIFSR FT DDGFSTKTPSGGLLLEKRAC" FT mRNA complement(join(<129678..130003,130028..130103, FT 130155..130691,130749..>131246)) FT /locus_tag="An14g03370" FT exon complement(129678..130003) FT /locus_tag="An14g03370" FT /number=1 FT intron complement(130004..130027) FT /locus_tag="An14g03370" FT /number=1 FT exon complement(130028..130103) FT /locus_tag="An14g03370" FT /number=2 FT intron complement(130104..130154) FT /locus_tag="An14g03370" FT /number=2 FT exon complement(130155..130691) FT /locus_tag="An14g03370" FT /number=3 FT intron complement(130692..130748) FT /locus_tag="An14g03370" FT /number=3 FT exon complement(130749..131246) FT /locus_tag="An14g03370" FT /number=4 FT CDS join(131886..131968,132062..132113,132201..132337, FT 132454..132534,132627..132732) FT /locus_tag="An14g03380" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R383" FT /protein_id="CAK46575.1" FT /translation="MGRGIGRLRHPPSDLSCWLLQVIASSPLPRPPALANLMHPRFGRT FT RVQRTKVNCMLRFAYTPVIDRDHRAKNRGFSGTPGSGRTLQWSVAKLQKKWEADHRRLE FT CGGKKGERQQASEMPQVLLQTSSPPLLNTESLLSRMRRWGRQYYSSVT" FT mRNA join(<131886..131968,132062..132113,132201..132337, FT 132454..132534,132627..>132732) FT /locus_tag="An14g03380" FT sig_peptide join(131886..131968,132062..132083) FT /locus_tag="An14g03380" FT /inference="protein motif:SignalP:2.0" FT exon 131886..131968 FT /locus_tag="An14g03380" FT /number=1 FT intron 131969..132061 FT /locus_tag="An14g03380" FT /number=1 FT exon 132062..132113 FT /locus_tag="An14g03380" FT /number=2 FT mat_peptide join(132084..132113,132201..132337,132454..132534, FT 132627..132729) FT /locus_tag="An14g03380" FT /product="hypothetical protein" FT intron 132114..132200 FT /locus_tag="An14g03380" FT /number=2 FT exon 132201..132337 FT /locus_tag="An14g03380" FT /number=3 FT intron 132338..132453 FT /locus_tag="An14g03380" FT /number=3 FT exon 132454..132534 FT /locus_tag="An14g03380" FT /number=4 FT intron 132535..132626 FT /locus_tag="An14g03380" FT /number=4 FT exon 132627..132732 FT /locus_tag="An14g03380" FT /number=5 FT CDS join(134719..135849,135906..137154,137217..137446) FT /locus_tag="An14g03390" FT /note="Remark: FluG from E. nidulans has no apparent role FT in glutamine biosynthesis, but has an enzymatic role in FT sporulation factor production." FT /note="Remark: interaction between fluG and veA influences FT the production of the extracellular signal and regulates FT the initiation of conidiation." FT /note="Remark: mutations in the Aspergillus nidulans fluG FT gene disrupt the programmed induction of asexual FT sporulation and result in formation of fluffy colonies that FT are characterized by undifferentiated cotton-like masses of FT vegetative cells." FT /note="Similarity: to glutamate-ammonia ligases." FT /note="Title: strong similarity to fluG - Aspergillus FT nidulans" FT /db_xref="GOA:A2R384" FT /db_xref="InterPro:IPR014746" FT /db_xref="UniProtKB/TrEMBL:A2R384" FT /citation=[31] FT /citation=[40] FT /citation=[66] FT /citation=[89] FT /inference="profile:COGS:COG0174" FT /inference="profile:PFAM:PF00120" FT /inference="similar to AA sequence:PIR:A53186" FT /protein_id="CAK46576.1" FT /translation="MDPLASLRRLIQTHPLIDNHAHNLLAQAAARNYAKYPFEQITSEA FT QGSALHNAPSTLPLQRAAAQLATLYDCPTSEWDRVKAARDQYVERDYDGLIRRCLEGTH FT SLLLDDLLTDQDIEPFTWHDRFTTAPTKRIVRIEVVAAQVLTSILPNGYDQSSSDITVL FT RQYLDQFSQGFNQKISEAIADPVVVGFKSVICYRTGLNVQVADDKDDSNLLESFSRTLS FT QGSGSTYRVEDKPLNDWLVRQALNQLQSAKEKDASEPNKPLQLHTGLGDNDINLILSNP FT AYLQDLVARYPKVDFVLLHSAYPYTREAGYLACVYPNVYLDLGEVFPMVSRDAQESIIR FT ESLEIVPTTRLLWSTDGHFFPETYWLANKQFRDALEKVLVDYVIQGDHSVDQAKLAAAD FT ILFHNSNRLYSLNETVSYDDRLVPAVSNLSGLSSTDALESFMHSNPDVKYIWMQFFDYT FT STVRVRMFPIREFAKIVRKQRRIGICTATFLMLQSDTVCPEGSTTGQFYLEPDLSTLSR FT NVGIDSKSATVMTWGRSEEGLEVEGCPRTLLRRVTTDLRANHGIEILCGFEIEVILLKC FT VTKPDTDEEEFVPCVRNHSWSQMTRDTRRMVPLLEEIVDTLASIGIDLEQFHAESAPGQ FT FEFILPPGSPVAAVDTLLKARQVVTYIAEQHGYRATLHPRPFSHAAGSAAHAHVSITPA FT TQEESFLAGVLKHFTSLTAFTLSNDVSYERMHSGLWAGSEWVAWGTQNRETPIRKISAG FT HWEIKALDGLSNMYLAMAAILAAGYLGVQDKLPLTLQDCLYDAATLSEADRSAIGITTQ FT IPTTLAQSLDNMAADKALRDVLGNTLVENYITVKRAESKKLNAMEAEARRKWLVERY" FT mRNA join(<134719..135849,135906..137154,137217..>137446) FT /locus_tag="An14g03390" FT exon 134719..135849 FT /locus_tag="An14g03390" FT /number=1 FT intron 135850..135905 FT /locus_tag="An14g03390" FT /number=1 FT exon 135906..137154 FT /locus_tag="An14g03390" FT /number=2 FT intron 137155..137216 FT /locus_tag="An14g03390" FT /number=2 FT exon 137217..137446 FT /locus_tag="An14g03390" FT /number=3 FT exon 137763..138878 FT /gene="argB" FT /locus_tag="An14g03400" FT /number=1 FT CDS 137763..138878 FT /gene="argB" FT /locus_tag="An14g03400" FT /product="ornithine carbamoyltransferase argB-Aspergillus FT niger [putative sequencing error]" FT /EC_number="2.1.3.3" FT /note="Catalytic activity: carbamoyl phosphate + FT L-ornithine = orthophosphate + L-citrulline." FT /note="Gene-ID: argB" FT /note="Mapping: argB from A. niger is mapped to chromosome FT I; see list from DSM." FT /note="Pathway: urea cycle and metabolism of amino groups; FT arginine and proline metabolism." FT /note="Remark: putative sequencing error at positions 56475 FT ,56488 and 56513 generating Frame shifts." FT /note="Remark: the N terminus, which shows little or no FT homology to other OCTases, is highly basic and is probably FT involved in mitochondrial targeting." FT /note="Remark: the differences in the sequence are caused FT by strain variations or sequencing errors." FT /note="Similarity: belongs to the OCTase family." FT /note="localisation:mitochondrion" FT /db_xref="GOA:A2R385" FT /db_xref="InterPro:IPR006130" FT /db_xref="UniProtKB/TrEMBL:A2R385" FT /citation=[17] FT /inference="profile:COGS:COG0078" FT /inference="profile:PFAM:PF00185" FT /inference="profile:PFAM:PF02729" FT /inference="similar to AA sequence:PIR:OWASG" FT /protein_id="CAK46577.1" FT /translation="MPSPLRTAAAAARYGPSTTRHALRRLYSSTSHSAATPATSPFAPR FT HLLSIADLTPTEFATLVRNASSHKRAIKSGSIPQSLHGALSGKTVAMMFSKRSTRTRIS FT TEGAVVQMGGHPMFLGKDDIQLGVNESLYDTAVVVSSMVECIVARVGKHADVADLAKHS FT TKPVINALCDSYHPLQAIADFQTISEHFAASGKGKLEGLGLNGLKIAWVGDANNVLFDM FT AISARKMGVDVAVATPKGYEIPKEMLEIIEKAGEGVKSPGKLVQTNVPEEAVKGADVLV FT TDTWVSMGQEEEAAKRLRDFAGFQITSELAKRGGAKEGWRFMHCLPRHPEEVADEVFYG FT HRSLVFPEAENRLWAAISALEGFVVNKGKIE" FT mRNA <137763..>138878 FT /gene="argB" FT /locus_tag="An14g03400" FT CDS complement(join(139361..140050,140107..140487)) FT /locus_tag="An14g03410" FT /note="Remark: also strong similarity with EST an_3520 FT Aspergillus niger." FT /note="Remark: strong similarity to the 3'-untranslated FT region of the A. niger argB gene encoding ornithine FT carbamoyl transferase." FT /note="Remark: the corresponding gene in potato is of low FT copy number, is expressed in a variety of tissues, and FT encodes a protein which includes several domains with FT similarity to database sequences, including ferredoxin from FT Clostridium pasteurianum. Expression of the cDNA in E. coli FT yields a fusion protein with sucrolytic activity." FT /note="Title: similarity to sucrose cleavage protein FT -Solanum tuberosum" FT /db_xref="InterPro:IPR009737" FT /db_xref="UniProtKB/TrEMBL:A2R386" FT /citation=[33] FT /inference="similar to AA sequence:PIR:S51376" FT /protein_id="CAK46578.1" FT /translation="MRAASLYSLPSISRPNRSAATSARLFSCTSLRSNRSRIPLDIPPP FT FPITKTCPEPSCSCPSTPSMPAPIDYDQPLNGTMAAYAQQLLICTGQRDWTSRIEEDGQ FT GQNWGELVRGLKSLLGRGGKYADPFNNILVTNASFLPSSSSSSSSTSTSTSQTASAFLF FT PSFKYFPSVPVNLPDSAPATTDLSTFVRAFLLPIESRHGGQIRDQALAAEFPDAVDLQH FT SPVVLICGHGGRDMRCGVMAPVLETEFQRVLQSKGYTSAGSDNSVVDSPEHAHIGLISH FT VGGHKYAGNVIVYIPPGMKEAGSSSPHPLAGKGIWYGRIEPKHVQGVVEETILGGKVIT FT DHFRGAVDRESGVLRL" FT mRNA complement(join(<139361..140050,140107..>140487)) FT /locus_tag="An14g03410" FT exon complement(139361..140050) FT /locus_tag="An14g03410" FT /number=1 FT intron complement(140051..140106) FT /locus_tag="An14g03410" FT /number=1 FT exon complement(140107..140487) FT /locus_tag="An14g03410" FT /number=2 FT CDS complement(join(141333..141854,141910..142290, FT 142384..142424,142477..142531)) FT /locus_tag="An14g03420" FT /note="Remark: proteins containing C-terminal 'CAAX' FT sequence motifs undergo three sequential post-translational FT processing steps: modification of the cysteine with either FT a 15-carbon farnesyl or 20-carbon geranylgeranyl isoprenyl FT lipid, proteolysis of the C-terminal -AAX tripeptide, and FT methylation of the carboxyl group of the now C-terminal FT prenylcysteine." FT /note="Remark: the human RCE1 gene product is bona fide a FT prenyl protein protease and play a major role in the FT processing of CAAX-type prenylated proteins." FT /note="Title: strong similarity to CAAX prenyl protein FT protease RCE1 - Homo sapiens" FT /db_xref="GOA:A2R387" FT /db_xref="InterPro:IPR003675" FT /db_xref="UniProtKB/TrEMBL:A2R387" FT /citation=[69] FT /inference="profile:PFAM:PF02517" FT /protein_id="CAK46579.1" FT /translation="MAPVGLLTKLRTLITKDYDEPAISTQTAAFLSVCLTLVYVVPFYV FT NPTTRPSPTLSRDAPSVIRARIRAVTFSCTISSLVVLWLVAAKENASFSRALHFLGWWP FT VGLVDIFRSLLLTAILFAGPLFERGVAEGEWREWIRGGRVTASLRSWIGWRNYVAGPIT FT EEVMFRSAIVPLHLLAKVDPGRIVFVAPLYFGIAHVHHFYEFRLTHPDTSIVAAILRSV FT FQFGYTTIFGWYATFVYLRTGSLLAVILAHTFCNWCGLPRLWGRVEAGVPIGPPMVKGK FT GSSDVTYGQLSLGWTVAYYVILVAGAIGFFQTLWPLTESLNALASFSGATK" FT mRNA complement(join(<141333..141854,141910..142290, FT 142384..142424,142477..>142531)) FT /locus_tag="An14g03420" FT exon complement(141333..141854) FT /locus_tag="An14g03420" FT /number=1 FT intron complement(141855..141909) FT /locus_tag="An14g03420" FT /number=1 FT exon complement(141910..142290) FT /locus_tag="An14g03420" FT /number=2 FT intron complement(142291..142383) FT /locus_tag="An14g03420" FT /number=2 FT exon complement(142384..142424) FT /locus_tag="An14g03420" FT /number=3 FT intron complement(142425..142476) FT /locus_tag="An14g03420" FT /number=3 FT exon complement(142477..142531) FT /locus_tag="An14g03420" FT /number=4 FT CDS join(143709..144002,144054..144064,144112..144364, FT 144418..145722) FT /locus_tag="An14g03430" FT /EC_number="1.14.13.-" FT /note="Remark: aflatoxins are polyketide-derived secondary FT metabolites." FT /note="Remark: northern blot analysis and reverse FT transcriptase-polymerase chain reaction (RT-PCR) studies FT demonstrated that the gene moxY, is expressed concurrently FT with genes involved in aflatoxin biosynthesis. FT Therefore,the two putative aflatoxin pathway genes cypX and FT moxY followed by a 5-kb non-coding region of DNA define one FT end of the boundary of the aflatoxin pathway gene cluster FT in A. parasiticus." FT /note="Similarity: the ORF is longer than moxY of A. FT parasiticus (620 compared to 481 amino acids)." FT /note="Title: strong similarity to monooxygenase moxY FT -Aspergillus parasiticus" FT /db_xref="GOA:A2R388" FT /db_xref="UniProtKB/TrEMBL:A2R388" FT /citation=[80] FT /inference="profile:COGS:COG2072" FT /protein_id="CAK46580.1" FT /translation="MAAVKGPELIRHEPVIEADPKHLPAVSLGSLINELSVSEKADGQA FT RPAFEIEEHPIDEVRPIKVGVIGAGLAGITAGVLLPAKLPGLDLRIYEKNSGVGGTWFE FT NTYPGVRCDIPAHVYQSGFEPNTQWSEEFAQGAEIREYWQSIARTYDVHKYLRLQQKVD FT QAVWLPELGKWRVTLQDLGDSNRIYEEDLDVLINAIGHFNEWKLPEYPGREEYTGVLFH FT SSHWNHNVDLNGKRIALIGNGASGLQVLPSIQPIAQHVDHYARNRTWIADSFGTSGVRR FT LEANLFSPEQLESFRDPDTYLAYRKSVEAGYFSRFGAIFKDSPENRGLREKWTELMKSR FT VGDQPELIDKLIPDFPPNCRRPTPGPGYLEALTKDNVSYIQTPIQRFTPTGIVTTDGIE FT RPVDIVICSTGANVDHAPPFSIISNGIDLKKAWKHDGLYGYPYNYLGVATPGFPNLLWI FT GGPQSTGPSGSVPNSLENQITYIAKLLRKIRSQGIKAMVPSKQAADDFVEYCDKFYPRT FT VWTANDDSTPGQKNCSSWYNGGRPGGKVHGQFPGSAAALNYLRRDPRWEDWDYSYTNPS FT GNRFAYFGNGWTTRETIPDADLTPHLKRPDTIDLRSYLEGWWDV" FT mRNA join(<143709..144002,144054..144064,144112..144364, FT 144418..>145722) FT /locus_tag="An14g03430" FT exon 143709..144002 FT /locus_tag="An14g03430" FT /number=1 FT intron 144003..144053 FT /locus_tag="An14g03430" FT /number=1 FT exon 144054..144064 FT /locus_tag="An14g03430" FT /number=2 FT intron 144065..144111 FT /locus_tag="An14g03430" FT /number=2 FT exon 144112..144364 FT /locus_tag="An14g03430" FT /number=3 FT intron 144365..144417 FT /locus_tag="An14g03430" FT /number=3 FT exon 144418..145722 FT /locus_tag="An14g03430" FT /number=4 FT CDS complement(join(145840..146471,146524..146801, FT 146869..147599)) FT /locus_tag="An14g03440" FT /note="Remark: cercosporin, a photosensitizing FT perylenequinone toxin produced by the plant pathogenic FT Cercospora fungi, generates the highly toxic singlet oxygen FT (1O2) upon exposure to light. Cercosporin shows broad FT toxicity against a wide range of organisms, including FT bacteria, fungi, plants, and animals; however, Cercospora FT fungi are resistant to its effects." FT /note="Remark: targeted disruption of crg1 resulted in FT mutants that, like CS10, are sensitive to cercosporin. FT However, unlike CS10, crg1 disruption mutants are not FT down-regulated in toxin production. Both CS10 and the crg1 FT disruption mutants are unaffected in their response to FT other 1O2-generating photosensitizers, suggesting that CRG1 FT functions specifically against cercosporin, rather than FT against 1O2." FT /note="Title: similarity to cercosporin resistance protein FT crg1 - Cercospora nicotianae" FT /db_xref="UniProtKB/TrEMBL:A2R389" FT /citation=[75] FT /protein_id="CAK46581.1" FT /translation="MLRSVAHAAGVSSNLQTSSNASTNEDLSNLAIPDTNHDSILVPPS FT LTTAPSHSTTTPSLCNGSSQPLALQPPLYELNLDEASWYLERFTTNMLLCFPFICLPPN FT TTTQQLQEDRPFLLEAIIAVATPSTQAKLARTDRLKSRLTKSAMLENQSSIDMLLSILT FT YIAWSTDPFVKRASNLSRMIMLAISMVYDLQLDKQPPPEVPIIAKMAPGLENPEQNASN FT NSLQWISEQHRAKLACFVLSSIISSTIGRIASLRWDIQMEHALNIIETNKESPSDEYLT FT AQIRLQILAQKALSLRDPDEPSPSTTPPATTMYLKVLQRQLAELQSSVLPHLPHYELLH FT LQTHYTSLLLHETPRPASSSTPLLPSTPDSLTSLWNSVQAIKSWLSTFQALPASTITGF FT PFFMWFQLVRCIVLLKHLSTFEDPAWDRDAVRQEVDMLALLEWMGEKAEMASLEAGEGS FT DDDLFRRVGRMLRLAREWVVKKMRGEVGGDGLVSEENSAGSNEGSSGTMGIDMDMDMTD FT MAWMHALESGDGGWLEEVLGWSPLAVYNI" FT mRNA complement(join(<145840..146471,146524..146801, FT 146869..>147599)) FT /locus_tag="An14g03440" FT exon complement(145840..146471) FT /locus_tag="An14g03440" FT /number=1 FT intron complement(146472..146523) FT /locus_tag="An14g03440" FT /number=1 FT exon complement(146524..146801) FT /locus_tag="An14g03440" FT /number=2 FT intron complement(146802..146868) FT /locus_tag="An14g03440" FT /number=2 FT exon complement(146869..147599) FT /locus_tag="An14g03440" FT /number=3 FT CDS complement(join(148138..148775,148836..149190)) FT /locus_tag="An14g03450" FT /note="Remark: similarity to human secreted protein, SEQ ID FT NO: 8103 patent EP1033401-A2." FT /note="Similarity: to dehydrogenases with different FT specificities (related to short-chain alcohol FT dehydrogenases)." FT /note="Title: similarity to secreted protein SEQ ID NO:8103 FT from patent EP1033401-A2 - Homo sapiens" FT /db_xref="GOA:A2R390" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2R390" FT /inference="profile:COGS:COG1028" FT /protein_id="CAK46582.1" FT /translation="MASISEIRASNSRITSETVPRTAVFTGATDGIGKATLTRLISTNL FT PVRVYVIGRNGKRHQAFLDELRLSNRQAQITWLEGQLSLLADTKKLCDEIKRRETSLDC FT LYLSAGFISSGERIETSEGKSLSLSLNYYSRILMMTLLLPLLNSSPNSPRIVSILNAGY FT ESSSIYLDDLDLEKPGHFSLLSLTKSMSTYTTLSMSTLAQENPHVVFVHHYPGGVTTDA FT FKKAWGGKWYFPLFRAALSAFGTSPEDAAEKVLYLITSAKYGGRGVPLREGQKAGMTMA FT TSVKGGELFAIDNKMKELFQGKVMLELQAMNAGEIVWRKTVETLAPYSS" FT mRNA complement(join(<148138..148775,148836..>149190)) FT /locus_tag="An14g03450" FT exon complement(148138..148775) FT /locus_tag="An14g03450" FT /number=1 FT intron complement(148776..148835) FT /locus_tag="An14g03450" FT /number=1 FT exon complement(148836..149190) FT /locus_tag="An14g03450" FT /number=2 FT CDS complement(join(149844..149906,149957..150050, FT 150091..150680,150746..151271,151328..151452, FT 151512..151622,151682..151858)) FT /locus_tag="An14g03460" FT /note="Remark: similarity to Leishmania antigen M15 protein FT patent WO9835045-A2." FT /note="Title: similarity to antigen M15 from patent FT WO9835045-A2 - Leishmania sp." FT /db_xref="GOA:A2R391" FT /db_xref="InterPro:IPR013026" FT /db_xref="UniProtKB/TrEMBL:A2R391" FT /inference="profile:PFAM:PF00646" FT /protein_id="CAK46583.1" FT /translation="MSDKGNATKKIGPQALSCKGADVMSILDNRAATYIKLTQYDRALN FT DSRQMIRRDTKDGRGVLRYGQTLLLTGDRAKALKAYGYGLKTLPEDHPRRKMILQMYCK FT VKERASVKRLDPFDTLPLELAMMVLQHFNFRELAVLLRVSKGWQRMLSQPDLWMHLDFT FT EARRKVHWRSFRAFVQRSRALLTHAVMTNISTPFQDRVLEALSRCPKLEHLEIRDPITQ FT PNGLYDVFRSSTQLKSLVIGKQTPVAQENIAKFLSSLTQLELLEIHNAQPSPESRVLWP FT SHLPNLRSIALFTEASMPAPGRVPALYIPPATESMSCSMPNLEELRLDSYPKVWAPYNL FT SFDPVQFPRLRKLDLKGVFVGPFGLPPSLEYLSIHAGAAPTGEEFPFSPEQLLHLPNLH FT TLILRDLIWVTYRTLHGFIVDSKASLRNLVVDRCPQLDTGKLSLVLVENSVNLTELGVP FT QLPGINDSTVKTLVEGLSNLTALDVSNTDVTGYLLKMLADARSSNVDFPRVEQLPTLGH FT MGSVSFGDVHASAQTHPEACWHAQIYKVCIRGMAVLRPRKSNVV" FT mRNA complement(join(<149844..149906,149957..150050, FT 150091..150680,150746..151271,151328..151452, FT 151512..151622,151682..>151858)) FT /locus_tag="An14g03460" FT exon complement(149844..149906) FT /locus_tag="An14g03460" FT /number=1 FT intron complement(149907..149956) FT /locus_tag="An14g03460" FT /number=1 FT exon complement(149957..150050) FT /locus_tag="An14g03460" FT /number=2 FT intron complement(150051..150090) FT /locus_tag="An14g03460" FT /number=2 FT exon complement(150091..150680) FT /locus_tag="An14g03460" FT /number=3 FT intron complement(150681..150745) FT /locus_tag="An14g03460" FT /number=3 FT exon complement(150746..151271) FT /locus_tag="An14g03460" FT /number=4 FT intron complement(151272..151327) FT /locus_tag="An14g03460" FT /number=4 FT exon complement(151328..151452) FT /locus_tag="An14g03460" FT /number=5 FT intron complement(151453..151511) FT /locus_tag="An14g03460" FT /number=5 FT exon complement(151512..151622) FT /locus_tag="An14g03460" FT /number=6 FT intron complement(151623..151681) FT /locus_tag="An14g03460" FT /number=6 FT exon complement(151682..151858) FT /locus_tag="An14g03460" FT /number=7 FT CDS join(152306..152485,152540..152620,152682..154163) FT /locus_tag="An14g03470" FT /note="Function: antibodies raised against different FT domains of C-Nap1 from H. sapiens prove that this protein FT dissociates from spindle poles during mitosis, but FT reaccumulates at centrosomes at the end of cell division." FT /note="Function: the centrosomal protein C-Nap1 from H. FT sapiens is required for cell cycle-regulated centrosome FT cohesion." FT /note="Localization: antibodies raised against recombinant FT C-Nap1 from H. sapiens produced strong labeling of FT centrosomes by immunofluorescence, and immunoelectron FT microscope revealed that C-Nap1 is associated specifically FT with the proximal ends of both mother and daughter FT centrioles." FT /note="Phenotype: antibody-mediated interference with FT C-Nap1 from H. sapiens function causes centrosome splitting FT , regardless of the cell cycle phase." FT /note="Remark: human C-Nap1 was first identified as a human FT Nek2-interacting protein in a yeast two-hybrid screen." FT /note="Title: similarity to centrosomal Nek2-associated FT protein C-NAP1 - Homo sapiens" FT /note="nucleus" FT /db_xref="UniProtKB/TrEMBL:A2R392" FT /citation=[65] FT /citation=[86] FT /protein_id="CAK46584.1" FT /translation="MEPQNLQAASTYINNVLLARGLLKSGQPIDFANPEDEEGGTAATM FT GRIINLINDLVLRRDREAEHRENLATTIRTLRAEESQKTAELEKVKTKASELTRSLALA FT EAQERALKANASSADSTIRGLKEQVQRMKTTIQQVRAQCANDIRKRDLEMQKLKSHLAE FT RQRGKREGLSMTTININPAASQSSWSRLAAGGEGINDPGYSLKQETNDFLTELCQNLSD FT ENDTLISLARNTVETLKDLQGLSQAEDEDKSATGMASVGAGRSLQGSVTALPTSCDELS FT AQMDHVLEHLRTLLTNPSFVPLEEVEMRDEEIKRLREGWEKMESRWSQAVTMMDGWHKR FT IADGGYSIQAEELRQGLDLRLDITQALSQDGGRDTTIQSPIFEDQEAEEEEEKQTAAKI FT TTEPSRPAQSPRRTRQSTRETRSRRASKALKERSDNIMTGRSPRKVSFTAGLQDSPCEP FT SADDETLQVKAHRSEAVTRRPSRRKAESKGLSRQGSSAQSPQPKESRRATAIQASSSQA FT RLSVPQKLAAAESEAREAEQARKESESRKRGRALKGSSKGHGDRRRSTLTSDELGELMG FT MPAK" FT mRNA join(<152306..152485,152540..152620,152682..>154163) FT /locus_tag="An14g03470" FT exon 152306..152485 FT /locus_tag="An14g03470" FT /number=1 FT intron 152486..152539 FT /locus_tag="An14g03470" FT /number=1 FT exon 152540..152620 FT /locus_tag="An14g03470" FT /number=2 FT intron 152621..152681 FT /locus_tag="An14g03470" FT /number=2 FT exon 152682..154163 FT /locus_tag="An14g03470" FT /number=3 FT CDS complement(join(154317..154422,154501..154833, FT 154926..155077)) FT /locus_tag="An14g03480" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R393" FT /protein_id="CAK46585.1" FT /translation="MEKEELLWLTRSKIASSQSVSVLWREKYERQRTKQPAGLYTNVRS FT YAFTMRTLLATRRFLACYDFYGMKEMGRQNLVAVLPFSVICGILKPPILPGELQIGVRV FT TWSVLLSGWVARNSGLFWGKSGHGSLGARTKYTTMRLRPGILADMIHSVRKIQPVDIDL FT DGHRQKLEHVEIRKYRMAALRNCSWYCGDTGMY" FT mRNA complement(join(<154317..154422,154501..154833, FT 154926..>155077)) FT /locus_tag="An14g03480" FT exon complement(154317..154422) FT /locus_tag="An14g03480" FT /number=1 FT intron complement(154423..154500) FT /locus_tag="An14g03480" FT /number=1 FT exon complement(154501..154833) FT /locus_tag="An14g03480" FT /number=2 FT intron complement(154834..154925) FT /locus_tag="An14g03480" FT /number=2 FT exon complement(154926..155077) FT /locus_tag="An14g03480" FT /number=3 FT CDS join(155261..155958,156020..156152,156202..156648) FT /locus_tag="An14g03490" FT /note="Title: weak similarity to Son of sevenless protein FT Sos from patent WO200005258-A1 - Drosophila melanogaster" FT /db_xref="GOA:A2R394" FT /db_xref="InterPro:IPR000504" FT /db_xref="UniProtKB/TrEMBL:A2R394" FT /protein_id="CAK46586.1" FT /translation="MASHHQLTRAIPYPGKEPFGALWNKCIWQWVFFTGARLRLRVLEK FT NRLFWIYFVIPPWCDPEESYHLPGVPEMAQWDVIHTESTMPNGYHVYVTSRITSHGFEG FT QQYIPAGNFPSFQHVSHNHHFSHMTHPGYQVHHGSPLQQVLKRSGPSWVTIPPQSSLQG FT SVQAQAGPSQGNVANNPCEPEQPESQSRELSPLESGHDIVCDVLIVGEIEVTDENAQDL FT LPLEARLFVGNIPSALCPTQIKFELKRILARYGCCYVKVKTNPNSGLRTAFAQFETPEV FT ANRVMQKSKDQPSEFDLHHRSLRFEMAKGKREISTRTRSREVFSQPDPCTTRVDNIEGR FT VEPAQEMNGEGRVEPAHNMNAEGNVEPTHRINGEGRVEPPQDNREVVSESGKSAGETRE FT SFYNVGARGSHSAPCLPLVWEASATA" FT mRNA join(<155261..155958,156020..156152,156202..>156648) FT /locus_tag="An14g03490" FT exon 155261..155958 FT /locus_tag="An14g03490" FT /number=1 FT intron 155959..156019 FT /locus_tag="An14g03490" FT /number=1 FT exon 156020..156152 FT /locus_tag="An14g03490" FT /number=2 FT intron 156153..156201 FT /locus_tag="An14g03490" FT /number=2 FT exon 156202..156648 FT /locus_tag="An14g03490" FT /number=3 FT CDS complement(join(157408..158280,158342..159449, FT 159508..159653)) FT /locus_tag="An14g03500" FT /EC_number="2.2.1.3" FT /note="Catalytic activity: D-Xylulose 5-phosphate + FT Formaldehyde = Glyceraldehyde 3-phosphate + Glycerone." FT /note="Cofactor: Thiamine diphosphate." FT /note="Phenotype: a das1 deletion strain of C. boidinii has FT completely lost the ability to grow on methanol," FT /note="Title: strong similarity to dihydroxyacetone FT synthase DAS1 - Candida boidinii" FT /note="peroxisome" FT /db_xref="GOA:A2R395" FT /db_xref="InterPro:IPR005475" FT /db_xref="UniProtKB/TrEMBL:A2R395" FT /citation=[67] FT /inference="profile:COGS:COG0021" FT /inference="profile:PFAM:PF00456" FT /inference="profile:PFAM:PF02779" FT /inference="similar to AA sequence:UniProtKB:AF086822.1" FT /protein_id="CAK46587.1" FT /translation="MAVGPVPQSNGASALPLVRQLSKDHDHVLKSFRLLISDLCQQFGG FT GHPGGAIGMAAIGVALWRYVMQYAPHSPDYFNRDRFILSNGHTCLFQYAFLHLTGYKAM FT TFEQLKSYHSDRVDALCPGHPEIEHEGIEVTTGPLGQGVANAVGLAMATKNLAANFNRP FT GYDVISNHTWCMIGDACLQEGVGLEAISFAGHLKLNNLTVIYDNNQITCDGSVDLTNTE FT DINAKMRACGWDVIDVEDGCYDVEGIVQALEKARASQEKPTFINVRTVIGLGSKVEGMA FT AAHGAAFGAPDVADMKRKYGFNPDEHFVISDTVRGFFQELPTRGEALVQQWNSLVKQYS FT AEYPELGAEFQRRMRGELPSNWKDLIPSSFPDKPTATRASSGLVFNPLAKDIESFMVGT FT ADLSPSVNMIWPGKVDFQHPDLRTTCKINGNYSGRYIHFGVREHAMCAISNGLAAFAPN FT TFIPITSSFFMFYLYAAPAVRMGALQHLQVIHAATHDSIGMGEDGPTHQPIELAALYRA FT MPNLLYIRPGDSEETAGAWIAALEAKKSSSIISTSRHALPQLKQTRREGVALGAYVLEE FT ADDASVTLIGVGAELSFALEVAQQLKETKGIAARVISFPCQRLFEQQPLEYKRTVLRRH FT QGIPAVVIEPYAPNGWERYGDAGINIRRFGHSLPGKAAYKFFGYETGVMAAKVSDYLDR FT LEKGEWQRGEFVDL" FT mRNA complement(join(<157408..158280,158342..159449, FT 159508..>159653)) FT /locus_tag="An14g03500" FT exon complement(157408..158280) FT /locus_tag="An14g03500" FT /number=1 FT intron complement(158281..158341) FT /locus_tag="An14g03500" FT /number=1 FT exon complement(158342..159449) FT /locus_tag="An14g03500" FT /number=2 FT intron complement(159450..159507) FT /locus_tag="An14g03500" FT /number=2 FT exon complement(159508..159653) FT /locus_tag="An14g03500" FT /number=3 FT CDS join(160178..160383,160439..160566,160620..160779, FT 160838..161306,161361..161564) FT /locus_tag="An14g03510" FT /EC_number="1.1.1.14" FT /note="Catalytic activity: L-iditol + NAD(+) = L-sorbose + FT NADH." FT /note="Pathway: the rat Sorbitol dehydrogenase SDH is FT involved in the fructose and mannose metabolism." FT /note="Remark: two isoforms of SDH from R. norvegicus are FT produced by use of alternative initiation codons in the FT same reading frame." FT /note="Title: strong similarity to sorbitol dehydrogenase FT SDH - Rattus norvegicus" FT /db_xref="GOA:A2R396" FT /db_xref="InterPro:IPR013154" FT /db_xref="UniProtKB/TrEMBL:A2R396" FT /citation=[34] FT /citation=[41] FT /inference="profile:COGS:COG1063" FT /inference="profile:PFAM:PF00107" FT /inference="similar to AA sequence:SWISSPROT:DHSO.RAT" FT /protein_id="CAK46588.1" FT /translation="MAPSVLLSSPAPTSTSKASLTEQVQLSPPLPNPSLQITADHNLKF FT VPAPVYAPQRGEVLLQIKATGVCGSDIHFWKTGRIGELVFEGDCIIGHEAAGVVLKCGD FT GVTHLQPGDRVAVEPGVPCEHCFLCDDGRYNLCEDVQFAGVYPYAGTIQRYKVHPAKWL FT HKLPDNISYLEGALLEPLSVVMRGIQVARLHLGRAVVVCGAGPIGLIALAAARASGAHP FT IVITDIEPKRLAFAKEFAPWCNTYQVNPALDAEGNAKAIRALFGPDEYNAPETVLECTG FT VENSVCTAAFTARRGGAVVVIGVGKAVMNNLPFMHISLAEIDLRFINRYRDTWPPAIAC FT LTGGILDLKKLVSHVFPLEKAVDALNLCADPRNGSIKVTIVDEVEATL" FT mRNA join(<160178..160383,160439..160566,160620..160779, FT 160838..161306,161361..>161564) FT /locus_tag="An14g03510" FT exon 160178..160383 FT /locus_tag="An14g03510" FT /number=1 FT sig_peptide 160178..160231 FT /locus_tag="An14g03510" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(160232..160383,160439..160566,160620..160779, FT 160838..161306,161361..161561) FT /locus_tag="An14g03510" FT intron 160384..160438 FT /locus_tag="An14g03510" FT /number=1 FT exon 160439..160566 FT /locus_tag="An14g03510" FT /number=2 FT intron 160567..160619 FT /locus_tag="An14g03510" FT /number=2 FT exon 160620..160779 FT /locus_tag="An14g03510" FT /number=3 FT intron 160780..160837 FT /locus_tag="An14g03510" FT /number=3 FT exon 160838..161306 FT /locus_tag="An14g03510" FT /number=4 FT intron 161307..161360 FT /locus_tag="An14g03510" FT /number=4 FT exon 161361..161564 FT /locus_tag="An14g03510" FT /number=5 FT CDS join(163695..163794,163999..164243,164314..164763, FT 164827..165405) FT /locus_tag="An14g03520" FT /note="Function: Dfg5 from S. cerevisiae is required for FT filamentous growth, cell polarity, and cellular FT elongation." FT /note="Phenotype: a dfg5 mutant of S. cerevisiae blocks FT filamentous growth." FT /note="Remark: the synonym for Dfg5 from S. cerevisiae is FT YMR238w." FT /note="Title: strong similarity to filamentous growth FT protein Dfg5 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R397" FT /db_xref="InterPro:IPR014480" FT /db_xref="UniProtKB/TrEMBL:A2R397" FT /citation=[49] FT /inference="profile:COGS:COG4833" FT /inference="profile:PFAM:PF03663" FT /protein_id="CAK46589.1" FT /translation="MRLVRDCLYGGLFLNTALFSQLSHAIDIDISSTSSIKDAASKTAY FT GSMTWYHGNETGQIPGAFPSKWWEGSALFTSLLLYWYYTGDSTYNDEVRQGMQWQAGDC FT DYMPANYSSYLGNDDQMFWGLAAITAAEIEFADSSSGYSWLALAQGVYNTQIDRWDDST FT CGGGLRWQIYPYEAGYAMKNSISNGGLFQLAARLARYTSNDTYADWAEKIFDWCASTPL FT LNNETWNVADSTDVDNSCSTQGNNQWSYNYGVFLTGAAYMYNYTGKAKWKTAAEGLLNV FT TLDTFFPAKYGGNIMSEILCEPTEVCNDNEILFKGLVTGWLGLVALVMPSTYDSILPKL FT QGSAEAAAASCSGMSNNTCGVRWWPKKWDGWNGMEEEIAVTNVLSSALVNTKKTAPVTS FT STGGNSSSDPNAGTGDNTGSSGSTESKITTGDKAGASILTIAFVGMWGGMIAWMVIGG" FT mRNA join(<163695..163794,163999..164243,164314..164763, FT 164827..>165405) FT /locus_tag="An14g03520" FT exon 163695..163794 FT /locus_tag="An14g03520" FT /number=1 FT sig_peptide 163695..163769 FT /locus_tag="An14g03520" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(163770..163794,163999..164243,164314..164763, FT 164827..165402) FT /locus_tag="An14g03520" FT intron 163795..163998 FT /locus_tag="An14g03520" FT /number=1 FT exon 163999..164243 FT /locus_tag="An14g03520" FT /number=2 FT intron 164244..164313 FT /locus_tag="An14g03520" FT /number=2 FT exon 164314..164763 FT /locus_tag="An14g03520" FT /number=3 FT intron 164764..164826 FT /locus_tag="An14g03520" FT /number=3 FT exon 164827..165405 FT /locus_tag="An14g03520" FT /number=4 FT CDS complement(join(166831..167240,167314..167378, FT 167443..167816,167968..168258)) FT /locus_tag="An14g03530" FT /note="Function: Pth11 of M. grisea is involved in host FT surface recognition but is not required for appressorium FT morphogenesis." FT /note="Function: Pth11 of M. grisea is involved in the FT response to both host cutin monomers and contact surface FT hydrophobicity." FT /note="Localization: a M. grisea Pth11-green fluorescent FT protein fusion was localized to the cell membrane and FT vacuoles." FT /note="Phenotype: pth11 mutants of the M. grisea strain FT 4091-5-8 are nonpathogenic due to a defect in appressorium FT differentiation." FT /note="Title: similarity to integral membrane protein PTH11 FT from patent WO9913094-A2 - Magnaporthe grisea" FT /note="plasma membrane" FT /db_xref="UniProtKB/TrEMBL:A2R398" FT /citation=[76] FT /protein_id="CAK46590.1" FT /translation="MTSSLETASRVPVVIAGYTVPIVCMTLCTGLRLFVKVRGPTEDRF FT HADDYLITLATVLLPPYRLVPVHTDDLCCLRLDAGGNIQYYHAGRRYGLHALGDYIASH FT LYNVGLASVKLGILALYYRIFAIQWFRRTVIGCVTFVCLWIATIEIFMGLLCRPLEAFW FT DASVKGHCFNSSALSYYVNTSNMITDLVIFALPIGVIVRLRTTRSNKIALCIIFSIGFI FT TCGISAARLAFVFAESSSDITWDGVDLGVLSGFESLGGILCANLPIIYRLFRQAAQKVT FT SRTGGSSSIPHLQYGRESKNFTSRSRPRRHRLSETLNEQWIQLQNGNSSNDSHVSRGQD FT FAVQKVVDMETGMEVVRLSNVPNAITVKREFHQTVEGRR" FT mRNA complement(join(<166831..167240,167314..167378, FT 167443..167816,167968..>168258)) FT /locus_tag="An14g03530" FT exon complement(166831..167240) FT /locus_tag="An14g03530" FT /number=1 FT intron complement(167241..167313) FT /locus_tag="An14g03530" FT /number=1 FT exon complement(167314..167378) FT /locus_tag="An14g03530" FT /number=2 FT intron complement(167379..167442) FT /locus_tag="An14g03530" FT /number=2 FT exon complement(167443..167816) FT /locus_tag="An14g03530" FT /number=3 FT intron complement(167817..167967) FT /locus_tag="An14g03530" FT /number=3 FT exon complement(167968..168258) FT /locus_tag="An14g03530" FT /number=4 FT CDS join(169076..169353,169448..171200) FT /locus_tag="An14g03540" FT /note="Title: similarity to hypothetical protein encoded by FT An08g01290 - Aspergillus niger" FT /db_xref="UniProtKB/TrEMBL:A2R399" FT /protein_id="CAK46591.1" FT /translation="MAFPPPVSSFSPLGVLQRSFPHLILLTREITRSGVECPSKDMIDC FT RHVHFVVVEPWPSNFIRLRFVASEDVPTQNPVPQRLSYVSSETGQMRRDKEAYSPMRPE FT AHPVCVRCQRSKNRCNYGVRLQWEDDMRAAGKCHGRTGIVTRRDSLRCKESEEDEDLLP FT SKRIERKDQPGSDGESALILTPPSSHSPLRAATSESVSFLTRDTYHSQYQHWKESKIKS FT SNTTFRTLPWTLGVPDVDDVCLSFYESIMCPAAVTIDNEETNPLRNTVMRMVFRSELAY FT YSVLMTSAQYLRSIDSRFELFEMQVRQRVLKGLRQALAESCFEFEDVLLPTIFLCSSAV FT CDVLALDVLMGVSIDSQQISHSCDASWVRHLTCFQMVIKQKIRRHTTTDVPQLFLSYFL FT AHLVLAKSLFPIDKALPVVELRNDLSLPVEEGASWTSSDSLSKAMDPDTLHEIDVWTGM FT SNRMLLLINDILSLKDDVRALYEEGTEAEEKQRVIEAKIITLQRNLQDTTHLLPKSLRR FT CQDSAEVVHRRRLLEYTGESYRLAACLLLSEASTPAFLGYISEPSLGLDTTRKQRHVDY FT ILSLVESIVSSLDHLPISWPLWPLFIASCCSTSESDKARALAQFQAAQAKAPYENTVRA FT QTVVELLWQRRELYVAGERTRTGRFEWELVMEFLGWQTSFA" FT mRNA join(<169076..169353,169448..>171200) FT /locus_tag="An14g03540" FT exon 169076..169353 FT /locus_tag="An14g03540" FT /number=1 FT intron 169354..169447 FT /locus_tag="An14g03540" FT /number=1 FT exon 169448..171200 FT /locus_tag="An14g03540" FT /number=2 FT CDS complement(join(171354..171497,171589..172059, FT 172125..172647,172697..172821,172871..173095)) FT /locus_tag="An14g03550" FT /note="Phenotype: the dal5 deletion mutant of S. cerevisiae FT is viable but unable to transport allontoate or FT ureidosuccinate." FT /note="Remark: synonyms for Dal5 from S. cerevisiae are FT Urep1 and YJR152w." FT /note="Repression: DAL5 is constitutively expressed in S. FT cerevisiae but DAL5 mRNA levels dropped precipitously when FT a repressive nitrogen source was provided." FT /note="Similarity: S. cerevisiae DAL5 specifies the Dal5p FT subfamily of the major facilitator family, which also FT includes YGR260w and YLR004c." FT /note="Title: strong similarity to allantoate permease Dal5 FT - Saccharomyces cerevisiae" FT /note="cytoplasm" FT /db_xref="InterPro:IPR011701" FT /db_xref="UniProtKB/TrEMBL:A2R3A0" FT /citation=[15] FT /citation=[16] FT /citation=[19] FT /inference="profile:COGS:COG0477" FT /inference="profile:COGS:COG2271" FT /protein_id="CAK46592.1" FT /translation="MSASDSTNSPPMEDEKRFHKGPNESIQPLSEREEKAIIRRIDLCL FT LPLMFFSYLLQYLDKTTLSYASILGLLSGTHMTTALYSWTSSAFYFGYLVASYPVSLGF FT VKFPLGKYLSTMMILWAIILTCHAAASNFAGMTALRVLLGVFESAISPGFTLVVSMWYT FT PSEHALRSCIWFAGNGVAAIFGGVLAYAIGHIEDRLGPWQWLFIIFGLITLGWSVFLFF FT ALPDSPHNAKFLQPNQRESAYLRAQACQKSYQSREWKKDQFIEAWLDPKTWFLFVYNFM FT VSLPNGGITNFSSLVIESFGFDTFNTLLYSIPMAAVALVFLLISAFTCNRFRGLRCYWM FT IATLLVSLVGILLMRQLPTEKKWGRLVGVWLVSVFGAGWPLSLSLVSSNFAGFTKKSTV FT TAILFIGYCVGNIAGPQLFKTNEAPKYLVRELSLISVGLRLSAVIEALTNKRRNRKQGR FT TIEPESPEMEDAVQSHSDHSESGDITDWQNESYRYCL" FT mRNA complement(join(<171354..171497,171589..172059, FT 172125..172647,172697..172821,172871..>173095)) FT /locus_tag="An14g03550" FT exon complement(171354..171497) FT /locus_tag="An14g03550" FT /number=1 FT intron complement(171498..171588) FT /locus_tag="An14g03550" FT /number=1 FT exon complement(171589..172059) FT /locus_tag="An14g03550" FT /number=2 FT intron complement(172060..172124) FT /locus_tag="An14g03550" FT /number=2 FT exon complement(172125..172647) FT /locus_tag="An14g03550" FT /number=3 FT intron complement(172648..172696) FT /locus_tag="An14g03550" FT /number=3 FT exon complement(172697..172821) FT /locus_tag="An14g03550" FT /number=4 FT intron complement(172822..172870) FT /locus_tag="An14g03550" FT /number=4 FT exon complement(172871..173095) FT /locus_tag="An14g03550" FT /number=5 FT exon 173682..174944 FT /locus_tag="An14g03560" FT /number=1 FT CDS 173682..174944 FT /locus_tag="An14g03560" FT /EC_number="3.4.13.9" FT /note="Catalytic activity: hydrolysis of Xaa-|-Pro FT dipeptides; also acts on aminoacyl-hydroxyproline analogs; FT no action on Pro-|-Pro." FT /note="Cofactor: Manganese." FT /note="Remark: Microbacterium esteraromaticum = FT Aureobacterium esteraromaticum." FT /note="Remark: the best substrate for the prolidase from A. FT esteraromaticum is Pro-Hyp." FT /note="Title: strong similarity to prolidase FT -Aureobacterium esteraromaticum" FT /db_xref="GOA:A2R3A1" FT /db_xref="InterPro:IPR006680" FT /db_xref="UniProtKB/TrEMBL:A2R3A1" FT /citation=[68] FT /inference="profile:COGS:COG1228" FT /inference="profile:PFAM:PF01979" FT /protein_id="CAK46593.1" FT /translation="MHRPLTDSTFYRINADILIPGRGAPIARGAVVWKSKTILYSGPQH FT EVPVEYQDAVTTHVPVAMPGMWDCHIHFLGATAATMDSIVNTPQALAGARSVPYLYATI FT IAGFTSVREVGGYGCELAKVIDEGRIPGPTIYGAHSAISMTAGHGDVHGVNPEGLRDLC FT THGLPLTIADGVPECLQAVRKQLRHGARIIKVCASGGVVSAIDDPQHQEFSFEELKAIV FT DEAARARRVVAAHCHGKAGIMNALRAGCRTIEHGSYLDEEAIDLMLEKGAMLVATRSVI FT ESGLAMRDLFTPGSYQKLLEVADTHKRAYELAVRRGVPIALGTDQFISSDNPALGYGRN FT GKELVYAVAAGMTPLAAIEAATANGPLTLGDQAPKSGQLREGFDADIIALTANPLENII FT VVSDPKNVTHVWRYGKLVKSN" FT mRNA <173682..>174944 FT /locus_tag="An14g03560" FT CDS join(176709..177801,177861..178543,178591..181113) FT /locus_tag="An14g03570" FT /note="Function: AtrB from A. nidulans is a multidrug ABC FT transporter and has affinity to substrates belonging to all FT major classes of agricultural fungicides and some natural FT toxic compounds." FT /note="Function: AtrB of A. nidulans acts by preventing FT intracellular accumulation of the toxicant." FT /note="Function: cDNA of atrB from A. nidulans can FT complement the drug hypersensitivity associated with PDR5 FT deficiency in S. cerevisiae." FT /note="Induction: The transcription of atrB in mycelium of FT A. nidulans is strongly enhanced by treatment with several FT drugs, including antibiotics, azole fungicides and plant FT defense toxins." FT /note="Phenotype: atrB deletion mutants of A. nidulans FT displayed increased sensitivity to FT anilinopyrimidine,benzimidazole, phenylpyrrole, FT phenylpyridylamine,strobirulin and some azole fungicides." FT /note="Remark: Emericella nidulans = Aspergillus nidulans." FT /note="Title: strong similarity to ATP-binding cassette FT multidrug transport protein atrB - Aspergillus nidulans" FT /note="plasma membrane" FT /db_xref="GOA:A2R3A2" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A2R3A2" FT /citation=[55] FT /citation=[83] FT /inference="profile:COGS:COG1132" FT /inference="profile:PFAM:PF00005" FT /inference="similar to AA sequence:PIR:T30567" FT /protein_id="CAK46594.1" FT /translation="MNPPEFPEDEKSSDLPIPERKSLDTLNVPHINVREAPSAETLIVP FT HAVNASAPGKDAEWSMTPQVIRSQEREAAAGFKKRELGVTWKNLGVDVLAAEAAVNENL FT FSQFNLPQRIRDFTRKPPLKSILTESHGCVKPGEMLLVLGRPGSGCTTLLNLLSNRRHG FT YHTIKGDVSFGNMSHEEAAQYRSHIVMNTEEELFYPRLTVGQTMDFATRLKVPSHLPDG FT AASVKEYTAETKQFLMESMGISHTADTKVGNEFVRGVSGGERKRVSIIECLATRGSVFC FT WDNSTRGLDASTALEWAKALRAMTNVLGLSTIVTLYQAGNGIYNLFDKVLVLDEGKQIF FT YGPAAAAKPFMENLGFVYTDGANVGDFLTGVTVPTERRIRPGYENRFPRNADSIMVEYK FT ASAIYSHMTAEYDYPTSAIAQERTEAFKESVAFEKTTHQPKKSPFTTGFGTQVLACTRR FT QYQILWGEKSTFLIKQILSLVMALIAGSCFYNAPQTSAGLFTKGGAVFFSLLYNTIVAM FT SEVTESFKGRPVLIKHKAFAFYHPAAFCLAQITADFPVLLFQCTIFSVVLYWMVGLKAT FT AAAFFTFWIILFTTTLCVTALFRCIGAGFSTFEAASKISGTAIKGIVMYAGYMIPKPKV FT KNWFLELYYTNPMAYAFQAALSNEFHGQHIPCVGKNIVPNGPGYEDVDSANKACTGVGG FT ALPGADYVTGDQYLSSLHYKHSQLWRNFGVVWAWWGFFAVLTIICTTYWKAGAGGSASL FT LIPRENLKQHQKSIDEESQVKEKEQAKAATSDTTAEVDGNLSRNTAVFTWKNLKYTVKT FT PSGDRVLLDNIHGWVKPGMLGALMGSSGAGKTTLLDVLAQRKTEGTITGSIMVDGRPLP FT VSFQRMAGYCEQLDVHEPFATVREALEFSALLRQPRTTPKEEKLKYVETIIDLLELHDL FT ADTLIGTVGNGLSVEQRKRVTIGVELVSKPSILIFLDEPTSGLDGQSAYNTVRFLRKLA FT DVGQAVLVTIHQPSAQLFAQFDTLLLLARGGKTVYFGDIGENGQTIKNYFGKYGAQCPI FT EANPAEFMIDVVTGGIESVKDKDWHHVWLESPEHQQMITELDHLISEAASKPSGVNDDG FT CEFSMPLWEQTKIVTHRMNVALFRNTNYVNNKFSLHIISALLNGFSFWRVGPSVTALQL FT KMFTIFNFVFVAPGVINQLQPLFIQRRDIYDAREKKSKMYSWISFVIGLIVSEFPYLCV FT CAVLYFLCWYYCVRLPHDSNKAGATFFIMLIYEFIYTGIGQFIAAYAPNPTFAALVNPM FT IISVLVLFCGIFVPYTQLNVFWKYWLYYLNPFNYVVSGMLTFDMWDAKVTCNEDEFALF FT NPTNGTCAEYLKDYIAGQGWRVNLTNPDATSTCRVCEYRRGSDFLTTLNINHYYYGWRN FT AGITVIFAISGYALVFALMKLRTKASKKAE" FT mRNA join(<176709..177801,177861..178543,178591..>181113) FT /locus_tag="An14g03570" FT exon 176709..177801 FT /locus_tag="An14g03570" FT /number=1 FT intron 177802..177860 FT /locus_tag="An14g03570" FT /number=1 FT exon 177861..178543 FT /locus_tag="An14g03570" FT /number=2 FT intron 178544..178590 FT /locus_tag="An14g03570" FT /number=2 FT exon 178591..181113 FT /locus_tag="An14g03570" FT /number=3 FT exon complement(181539..182855) FT /locus_tag="An14g03580" FT /number=1 FT CDS complement(181539..182855) FT /locus_tag="An14g03580" FT /note="Remark: the matching coding sequence was isolated by FT RT-PCR on all of the mRNA from A. thaliana." FT /note="Remark: there are no further informations about the FT patent available." FT /note="Title: strong similarity to protein fragment SEQ ID FT NO:23028 from patent EP1033405-A2 - Arabidopsis thaliana" FT /db_xref="GOA:A2R3A3" FT /db_xref="InterPro:IPR011547" FT /db_xref="UniProtKB/TrEMBL:A2R3A3" FT /protein_id="CAK46595.1" FT /translation="MNLRQINAHNLSTFRHHYVSEISGSLGDLGTFLPIAIALAVNNTV FT SLSSTLIFSGLFNILTGVFFGIPLPVQPMKAIAAVAIARTFTNGAIAAAGLFVAAFILL FT FSVTGLLTRFANAIPIPIIKGIQVGAGLSLIIASCNSLLSNLSWLSPSWADNRLWALAA FT FCFLLFTTVYRTVPYALLVFLLGLIFALILSTLASDLPSLSLWHPYTVLPSPSDWSTGI FT LDAGIGQIPLTTLNSIVAVVHLAHDLLPTHTNSSHLNVTSIALSVSAMNLLGCWFGAMP FT VCHGSGGLAAQYRFGARSGASIIFLGVFKLVIGVFFGESLVGLLKRFPTALLGVMVIAA FT GMELLSVGESLNTTGARDIRKAVAGQGGLTGEDMGPMLSDFERKKRWMVMMVTVGLLVG FT FKNDAVGFLGGLLCHLAFEIPAVVERGVTRWREGRVRLE" FT mRNA complement(<181539..>182855) FT /locus_tag="An14g03580" FT exon complement(183669..184457) FT /locus_tag="An14g03590" FT /number=1 FT CDS complement(183669..184457) FT /locus_tag="An14g03590" FT /note="Function: Nopp 140 functions as a transcriptional FT activator ." FT /note="Localization: Nopp140 from R. norvegicus shuttles on FT tracks between nucleolus and cytoplasm." FT /note="Remark: Nopp140 is one of the most phosphorylated FT proteins in the cell, and nuclear localization signal (NLS) FT binding of Napp140 was dependent on phosphorylation." FT /note="Similarity: the similarities are mainly based on FT repetetive structures." FT /note="Title: similarity to nucleolus-cytoplasm shuttle FT phosphoprotein Nopp140 - Rattus norvegicus" FT /note="nucleus" FT /db_xref="UniProtKB/TrEMBL:A2R3A4" FT /citation=[44] FT /citation=[6] FT /protein_id="CAK46596.1" FT /translation="MEPEKRKYAAGPSLPSTSEDDSSKRRKVIGPAPPPPSTTADANSS FT DNSSSDDDSDDDFGPSLPPPEGTVPSVPNTGATQPIPSESTSEAPKQPQRDAWMLEPID FT GSNRNSRVDPTKLRNRKFQTGRGANTTPSAGGLDVSWTETPEQKMKRLQDEVLGVQTRP FT TAPNAGDSAGGARGAQPSRAMQEKIHRFNEEKRKEEAKARDAERKKKKDGEEEEDDPSA FT RAFDKEKDMALSSKITHAQRREMMNKAADFGSRFTSGKFL" FT mRNA complement(<183669..>184457) FT /locus_tag="An14g03590" FT CDS complement(join(184832..185795,185854..186407)) FT /locus_tag="An14g03600" FT /note="Title: similarity to hypothetical protein FT SPAC56F8.12 - Schizosaccharomyces pombe" FT /db_xref="InterPro:IPR018830" FT /db_xref="UniProtKB/TrEMBL:A2R3A5" FT /inference="similar to AA sequence:PIR:T38922" FT /protein_id="CAK46597.1" FT /translation="MPLLYVRAVVPFEAGANATDVLINEVHFNRTALNYYHYTLFSNGT FT LSNGTDCYLAFNQFQPHMNENGTFVNGTSCYAPIRDIGRHASAGLAFAFMFVFAIVFTL FT INMRKHSRRYLPADRRWTLLGRRAKWIWMLFIAACGTISCFMSIDVDRGYIVSVPLILQ FT SVFYTLLTPGMMAAVWEAVRHWGSWQERQIYDRDPYAFQVSSSRQGQEFVLPIIFYGCA FT LANFVLTVPRSWTAIEMQRSLDQQLNEAKPVATDVRWRAAGFVAVAGVLVICYSLEHSI FT YRYRARPTSTIGQLLFYLNAAPSQFLIAIVLLGVKIGYAIASAFDWTVSPLRYGVDSGW FT LYGLGYTPVLLLLILFNICGFCELNEDKALIVQRDEFNHAVADAVGVGQRKPSWWKKSR FT TFVRELSDHRQRQGSQQDDRDMSRFVEMGIIKPREQPQEDEPKPETWVTTRTASQGSES FT TAVARTESSPETSPPYVEYTLQPELSRNTSNEMEVHGRPQTERDILG" FT mRNA complement(join(<184832..185795,185854..>186407)) FT /locus_tag="An14g03600" FT exon complement(184832..185795) FT /locus_tag="An14g03600" FT /number=1 FT mat_peptide complement(join(184835..185795,185854..186353)) FT /locus_tag="An14g03600" FT intron complement(185796..185853) FT /locus_tag="An14g03600" FT /number=1 FT exon complement(185854..186407) FT /locus_tag="An14g03600" FT /number=2 FT sig_peptide complement(186354..186407) FT /locus_tag="An14g03600" FT /inference="protein motif:SignalP:2.0" FT CDS join(187512..187625,187719..187863,187925..188310, FT 188376..188983,189049..189125,189186..189364) FT /exception="reasons given in citation" FT /locus_tag="An14g03610" FT /EC_number="1.14.-.-" FT /note="Phenotype: Disruption of TRI11 of F. FT sporotrichioides results in an altered trichothecene FT production phenotype characterized by the accumulation of FT isotrichodermin, a trichothecene pathway intermediate." FT /note="Remark: The TRI11 gene of F. sporotrichioides FT encodes a cytochrome P-450 monooxygenase required for C-15 FT hydroxylation in trichothecene biosynthesis." FT /note="Remark: trichothecenes are sesquiterpenoid FT mycotoxins and act as protein synthesis inhibitors for FT eukaryotic organisms" FT /note="Title: strong similarity to cytochrome P450 FT monooxygenase TRI11 - Fusarium sporotrichioides [putative FT sequencing error]" FT /note="putative sequencing error" FT /db_xref="GOA:A2R3A6" FT /db_xref="InterPro:IPR017973" FT /db_xref="UniProtKB/TrEMBL:A2R3A6" FT /citation=[58] FT /inference="profile:COGS:COG2124" FT /inference="profile:PFAM:PF00067" FT /protein_id="CAK46598.1" FT /translation="MLTIIYLESSDSSSISSLGIRYRFTQQAQCGPASWLAMRVEVYRE FT RRNPLSSIPGPFLCKWTDIFVRYQTVTGNRPRYVQGLHKIYGPVVRVGPNAVDIAKIAE FT AREIHRIGSGFLKSPVYELLKHDNAKSIFSTTDPKFHSKHRRLLSSPFADANLHSLEPL FT IEARIRLTMQRMREEMTTRKVADVQKWFFFMSSDIIGELSFGDSFRMLEQGKHIKDLEI FT AALVGESRVAFPFIFRLAEFLPLPILREANKSRNRFGNYADECVNRYKRLLAASPEDVK FT PTLFTKLYNAGKEGLSDAEIRDDASDLIIAGSDTTANTLTYLTWAVCKAPVIRQALVAE FT VATLPERFSDKDVXSLSYLNQVIDEALRLYPAVPCALPRVVPPQGATFSDHWVPGGSTV FT TTQIWSLHRDPVAFPEPEKFDPSRWASPTKEMKDAFMPFGAGTRNCLGLHLARIELRLA FT TAHFFRQFPRSEVSSREGMSDEDMEQVLHFLLSTKGHRCLLEVQ" FT mRNA join(<187512..187625,187719..187863,187925..188310, FT 188376..188983,189049..189125,189186..>189364) FT /locus_tag="An14g03610" FT exon 187512..187625 FT /locus_tag="An14g03610" FT /number=1 FT intron 187626..187718 FT /locus_tag="An14g03610" FT /number=1 FT exon 187719..187863 FT /locus_tag="An14g03610" FT /number=2 FT intron 187864..187924 FT /locus_tag="An14g03610" FT /number=2 FT exon 187925..188310 FT /locus_tag="An14g03610" FT /number=3 FT intron 188311..188375 FT /locus_tag="An14g03610" FT /number=3 FT exon 188376..188983 FT /locus_tag="An14g03610" FT /number=4 FT intron 188984..189048 FT /locus_tag="An14g03610" FT /number=4 FT exon 189049..189125 FT /locus_tag="An14g03610" FT /number=5 FT intron 189126..189185 FT /locus_tag="An14g03610" FT /number=5 FT exon 189186..189364 FT /locus_tag="An14g03610" FT /number=6 FT CDS join(189849..189989,190044..191981) FT /locus_tag="An14g03620" FT /note="Phenotype: deletion of YJL010C in S. cerevisiae is FT lethal." FT /note="Remark: there are no further informations about the FT patent available." FT /note="Title: strong similarity to essential protein FT YJL010c from patent WO200039342-A2 - Saccharomyces FT cerevisiae" FT /db_xref="GOA:A2R3A7" FT /db_xref="InterPro:IPR001313" FT /db_xref="UniProtKB/TrEMBL:A2R3A7" FT /protein_id="CAK46599.1" FT /translation="MPREKVKRGRRATEKANKEASKRKRDDAPEDVVPKRVKPSDDETN FT DFGAQTGDMPFYGLLDPEEQEYFSRANEVLETNQFGDAEERRVFVESVYKEAEGKELKI FT SCSQSCSRLMEKLISMSDIHQIRRLFSKFIGHFLHLVQHRFASHCCETLFIHAAPGVSQ FT KPSKKASKTEAEEGDEPEPELSLAEMFMKVIEELEGNWGYLLTERFASHTIRVLLLVLA FT GEPVDLSLSDSVVASRKKERHGVLNEVQDENPVAQKRSVPESFEGTLKKIMQDMVSVLD FT DTYLRALATHPVGNPVLQVLVYLELSHFGKASAKDPKSIIRRLIPDDTFEEGTESTVFI FT RGLLYDPVGSRLLETIVRYMPGKLFKGLYKNFLRDQLRSLSRNITAGYVVLKVLERLGK FT DDLENAVELLVPQIPNLIERSRVIVPKTLVERCIVRGVDTTPIARSLETAYDSDPAKRL FT SQMLTLEDTTTTSEPQQQNQAQDQDDHQQPPAIPDFGPDNANANINTNPKGAKLHNSLF FT VQTILTAPGPLSALVYSSLLSQTPESLLTIAKDPTASHVIQKSLTLPTSTPQFRRQFAV FT RFTGHLEELALDSSGSRVVDALWHATKDVFFVKERMAQELARSEMALRDSFVGRAVWRN FT WSMDLYKRRRGEWAAKAKGLDVGGEGGQKPKSRIELARERFAAKAAESEKKKNGEDA" FT mRNA join(<189849..189989,190044..>191981) FT /locus_tag="An14g03620" FT exon 189849..189989 FT /locus_tag="An14g03620" FT /number=1 FT intron 189990..190043 FT /locus_tag="An14g03620" FT /number=1 FT exon 190044..191981 FT /locus_tag="An14g03620" FT /number=2 FT CDS complement(join(192564..194151,194233..194597)) FT /locus_tag="An14g03630" FT /note="Remark: the matching coding sequence was isolated by FT RT-PCR on all of the mRNA from A. thaliana." FT /note="Remark: there are no further informations about the FT patent available." FT /note="Similarity: the ORF encoded protein shows also FT strong similarities to RNA helicases." FT /note="Title: strong similarity to protein fragment SEQ ID FT NO:48636 from patent EP1033405-A2 - Arabidopsis thaliana" FT /db_xref="GOA:A2R3A8" FT /db_xref="InterPro:IPR011545" FT /db_xref="UniProtKB/TrEMBL:A2R3A8" FT /inference="profile:COGS:COG0513" FT /inference="profile:PFAM:PF00270" FT /inference="profile:PFAM:PF00271" FT /protein_id="CAK46600.1" FT /translation="MLGAFRRSGAVHALRASRSLLARSIPQQPQWLSASAPAVSYVARA FT LYHPSPAFLDATAAAQAQLNVAADIEPRLPNSKFHSLAQDGLVNDRLIRTVTNSMKIET FT MTDVQAKTIRETLSGDDVLAQAKTGTGKTLAFLIPVVQRLVSDPSVKRSRPSYRGQQGR FT RNTPDIRAIVISPTRELAEQIAHEAQRLVYGLGLTVQTAVGGTQKRLHLNKIRNEGCNI FT LVGTPGRLKDLLSDPYSGVTAPQLQALVFDEADRLLDDGFSQEIGQIKDLLPNPEEVDR FT QTLMFSATVPGEVMNMVRQTMKPDFKFIKTVSEDEVPTHLRVPQKVVYLDGFQNGLPAI FT LELAKQGYVNSPNFKAIVYLNATTMVSLANDIFRRLQNDPEDRTKGHALGRLPILQIHS FT RLTQAQRTRVTSTFRNARSGILFSSDVTARGLDFPDVTHVIQYGLPSERQTYIHRVGRT FT GRANKEGEGWILLHNNEKRAFKQMLGDLPIEEDQTTIPVAKVNMREEIEDDGSETSRTL FT QQIKLAAQQVPIDDRVEAWKSQTGTIIGKLQPLSATLPAMHDLSKYGYVLPKPPHLPSR FT IQQALEKGDRPPPRSNRGGPRDSFRSRDSYRPRSSGGYNDRYQRSSSRDREPRNPWNER FT GSSRGRRESRSYNRY" FT mRNA complement(join(<192564..194151,194233..>194597)) FT /locus_tag="An14g03630" FT exon complement(192564..194151) FT /locus_tag="An14g03630" FT /number=1 FT intron complement(194152..194232) FT /locus_tag="An14g03630" FT /number=1 FT exon complement(194233..194597) FT /locus_tag="An14g03630" FT /number=2 FT CDS complement(join(195969..196328,196392..197381)) FT /locus_tag="An14g03640" FT /EC_number="1.14.13.1" FT /note="Catalytic activity: Salicylate + NADH + O2 = FT Catechol + NAD+ + H2O + CO2." FT /note="Cofactor: FAD." FT /note="Function: salA from Acinetobacter was cloned into FT pUC18 together with salR and salE, and its gene product FT showed salicylate-inducible hydroxylase activity against a FT range of substituted salicylates." FT /note="Title: strong similarity to salicylate hydroxylase FT salA - Acinetobacter sp." FT /db_xref="GOA:A2R3A9" FT /db_xref="InterPro:IPR003042" FT /db_xref="UniProtKB/TrEMBL:A2R3A9" FT /citation=[78] FT /inference="profile:COGS:COG0644" FT /inference="profile:COGS:COG0654" FT /inference="profile:PFAM:PF01360" FT /protein_id="CAK46601.1" FT /translation="MQSTPVPRDILIVGAGIAGLASAISLAKELASSIPDLKISVFEGA FT PGLSASGGAISLTPTAQNYLDKLGVLSELNRMGSEAGIEVDRIELFSLRSGRRLGPLKF FT TDENGFGYGGYKGRRVMRNALSRAMLSVIQTHLPTVSVYFNKKVVGGTTTDSSVTLSFE FT DGSFATGELVLGCDGVHSITRTRIVDPGNRSEYTGISFIQSVTDAHDLSVPMHFNQTAI FT HLTRHSSLLTSYCDPDRQKIFSAAILRVNEHLIERYQATSKSDCPEQASMKMSIRYLVR FT TQFAKSALPSIRALLDHTEDWALYPVYQVRQRGKWHKGRILLLGDAAHAMPPRDESAAY FT SIEDALIFTQIFSRNLHAPLATTFQEYESLRRELVNKVFDASRRLWQSDLDKGLFPGHV FT RELMSPVHMSPGGCTTIASARPAVPAATHQSFSDLSVYSLTREFQGEIES" FT mRNA complement(join(<195969..196328,196392..>197381)) FT /locus_tag="An14g03640" FT exon complement(195969..196328) FT /locus_tag="An14g03640" FT /number=1 FT mat_peptide complement(join(195972..196328,196392..197300)) FT /locus_tag="An14g03640" FT intron complement(196329..196391) FT /locus_tag="An14g03640" FT /number=1 FT exon complement(196392..197381) FT /locus_tag="An14g03640" FT /number=2 FT sig_peptide complement(197301..197381) FT /locus_tag="An14g03640" FT /inference="protein motif:SignalP:2.0" FT CDS join(198267..198849,198889..199003,199111..199117) FT /locus_tag="An14g03650" FT /note="Similarity: the similarities are mainly based on FT repetetive structures." FT /note="Title: weak similarity to syndecan-1 gene Xsyn-1 FT -Xenopus laevis" FT /db_xref="UniProtKB/TrEMBL:A2R3B0" FT /protein_id="CAK46602.1" FT /translation="MNVFDEEPSTITLSTPKASTTGTTIAIILEELRLPYTFHLLPHSS FT STTTLTDIHRTGHGPTLHSLPSITTYLLTRYDGDHHHHHHLSYPPHSPEHVAVEESLSK FT LADRMGIIHQHHQDNEPDNKHEHKHHHNKQHLPAIKETEVVDNNNNTAKETATATVPFA FT RRLLSLYLHLEEYLSRQRRGGGGWLIGERWYCRIWLMGHSTVADIAHFPYVAAASQYGF FT DLERFPELTGWY" FT mRNA join(<198267..198849,198889..199003,199111..>199117) FT /locus_tag="An14g03650" FT exon 198267..198849 FT /locus_tag="An14g03650" FT /number=1 FT intron 198850..198888 FT /locus_tag="An14g03650" FT /number=1 FT exon 198889..199003 FT /locus_tag="An14g03650" FT /number=2 FT intron 199004..199110 FT /locus_tag="An14g03650" FT /number=2 FT exon 199111..199117 FT /locus_tag="An14g03650" FT /number=3 FT CDS complement(join(199421..200247,200304..200702, FT 200764..201090,201146..201760,201820..202288, FT 202372..202422)) FT /locus_tag="An14g03660" FT /note="Remark: the matching coding sequence was isolated by FT RT-PCR on all of the mRNA from A. thaliana." FT /note="Remark: there are no further informations about the FT patent available." FT /note="Similarity: the ORF encoded protein shows also FT strong similarities to putative membrane proteins." FT /note="Title: strong similarity to protein fragment SEQ ID FT NO:22357 from patent EP1033405-A2 - Arabidopsis thaliana" FT /note="plasma membrane" FT /db_xref="GOA:A2R3B1" FT /db_xref="InterPro:IPR003864" FT /db_xref="UniProtKB/TrEMBL:A2R3B1" FT /inference="profile:COGS:COG5594" FT /inference="profile:PFAM:PF02714" FT /protein_id="CAK46603.1" FT /translation="MAIRDVGLEGLHQLFQRSSSDDPQSASNSASGLVTTLVPSLISAA FT AMVIIFIILRRSETRMYMPRTYLGVLRPSERTPASPTGLWNWIMQMYRLPDEYVLQHHS FT MDAYLLLRFLKIVSMICFVGACMTWPILFPVNATGGGGRSQLDMLSMSNVSSDKYARYF FT AHAFVAWLFVGFVFYTITRECLFYINLRHAYALAPAYASRLSSRTVLFTAVTEDYLSRD FT KIRQMFGPEKVKNVWLTTNTSELDDKVAERDDAAMKLEAAETKLIKLANAARLKALKKQ FT GSVEEGQNAGDSLCDDDDESGSVAARWVRPQDRPTHRLTLLVGKKVDTINWARSEIERL FT TPEIEELQAKHREGNADLVSSVFVEFHAQADAQQAFQSVAHNYPLHMAPRYIGLEPTQV FT IWSNLRIKWWERLIRYSATIAFVVALIVFWAIPTAVVGCISNINFLTDKVPFLRFINDV FT PSWILGVITSLLPTVLMSVLMALLPIVLRLMAKFGGAPSLAAVELTTQNFYFAFEVIQV FT FLVVTISSSASSVVTKIINNPTSAASLLAENIPTASNFYISYIILQGLSFSAGALLQIS FT GLILGKVLGRLLDNTPRKMYSRWSNLAGLGWGTVYPVFTLLAVIAIVYSCIAPLVLGFA FT TIGLYLFYFAYRYNMLYVSNANIDTQGKAYVQGLKHLTVGCYLLMVCLIGLFAIGTAAD FT NIATGPLVLMIILLVFCVLYHVALNNALEPLIQYLPKNLESEEEALLSREQTKVSQSGE FT ASDDAAAEGSKARDSGVANIDSAERGLTSDEPQAKPNFLLRYLRPDKYDSYAQMRRLVP FT SGQEITKYAPEVERDAYFNPSIKAQPPLLWIPRDELGVSRQEVRHTSRVIKITDEDAWL FT DEKNHICWDLDKGVPPIFKEKVYY" FT mRNA complement(join(<199421..200247,200304..200702, FT 200764..201090,201146..201760,201820..202288, FT 202372..>202422)) FT /locus_tag="An14g03660" FT exon complement(199421..200247) FT /locus_tag="An14g03660" FT /number=1 FT intron complement(200248..200303) FT /locus_tag="An14g03660" FT /number=1 FT exon complement(200304..200702) FT /locus_tag="An14g03660" FT /number=2 FT intron complement(200703..200763) FT /locus_tag="An14g03660" FT /number=2 FT exon complement(200764..201090) FT /locus_tag="An14g03660" FT /number=3 FT intron complement(201091..201145) FT /locus_tag="An14g03660" FT /number=3 FT exon complement(201146..201760) FT /locus_tag="An14g03660" FT /number=4 FT intron complement(201761..201819) FT /locus_tag="An14g03660" FT /number=4 FT exon complement(201820..202288) FT /locus_tag="An14g03660" FT /number=5 FT intron complement(202289..202371) FT /locus_tag="An14g03660" FT /number=5 FT exon complement(202372..202422) FT /locus_tag="An14g03660" FT /number=6 FT CDS join(202438..202626,202688..202750,202822..202925, FT 203009..203303) FT /locus_tag="An14g03670" FT /note="Title: weak similarity to retinitis pigmentosa FT GTPase regulator RPGR - Bos taurus" FT /db_xref="UniProtKB/TrEMBL:A2R3B2" FT /protein_id="CAK46604.1" FT /translation="MAVRVCRGQVEYRCGYVKRQNVARSRAVDRREGGGDHRQGHGQDR FT KSVRSKQGSWTGRKGGREGEGEPPKGKKPFSVWVAWDLKGRKELAKQIGCTAQRMPIGL FT PGMAMGSAEAKEWFPGFEASATHEGTSHSTWGRAGRVRGDATGRSTLDLRWDRWVARVT FT LLWVEESMTIEGRASVRGIPIRSTNARFAFDFWADQQQSDDRTPFQPLLVIMI" FT mRNA join(<202438..202626,202688..202750,202822..202925, FT 203009..>203303) FT /locus_tag="An14g03670" FT exon 202438..202626 FT /locus_tag="An14g03670" FT /number=1 FT intron 202627..202687 FT /locus_tag="An14g03670" FT /number=1 FT exon 202688..202750 FT /locus_tag="An14g03670" FT /number=2 FT intron 202751..202821 FT /locus_tag="An14g03670" FT /number=2 FT exon 202822..202925 FT /locus_tag="An14g03670" FT /number=3 FT intron 202926..203008 FT /locus_tag="An14g03670" FT /number=3 FT exon 203009..203303 FT /locus_tag="An14g03670" FT /number=4 FT CDS complement(join(203525..203917,204039..204044)) FT /locus_tag="An14g03680" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3B3" FT /protein_id="CAK46605.1" FT /translation="MIPLEHEPTSRPSGGGRDCVPRFLSWPELGTEELKGSGRFKFATF FT ATGRKSHSIDSGSTTWVATRIQRVYEAFQCECMGDATAKSASEQYHTVSELRVRLRDTS FT NLLRPIYWDQLIHSCALSSSLVWSLQPQ" FT mRNA complement(join(<203525..203917,204039..>204044)) FT /locus_tag="An14g03680" FT exon complement(203525..203917) FT /locus_tag="An14g03680" FT /number=1 FT intron complement(203918..204038) FT /locus_tag="An14g03680" FT /number=1 FT exon complement(204039..204044) FT /locus_tag="An14g03680" FT /number=2 FT exon 204844..205116 FT /locus_tag="An14g03685" FT /number=1 FT CDS 204844..205116 FT /locus_tag="An14g03685" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3B4" FT /protein_id="CAK46606.1" FT /translation="MQALLALLLIASAEEYLCVRVCCCHLREAMLFSLCSAHHHYAYRN FT RCCLCVCSADDDDSIYNWHHHIIHRRKLEERETNISRVAADFAAK" FT mRNA <204844..>205116 FT /locus_tag="An14g03685" FT sig_peptide 204844..204882 FT /locus_tag="An14g03685" FT /inference="protein motif:SignalP:2.0" FT mat_peptide 204883..205113 FT /locus_tag="An14g03685" FT /product="hypothetical protein" FT CDS join(205410..205544,205587..205778) FT /locus_tag="An14g03690" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3B5" FT /protein_id="CAK46607.1" FT /translation="MAFAFGGIRDGSMPGLASLPRLVSETGPYEDVYTGTNDCCTSPEE FT GVYRGETIFCHTRENCPESKADVWSIIPVNSLKHKMQGLHEEVTKYITQPQTRQRSRPL FT TILP" FT mRNA join(<205410..205544,205587..>205778) FT /locus_tag="An14g03690" FT exon 205410..205544 FT /locus_tag="An14g03690" FT /number=1 FT intron 205545..205586 FT /locus_tag="An14g03690" FT /number=1 FT exon 205587..205778 FT /locus_tag="An14g03690" FT /number=2 FT CDS complement(join(207890..208855,208950..209320, FT 209362..209455)) FT /locus_tag="An14g03700" FT /note="Title: weak similarity to protein fragment SEQ ID FT NO:52297 from patent EP1033405-A2 - Arabidopsis thaliana" FT /db_xref="UniProtKB/TrEMBL:A2R3B6" FT /protein_id="CAK46608.1" FT /translation="MSADRLPLADSTPLDSTSGVRGTSSSESEQQLDELTNTISSGTSS FT DPPQIPVRLRRRRHLPMSDDQSSRNQIFYFVDSNSSSREKRAHVMRHHVQEKRRQRKSS FT HSRADGDRRGSRPLRYSPWPHKRTDVDNHDDYESIAPQEVPSETSVNGHSLIRFGLPPV FT QSPPESVDGYQSPSPVTMLDASRKDPFNSLPGVYSRDDQELADYWTNRLTYWSGQNKYI FT KDLVFKAAMSHPLCFQAVILTYCARWKAQLYNLQDSKEAHYHLDKAVQGIEEAKIGSAG FT VDEDNLALALSGMSLHEDRFGDKQVARKYEDQAVEILRSRSGTQSTVEVFMHYVRYVMI FT PPPMEMSEEGKRWLVSFLHAAEQLMHQHSTPSYLESVPQRRTAFQMDSPLFPLLSSGPR FT PSQVPQDYRMYVVRNAPTQEITRTAALIYITAALWDLAASENKTGRFLNHLHHLVRLHN FT LDRYPACETFIWLLLEEG" FT mRNA complement(join(<207890..208855,208950..209320, FT 209362..>209455)) FT /locus_tag="An14g03700" FT exon complement(207890..208855) FT /locus_tag="An14g03700" FT /number=1 FT intron complement(208856..208949) FT /locus_tag="An14g03700" FT /number=1 FT exon complement(208950..209320) FT /locus_tag="An14g03700" FT /number=2 FT intron complement(209321..209361) FT /locus_tag="An14g03700" FT /number=2 FT exon complement(209362..209455) FT /locus_tag="An14g03700" FT /number=3 FT CDS join(210596..212244,212308..212447,212508..213478, FT 213543..213665) FT /locus_tag="An14g03710" FT /note="Phenotype: mis5 deletion in S. pombe results in DNA FT replication defect and hypersensitivity to UV ray and FT hydroxyurea." FT /note="Phenotype: mis5 mutation in S. pombe leads to high FT loss rates of minichromosomes." FT /note="Remark: mis5 is essential for viability." FT /note="Similarity: mis5 from S. pombe encodes a novel FT member of the ubiquitous MCM family required for the onset FT of replication." FT /note="Title: strong similarity to replication licensing FT factor mis5p - Schizosaccharomyces pombe" FT /db_xref="GOA:A2R3B7" FT /db_xref="InterPro:IPR001208" FT /db_xref="UniProtKB/TrEMBL:A2R3B7" FT /citation=[29] FT /inference="profile:COGS:COG1241" FT /inference="profile:PFAM:PF00493" FT /inference="similar to AA sequence:PIR:T50339" FT /protein_id="CAK46609.1" FT /translation="MSSLFDAVLQSELGSTAGSRDHRLHSDQIPSSRPQPPSESNGPMS FT DMHGFADDQIADSSASTVTRLRNPYLPGPPPVSDVAGEKVQQAFAELLETYQEETPSSA FT QAAPSSQVLSEKYYIAQIMGMAKWELSTLYVDFTHLTSMSNPILADAIANQYYRFQPFL FT TKALHDLIAKYEPDYFASHRQATAAGSVSSQAGTSMIAGNSSVSDNPELERNIREKTRH FT QQTDKLFSLAFYNLPLVSRLRQLRTSQIGKLVSVSGTVTRTSEIRPELSLGTFICEECK FT AVVTNVEQTFRYTEPSQCPNNTCGNRSGWRLDIGKSTFVDWQKVKLQESSHEIPTGSMP FT RTMDVILRGEMVDRAKAGERCIFTGTLIVVPDVSQLGLPGVRPEAVRDDGAFRGSDIGG FT GGVTGLKALGIKDLTYRLAFLSCMVTPDTTTPGQQSNQQLNGQSQNILASLNQNRDPES FT NEDQAQEALLQSLTPYEVQDLKNLVHSEYIYSRLIDSIAPMIYGHRQIKKGLLLQLIGG FT VGKSTEQENLQLRGDINICIVGDPSTSKSQFLKYICSLHPRAVYTSGKASSAAGLTASV FT VKDAETGEFTIEAGALMLAVGGICCIDEFDKMDISDQVAIHEAMEQQTISIAKAGIHTT FT LNARASILAAANPIGGRYNPKTTLRGNLNFSAPIMSRFDLFFVIRDDPNETVDRNLADH FT IVNVHMNRDEAVNPELSTEQLLRYIRFARTFKPVFTEEAKAYLVEKYKELRAGDAQGGM FT GRSSYRITVRQLESLIRLSEAVAKANCVEEIIPKFVREAYDLLRQSIVTVEKDDVEVDD FT DEPAAADGPAVEEDHEMGDRDGDSPMREDAEPAQPKRSRTKITYDKYMKILNLMVRRVR FT DDEANSGEGVEQEDLLIWYLEQIESEIDTEDDLQNERDLAVKVLKRMIKDNILMPIRGQ FT GLVDADDEGQSEQVQRTVYVMHPNCAIDEM" FT mRNA join(<210596..212244,212308..212447,212508..213478, FT 213543..>213665) FT /locus_tag="An14g03710" FT exon 210596..212244 FT /locus_tag="An14g03710" FT /number=1 FT intron 212245..212307 FT /locus_tag="An14g03710" FT /number=1 FT exon 212308..212447 FT /locus_tag="An14g03710" FT /number=2 FT intron 212448..212507 FT /locus_tag="An14g03710" FT /number=2 FT exon 212508..213478 FT /locus_tag="An14g03710" FT /number=3 FT intron 213479..213542 FT /locus_tag="An14g03710" FT /number=3 FT exon 213543..213665 FT /locus_tag="An14g03710" FT /number=4 FT CDS join(214576..214795,214852..215353,215406..216117, FT 216247..216331,216379..216466,216516..216644, FT 216702..216859,216927..217026,217095..217182, FT 217335..217467,217500..217568,217608..218398, FT 218455..218634,218684..218998) FT /locus_tag="An14g03720" FT /note="Function: RAD5 of S. cerevisiae has single-stranded FT DNA-dependent ATPase activity, and is involved in FT error-free DNA repair." FT /note="Remark: RAD5 of S. cerevisiae is also called FT REV2,SNM2 or YLR032W." FT /note="Similarity: the predicted ORF shows equally strong FT similarity to the S. cerevisiae RAD5 protein, a putative FT helicase of S. pombe, the DNA repair protein RAD16 of S. FT cerevisiae and other related proteins from diverse FT eucaryotic species." FT /note="Title: strong similarity to DNA repair protein Rad5 FT - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R3B8" FT /db_xref="InterPro:IPR017907" FT /db_xref="UniProtKB/TrEMBL:A2R3B8" FT /citation=[35] FT /citation=[3] FT /citation=[46] FT /citation=[64] FT /citation=[73] FT /inference="profile:COGS:COG0553" FT /inference="profile:PFAM:PF00176" FT /inference="similar to AA sequence:PIR:S64859" FT /protein_id="CAK46610.1" FT /translation="MEGLSKGLEPPRNTEDLLAGSGDVQEPDEQESSLQPESLDPDQMR FT LEAIDRRRQQDNSRQALFFSRLGLDTHNPVQHTESAPSTIPSVQDDQAPAAQAVLDESL FT FVPQEVSFSWNHLSTETDVPPMSPDDQNIFDLFQGLNSEGDTSPPIEQLLQNSPHSIAS FT ASQTGNAGTTAAPAANEEDPKPSAPTCVEIISSSSSASGDTDVPVEDFPDDAGDQSCPT FT EWPDEELEASTRADLSKRKFNSIKKWFDSLEKPSVADEIRLETARQQESARKNRVARRK FT ALENQSELFDPEIDEPDEFTSRQVPIEQKTGSSHDVPVKPQPKKRRQNRISADEKQKSK FT ELGLAAVLVQQKKRGPPKGAPRKRKERGSDNAIPGPSKKRKRGPLGSKKYLEALLSSTI FT VADAHANASLDAIPELKNKDKMKALTHLVASLPSADQQEAKSDKRSIIAATRNFTNVPR FT SDGKSGWRLKGLNTSLYHYQRKRESSSERPFGGLLCDIMGFGKTIQALANIIDGKPSDP FT EDPNKTTLIVVPSHLVTHWKTQINKHCEKKAIGDVLIYKANSRLETLDTLDTVESLVRY FT DVIITTYDEVRKSYPRIKVADSVADNDKLAAWWDQSYEDEIGPLHRIKFHRIILDEGHT FT IKNHLSSVSIAVRSLTGHFKWILSGTPVHNYLEEFYPLFDFLGVPGIRDPGFFIKNFCS FT LPDVNERIVRVAFCAVERELYNAISEVFIENINGAPNTPRAILRSCAHLEQPKLAQYRC FT FLSMILMLLKRLLSEGNLMKRLSRLAKQSGDRDPSFTIVKWLVSVRRNTTVLDERENED FT TFQYATELHGDETALMQNFRQLMDELHDTEIWEERLARTNCPQCDFVPVNPVITSCRHL FT YCEECYYSLRMDKDKMLMEPNCVSCRVPIMEAAYFKEDGDEKTRPATTLGAVNRKKKQG FT KKTTTTKKQARSSMRRVTAPQIEESDEEPDADEDTDWIKACARHMPSAKLTKIREILTE FT WLAQDSPGKIVIFTQFLDFVQILATMCQAENWPYVLLTGKLSLAVRENNMTLFSDKDSE FT KRIMIASLKAGGTGLDLSAANKCILVDLWWNEAIQEQLLTLPFQAFCRLFRIGQESEVE FT FVKLIIENSIDDYLLNLQTHKTAIITGAMGERALAGRDTIEDLLRMFADVEKDPRGVLH FT LKAKTASRDIRIGAGFRPTFGVF" FT mRNA join(<214576..214795,214852..215353,215406..216117, FT 216247..216331,216379..216466,216516..216644, FT 216702..216859,216927..217026,217095..217182, FT 217335..217467,217500..217568,217608..218398, FT 218455..218634,218684..>218998) FT /locus_tag="An14g03720" FT exon 214576..214795 FT /locus_tag="An14g03720" FT /number=1 FT intron 214796..214851 FT /locus_tag="An14g03720" FT /number=1 FT exon 214852..215353 FT /locus_tag="An14g03720" FT /number=2 FT intron 215354..215405 FT /locus_tag="An14g03720" FT /number=2 FT exon 215406..216117 FT /locus_tag="An14g03720" FT /number=3 FT intron 216118..216246 FT /locus_tag="An14g03720" FT /number=3 FT exon 216247..216331 FT /locus_tag="An14g03720" FT /number=4 FT intron 216332..216378 FT /locus_tag="An14g03720" FT /number=4 FT exon 216379..216466 FT /locus_tag="An14g03720" FT /number=5 FT intron 216467..216515 FT /locus_tag="An14g03720" FT /number=5 FT exon 216516..216644 FT /locus_tag="An14g03720" FT /number=6 FT intron 216645..216701 FT /locus_tag="An14g03720" FT /number=6 FT exon 216702..216859 FT /locus_tag="An14g03720" FT /number=7 FT intron 216860..216926 FT /locus_tag="An14g03720" FT /number=7 FT exon 216927..217026 FT /locus_tag="An14g03720" FT /number=8 FT intron 217027..217094 FT /locus_tag="An14g03720" FT /number=8 FT exon 217095..217182 FT /locus_tag="An14g03720" FT /number=9 FT intron 217183..217334 FT /locus_tag="An14g03720" FT /number=9 FT exon 217335..217467 FT /locus_tag="An14g03720" FT /number=10 FT intron 217468..217499 FT /locus_tag="An14g03720" FT /number=10 FT exon 217500..217568 FT /locus_tag="An14g03720" FT /number=11 FT intron 217569..217607 FT /locus_tag="An14g03720" FT /number=11 FT exon 217608..218398 FT /locus_tag="An14g03720" FT /number=12 FT intron 218399..218454 FT /locus_tag="An14g03720" FT /number=12 FT exon 218455..218634 FT /locus_tag="An14g03720" FT /number=13 FT intron 218635..218683 FT /locus_tag="An14g03720" FT /number=13 FT exon 218684..218998 FT /locus_tag="An14g03720" FT /number=14 FT CDS complement(join(219472..220287,220392..220976, FT 221258..221459,221591..221742,221773..221815, FT 221942..224066,224189..224333,224398..224463)) FT /locus_tag="An14g03730" FT /note="Induction: transcription of M14 from M. musculus is FT dramatically induced (about 70-fold) by isoproterenol FT treatment." FT /note="Similarity: the ORF also shows strong similarity to FT the EST SEQ ID NO:4359 of patent WO200056762-A2 from FT Aspergillus niger." FT /note="Similarity: the similarities are based on repetetive FT structures." FT /note="Title: similarity to hypothetical proline-rich FT protein M14 - Mus musculus" FT /db_xref="UniProtKB/TrEMBL:A2R3B9" FT /citation=[13] FT /inference="profile:COGS:COG0515" FT /inference="profile:COGS:COG1674" FT /inference="profile:COGS:COG2319" FT /protein_id="CAK46611.1" FT /translation="MAAVVASGHKAYQFTAGRRMDGSFLRASPIPDPATQRKATNSRDP FT NNPHETTPRRPSLFETRHGSRNSNSEDIILGPPKTAFASASRIPGKGSIDATERSSRPN FT DQDESKNDRFNLREKFFKDRETGDRDFDRRDGKLGTFNNNNTNNNNRRGDREDWNSGRP FT RRTFGPEEQDRKPRRNGEFDRWENRDQREPNNDRGVRDKDARFFPRKDGTPGRARHEGS FT WFRDENTHDAPEAEEEKTPIRNREWRRDRHGADRDWTRGAKFEQDPEWMDSTDRDEPRR FT VHTQEDFERWKERMKAGSSQVQAEEKEVPLETTPAPAPAPKPEPRPTDGEIFSSNGAPF FT TSDSAMERFFGLLGDSKPPQAPPLPQEISAPPPMMEPTMKKEPLPGKLGKSSRFAGLFS FT PPPGSPAKEPESHPETRSSPSMNTVNTDADQEGFQRILQMLGGGKSRNATPHNDPVAYN FT RPPSQVQAEQIRSAVSSPARDQIKRQEYLAMQETVARGAGPNPYVQETHARDREHLLRL FT MQQVRVSPVANQGAQSQPQSAGPVGPAPGLLSMPEVLSPPPGIPTPQKGPNFLDDPAIA FT NMQRPDADHLRRRPANGPPMGYFEDMPFPQGGQLPMTPGGTRAPQAQGHPPMGMQRPPG FT FEHLPPPGWPGPQMPPQQAAGPAPLAPPPGIPTPTRGVNPSYMANMMPMHGNAPPLNER FT EPFPRPPPPGMMPPPGYMNGPPPAGFPPMPPNGEALMGLPHRGQGPFEGNPGPQVPPPS FT ARHLLDMFGQVGGEAPRGMLGPGQFRTMHLLIFLYLIHLCFEGVQERPSQLLRLGTDEE FT TVSQPDSFASGCITTLGDYIKDSNRQIADTEMCLRRSDCSEWPVDSELRTFKPSRFPLL FT FPTSYFHPLHLLEESATLSLTADVRHQLLIWIKIHHPKPQINPDPTMPHSTSPPSPSPT FT QNTSNHHHPQSIQTTTAMITTTTRKRRAACDNDNGDSKNTSPGTLINTTPNATNNETGH FT QPFKRPRIPSQFTRQAERFEEALNKEIQEQEDALRMNEYRMLAVRALENEAHDRAFRDA FT MDMSSTYQQQQQQYTPSPHPPVAVAASEDMDMDVDGDDYHNPQHEDHHGTGEGEGQMVA FT PTVQYTEGDTEPIITTRSGCLTSIIGMNNINPITRHRSNQHQHNNNNNHSTLTEFTIYE FT DLSPDPGGLLSFPTQPNPVGQLQPDYHHYHYNNHHNNQEVRAYHQDWDSDKENINNNIV FT AGPLHDPVGMITETEAESFSQVVDHSYHNADNVADEVDDEMRMDYEAGGSGGESGRWSS FT GVPPWRVESESEYADTEVDPDEAGLGLQDYAHRRRRRYHRLRWQSRVLGSQDRGSVASN FT SSVLVPRVLGEGLQDGAGAGGAGAGRGRRGSRRL" FT mRNA complement(join(<219472..220287,220392..220976, FT 221258..221459,221591..221742,221773..221815, FT 221942..224066,224189..224333,224398..>224463)) FT /locus_tag="An14g03730" FT exon complement(219472..220287) FT /locus_tag="An14g03730" FT /number=1 FT intron complement(220288..220391) FT /locus_tag="An14g03730" FT /number=1 FT exon complement(220392..220976) FT /locus_tag="An14g03730" FT /number=2 FT intron complement(220977..221257) FT /locus_tag="An14g03730" FT /number=2 FT exon complement(221258..221459) FT /locus_tag="An14g03730" FT /number=3 FT intron complement(221460..221590) FT /locus_tag="An14g03730" FT /number=3 FT exon complement(221591..221742) FT /locus_tag="An14g03730" FT /number=4 FT intron complement(221743..221772) FT /locus_tag="An14g03730" FT /number=4 FT exon complement(221773..221815) FT /locus_tag="An14g03730" FT /number=5 FT intron complement(221816..221941) FT /locus_tag="An14g03730" FT /number=5 FT exon complement(221942..224066) FT /locus_tag="An14g03730" FT /number=6 FT intron complement(224067..224188) FT /locus_tag="An14g03730" FT /number=6 FT exon complement(224189..224333) FT /locus_tag="An14g03730" FT /number=7 FT intron complement(224334..224397) FT /locus_tag="An14g03730" FT /number=7 FT exon complement(224398..224463) FT /locus_tag="An14g03730" FT /number=8 FT CDS complement(join(225592..225909,225964..226290, FT 226360..228935,228990..229134)) FT /locus_tag="An14g03740" FT /note="Title: strong similarity to hypothetical protein FT SPCC14G10.02 - Schizosaccharomyces pombe" FT /db_xref="UniProtKB/TrEMBL:A2R3C0" FT /inference="similar to AA sequence:PIR:T41013" FT /protein_id="CAK46612.1" FT /translation="MSSHEGQLRNKRRKLDNGQDVDATATISSHTQLRSSLAFQQNPNE FT SKQGIRKFKDFLTSIGQSEDEAEKARKFRILKAYCDSQFSRVNENEAVCFTDLVQTWGF FT ADSNNNESLLTVVPSVLAQFLKTVSSNLDFRDFGVALCKYLLQKEQLRLFNRGLTALKS FT KEHLISPCLRLLTEMVSFDGGAVARHVHAARYITFKRIEVFLTPNKAQLEEISEESSKP FT TLRRNAQKYVLANLRFLQSNGKSDIIEQHKVIRAFFEYIRKDARDIVLETIRCIDKDII FT QDASISRIAKSKFFNRWNLERLVTLYGYDRESEEPNPANVSTTDEIHKILMNVCTNTEL FT GVLLPESGWYPHGSDPEALPTDDETLIDLGLDSALHVDKYSQSVPVRNGTLSYLIQTLR FT PDTDSLQIELLVAIFKAAPELVADFFTKKSMFTADPKPTPSWMAESALLFSSVQLPVPV FT NCGWKDKLPPTPPPVSVVIENVLPRPLTQKILTRCLNMNAEIVTLFAVRILTIAFNKLR FT AVLKIFNGDHGVSQPLWTQAASKLVAEFSRRCPGVKEVILLFKRTDKEDFQQQDAVSEL FT LASFYEVVPDAAFEEGLDVSLILVDVLKRLDEGKLDEDDTESVLSQLQNIMRIVQQSTS FT MRWWQQPGSMQYSAFTSILKVLVETASRYSLREIDQLLRTVLTEYSVLQNPSSFPAILS FT SFEISDSEKLQRQLSFFDNCACRIAKKPVHYQDLVDSLFEGFSSPVSPLVAAVIEQWPF FT VVKSGDPAVESAVVAWIAQTLGSLKRAGENAKALKSARDKLVESAENKKSKSAFKKALK FT DIEDAEEDHEMDIDAPSQDTTTTAKKEEVDLEEVFGTLPTESTTHNELHRWEKEDIEVA FT VEQGRIAELVLCLCSAYEEVRKQAFTSIIRFMGKLKESKYVEWRSVYILTGELLETVKQ FT IGLDSPVPWIVGECASSCLTVLTDPMHKMYGKVNKFLQKAPSWEVEKIPSYWIDKILLH FT EPELDDGYFDETSWLLDLLIKGLRTEADMDIYRRANVFERALSFYESPSAGYSAKRKIL FT QLVYRATQVQGSTTLVTRAGILSWIQGQIPAVKGKETSTLAAIADSLKQTSDNDRVSKW FT SGGAALQVVENIVG" FT mRNA complement(join(<225592..225909,225964..226290, FT 226360..228935,228990..>229134)) FT /locus_tag="An14g03740" FT exon complement(225592..225909) FT /locus_tag="An14g03740" FT /number=1 FT intron complement(225910..225963) FT /locus_tag="An14g03740" FT /number=1 FT exon complement(225964..226290) FT /locus_tag="An14g03740" FT /number=2 FT intron complement(226291..226359) FT /locus_tag="An14g03740" FT /number=2 FT exon complement(226360..228935) FT /locus_tag="An14g03740" FT /number=3 FT intron complement(228936..228989) FT /locus_tag="An14g03740" FT /number=3 FT exon complement(228990..229134) FT /locus_tag="An14g03740" FT /number=4 FT tRNA 229730..229802 FT /gene="tRNA-Thr (AGT)" FT /locus_tag="An14e03750" FT /product="transfer RNA-Thr (AGT)" FT /inference="profile:tRNAscan:1.4" FT CDS join(230504..230941,231096..231146) FT /locus_tag="An14g03760" FT /note="Title: weak similarity to endoglucanase from patent FT WO9110732-A - Bacillus sp." FT /db_xref="UniProtKB/TrEMBL:A2R3C1" FT /protein_id="CAK46613.1" FT /translation="MSPTPITKSSLIGAWTLISYTVEPPNPQDDDSPTHYPMGPDARGT FT LVYTPDGQVTVSVLPKVTKKAWENSNDGVMYAGRYWIEYSNGSECDNGGDKRQQPGGAP FT VVHHEVDMAYSAEFAGSQKREAMIFPEGRLRLSGLKLFEVGMREGKNELAAGSQSTDA" FT mRNA join(<230504..230941,231096..>231146) FT /locus_tag="An14g03760" FT exon 230504..230941 FT /locus_tag="An14g03760" FT /number=1 FT intron 230942..231095 FT /locus_tag="An14g03760" FT /number=1 FT exon 231096..231146 FT /locus_tag="An14g03760" FT /number=2 FT exon complement(231387..235082) FT /locus_tag="An14g03770" FT /number=1 FT CDS complement(231387..235082) FT /locus_tag="An14g03770" FT /note="Remark: expression of human HRH1 in a S. cerevisiae FT prp22 (RNA helicase) mutant can partially rescue its FT temperature-sensitive phenotype." FT /note="Title: strong similarity to RNA helicase 1 HRH1 FT -Homo sapiens" FT /note="nucleus" FT /db_xref="GOA:A2R3C2" FT /db_xref="InterPro:IPR003029" FT /db_xref="UniProtKB/TrEMBL:A2R3C2" FT /citation=[32] FT /inference="profile:COGS:COG1643" FT /inference="profile:PFAM:PF00271" FT /inference="profile:PFAM:PF04408" FT /inference="similar to AA sequence:PIR:A56236" FT /protein_id="CAK46614.1" FT /translation="MDDLQSLELFSLVSRITSEIQNHLGVNDKTLAEFVIDQHLKCGSF FT ADFSKSMEEMGAEFPRSLLESIDRLVLTMHPKYKSKKMETTNTSAGDDDMDVLDALEKK FT ARVFKGLAVPDKVQQWDEEDVEEGDAKADAMDDTFAMLEGLAGKARQEKPAPALQSSSR FT NDRGSTRKRSRSPDYDDHRRGRRRHDRYRSRSRSHSPRYSRKGGDDEVDEFGRSKSKYS FT SRDDYRNGHSERKSRRDRDEDGEYFRKPPPVELDDQPVLYKVYDGRVTGVKDFGAFVNL FT LGVKGKVDGLVHVSAMQEGARVNHPSDLVSRGQPVKVKVVSIQGSRIGLSMKEVDQVTG FT LDLIPQRRLASGANMERLDGMTGKDRYGNLSSEVPVIEESDGKPMKNRKRMTSPERWEI FT KQLIASGAVSAADYPDIDEEYHATLTGEGTFEEEEDVDIEVRDEEPPFLAGQTKMSLEL FT SPIRVVKAPDGSMNRAAMAGTNLAKERRDIRQQEAQDKAAEQAAAVDLNAQWQDPMVAP FT EERKFAADLRSTQQSKPDDSVPEWKRVTMGKNQSFGKRTSMSIKQQRESLPVYKFRKQL FT LDAVRDNQLLIVVGDTGSGKTTQVTQYLAEGGYANNGIIGCTQPRRVAAMSVAKRVAEE FT VGCKLGAEVGYTIRFEDCTSPDTKIKYMTDGMLQREVLLDPDLKKYSVIMLDEAHERTI FT ATDVLFGLLKKTIKRRPDLRLIVTSATLDAEKFSEYFNGCPIFSIPGRTFPVEIMYSKE FT PESDYLDAALITVMQIHLTEPSGDILLFLTGQEEIDTACEILYERMKALGSTVPELVIL FT PVYSALPSEMQSRIFEPAPPGGRKVVIATNIAETSITIDNIYYVIDPGFVKQNAYDPKL FT GMDSLVVTPISQAQAKQRAGRAGRTGPGKCFRLYTEAAYQSEMLPTTIPEIQRQNLSHT FT ILMLKAMGINDLLHFDFMDPPPTNTMLTALEELYALSALDDEGLLTRLGRKMADFPMEP FT ALAKVLIASVDMGCSEEMLSIVAMLSIQSVFYRPKEKQQQADQKKAKFHDPHGDHLTLL FT NVYNGWKHSNFNNAWCFENFIQARQIRRAQDVRQQLLGIMDRYHHKIVSCGRNTLKVRQ FT ALCTGFFRNAARKDPQEGYKTLVEGTPVYMHPSSALFGKPSEHVIYHTLVLTTKEYMHC FT TTSIEPKWLVEAAPTFFKVAPTDRLSKRKKAERIQPLHNRFAGEDDWRLSAQRRQGRGG FT GGGTWG" FT mRNA complement(<231387..>235082) FT /locus_tag="An14g03770" FT CDS complement(join(235537..236521,236571..237514)) FT /locus_tag="An14g03780" FT /note="Function: the DExH box protein Suv3p from S. FT cerevisiaeis a component of a yeast mitochondrial 3'-to-5' FT exoribonuclease that suppresses group I intron toxicity." FT /note="Remark: synonyms for Suv3 from S. cerevisiae are FT Lpb2 and YPL029w." FT /note="Title: strong similarity to mitochondrial RNA FT helicase Suv3 - Saccharomyces cerevisiae" FT /note="localisation:mitochondrion" FT /db_xref="GOA:A2R3C3" FT /db_xref="InterPro:IPR001650" FT /db_xref="UniProtKB/TrEMBL:A2R3C3" FT /citation=[39] FT /citation=[4] FT /inference="profile:COGS:COG0513" FT /inference="profile:COGS:COG1197" FT /inference="profile:PFAM:PF00271" FT /inference="similar to AA sequence:UniProtKB:SCSUV3A.1" FT /protein_id="CAK46615.1" FT /translation="MLNACKMDERKSVGPLRHIKDALHRSYLQNGVRGLINELEFHMYA FT EDVTSRYSAPNLEAQKKVADLRRPAEWYPQARALQRTIHLHVGPTNSGKTYHALKRLEA FT SKRGFYAGPLRLLAQEVFHRFQANGTSCSLITGDDVKIPEDGKPSRIVSNTVEMVSLGD FT QYEVGVVDEIQMIADPHRGWAWTRAVLGARATELHLCGEVRAVPLIKELAALTGDKLEI FT HRYERLNPLKVQNRSLKGDLKNLQKGDCLVSFSRVGIHALKADIEKTTGKRAAIVYGSL FT PAEIRTQQASLFNDPDNDYDFLVASDAIGMGLNLSCKRIIFETLIKRVPGGLQRLSVPE FT IKQIGGRAGRYRSAAQQQENGSSSEDDTNVGYVTSLEDIDLPYIREAMESEPPPLVSAG FT ILPPDSVYQKVAAYFPSNVPLEYLIKRLMVVSQVHPLFFLCDPRNQLENAEVIDTVDGL FT RTADQLTFMASPMHTRLIAGRDAAIAFIQCVAEHSDGRLLDIQALNLEILEEPVSGNKE FT YLNELETLHKSVILYLWLSYRCGGVFTDRTLASHVKQLVEERMVRALTEFSANKKLRKD FT ASLRRQIALQKQIQEQKRLLADADVDSYGTEDETAAVDLSADEEQMEEQLQERPEESGE FT APQARAA" FT mRNA complement(join(<235537..236521,236571..>237514)) FT /locus_tag="An14g03780" FT exon complement(235537..236521) FT /locus_tag="An14g03780" FT /number=1 FT intron complement(236522..236570) FT /locus_tag="An14g03780" FT /number=1 FT exon complement(236571..237514) FT /locus_tag="An14g03780" FT /number=2 FT CDS join(238632..238665,238727..238764,238856..238943, FT 239004..239150,239201..239403,239450..239916, FT 239968..241078) FT /locus_tag="An14g03790" FT /note="Function: Microinjection of Sec1 from L. pealei into FT the presynaptic terminal of the giant synapse inhibited FT evoked neurotransmitter release, but this effect was FT prevented by coinjecting the cytoplasmic domain of L. FT pealei syntaxin, one of the binding partners of Sec1." FT /note="Remark: Sec1-related proteins are essential for FT membrane fusion at distinct stages of the constitutive and FT regulated secretory pathways in eukaryotic cells." FT /note="Title: strong similarity to sec1-like protein FT -Loligo pealei" FT /db_xref="GOA:A2R3C4" FT /db_xref="InterPro:IPR001619" FT /db_xref="UniProtKB/TrEMBL:A2R3C4" FT /citation=[61] FT /inference="profile:COGS:COG5158" FT /inference="profile:PFAM:PF00995" FT /inference="similar to AA sequence:UniProtKB:LPSEC1HOM.1" FT /protein_id="CAK46616.1" FT /translation="MSTSILNIQRDLILNTIRYAAGNEWKVLVVDETSRKLIDNAVSED FT DILNLNVTNVEQIEHRRSPNPTMDALYILSPLPHIVDCIMADFERKRYRKAWLVWTSFL FT DPEQRARLDRSQLARDQIANVQIMNADYFPRESRLITFRDPWSFPVLFHPGCNHLIRAH FT LEGLAQKIVSLCASLGEYPVIRYYRPRAPTHEASVLCSHLARFIQNELDQFAQFQRDFP FT PPSPRPRGVLLIVDRSMDLIAPLLHEFTYQSMVHDLLPISDGDKVTYKTVINEGSHNEE FT LKDMEINEEDNVWVEYRHMHMKDVLGKLGEDFAKFRAANPQFAEDNNKANVNTIKDMLA FT GLTEFQKGRDAYTLHLNMAQECMSYFQKHKLLEVSSVEQCFATGMDENYKKAKNLASQL FT VQLLDDDAIKQPERLRLLLLYIIYRGGILAGDIRKLLAHAQLAPQDGEIVANLDLLGAR FT VEKPLKDDKPPVQPLFTRKPPSGPIDEEESLSRYDLNLKLILEELVRGTLDPSVFPFTR FT PHTDTDTPGQQEGLSQASLRSAKPTWARTRSTGEQPKQRIIVFMAGGATYGEARTCYEI FT SQTCGKDVFLATSHMLSPGLFLRQVGDLSVDRRRLDIPAERPKPTAPAHLFEREAPPAP FT AQPVKKPVPVNLKPMAPTSALATMSLGTNGKAANGAAPPEKEKDKKEKKEKKEKKHRFF FT R" FT mRNA join(<238632..238665,238727..238764,238856..238943, FT 239004..239150,239201..239403,239450..239916, FT 239968..>241078) FT /locus_tag="An14g03790" FT exon 238632..238665 FT /locus_tag="An14g03790" FT /number=1 FT intron 238666..238726 FT /locus_tag="An14g03790" FT /number=1 FT exon 238727..238764 FT /locus_tag="An14g03790" FT /number=2 FT intron 238765..238855 FT /locus_tag="An14g03790" FT /number=2 FT exon 238856..238943 FT /locus_tag="An14g03790" FT /number=3 FT intron 238944..239003 FT /locus_tag="An14g03790" FT /number=3 FT exon 239004..239150 FT /locus_tag="An14g03790" FT /number=4 FT intron 239151..239200 FT /locus_tag="An14g03790" FT /number=4 FT exon 239201..239403 FT /locus_tag="An14g03790" FT /number=5 FT intron 239404..239449 FT /locus_tag="An14g03790" FT /number=5 FT exon 239450..239916 FT /locus_tag="An14g03790" FT /number=6 FT intron 239917..239967 FT /locus_tag="An14g03790" FT /number=6 FT exon 239968..241078 FT /locus_tag="An14g03790" FT /number=7 FT exon complement(241279..242097) FT /locus_tag="An14g03800" FT /number=1 FT CDS complement(241279..242097) FT /locus_tag="An14g03800" FT /note="Title: weak similarity to sexual differentiation FT protein esc1p - Schizosaccharomyces pombe" FT /db_xref="GOA:A2R3C5" FT /db_xref="InterPro:IPR000467" FT /db_xref="UniProtKB/TrEMBL:A2R3C5" FT /inference="profile:PFAM:PF01585" FT /protein_id="CAK46617.1" FT /translation="MPPPHQNNNNEENNNNNDDDDEYFLPLEDQRVFGAGIRRKRVPFV FT RSSEHHLSTTDSTTHISSEPATPASTGQSIANKYLSIVLSKSNPATPTPESEPSSHPQK FT DDADDDDICPVCNLPYTTPTHHTSDTTTDNGEGEERSRRRRHIHEATLPHQLSLPHSHP FT PSHLDRTRPGLRYLAAYGWDPDSRVGLGPQGREGIREPVKGKLKEDTVGLGAVVPEVKD FT KSGRVQKKQKAKVLNAKEVRRGQLEERKKGERLRELFFRDEDVLRYLGGK" FT mRNA complement(<241279..>242097) FT /locus_tag="An14g03800" FT CDS join(242347..242523,242595..243053,243147..243740) FT /locus_tag="An14g03810" FT /note="Similarity: the protein shows weaker similarity to a FT human patented sequence (patent number EP1067182-A2) and a FT number of hypothetical proteins, some of which annotated as FT oxidoreductases with various specificity; the predicted FT protein indeed contains structural features common to FT short-chain alcohol dehydrogenases." FT /note="Title: strong similarity to hypothetical protein FT SPAC19A8.06 - Schizosaccharomyces pombe" FT /db_xref="GOA:A2R3C6" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2R3C6" FT /inference="profile:COGS:COG1028" FT /inference="similar to AA sequence:PIR:T37955" FT /protein_id="CAK46618.1" FT /translation="MPIPIITTAITEGTNSIPHLWTVLKILPWAVLLAALKYYFGGARN FT TSERLMHSKVVMITGGTSGIGAQVTSALASRGAQIILLTQHPPTDIFLAEYIEDLRRST FT NNQLIYAEQVDLSSLHSIRTFATKWIDNVAPRRLDMVILCGNAAPPVSQKRKLTVDGID FT EEWMVNYLANFHLLSILSPALRAQPAHRDVRVVFTTCSSYIGAKWDLRQLQREKPKNKK FT KKTKGVSLYGLSKLSLMVFAQSFQKHLNSFKRPDGQPCSARVIMVDPGFSRTPGMRRWM FT TGGSLWGLLVYLVTWPVWWLVLKSPQQGAQSVLYAAMEAEYGRGEGGWMIKECKEVDLA FT RKEVKDEEAGKMLWEFSEKLIEAKERESAVRRALANKEKEVAEENEKNKASGSGAKEQT FT PGSRRSRKGK" FT mRNA join(<242347..242523,242595..243053,243147..>243740) FT /locus_tag="An14g03810" FT exon 242347..242523 FT /locus_tag="An14g03810" FT /number=1 FT intron 242524..242594 FT /locus_tag="An14g03810" FT /number=1 FT exon 242595..243053 FT /locus_tag="An14g03810" FT /number=2 FT intron 243054..243146 FT /locus_tag="An14g03810" FT /number=2 FT exon 243147..243740 FT /locus_tag="An14g03810" FT /number=3 FT CDS complement(join(244025..244419,244478..244934, FT 245035..245269,245338..245366)) FT /locus_tag="An14g03820" FT /EC_number="5.1.3.2" FT /note="Function: GAL10 of S. cerevisiae converts FT UDP-glucose to UDP-galactose, being involved in the FT galactose metabolism pathway." FT /note="Similarity: the predicted protein shows a very FT strong similarity to the N-terminal half of GAL10 of S. FT cerevisiae; the C-terminal half of the yeast gene is FT missing from the predicted protein." FT /note="Title: strong similarity to UDP-glucose 4-epimerase FT Gal10 - Saccharomyces cerevisiae" FT /note="cytoplasm" FT /db_xref="GOA:A2R3C7" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2R3C7" FT /citation=[22] FT /inference="profile:COGS:COG1087" FT /inference="profile:PFAM:PF01370" FT /inference="similar to AA sequence:PIR:XEBYUG" FT /protein_id="CAK46619.1" FT /translation="MPAGSVLVTGGTGYIGSFTTLALLEAGYKVVVADNLYNSSAEALK FT RIELISGKKAEFAQLDVTDEAGFDRVFEAHPDIDSVIHFAALKAVGESGEKPLDYYHVN FT VYGTICLLRSMVRHNVTNIVFSSSATVYGDATRFPNMIPIPEECPLGPTNPYGNTKFAV FT ETAITDVINAQRNNAIKAGNEAEAQKWNGALLRYFNPAGAHPSGIMGEDPQGVPYNLLP FT LLAQVATGKREKLLVFGDDYASHDGTAIRDYIHILDLADGHLKALNYLRANNPGVRAWN FT LGTGKGSTVYEMIRAFSAAVGRDLPYEVAPRRAGDVLNLTSNPTRANNELGWKAERTLE FT QACEDLWLWTRNNPQGYRQQPPAELLEKLQK" FT mRNA complement(join(<244025..244419,244478..244934, FT 245035..245269,245338..>245366)) FT /locus_tag="An14g03820" FT exon complement(244025..244419) FT /locus_tag="An14g03820" FT /number=1 FT intron complement(244420..244477) FT /locus_tag="An14g03820" FT /number=1 FT exon complement(244478..244934) FT /locus_tag="An14g03820" FT /number=2 FT intron complement(244935..245034) FT /locus_tag="An14g03820" FT /number=2 FT exon complement(245035..245269) FT /locus_tag="An14g03820" FT /number=3 FT intron complement(245270..245337) FT /locus_tag="An14g03820" FT /number=3 FT exon complement(245338..245366) FT /locus_tag="An14g03820" FT /number=4 FT CDS join(246046..246057,246221..246309,246396..246529, FT 246704..246755,247045..247120) FT /locus_tag="An14g03830" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3C8" FT /protein_id="CAK46620.1" FT /translation="MCMSYLLGLNCTTTTTTYYLFAYLFPASYKVPYPSRSRYHQFGRV FT QDTHLEAKVPTPRLSSKCEVDRFHPIPRVQSIVESAGDDDGDDQGDEGLSMQAICPQRG FT LPVRIIPHCREKALSK" FT mRNA join(<246046..246057,246221..246309,246396..246529, FT 246704..246755,247045..>247120) FT /locus_tag="An14g03830" FT exon 246046..246057 FT /locus_tag="An14g03830" FT /number=1 FT intron 246058..246220 FT /locus_tag="An14g03830" FT /number=1 FT exon 246221..246309 FT /locus_tag="An14g03830" FT /number=2 FT intron 246310..246395 FT /locus_tag="An14g03830" FT /number=2 FT exon 246396..246529 FT /locus_tag="An14g03830" FT /number=3 FT intron 246530..246703 FT /locus_tag="An14g03830" FT /number=3 FT exon 246704..246755 FT /locus_tag="An14g03830" FT /number=4 FT intron 246756..247044 FT /locus_tag="An14g03830" FT /number=4 FT exon 247045..247120 FT /locus_tag="An14g03830" FT /number=5 FT tRNA 247178..247269 FT /gene="tRNA-Gln (TTG)" FT /locus_tag="An14e03840" FT /product="transfer RNA-Gln (TTG)" FT /inference="profile:tRNAscan:1.4" FT CDS complement(join(247626..247678,247815..247897, FT 247947..248113,248172..248282,248337..249187, FT 249239..249449)) FT /locus_tag="An14g03850" FT /EC_number="1.14.-.-" FT /note="Function: TRI4 gene of Fusarium sporotrichioides FT encodes a cytochrome P450 monooxygenase involved in FT trichothecene biosynthesis." FT /note="Phenotype: disruption of TRI4 results in the loss of FT production of both trichothecenes and apotrichodiol and the FT accumulation of the unoxygenated pathway intermediate FT trichodiene." FT /note="Remark: trichothecenes are sesquiterpenoid toxins FT that act by inhibiting protein biosynthesis." FT /note="Similarity: the TRI4 gene has been placed in a new FT cytochrome P450 gene family designated CY P58." FT /note="Title: strong similarity to cytochrome P450 FT monooxygenase TRI4 - Fusarium sporotrichioides" FT /db_xref="GOA:A2R3C9" FT /db_xref="InterPro:IPR017973" FT /db_xref="UniProtKB/TrEMBL:A2R3C9" FT /citation=[26] FT /inference="profile:COGS:COG2124" FT /inference="profile:PFAM:PF00067" FT /inference="similar to AA sequence:UniProtKB:AF359360.10" FT /protein_id="CAK46621.1" FT /translation="MALDTSHIWLALVGIASFYVLRSIYRLYFHPLSGIPGPKLAAVTH FT LYEFYYDVVIHGRFLFQIEKMHQQYGPIVRINPREVHISDPSFYDEIYASSTRKRERDP FT LAYGAFALPYSMIGTMGHEHHRFRRNILNDFFSKRSVLAISPFIEERVEKLRGRFEGFY FT RDQSVVNLSDAFAALTSDVITYYCYGKRWGFIEDKDFRSDVHGGNEENTGLAHFNRFFP FT IVPETMRKIPLHLMALCLPGKAGMLQFQGSILSTISENTHDKASEKEDRTIFKRLTDPN FT LPVAERSQRRIEDEVFTLLGAGTETTASTLMIMTYYVSRDRSIRDKLRSELKQVLPTPT FT STATWPELEKLPYLTAVVNESLRLSYGLIMRLPRVAPTETLKYKDYVLPPGTPMSTSTW FT FVHRDPSLFPEPDRFDPERWIKAAEEGVNLTRYIVSFMRGSRACIGMNLAYIELYLTIA FT HVVRRFNFDVEITSPEIWAILLVLATTIQSYQA" FT mRNA complement(join(<247626..247678,247815..247897, FT 247947..248113,248172..248282,248337..249187, FT 249239..>249449)) FT /locus_tag="An14g03850" FT exon complement(247626..247678) FT /locus_tag="An14g03850" FT /number=1 FT intron complement(247679..247814) FT /locus_tag="An14g03850" FT /number=1 FT exon complement(247815..247897) FT /locus_tag="An14g03850" FT /number=2 FT intron complement(247898..247946) FT /locus_tag="An14g03850" FT /number=2 FT exon complement(247947..248113) FT /locus_tag="An14g03850" FT /number=3 FT intron complement(248114..248171) FT /locus_tag="An14g03850" FT /number=3 FT exon complement(248172..248282) FT /locus_tag="An14g03850" FT /number=4 FT intron complement(248283..248336) FT /locus_tag="An14g03850" FT /number=4 FT exon complement(248337..249187) FT /locus_tag="An14g03850" FT /number=5 FT intron complement(249188..249238) FT /locus_tag="An14g03850" FT /number=5 FT exon complement(249239..249449) FT /locus_tag="An14g03850" FT /number=6 FT CDS join(249599..249648,249742..249856,249924..250024, FT 250070..250217,250309..250350) FT /locus_tag="An14g03860" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3D0" FT /protein_id="CAK46622.1" FT /translation="MAEEGNGKRSNWLTNYCLEQDGDALARRNPAYHCRRDIVVAFGGK FT NDTSILRIRHGFLFTPNWCAKSEVAKGQQLLVDTKSAGSQALMLLMELPMQALSPSEAT FT TLGWPAENTGVWHESCSQQVISLLTGLRIRQIRAAKAGKMLDCCLGI" FT mRNA join(<249599..249648,249742..249856,249924..250024, FT 250070..250217,250309..>250350) FT /locus_tag="An14g03860" FT exon 249599..249648 FT /locus_tag="An14g03860" FT /number=1 FT intron 249649..249741 FT /locus_tag="An14g03860" FT /number=1 FT exon 249742..249856 FT /locus_tag="An14g03860" FT /number=2 FT intron 249857..249923 FT /locus_tag="An14g03860" FT /number=2 FT exon 249924..250024 FT /locus_tag="An14g03860" FT /number=3 FT intron 250025..250069 FT /locus_tag="An14g03860" FT /number=3 FT exon 250070..250217 FT /locus_tag="An14g03860" FT /number=4 FT intron 250218..250308 FT /locus_tag="An14g03860" FT /number=4 FT exon 250309..250350 FT /locus_tag="An14g03860" FT /number=5 FT CDS complement(join(250523..251169,251248..252136)) FT /locus_tag="An14g03870" FT /EC_number="1.14.-.-" FT /note="Function: AvnA is involved in the conversion of FT averantin to averufin in aflatoxin biosynthesis in FT Aspergillus parasiticus." FT /note="Remark: Aflatoxins are toxic and carcinogenic FT secondary metabolites produced by the fungi Aspergillus FT flavus and A. parasiticus." FT /note="Remark: as other polyketides, aflatoxins are FT synthesized by condensation of acetate units." FT /note="Similarity: The avnA gene encodes a cytochrome FT P-450-type monooxygenase that has been assigned to a new FT P-450 gene family named CYP60A1." FT /note="Title: strong similarity to cytochrome P450 FT monooxygenase avnA - Aspergillus parasiticus" FT /db_xref="GOA:A2R3D1" FT /db_xref="InterPro:IPR017973" FT /db_xref="UniProtKB/TrEMBL:A2R3D1" FT /citation=[28] FT /citation=[52] FT /inference="profile:COGS:COG2124" FT /inference="profile:PFAM:PF00067" FT /protein_id="CAK46623.1" FT /translation="MDLLGCVVIAVAGYIIYQVWFHPLSSYPGPFVAKLTNLYSVVHAI FT RGDRHEDLYHLHQRYGPVVRVGPRRVSILDAKALEPIYGFHANVQKAKSYNIFYGVSIF FT NAIDRTVHARKRRVMSHAFSSQALRGMEPHILSAIRDWCAALGDQHPDKQVLSACSRPG FT SWSRPKNMVHWSACVVFDALGEICFGKTFNTSFSDANHFFFPLMALNLRIMNICGQMPI FT LCSLGLERYLRRGTVANRQRQIDFSRQQLQTRLAAESTQRRDIIFYLQQARDPKTNEGY FT SEAELMSEVMTLLGAGNDTTNTTLTAIFYYLAHNPAILARLSAEIRAVFPTLEAIVAGP FT DLSQMAYLHACIDETMRVCPPVPTDLPREVLPGGLRVGEWYFPAGTVVAVPTYALHHSE FT DHFYRAFVYDPSRWLLCGSKGTEQGEGVSAEVLSRQRQAFAPFSMGPRACIGRNVAILE FT LELTISRALWLYDIRLAPGTEQLGVGYQGEYKIKDHFAVGKEGPVLQFRMRQK" FT mRNA complement(join(<250523..251169,251248..>252136)) FT /locus_tag="An14g03870" FT exon complement(250523..251169) FT /locus_tag="An14g03870" FT /number=1 FT mat_peptide complement(join(250526..251169,251248..252073)) FT /locus_tag="An14g03870" FT intron complement(251170..251247) FT /locus_tag="An14g03870" FT /number=1 FT exon complement(251248..252136) FT /locus_tag="An14g03870" FT /number=2 FT sig_peptide complement(252074..252136) FT /locus_tag="An14g03870" FT /inference="protein motif:SignalP:2.0" FT CDS complement(join(252645..252739,252821..252866, FT 252905..252970,253079..253214,253262..253557)) FT /locus_tag="An14g03880" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3D2" FT /protein_id="CAK46624.1" FT /translation="MSSCVLFNPISFILEYSVGSRGFCMDQPSSLALQCGGTPIISHLF FT IFHSPAIPRSILNHSLSSLSANTFQEDISTSFSKSIQAWLDAIQFGCITITQITFGILV FT SLCGSSHMPDFLCRHASIRTLKVPSAPPRASSLGLRNDQQALRVQQVLTIIDISVVEAE FT GTDTNAQIIDLQRGLFIAAPTVLMQGYMFPNASTCDALQHYPCKVGNCD" FT mRNA complement(join(<252645..252739,252821..252866, FT 252905..252970,253079..253214,253262..>253557)) FT /locus_tag="An14g03880" FT exon complement(252645..252739) FT /locus_tag="An14g03880" FT /number=1 FT intron complement(252740..252820) FT /locus_tag="An14g03880" FT /number=1 FT exon complement(252821..252866) FT /locus_tag="An14g03880" FT /number=2 FT intron complement(252867..252904) FT /locus_tag="An14g03880" FT /number=2 FT exon complement(252905..252970) FT /locus_tag="An14g03880" FT /number=3 FT intron complement(252971..253078) FT /locus_tag="An14g03880" FT /number=3 FT exon complement(253079..253214) FT /locus_tag="An14g03880" FT /number=4 FT intron complement(253215..253261) FT /locus_tag="An14g03880" FT /number=4 FT exon complement(253262..253557) FT /locus_tag="An14g03880" FT /number=5 FT CDS complement(join(253990..254083,254169..255870, FT 255925..256409,256500..256648)) FT /locus_tag="An14g03890" FT /note="Complex: PAT1 of S. cerevisiae interacts with the FT Lsm decapping complex." FT /note="Function: PAT1 of S. cerevisiae is involved in mRNA FT decapping and degradation, as well as for faithful FT chromosome transmission during mitosis and meiosis." FT /note="Similarity: the alignment of the predicted protein FT to PAT1 of S. cerevisiae has several gaps; a better FT alignment is obtained to the putative S. pombe homologue of FT S. cerevisiae PAT1." FT /note="Title: similarity to topoisomerase II-associated FT protein Pat1 - Saccharomyces cerevisiae" FT /note="cytoplasm" FT /db_xref="InterPro:IPR019167" FT /db_xref="UniProtKB/TrEMBL:A2R3D3" FT /citation=[42] FT /citation=[45] FT /citation=[50] FT /citation=[72] FT /citation=[81] FT /inference="similar to AA sequence:UniProtKB:SCCHRIII.148" FT /protein_id="CAK46625.1" FT /translation="MSFFGFNTTLPRDRAPAGEQRGIFDTPDPFAEVARARLAANFQSG FT EDDDVIDFEDTYDGLGDQLDDDQDAFNDDTFGGGFDTGPVGKDFDFFGKTAQVADVIGE FT EQIRYSLQKPGAPATAPSQPSADTALPDTTAQKPKRSGYEKYNDPGYIPDLQAKSSVWG FT MSKKPEQQLQQQQLQQQLQQLQQPTPQMVAQAKKMLSLEEVEAQLRRQEPTQPLQRAQM FT PPLPEGFPQLPPEILQAQFAKGVPPAQLLHQPPMVPEPYPLPPNLPIHMLQNANLPPQH FT MVPPQRQAMPPAAQRPQQQQPPLPQAPRGNNAQLPVITNSQQLMHLTEEQRVAYLMEDA FT KRAKRNHKIFLLSRGNGLMTPQDKNFITRIQLQQLVAAAGNVADSDAEAVLAEDFYYQV FT YSQIRGAPRQHPHQPLGHFAQTYLLQTGNRLGGHGSRRQFQSADNHMQRMQQQVQRAVE FT AAKQKPKNKQLIIEGSLGKISFSNAKTPKPMLNIKRPESSEGAKTVKKPHTDLSVSDRK FT SVLTNLESVYSTLMDMEDMERTMPPPPDENDPEAIQKHMEWRQKIRSLNQKLWRDLKVM FT EPIVPNTNTPHPFIAFLAYPKGKKAIPRIFRHIDQEQRVTILTMIVVHLDSLDVVRRAQ FT PVPGETQPSLAVREAIELFSQAVMPSLLGYVNEAPFNIIIGLLGLVIAQTHVQMIARTR FT IGLGILTMLLSRAEIVKEAGQATERDWQQWVEKFNVLFDTLEPTFADIFPSSINAGDDM FT YVWQFLAAVGIGASPEQQQRLVIAVNKTLPADMASARLGNVNLFMRAIGLDVELLG" FT mRNA complement(join(<253990..254083,254169..255870, FT 255925..256409,256500..>256648)) FT /locus_tag="An14g03890" FT exon complement(253990..254083) FT /locus_tag="An14g03890" FT /number=1 FT intron complement(254084..254168) FT /locus_tag="An14g03890" FT /number=1 FT exon complement(254169..255870) FT /locus_tag="An14g03890" FT /number=2 FT intron complement(255871..255924) FT /locus_tag="An14g03890" FT /number=2 FT exon complement(255925..256409) FT /locus_tag="An14g03890" FT /number=3 FT intron complement(256410..256499) FT /locus_tag="An14g03890" FT /number=3 FT exon complement(256500..256648) FT /locus_tag="An14g03890" FT /number=4 FT CDS complement(join(257085..257207,257296..257371, FT 257478..257690,257744..257757)) FT /locus_tag="An14g03900" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3D4" FT /protein_id="CAK46626.1" FT /translation="MRIRMNSEKWGLSINAGYDRPGEKCASQVFLEINLWAIGNDNADD FT GPAAHQAKIKVSWQFGALVVDPDHGARAPQPLAYSPRYGEGDVISPVIGRATYVALGGV FT YTENDVKEGTRSMLECISPSGRASIHPALGLGATYSP" FT mRNA complement(join(<257085..257207,257296..257371, FT 257478..257690,257744..>257757)) FT /locus_tag="An14g03900" FT exon complement(257085..257207) FT /locus_tag="An14g03900" FT /number=1 FT intron complement(257208..257295) FT /locus_tag="An14g03900" FT /number=1 FT exon complement(257296..257371) FT /locus_tag="An14g03900" FT /number=2 FT intron complement(257372..257477) FT /locus_tag="An14g03900" FT /number=2 FT exon complement(257478..257690) FT /locus_tag="An14g03900" FT /number=3 FT intron complement(257691..257743) FT /locus_tag="An14g03900" FT /number=3 FT exon complement(257744..257757) FT /locus_tag="An14g03900" FT /number=4 FT CDS join(257881..257922,257976..258758,258810..259098, FT 259149..259213) FT /locus_tag="An14g03910" FT /EC_number="2.4.1.131" FT /note="Function: kre2 of C. albicans is involved in the FT synthesis of mannoproteins, the third major class of FT macromolecule found in the cell wall." FT /note="Function: kre2 of C. albicans transfers an FT alpha-D-mannosyl residue from GDP-mannose into lipid-linked FT oligosaccharide, forming an alpha-1,2-D-mannosyl-D-mannose FT linkage." FT /note="Golgi" FT /note="Phenotype: both heterozygous and homozygous kre2 FT null mutants of C. albicans showed strong attenuation of FT virulence in guinea pig and mouse models of systemic FT candidosis, which, in guinea pigs, could be attributed to a FT decreased ability to reach and/or adhere internal organs." FT /note="Phenotype: the absence of kre2 in C. albicans FT reduced the ability of C. albicans cells to adhere to each FT other, to human buccal epithelial cells, and to rat vaginal FT epithelial cells." FT /note="Remark: kre2 of C. albicans is also called mnt1." FT /note="Title: strong similarity to FT alpha-1,2-mannosyltransferase kre2 - Candida albicans" FT /db_xref="GOA:A2R3D5" FT /db_xref="InterPro:IPR002685" FT /db_xref="UniProtKB/TrEMBL:A2R3D5" FT /inference="profile:COGS:COG5020" FT /inference="profile:PFAM:PF01793" FT /inference="similar to AA sequence:SWISSPROT:KRE2.CANAL" FT /protein_id="CAK46627.1" FT /translation="MAIGPLRYLLFAITGLAIFFFISRSAIPIPENIGTKLTPATYKDT FT FSSSHSSQNDALSSSGPIKDIPTDRVNATFVTLARNTDLWEMVKSIRTVEDRFNHNYHY FT DWVFLNDKPFDEEFKKVTSALISGNTHYGVIPKEHWSYPEWIDQDKAKKVRQEMGEKKI FT IYGDSESYRHMCRYESGFFFRHPLMLNYEYYWRVEPSIELFCDVSFDPFRYVKENDKKY FT SFVLSLYEYYDTIPSLWGTVQKFMEEHPEHIADGNSMGFLSDDGGKTYNKCHFWSNFEI FT GSLEWLRSKEYIDYFETLDHAGGFFYERWGDAPVHSIAAGLLLKKEQIHFFNEIGYYHV FT PFTHCPTGEQLRLDLKCHCNPKDNFDWKGYSCTSRFFQVNDMDKPKGYENES" FT mRNA join(<257881..257922,257976..258758,258810..259098, FT 259149..>259213) FT /locus_tag="An14g03910" FT sig_peptide join(257881..257922,257976..258008) FT /locus_tag="An14g03910" FT /inference="protein motif:SignalP:2.0" FT exon 257881..257922 FT /locus_tag="An14g03910" FT /number=1 FT intron 257923..257975 FT /locus_tag="An14g03910" FT /number=1 FT exon 257976..258758 FT /locus_tag="An14g03910" FT /number=2 FT mat_peptide join(258009..258758,258810..259098,259149..259210) FT /locus_tag="An14g03910" FT intron 258759..258809 FT /locus_tag="An14g03910" FT /number=2 FT exon 258810..259098 FT /locus_tag="An14g03910" FT /number=3 FT intron 259099..259148 FT /locus_tag="An14g03910" FT /number=3 FT exon 259149..259213 FT /locus_tag="An14g03910" FT /number=4 FT CDS complement(join(259799..259864,259929..260029, FT 260155..260608)) FT /locus_tag="An14g03920" FT /note="Similarity: the predicted ORF is 60 amino acids FT longer at its N-terminus than other S12 proteins." FT /note="Title: strong similarity to ribosomal protein of the FT small subunit Rps12 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R3D6" FT /db_xref="InterPro:IPR012340" FT /db_xref="UniProtKB/TrEMBL:A2R3D6" FT /citation=[88] FT /inference="profile:COGS:COG0048" FT /inference="profile:PFAM:PF00164" FT /inference="similar to AA sequence:PIR:S63367" FT /protein_id="CAK46628.1" FT /translation="MAPLVSSLALRTLRTLVQRPAAIKSTSCSITTLAAAAPRRPFQPV FT LRTPTAVAAAAAARKTSIPSSSSSILRQFSTSPFRQATYNQVRRGCRVAQRARRSRSPA FT LIGRSQMKGVCLKTGITKPKKPNSGERKTARVRLSSGKVVTAYIPGEGHNIQQHSVVMV FT RGGRVPDCPGVKYHLVRGAMDLGGVASRLNSRSKYGTKKPKKD" FT mRNA complement(join(<259799..259864,259929..260029, FT 260155..>260608)) FT /locus_tag="An14g03920" FT exon complement(259799..259864) FT /locus_tag="An14g03920" FT /number=1 FT mat_peptide complement(join(259802..259864,259929..260029, FT 260155..260500)) FT /locus_tag="An14g03920" FT intron complement(259865..259928) FT /locus_tag="An14g03920" FT /number=1 FT exon complement(259929..260029) FT /locus_tag="An14g03920" FT /number=2 FT intron complement(260030..260154) FT /locus_tag="An14g03920" FT /number=2 FT exon complement(260155..260608) FT /locus_tag="An14g03920" FT /number=3 FT sig_peptide complement(260501..260608) FT /locus_tag="An14g03920" FT /inference="protein motif:SignalP:2.0" FT CDS join(261013..261015,261102..261537,261630..261697) FT /locus_tag="An14g03930" FT /note="Function: the S. cerevisiae Ump1p is a chaperone and FT component of proteasome precursor complexes containing FT unprocessed beta subunits but is not detected in the mature FT 20S proteasome." FT /note="Induction: the propeptide of the Pre2p/Doa3p beta FT subunit is required for ump1p's function in proteasome FT maturation." FT /note="Induction: transcript levels of mammalian ump1 are FT increased after IFN-gamma treatment." FT /note="Phenotype: S. cerevisiae cells lacking ump1 exhibit FT a lack of coordination between the processing of beta FT subunits and proteasome assembly, resulting in functionally FT impaired proteasomes." FT /note="Remark: UMP1 of S. cerevisiae is also called YBR173C FT or YBR12." FT /note="Title: strong similarity to proteasome 20S FT maturation factor Ump1 - Saccharomyces cerevisiae" FT /db_xref="InterPro:IPR008012" FT /db_xref="UniProtKB/TrEMBL:A2R3D7" FT /citation=[60] FT /citation=[79] FT /citation=[85] FT /inference="profile:PFAM:PF05348" FT /inference="similar to AA sequence:PIR:S46044" FT /protein_id="CAK46629.1" FT /translation="MSLRIAPPSSNPTQTTNTTTRAVIDLPHPSKGAPSAPGLPDTLRD FT NITLPAPRGPPSTATATPSSTHPLEARLLAWRATQDALKMESLRRAYGIAEPVRRGMEL FT KIVRDGTFRPAALGGLGMGNLHEDILVLGGRDAEVGWEDVFKGDEFREPPAFHDEMEKR FT LRMDH" FT mRNA join(<261013..261015,261102..261537,261630..>261697) FT /locus_tag="An14g03930" FT exon 261013..261015 FT /locus_tag="An14g03930" FT /number=1 FT intron 261016..261101 FT /locus_tag="An14g03930" FT /number=1 FT exon 261102..261537 FT /locus_tag="An14g03930" FT /number=2 FT intron 261538..261629 FT /locus_tag="An14g03930" FT /number=2 FT exon 261630..261697 FT /locus_tag="An14g03930" FT /number=3 FT CDS join(262070..262177,262258..262385,262460..262610) FT /locus_tag="An14g03940" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3D8" FT /protein_id="CAK46630.1" FT /translation="MAGQIGRGPPGSSVSTANWSVQALTQQKHSRTAKDHGSGRASENM FT SLGYIRNKRKRSSIKQLMELCKPNGDHVVEQTTGQPHAMPCSKKANKREGGPKPTRTQQ FT REATRLHRGLKETRVDESSSSTSK" FT mRNA join(<262070..262177,262258..262385,262460..>262610) FT /locus_tag="An14g03940" FT exon 262070..262177 FT /locus_tag="An14g03940" FT /number=1 FT intron 262178..262257 FT /locus_tag="An14g03940" FT /number=1 FT exon 262258..262385 FT /locus_tag="An14g03940" FT /number=2 FT intron 262386..262459 FT /locus_tag="An14g03940" FT /number=2 FT exon 262460..262610 FT /locus_tag="An14g03940" FT /number=3 FT CDS complement(join(262741..262895,262952..263035, FT 263100..263622)) FT /locus_tag="An14g03950" FT /note="Title: strong similarity to hypothetical protein FT EAA60774.1 - Aspergillus nidulans" FT /db_xref="UniProtKB/TrEMBL:A2R3D9" FT /protein_id="CAK46631.1" FT /translation="MSVTEDAKVDPMSPTSDPNLTSQSTTIAVPSSESQELPSAAPHPD FT NAQAESQEPSSVDAKPTENNEDNTSAPVLKQDPVDAAPSASASPQQHDEAKAPAAGSEP FT SSQGSDEAAKEEEDTGPSLVITLLLITGSRHPFKIDGKYLRKRSVNVENYDPFAMSVYT FT LKELIWREWRQDWEPRPSSPSSIRLISFGKLLDDKAPLSDSKFSRDAPNVVHMTVKPQE FT IVDEEDAKSKPQYTRERESSERSPGCRCIIQ" FT mRNA complement(join(<262741..262895,262952..263035, FT 263100..>263622)) FT /locus_tag="An14g03950" FT exon complement(262741..262895) FT /locus_tag="An14g03950" FT /number=1 FT intron complement(262896..262951) FT /locus_tag="An14g03950" FT /number=1 FT exon complement(262952..263035) FT /locus_tag="An14g03950" FT /number=2 FT intron complement(263036..263099) FT /locus_tag="An14g03950" FT /number=2 FT exon complement(263100..263622) FT /locus_tag="An14g03950" FT /number=3 FT CDS join(263730..263793,263837..263897,263979..264026, FT 264080..264155,264290..264415,264555..264662) FT /locus_tag="An14g03960" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3E0" FT /protein_id="CAK46632.1" FT /translation="MDRSEFSVGDSCNRYGSLTGEGADEARRCAHGGGKGGQAERGGPC FT DPKETSESEKGTAGGGEGMRVVKRIEYPVCKAERETKKGKGERERERDRVLKRGRRRSK FT PVTAEGSPDLVGGSPGRHLGSASAVCLNGRNEHQFPRAAEASVAADPGRFRTYLRH" FT mRNA join(<263730..263793,263837..263897,263979..264026, FT 264080..264155,264290..264415,264555..>264662) FT /locus_tag="An14g03960" FT exon 263730..263793 FT /locus_tag="An14g03960" FT /number=1 FT intron 263794..263836 FT /locus_tag="An14g03960" FT /number=1 FT exon 263837..263897 FT /locus_tag="An14g03960" FT /number=2 FT intron 263898..263978 FT /locus_tag="An14g03960" FT /number=2 FT exon 263979..264026 FT /locus_tag="An14g03960" FT /number=3 FT intron 264027..264079 FT /locus_tag="An14g03960" FT /number=3 FT exon 264080..264155 FT /locus_tag="An14g03960" FT /number=4 FT intron 264156..264289 FT /locus_tag="An14g03960" FT /number=4 FT exon 264290..264415 FT /locus_tag="An14g03960" FT /number=5 FT intron 264416..264554 FT /locus_tag="An14g03960" FT /number=5 FT exon 264555..264662 FT /locus_tag="An14g03960" FT /number=6 FT CDS join(266799..266937,267031..267126,267257..267348, FT 267415..267519) FT /locus_tag="An14g03970" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3E1" FT /protein_id="CAK46633.1" FT /translation="MANLDTGIELFTTVGAEYDIENCEPRIFGPDKAWQFRILYLCNDD FT AVLYNPVTVLQYLRALKTHSQYKGIRRKCIGLVGICRVIQGSAVKRWCSSPMAMEVGYR FT GPLRGAIGPTNAMCCFEKGFRPLDRTGIFELAFTVEKEI" FT mRNA join(<266799..266937,267031..267126,267257..267348, FT 267415..>267519) FT /locus_tag="An14g03970" FT exon 266799..266937 FT /locus_tag="An14g03970" FT /number=1 FT intron 266938..267030 FT /locus_tag="An14g03970" FT /number=1 FT exon 267031..267126 FT /locus_tag="An14g03970" FT /number=2 FT intron 267127..267256 FT /locus_tag="An14g03970" FT /number=2 FT exon 267257..267348 FT /locus_tag="An14g03970" FT /number=3 FT intron 267349..267414 FT /locus_tag="An14g03970" FT /number=3 FT exon 267415..267519 FT /locus_tag="An14g03970" FT /number=4 FT CDS join(269000..269237,269304..270220,270295..270462) FT /locus_tag="An14g03980" FT /note="Title: strong similarity to hypothetical 57.9 kd FT protein - Schizosaccharomyces pombe" FT /db_xref="InterPro:IPR011021" FT /db_xref="UniProtKB/TrEMBL:A2R3E2" FT /inference="similar to AA sequence:PIR:T40107" FT /protein_id="CAK46634.1" FT /translation="MLRQSFSIAKKATRKLYAHDDSSDLSLDLNITEPAVFVPTFTNKP FT AVLRGTCQLRLKHDLTVKRLTVNFRGTSRVTWPHGLHDTQTVTDSTLTLVSPQSSDPAL FT PCYSSALSEGRKSTWHKDKRKLQNAAPSTLCVDGNWGKAAGSKYQRLPAGTHTYEFEMV FT LHSHLPESIEIRQSHVQYRVRACVECPGFLRRSFAKKQAIATVHCPAEDDVEDAEPAYI FT ARAWKGLLQCGILVSRRGAPLGDRLPVTVSLTELRKAEFRGLQVFLSENVQYHQKDGLA FT CCPGPFRRVILYEKVEMTGPTMSLHRAENVDDERPVSATKGDGAHAKLVGDPEIPNGLE FT TAEEETVLNLTLQLPGCHLHCVSTGTQGMHYDTNYKNVRVSHWLEFVFMVTPRDNTLGS FT STERIVQKVAKVPLTLRSCYAQHANASLPAYCDAEEFRFGR" FT mRNA join(<269000..269237,269304..270220,270295..>270462) FT /locus_tag="An14g03980" FT exon 269000..269237 FT /locus_tag="An14g03980" FT /number=1 FT intron 269238..269303 FT /locus_tag="An14g03980" FT /number=1 FT exon 269304..270220 FT /locus_tag="An14g03980" FT /number=2 FT intron 270221..270294 FT /locus_tag="An14g03980" FT /number=2 FT exon 270295..270462 FT /locus_tag="An14g03980" FT /number=3 FT CDS join(271389..271485,271549..271656,271717..272257, FT 272312..273164) FT /locus_tag="An14g03990" FT /note="Remark: the systematic name of hxt5 from S. FT cerevisiae is YHR096C." FT /note="Similarity: the ORF shows similarity to several FT sugar transporter from different species." FT /note="Title: strong similarity to hexose transporter Hxt5 FT - Saccharomyces cerevisiae" FT /note="plasma membrane" FT /db_xref="GOA:A2R3E3" FT /db_xref="InterPro:IPR005828" FT /db_xref="UniProtKB/TrEMBL:A2R3E3" FT /citation=[25] FT /inference="profile:COGS:COG0477" FT /inference="profile:PFAM:PF00083" FT /protein_id="CAK46635.1" FT /translation="MAPPKYAGMSGRPLSLFLSGIATMGFLLFGYDQGVMSGIISDAAF FT NNVFTATRNDNVMQATVTAVYEVGCLVGAIFALIFGETLGRRLMVISGAWVMIIGVIIQ FT VTAMPGHIPLLQFIFGRVITGIGNGMNTSTIPTYQAECSKSTNRGLLICIEGGIIAIGT FT AIAYWIDFGAHYGPPDLVWRFPIAFQIFFGILIIVGMMYLPDSPRYLIAHGKVEEGTRV FT LAALAGSEIDDPHVQLEKQLTLDSIRASGSSQARFRDLLTGGPSQHFRRMIVGSSSQFF FT QQISGCNAVIYYLPVLLEQSIGQSHDFALLIGGVNMICYAIFATFSWFFIEKIGRRKLF FT LGGSYGQCAAMIIVFGCLIPGDSESAKGAVFGFFLYMCVFGATWLPLPWLYPAEISPLK FT TRSKANAVSTCSNWLFNFTVVMITPVMVQHIGWGTYLFFAAWNGLFIPVIWFFYPETAG FT RSLEEIDLIFAKGYVENMSYVRASKELPKLTDEEIEAKAAEYGILGDEEKAEERIAEKD FT PPASAEFSQFQPTQL" FT mRNA join(<271389..271485,271549..271656,271717..272257, FT 272312..>273164) FT /locus_tag="An14g03990" FT exon 271389..271485 FT /locus_tag="An14g03990" FT /number=1 FT intron 271486..271548 FT /locus_tag="An14g03990" FT /number=1 FT exon 271549..271656 FT /locus_tag="An14g03990" FT /number=2 FT intron 271657..271716 FT /locus_tag="An14g03990" FT /number=2 FT exon 271717..272257 FT /locus_tag="An14g03990" FT /number=3 FT intron 272258..272311 FT /locus_tag="An14g03990" FT /number=3 FT exon 272312..273164 FT /locus_tag="An14g03990" FT /number=4 FT CDS join(274363..274974,275025..276719,276783..276854) FT /locus_tag="An14g04000" FT /note="Function: the regulatory gene amdR of A. oryzae FT positively regulates the expression of genes involved in FT the catabolism of certain amides, omega amino acids and FT lactams." FT /note="Induction: amdR of A. oryzae can be induced by omega FT amino acids." FT /note="Phenotype: inactivation of the A. oryzae gene FT results in the inability to grow on gamma-amino-butyric FT acid (GABA) as a carbon and/or nitrogen source indicating FT that GABA utilization is amdR-dependent in A. oryzae." FT /note="Similarity: the similarity of the predicted ORF to FT amdR from A. oryzae is locally high the N-terminal part of FT the ORF, ending around amino acid 457." FT /note="Title: similarity to transcription regulator amdR FT -Aspergillus oryzae" FT /note="nucleus" FT /db_xref="GOA:A2R3E4" FT /db_xref="InterPro:IPR007219" FT /db_xref="UniProtKB/TrEMBL:A2R3E4" FT /citation=[11] FT /citation=[5] FT /inference="profile:PFAM:PF00172" FT /protein_id="CAK46636.1" FT /translation="MADTEPRKRRRPAKSCEQCRQRKVRCDRNVPCGPCTRARSSLGCS FT YRRDSRFSTPTDHQASPIISREPQRNARSYPLPSGMPEGSTGSLGETLHIEPRCGSKEC FT ISSQLGSTIRDLQLRLQRLEERLTDTDIVRPSAPEPDIQQALRELCDKVQRLEQRLLSC FT TDSPQAPKGELSIAATPPRLHTSSRKMKLFGPTHYMHTMDKLQLVGSLETRGPQPLCPE FT LKAELTARTKELRLLRGSVKAAQSPRLNDPVPDLLSTIPTRSVCDELVQCYLRTFERVY FT RIVHIPSFNKEYQQFWDQPLAAPTPFLMKLALILAIGTTFHPQRGKAGKEYDTRLIQTW FT IYAAQWWLTGPAEKNTFNLDGLQIFCLLLLARQMGSPGPSLYLSAGYLLQTATAMGLHR FT DSAYFPFLPPFQSEMRARLWATVLELTLQSSLDSASPITIPYFDTKPPSNFNDTDINPD FT IKPLPNPHPSTTHTDTSLQLLLNASFSLRAETIHLIHSPDRIPYQKALYLATKLRTTCH FT TITTFFQSNTTTITTSPFHKSHLLTTLNRYILHLHLPFAHAASTTPQYHYSRKLCLESA FT LTIASFAPSSSTSIPIPLDDFPLLTLTARGPLRGPLNLDIICTLALELITQIEEAPAVP FT NTTTAPNPLTLLSSTIRAPILQTLENLALQSAHVLRMHGKSPALKRYIISEALVAQIRA FT LEDGGGGGDVQGVVYEAVRGCLREGVGMLKGMEREGRDGDGDVGSLGMGMMVTPDSAGG FT AVGGSDGMGLGIGIGMDDLEGWGLASFLYAPGFVDLGGW" FT mRNA join(<274363..274974,275025..276719,276783..>276854) FT /locus_tag="An14g04000" FT exon 274363..274974 FT /locus_tag="An14g04000" FT /number=1 FT intron 274975..275024 FT /locus_tag="An14g04000" FT /number=1 FT exon 275025..276719 FT /locus_tag="An14g04000" FT /number=2 FT intron 276720..276782 FT /locus_tag="An14g04000" FT /number=2 FT exon 276783..276854 FT /locus_tag="An14g04000" FT /number=3 FT CDS complement(join(277089..278193,278245..278368, FT 278431..278593)) FT /locus_tag="An14g04010" FT /EC_number="2.7.4.2" FT /note="Catalytic activity: Erg8 of S. cerevisiae converts FT ATP + (R)-5-phosphomevalonate = ADP + FT (R)-5-diphosphomevalonate." FT /note="Pathway: second step in isopentenyl diphosphate FT formation." FT /note="Phenotype: disruption of the chromosomal erg8 coding FT region in S. cerevisiae by integration of URA3 or HIS3 FT marker fragments was lethal in haploid cells, indicating FT that this gene is essential." FT /note="Remark: Erg8 of S. cerevisiae is also called YMR220W FT or YM9959. 02." FT /note="Similarity: the ORF overlaps with A. niger EST FT EMBLEST:BE760517." FT /note="Title: strong similarity to phosphomevalonate kinase FT Erg8 - Saccharomyces cerevisiae" FT /note="cytoplasm" FT /db_xref="GOA:A2R3E5" FT /db_xref="InterPro:IPR014721" FT /db_xref="UniProtKB/TrEMBL:A2R3E5" FT /inference="profile:COGS:COG1577" FT /inference="profile:COGS:COG3890" FT /inference="profile:PFAM:PF00288" FT /inference="similar to AA sequence:UniProtKB:SCERG8.1" FT /protein_id="CAK46637.1" FT /translation="MSYKAPTVTAVSAPGKVLLAGGYLVLDRDYTGTVFALDARIHVVV FT QQLRRSHRSDEQASEDVIVVRSPQFVDAVWEYGIQRCDNGGGVKVVQKGDGRANPFVET FT SLNYALTYISYVAASKDFGSLSITILADNDYYSETAFSKISSLQSPGRFVNFGVPLHEA FT HKTGLGSSAALVTAFVSALVIHRTLQPEDLGAAREKLHNLAQAAHCAAQGKVGSGFDVA FT AAIYGSCLYRRFSPSILESVGDAGSPGFEERLFSIVEDADPNHTWDTECLDFGMKLPRG FT MQMVLCDVECGSQTPSMVRKVLEWRKQNPEESLMLWQALQSNNERLCLELKQLAQSPDV FT EAPNSFDDTRRLIERSRDLIRTMTQKAGVPIEPKVQTELLDAITSIEGVVGGVVPGAGG FT YDALAVLIEDKAEVIQRLNELFETWESKLEDDFGGKIGNVRLLGVRHGSAGVQNESLDQ FT YAGWF" FT mRNA complement(join(<277089..278193,278245..278368, FT 278431..>278593)) FT /locus_tag="An14g04010" FT exon complement(277089..278193) FT /locus_tag="An14g04010" FT /number=1 FT intron complement(278194..278244) FT /locus_tag="An14g04010" FT /number=1 FT exon complement(278245..278368) FT /locus_tag="An14g04010" FT /number=2 FT intron complement(278369..278430) FT /locus_tag="An14g04010" FT /number=2 FT exon complement(278431..278593) FT /locus_tag="An14g04010" FT /number=3 FT exon complement(278775..279173) FT /locus_tag="An14g04020" FT /number=1 FT CDS complement(278775..279173) FT /locus_tag="An14g04020" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3E6" FT /protein_id="CAK46638.1" FT /translation="MQITRPEWGWQPPVKPHMESSSHSLPVCLEMSGKWHINMSNSSVK FT STVQTTDRCWMPLQLYTYLRSSATRRRSVSHHASALDLLLILFLLAGCLPRKTCRLSPL FT SGAPPYRRSSQTIPSPICFCRPLLLPTH" FT mRNA complement(<278775..>279173) FT /locus_tag="An14g04020" FT CDS join(279533..279618,279708..279728,279789..279983, FT 280073..280253) FT /locus_tag="An14g04030" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3E7" FT /protein_id="CAK46639.1" FT /translation="MPQAHHGAKAMLGAGTEVRPVVTAHNLLKGPGPQTSVFRTEISLG FT PRRKYVLRSETAGAKGHHPFGESQTQDGESAIRVSGGLSGSGSQTPGPKKKSRNGGCQE FT RIQKMALLFFPTAPVCRVPRLGLAYDPGLAVRPPDQLLLGIPANPAPQATTTLLEG" FT mRNA join(<279533..279618,279708..279728,279789..279983, FT 280073..>280253) FT /locus_tag="An14g04030" FT exon 279533..279618 FT /locus_tag="An14g04030" FT /number=1 FT intron 279619..279707 FT /locus_tag="An14g04030" FT /number=1 FT exon 279708..279728 FT /locus_tag="An14g04030" FT /number=2 FT intron 279729..279788 FT /locus_tag="An14g04030" FT /number=2 FT exon 279789..279983 FT /locus_tag="An14g04030" FT /number=3 FT intron 279984..280072 FT /locus_tag="An14g04030" FT /number=3 FT exon 280073..280253 FT /locus_tag="An14g04030" FT /number=4 FT exon 281099..284926 FT /locus_tag="An14g04040" FT /number=1 FT CDS 281099..284926 FT /locus_tag="An14g04040" FT /note="Remark: a splice site was detected upstream of the FT START codon." FT /note="Similarity: the similarity of the predicted ORF to FT the hypothetical protein from S. pombe is locally high at FT its C-terminal end starting around amino acid 850." FT /note="Title: strong similarity to hypothetical protein FT SPAC1093.01 with conserved domain PF01535 duf17p FT -Schizosaccharomyces pombe" FT /db_xref="InterPro:IPR002885" FT /db_xref="UniProtKB/TrEMBL:A2R3E8" FT /inference="profile:PFAM:PF01535" FT /inference="similar to AA sequence:PIR:T50065" FT /protein_id="CAK46640.1" FT /translation="MVFKPFTHLARQSFTKAFTHGYAQSVVAASQSSYASTTTFNQIAS FT QPAAKLSRTTQLQNVFQPSSSSGAGAKASQGTSGSGDLGLAAYYAAWQHAQQTGDDSDW FT KQMQLKRKVGWKPSLNEDGVKSKESDHLPSADNNFHNSPHITKASANADVSAKVEEAVA FT REIQIQEEQAQVDEASEAKENTDTEAFPDLPPDVAAVADASTEQSRLASEHITDLASNN FT KYAEIPGAFATILRDGLTPTVGAYNALLESAIQLHGDTAQAIQKALDVYSDMLRRRVVP FT DEQTYQTLVQLFVVRANDAIKSKSLLEQERARYGGMEEPGKFMLHSSELERAILAEDHS FT LGIAMKLFNTAATRHADLVFPLDTYRHLISACAKEGQVEDMVRVYGHMESHKVTPHASI FT FPSMIDAFASTGDLQSAVECYNEYKGLAVSDDNGTFCIVQRLDGQVYAALVRAYLVCGK FT EQQALRFLERIQASFEEVTENREARQQALESAVVQDGLVQHALTSGEHGRALDQAKTRL FT RDGALDHAMSQICIAAADAGNLQTASEAYDALPTDMTIRQRPAISMLALHVRQGNVSAA FT RAVWLTLNTTGQATPDMVQPTAMYAVALLKSGQIEEALVQARNMFSRVRNASAVADNSS FT LNPIREQINESLHLIGRVLVQTAAVLSPQAAMSLLWSMVENGGLISPVAEHVVASLGPI FT GISQLNARDLMLALQVQAGMLVNHSAVFDVAHPIRFSHMLDIALATGLPMDAVTTRVVD FT QAVGKLFNSRPDMVKRWHDHLALTSSPSSFMSGRHSPSSDVSTMTPMSSTDDSFDPYAY FT ATDFRGSSMISDELESTSGKLEAHLNDALSRVRNMRRNGRHPRYITYAKMITAATKCNR FT VDLAYEILSMARRDVPLLPQYSAVKYGWVSILDAMVASCLTLGDRSQASKFHQELLKLG FT SAPSANTFGLYITTLKESTKTFDEATEALKIFHRAVAEGVEPTSFLYNALIGKLGKARR FT IDDCLLYFAEMRANGVRPTSVTYGTIVNALCRVSDERFAEEMFEEMESMPNYKPRPAPY FT NSMIQYFLNTKRDRSKVLAYYERMLTRNIQPTMHTYKLLIDAHASLEPVDMPAAEKVLE FT TIKAAGQRPDAVHYASLIHAKGCVMHDMEAAHAVFKSVAEERKVRMQPCLYQALLEAMV FT ANHQVAQTEEIVRDMARRGVEMTAYIANTLIHGWATEGSVAQAKTVYDSIGIEKREPST FT YEAMTRAFLANNDREGASRTVQEMLSRGYPAAVASKIADLVGTGAAVAAL" FT mRNA <281099..>284926 FT /locus_tag="An14g04040" FT CDS join(285595..285658,285712..286134,286234..286409, FT 286491..286684,286999..287209) FT /locus_tag="An14g04050" FT /EC_number="1.4.3.5" FT /note="Catalytic activity: pdx3 of S. cerevisiae converts FT pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal FT 5'-phosphate + NH3 + H2O2." FT /note="Induction: due to the presence of gcn4p binding FT sequences in the pdx3 promoter region it is assumed that FT transcription of this gene is under the general control of FT nitrogen." FT /note="Pathway: de novo synthesis of pyridoxine (vitamine FT B6) and pyridoxal phosphate." FT /note="Remark: alternate names for pdx3 of S. crevisiae are FT YBR032 or YBR035c." FT /note="Similarity: the ORF overlaps with A. niger EST FT PATENTDNA:AAF11550 EST SEQ ID NO:4073." FT /note="Similarity: the similarity of the ORF to pdx3 of S. FT cerevisiae is restricted to the inner part of the FT ORF,spanning the region between amino acid 105 and 285." FT /note="Title: strong similarity to pyridoxamine-phosphate FT oxidase Pdx3 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2R3E9" FT /db_xref="InterPro:IPR019576" FT /db_xref="UniProtKB/TrEMBL:A2R3E9" FT /inference="profile:COGS:COG0259" FT /inference="profile:PFAM:PF01243" FT /inference="similar to AA sequence:PIR:S41301" FT /protein_id="CAK46641.1" FT /translation="MNPGSLPDGPSHDAKHPKKLIFAPGDIQTTPEPKITPTETPDPSA FT TATGVTTAPAPISRLAAEALRSNASTPDSVTENEIVSHPARAHQFVSNPPLTISQMHPT FT NPLHQFHNWFRDPRLLPSSAPETCTLATASMPSGRVSARVVYLKELDERGWVVYSNWGT FT GLQEGNKWAALTFCWSNLERQVRIEGLVEPLSRDESEMYWRTRERGSQIGAWASWQSKV FT PGDVDATDIDDGRALLEKRVKEMEERFAGVEQIPLPPFWGGVRLVPESVEFWQGRRSRL FT HDRFRSITPSNTLHTNTFNMSEPQSPSQEPQSHPNPEQQQQQQQQQQKPHQTKWLLLAL FT SSGAFAALNGLFAKL" FT mRNA join(<285595..285658,285712..286134,286234..286409, FT 286491..286684,286999..>287209) FT /locus_tag="An14g04050" FT exon 285595..285658 FT /locus_tag="An14g04050" FT /number=1 FT intron 285659..285711 FT /locus_tag="An14g04050" FT /number=1 FT exon 285712..286134 FT /locus_tag="An14g04050" FT /number=2 FT intron 286135..286233 FT /locus_tag="An14g04050" FT /number=2 FT exon 286234..286409 FT /locus_tag="An14g04050" FT /number=3 FT intron 286410..286490 FT /locus_tag="An14g04050" FT /number=3 FT exon 286491..286684 FT /locus_tag="An14g04050" FT /number=4 FT intron 286685..286998 FT /locus_tag="An14g04050" FT /number=4 FT exon 286999..287209 FT /locus_tag="An14g04050" FT /number=5 FT CDS complement(join(287775..288707,288757..289484, FT 289535..289612,289661..290020,290072..290139, FT 290202..290673)) FT /exception="reasons given in citation" FT /locus_tag="An14g04060" FT /note="Function: clcn3 of M. musculus is an voltage-gated FT channel, which is active in chloride transport." FT /note="Remark: an alternative name for clcn3 is clc3." FT /note="Title: strong similarity to chloride channel 3 clcn3 FT - Mus musculus [putative frameshift]" FT /note="putative frameshift" FT /db_xref="GOA:A2R3F0" FT /db_xref="InterPro:IPR000644" FT /db_xref="UniProtKB/TrEMBL:A2R3F0" FT /citation=[27] FT /inference="profile:COGS:COG0038" FT /inference="profile:PFAM:PF00654" FT /inference="similar to AA sequence:UniProtKB:AF029347.1" FT /protein_id="CAK46642.1" FT /translation="MPVSPSSARPPPLSSERRNWRRLSGLSVVSPIHERPTPENGQPSA FT ITEEISEIKRYEDFTTIDWVQDAVHEQARRRAKRRDGSGFWDQEETFGWRRKVRESYDA FT GQAWLVITIVGAAIGLISAILNIITEWLSDVKLGHCTTAFYLNEQFCCWGAEGGCPEWR FT PWTSYWIVNYFIYIFYAVLFAFVAASLVKSFAPYAAGSGISEIKCIIAGFVMKGFLGAW FT TLLIKSIALPLAIASGLSVGKEGPSVHFAVCTGNVISRFFSKYKQNASKTREVLTATAA FT AGVAVAFGSPIGGVLFSLEEVASYFPLKTLWRSYFCALVATGVLAVMNPFRTGQLVMFQ FT VQYDRTWHFFELIFFVLIGVFGGLYGAFVIKWNLRVQAFRKKYLSQHAIMESVVLAGIT FT AILCYPNMFLKINMTEMMEILFRECEGGHDYNGLCEYSGIIRLAQHVLTYYRAKNRWSM FT VMSLAVATILRIFLVIISYGCKVPAGIFVPSMAIGASFGRFVGILVQALHEAYPKSQFF FT ASCEPDIPCITPGTYAFLGAGAALSGIMHLTISVTVIMFELTGALNYILPTMIVVGVTK FT AVSDCFGKGGIADRMIWSNGFPFLDNKEDHVFNVPVSQAMTSDPVSLPASDFPVREAEH FT LLSDNKYQGFPIVDDRTRKTLVGYIGRTELRYAINRAKAEGPLSPTAKCLFTKEAAEAS FT VTRRASTASHLHVPETFDDIQTNTGADYVDFSRYADHTPLTVHPRLALETVMEIFKKMG FT PRVILVEHRGRLMGLVTVKDCLKYQFKVEAEEQALAATSPPQLALGGGGGRSGGDTLEE FT RLWNLLQRIGSLLPWQRPPPQQQQQQQQRQQQQSRRRDTTAPEHHRDAETTANEADEED FT AMLELEER" FT mRNA complement(join(<287775..288707,288757..289484, FT 289535..289612,289661..290020,290072..290139, FT 290202..>290673)) FT /locus_tag="An14g04060" FT exon complement(287775..288707) FT /locus_tag="An14g04060" FT /number=1 FT intron complement(288708..288756) FT /locus_tag="An14g04060" FT /number=1 FT exon complement(288757..289484) FT /locus_tag="An14g04060" FT /number=2 FT intron complement(289485..289534) FT /locus_tag="An14g04060" FT /number=2 FT exon complement(289535..289612) FT /locus_tag="An14g04060" FT /number=3 FT intron complement(289613..289660) FT /locus_tag="An14g04060" FT /number=3 FT exon complement(289661..290020) FT /locus_tag="An14g04060" FT /number=4 FT intron complement(290021..290071) FT /locus_tag="An14g04060" FT /number=4 FT exon complement(290072..290139) FT /locus_tag="An14g04060" FT /number=5 FT intron complement(290140..290201) FT /locus_tag="An14g04060" FT /number=5 FT exon complement(290202..290673) FT /locus_tag="An14g04060" FT /number=6 FT CDS join(290705..290743,290977..291103,291184..291315, FT 291396..291451,291530..291620,291679..291989) FT /locus_tag="An14g04070" FT /note="Function: cbf-C of R. norvegicus is forming together FT with cbf-A and cbf-B the cbf-DNA complex, which binds to FT CCAAT motifs present in many eukaryotic promoters." FT /note="Similarity: a significant similarity of the FT predicted ORF to CCAAT binding transcription factor C FT subunits of several species starts with amino acid 100 of FT the ORF." FT /note="Title: similarity to CCAAT binding transcription FT factor subunit C cbf-C - Rattus norvegicus" FT /note="nucleus" FT /db_xref="GOA:A2R3F1" FT /db_xref="InterPro:IPR009072" FT /db_xref="UniProtKB/TrEMBL:A2R3F1" FT /citation=[30] FT /inference="profile:COGS:COG5208" FT /inference="profile:COGS:COG5247" FT /protein_id="CAK46643.1" FT /translation="MGIAEASKRGNLGRLLESILFRTIHYSFTFLFRHAREWISTPHAP FT EFPSLQLHLLGAIRYRPEHYLHDYLRRDVAMPPKDKAAAEASSSREITGQSALPNDDIV FT QCSSNATFVIAMATELFIQYLTEQGHNVVKSERKPRKLIQYKDLATAVSRIDNLEFLSD FT VIPKTTTYKQFKEKRAKEKEPGPEKGQRTLNGNLPAAVEDKEELEEQQSLQPVDDKPSR FT GSRPPTVTMMVDRTVDTSAGDQDVEMTDQ" FT mRNA join(<290705..290743,290977..291103,291184..291315, FT 291396..291451,291530..291620,291679..>291989) FT /locus_tag="An14g04070" FT exon 290705..290743 FT /locus_tag="An14g04070" FT /number=1 FT intron 290744..290976 FT /locus_tag="An14g04070" FT /number=1 FT exon 290977..291103 FT /locus_tag="An14g04070" FT /number=2 FT intron 291104..291183 FT /locus_tag="An14g04070" FT /number=2 FT exon 291184..291315 FT /locus_tag="An14g04070" FT /number=3 FT intron 291316..291395 FT /locus_tag="An14g04070" FT /number=3 FT exon 291396..291451 FT /locus_tag="An14g04070" FT /number=4 FT intron 291452..291529 FT /locus_tag="An14g04070" FT /number=4 FT exon 291530..291620 FT /locus_tag="An14g04070" FT /number=5 FT intron 291621..291678 FT /locus_tag="An14g04070" FT /number=5 FT exon 291679..291989 FT /locus_tag="An14g04070" FT /number=6 FT CDS join(292603..292897,293056..293144,293230..293380, FT 293444..293625) FT /locus_tag="An14g04080" FT /EC_number="1.10.2.2" FT /note="Function: rip1 from S. pombe is part of the FT respiratory chain complex in the inner mitochondrial FT membrane (complex III or cytochrome b-c1)." FT /note="Remark: rip1 from S. pombe is also called Rieske FT iron-sulfur protein or rsp." FT /note="Remark: the systematic name of rip1 from S. pombe is FT SPBC16H5. 0." FT /note="Similarity: the ORF overlaps with A. niger ESTs FT EMBLEST:AN754, PATENTDNA:AAF11289 EST SEQ ID NO:3812 and FT PATENTDNA:AAF14587 EST SEQ ID NO:7110." FT /note="Title: strong similarity to iron-sulfur subunit of FT ubiquinol--cytochrome c reductase rip1p FT -Schizosaccharomyces pombe" FT /note="localisation:mitochondrion" FT /db_xref="GOA:A2R3F2" FT /db_xref="InterPro:IPR005805" FT /db_xref="UniProtKB/TrEMBL:A2R3F2" FT /inference="profile:COGS:COG0723" FT /inference="profile:PFAM:PF00355" FT /inference="similar to AA sequence:SWISSPROT:UCRI.SCHPO" FT /protein_id="CAK46644.1" FT /translation="MSLSAASSSILRACARQQLPSSRAAIASCQQRRGVADASKSTFDS FT PFGSSKEYSSTLKIPDFSKYQSKKPPRSNQVFSYFMAGSLGLASAVGAKATVQDFLVNM FT SASADVLAQAKVEIGLGAIPEGKNVIIKWRGKPVFIRHRTQDEIQEAQKTEWQSLRDPQ FT ADEDRVQKPEWLVMLGVCTHLGCVPIGESGDYGGWFCPCHGSHYDISGRIRKGPAPLNL FT EVPQYNFPSEDTLVIG" FT mRNA join(<292603..292897,293056..293144,293230..293380, FT 293444..>293625) FT /locus_tag="An14g04080" FT exon 292603..292897 FT /locus_tag="An14g04080" FT /number=1 FT sig_peptide 292603..292650 FT /locus_tag="An14g04080" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(292651..292897,293056..293144,293230..293380, FT 293444..293622) FT /locus_tag="An14g04080" FT intron 292898..293055 FT /locus_tag="An14g04080" FT /number=1 FT exon 293056..293144 FT /locus_tag="An14g04080" FT /number=2 FT intron 293145..293229 FT /locus_tag="An14g04080" FT /number=2 FT exon 293230..293380 FT /locus_tag="An14g04080" FT /number=3 FT intron 293381..293443 FT /locus_tag="An14g04080" FT /number=3 FT exon 293444..293625 FT /locus_tag="An14g04080" FT /number=4 FT CDS complement(join(294324..295240,295312..295894)) FT /locus_tag="An14g04090" FT /note="Similarity: the ORF shows similarity to the FT homologues protein of she9 from C. albicans, SPAC823. 13c FT from S. pombe and YDR393w from S. cerevisiae." FT /note="Similarity: the similarity of the ORF to these FT hypothetical proteins is restricted to its innner FT part,spanning the region from amino acid 150 to 350." FT /note="Title: strong similarity to hypothetical protein FT she9 - Candida albicans" FT /db_xref="GOA:A2R3F3" FT /db_xref="InterPro:IPR008839" FT /db_xref="UniProtKB/Swiss-Prot:A2R3F3" FT /inference="similar to AA sequence:UniProtKB:CAL277539.1" FT /protein_id="CAK46645.1" FT /translation="MQSMPLLLRQSFKSTLNLTRTTRPVQRRPLLPAVGPNSLYPAPRN FT FSICLQCQFRTQSSLYSSDSLKDGKPAEQPKEDASPVIALPAGNANLEADAGSQQQAPP FT AAAEAGESTQSQQQQQQQQQQQEEKSEANGKGWGDGGLPSYIEQRRSQFTKRFSDVMDN FT LQSNIFVAGQRLNDLTGYSAIEMLKKEIHRQEERLRTARLQVRTAKDAYAAAINNRSTS FT QREVNELLQRKHAWSPTDLERFTHLYRNDHTNEVAEHEAQEALSQAEHEAEEAAAQLSK FT SILSRYHEEQVWSDKIRQMSTWGTWGLMGVNVLLFLIFQIAVEPWRRKRLVKGFEEKVI FT EAIEKEKALDRIQIVTAQNQMAQESSTTSTASTATPETAETAETAEPSASPADEPIADT FT DAIVTIESTEPEVFSSDPADAEPPANTIVSKPTPDNIREYIKFQLARVSPLLESLRQYL FT HDLFSDRQVVLTQRDLSTVALQSAAAGAAVIGMLSMIIRQR" FT mRNA complement(join(<294324..295240,295312..>295894)) FT /locus_tag="An14g04090" FT exon complement(294324..295240) FT /locus_tag="An14g04090" FT /number=1 FT intron complement(295241..295311) FT /locus_tag="An14g04090" FT /number=1 FT exon complement(295312..295894) FT /locus_tag="An14g04090" FT /number=2 FT CDS complement(join(296476..296885,296949..297006)) FT /locus_tag="An14g04100" FT /note="Similarity: some of the hypothetical protein are FT putative membrane proteins and/or stress responsive." FT /note="Similarity: the similarity to several hypothetical FT proteins is restricted to the first third of the ORF,ending FT around amino acid 60." FT /note="Title: similarity to hypothetical protein ZK632.10 FT -Caenorhabditis elegans" FT /db_xref="GOA:A2R3F4" FT /db_xref="InterPro:IPR000612" FT /db_xref="UniProtKB/TrEMBL:A2R3F4" FT /inference="profile:COGS:COG0401" FT /inference="profile:PFAM:PF01679" FT /inference="similar to AA sequence:PIR:B88567" FT /protein_id="CAK46646.1" FT /translation="MCGSDIFLAILAVFFPPVSVWIKVGICTADSIINLALCCLGYVPG FT LLHAWYIILKYPEPDYDDPSYEPLPGDAENGRVTYYYVSHQPIQHPSQRGYGTLPPQQP FT QAANAPPQNQQPTPNHSQEQAQAGSSSQEHHDSRPPPTYAEAVKGDHKVQD" FT mRNA complement(join(<296476..296885,296949..>297006)) FT /locus_tag="An14g04100" FT exon complement(296476..296885) FT /locus_tag="An14g04100" FT /number=1 FT mat_peptide complement(296479..296883) FT /locus_tag="An14g04100" FT sig_peptide complement(join(296884..296885,296949..297006)) FT /locus_tag="An14g04100" FT /inference="protein motif:SignalP:2.0" FT intron complement(296886..296948) FT /locus_tag="An14g04100" FT /number=1 FT exon complement(296949..297006) FT /locus_tag="An14g04100" FT /number=2 FT CDS complement(join(298078..298202,298301..298386, FT 298487..298572)) FT /locus_tag="An14g04110" FT /note="Remark: the ORF is questionable due to its FT suboptimal intron-exon structure and short lenght" FT /note="Title: questionable ORF" FT /db_xref="GOA:A2R3F5" FT /db_xref="InterPro:IPR010526" FT /db_xref="UniProtKB/TrEMBL:A2R3F5" FT /protein_id="CAK46647.1" FT /translation="MLGSSNRDEELAYHRTWHAASALIRRRARSRPGCSEVPHIFSASL FT SVSWHLYHIPLADNITRGRGSCFTHRPSGIGTSWHDPVADGCVKYCPCCSTDI" FT mRNA complement(join(<298078..298202,298301..298386, FT 298487..>298572)) FT /locus_tag="An14g04110" FT exon complement(298078..298202) FT /locus_tag="An14g04110" FT /number=1 FT intron complement(298203..298300) FT /locus_tag="An14g04110" FT /number=1 FT exon complement(298301..298386) FT /locus_tag="An14g04110" FT /number=2 FT intron complement(298387..298486) FT /locus_tag="An14g04110" FT /number=2 FT exon complement(298487..298572) FT /locus_tag="An14g04110" FT /number=3 FT CDS complement(join(298824..298998,299076..299151, FT 299239..299364,299442..299570,299628..299658)) FT /locus_tag="An14g04120" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2R3F6" FT /protein_id="CAK46648.1" FT /translation="MLCACSKDANGGVAGFARNSGTSKRKKRRKGRINAGTGNFIALII FT ARNFVMHRSTDCAGHSEWPSLHYSDEVYPLPLALIKPAQYSVSGCKHLCSEPGKAAAAI FT RVGLANTGAEPNCATLWLTIPKCSGCKLETPSAEHLSVYRKYVTYIHFGPIAIVASLAW FT LCDTTAHERLLAAWL" FT mRNA complement(join(<298824..298998,299076..299151, FT 299239..299364,299442..299570,299628..>299658)) FT /locus_tag="An14g04120" FT exon complement(298824..298998) FT /locus_tag="An14g04120" FT /number=1 FT intron complement(298999..299075) FT /locus_tag="An14g04120" FT /number=1 FT exon complement(299076..299151) FT /locus_tag="An14g04120" FT /number=2 FT intron complement(299152..299238) FT /locus_tag="An14g04120" FT /number=2 FT exon complement(299239..299364) FT /locus_tag="An14g04120" FT /number=3 FT intron complement(299365..299441) FT /locus_tag="An14g04120" FT /number=3 FT exon complement(299442..299570) FT /locus_tag="An14g04120" FT /number=4 FT intron complement(299571..299627) FT /locus_tag="An14g04120" FT /number=4 FT exon complement(299628..299658) FT /locus_tag="An14g04120" FT /number=5 FT CDS join(299730..299774,299915..300268) FT /locus_tag="An14g04130" FT /note="Remark: the ORF is questionable due to its FT suboptimal intron-exon structure." FT /note="Title: questionable ORF" FT /db_xref="UniProtKB/TrEMBL:A2R3F7" FT /protein_id="CAK46649.1" FT /translation="MGVIMNRVGIGSCTSFNWKDAGYSCEPPARPPFESVFSSRGPSGA FT SASLPFFVSCASSVIQDCSVKEPTSIESNRAVLPVLCFPGSLPFGGPRTQAAITSSPDW FT ESTAFLQVPCLAPAFSAVDRRLFSFLLP" FT mRNA join(<299730..299774,299915..>300268) FT /locus_tag="An14g04130" FT exon 299730..299774 FT /locus_tag="An14g04130" FT /number=1 FT intron 299775..299914 FT /locus_tag="An14g04130" FT /number=1 FT exon 299915..300268 FT /locus_tag="An14g04130" FT /number=2 FT CDS join(300696..300790,300842..300925,300984..301146, FT 301205..302422) FT /locus_tag="An14g04140" FT /note="Function: c-cam105 is conferring the ability to pump FT out [3H]taurocholate when expressed in cos cells." FT /note="Function: c-cam105 of R. norvegicus is a FT calcium-independent cell adhesion molecule, which may play FT a role in the formation and maintainance of the structure FT of the apical surface of rat hepatocytes." FT /note="Induction: phosphorylation of the cytoplasmic tail FT of c-cam105 is essential for bile acid efflux activity but FT not for ATPase activity." FT /note="Remark: c-cam105 of R. norvegicus is also called FT C-CAM, ATP-dependent taurocolate-carrier protein or gp110." FT /note="Similarity: the ORF shows similarity to several FT serine-rich proteins." FT /note="Similarity: the predicted ORF is 184 amino acids FT shorter at its N-terminus than c-cam105 of R. norvegicus." FT /note="Title: similarity to ecto-ATPase c-cam105 - Rattus FT norvegicus" FT /note="plasma membrane" FT /db_xref="InterPro:IPR001452" FT /db_xref="UniProtKB/TrEMBL:A2R3F8" FT /citation=[37] FT /citation=[38] FT /inference="similar to AA sequence:SWISSPROT:ECTO.RAT" FT /protein_id="CAK46650.1" FT /translation="MSGTCISLSGSTQCPAFDSSSVSTNSSLYTDFPFMQYVSNLTQFD FT NELSSYVMQGYVREKYEEYLGCQGVNLTDTDDYYARYTTSVLCSSLVQSSKSDCNLSDE FT ESRPLCADTCASMAISEEAIVTDTNLCSGKASDYMSQIRSDFTICALPADSLTVTCITG FT AENEPKNCGFRSNVLGLCSYCASGSSNSTDSCCTDSNAATRCSNVTVPSSTLPPIFTST FT AASNSTAGSNDLSGGQIAGIVIGSVAGFALLAALAVLALIYWRRRRRAENDSSLNQPNP FT QRKGSPSMQQDQSPHEFAAIPGGRVARMSALREVPSSSPARSRYSALFGGAKYSDTSDS FT DHGASPGAMSKKIPPTTGKRHGSLSSNSALAGAGTDSSPRSGTGGQYSSPDGLTSGQSE FT QLSAFQDYYSQDDIHPGDKVAVLWAYQPRAGDEFALDRGEMLKVIGIWDDGWATGIRIP FT ETAEDHDARHREQRDSGVSNGSRRAATSPAPVGDIKAFPLVCVCLPQHWRKIIDGGQAE FT DD" FT mRNA join(<300696..300790,300842..300925,300984..301146, FT 301205..>302422) FT /locus_tag="An14g04140" FT exon 300696..300790 FT /locus_tag="An14g04140" FT /number=1 FT intron 300791..300841 FT /locus_tag="An14g04140" FT /number=1 FT exon 300842..300925 FT /locus_tag="An14g04140" FT /number=2 FT intron 300926..300983 FT /locus_tag="An14g04140" FT /number=2 FT exon 300984..301146 FT /locus_tag="An14g04140" FT /number=3 FT intron 301147..301204 FT /locus_tag="An14g04140" FT /number=3 FT exon 301205..302422 FT /locus_tag="An14g04140" FT /number=4 FT CDS join(302825..302917,303084..303230) FT /locus_tag="An14g04150" FT /note="Remark: the ORF is questionable due to its FT suboptimal intron-exon structure and short lenght" FT /note="Title: questionable ORF" FT /db_xref="UniProtKB/TrEMBL:A2R3F9" FT /protein_id="CAK46651.1" FT /translation="MSITGAVAGFFYVTTYSPSCRVNDGKLYGLEAAYTCIRLGQPGTM FT IFVMMTDSTRALPMSLGINLGTAQFSCPDVILLG" FT mRNA join(<302825..302917,303084..>303230) FT /locus_tag="An14g04150" FT exon 302825..302917 FT /locus_tag="An14g04150" FT /number=1 FT intron 302918..303083 FT /locus_tag="An14g04150" FT /number=1 FT exon 303084..303230 FT /locus_tag="An14g04150" FT /number=2 FT CDS join(304137..304142,304206..304216,304325..304585, FT 304653..304701,304764..304904) FT /locus_tag="An14g04160" FT /note="Function: cofilin cof1 of S. cerevisiae is an FT essential component of the yeast cortical cytoskeleton, a FT low-molecular weight actin-binding and depolymerizing FT protein with several activities in vitro." FT /note="Induction: cofilin activity is regulated by FT phosphorylation." FT /note="Remark: a splice site was detected upstream of the FT START codon." FT /note="Remark: the systematic name for cof1 of S. FT cerevisiae is YLL050C." FT /note="Similarity: the ORF overlaps with A. niger ESTs FT EMBLEST:BE759006 and EMBLEST:BE759053." FT /note="Title: strong similarity to cofilin Cof1 FT -Saccharomyces cerevisiae" FT /note="cytoskeleton" FT /db_xref="GOA:A2R3G0" FT /db_xref="InterPro:IPR002108" FT /db_xref="UniProtKB/TrEMBL:A2R3G0" FT /citation=[21] FT /citation=[51] FT /citation=[71] FT /inference="profile:PFAM:PF00241" FT /inference="similar to AA sequence:PIR:A44397" FT /protein_id="CAK46652.1" FT /translation="MSLASGVSITDECITAFNEFRMSGNSRGSKTKFIIFKIADNKKEV FT VIDEVSQDEDYEVFREKLAAAKDAKGNPAPRYAVYDVEYDLGGGEGKRSKIIFISWVPS FT DTATLWSMIYASTRENLKNALNIHTSIHADDKSDIEWKTVLAEASGGKAGK" FT mRNA join(<304137..304142,304206..304216,304325..304585, FT 304653..304701,304764..>304904) FT /locus_tag="An14g04160" FT exon 304137..304142 FT /locus_tag="An14g04160" FT /number=1 FT intron 304143..304205 FT /locus_tag="An14g04160" FT /number=1 FT exon 304206..304216 FT /locus_tag="An14g04160" FT /number=2 FT intron 304217..304324 FT /locus_tag="An14g04160" FT /number=2 FT exon 304325..304585 FT /locus_tag="An14g04160" FT /number=3 FT intron 304586..304652 FT /locus_tag="An14g04160" FT /number=3 FT exon 304653..304701 FT /locus_tag="An14g04160" FT /number=4 FT intron 304702..304763 FT /locus_tag="An14g04160" FT /number=4 FT exon 304764..304904 FT /locus_tag="An14g04160" FT /number=5 FT CDS join(305851..306160,306256..>306260) FT /gene="cox5" FT /locus_tag="An14g04170" FT /product="cytochrome c oxidase subunit V cox5-Aspergillus FT niger [truncated ORF]" FT /EC_number="1.9.3.1" FT /note="Function: cytochrome c oxidase subunit V cox5 of A. FT niger is part of the respiratory chain of the mitochondrial FT oxidative phosphorylation process." FT /note="Gene-ID: cox5" FT /note="Remark: the ORF is C-terminally truncated due to the FT contig border." FT /note="Similarity: the ORF overlaps with EMBL:ANI132229 (A. FT niger cox5 gene, exons 1-3) and PATENTDNA:AAF11256 (A. FT niger EST SEQ ID NO:3779)." FT /note="localisation:mitochondrion" FT /db_xref="GOA:A2R3G1" FT /db_xref="InterPro:IPR004203" FT /db_xref="UniProtKB/TrEMBL:A2R3G1" FT /citation=[74] FT /citation=[87] FT /inference="similar to AA sequence:UniProtKB:ANI132229.1" FT /protein_id="CAK46653.1" FT /translation="MFLRSVTRAAARSSAVPTTGLRSYRTVSGPMACLNARPQTEKKSI FT APQQTRAASEHAISNPTLAGIEKRWEAMPPQEQAELWMQLRDRMKVDWHQMTLQEKKAA FT Y" FT mRNA join(<305851..306160,306256..>306260) FT /gene="cox5" FT /locus_tag="An14g04170" FT exon 305851..306160 FT /gene="cox5" FT /locus_tag="An14g04170" FT /number=1 FT intron 306161..306255 FT /gene="cox5" FT /locus_tag="An14g04170" FT /number=1 FT exon 306256..>306260 FT /gene="cox5" FT /locus_tag="An14g04170" FT /number=2 XX SQ Sequence 306261 BP; 74054 A; 78553 C; 78759 G; 74895 T; 0 other; cgctaggtgg tcctctccat ccagtgcaat ccccatctct gccatcgctt tgtctttctt 60 cttgttctcc cggatcaggt agaagcggag gaagatcacc gccagtgtca tggctgagta 120 gcagccgagg tgcacgccaa aggcgatgaa gtaccgcggg gcgtcgcggt cgaggaacac 180 ttgagggcct acgtcattag taaggctctg agagatatag tgtgtaagct aggggtccta 240 ccgatggcgt ttccaacagc ccaagacaca aacgtcgcag ccacaacagt ggacttctta 300 gtagcgccgg caatgttcct cgtcaccatg gacaagccca agttctgggc agaccagaac 360 gacagcgtaa tgtagtagct gataagaaga cccactttgg tgctgaggga gtgattctgc 420 actgtcatga ggacgatagt tccgacgaag gacctacatc ttgttagtgt cacaattcag 480 gataagatac gagaagaagg ggggacgcac ggaataataa atcccaacat caccagcaag 540 ttctgctcaa acttcttgac caaccacgca ctcgtcaaca acacaataat gatgtaaaag 600 cccagtacca tcgccaacaa ctgcgtctgc aactccgtaa agttgaaccc actgatgatg 660 atatttgcaa acgcccccag accactcgtg ggcagcgtgg taaagatctg aatcgcgcag 720 tagcagtaca tctgcggatc ccggaacgct tcccacatct gatacgcgcg gaacttctta 780 ttctggagtc cagtctggtt ggcacgcaca cgctcaacca tcttgtgctt gtcctcttcg 840 gtgaagcatt tggcacgcat tggggaatcg ggcatccacc agaccacaaa cagcccccag 900 agcacggaaa tgcagccgta cgtgaggaaa agtgcttgcc aggatttaag cgcgcgatca 960 gacccaatta gactgaaaca gtaggctagg aggccgccga caatttgttg gccgccgttc 1020 atcatatacc tatgtcttgt tagtatacgt agatcaaggg tgtagagact ggactgtacc 1080 agaaggtgac ggtagcagct tgttcttcac gcttatacca cattccggaa aggacaacga 1140 aggagggctg gcatgcggct tcgaagatac caagcagagt gcgcacggtc actagaccgg 1200 caaagttgtg gcatgccgag tgcagggcta ggatggtgcc ccagcagatg atgttgaagc 1260 cgaggtattt ggcgatgcgg acgcgttgga tgatccagtt ggtgggatat tcgacaatga 1320 ggacggcaat gtagatacat gttgtgagcc aggagtacta tttagttagt gcttgaccat 1380 aagcagatat atgttcagac tcacctgttg tcccacaaga tgagcatcgt cgcgaatacc 1440 cataatggaa gcaaacgaca tggtaccctt gtccagtgcc tgcagaaagt atgtcacgat 1500 catgatgacc aacacacgac gatcaatcat gcggcgaaga cgccgacttt cggcttcgtc 1560 gacctcaatc tggccgcgcg cggcatactc cagcacctca ttgtcgacac ggttcgcatc 1620 gatcggggcc ttcagtttgt cggagggtga cagcacccgc tcgacatggg acacatcctg 1680 cggcggcttg tggtcctcca cagccgtgga agctccctta gagtcaggcc cgcctgcggg 1740 cgtcgagcta atattctcca tggacatgtt gcctgccaga attgccaggg ttggagaggg 1800 tcaaccccgg ctgggggacc cggacaccct tatatcggtc atgcgggaga tagagtctga 1860 ctagggcacg agtggctgct ccgtggctgc attttcactc caatgagagg aaggatgagc 1920 aggtctgata gtctgatagt ctgatgccag ggatggctgc tggctgggat tctccacgcg 1980 tacaatccgg gggcggcagg gtccgccccc gcgcggggac aattggcccg agcccttcgc 2040 ttaaaaagcg cttcacagcc tatcctcact ttagcatctt acacgaccaa tcttctctgt 2100 ttgccgagcg agcttggcat gattcagacg tggctgctcg gctgaagcta gcccgagggc 2160 attccccgca ttgctgctga agctcgacac gaggggtatc catcccacct tatagacacc 2220 agcatcacca gagtgtagca caatcaacaa ctccatcagt aataccactc aagtcctcat 2280 ctctcatcat ggcttctaca tctcctcccg ctgtccgatc caaaattgac cttctcatca 2340 ccaacctcgt caacatccaa gacaaaaccg gtcaattcct cctccccctc gccgatggcc 2400 gcatcatcga caccaagtcc tggcatggct gggaatggac gcatggaatc ggcctctatg 2460 gcatctggaa gtactacgaa atgaccggct ctccccacct cctgcagatt attgaggatt 2520 ggttcgccgc ccgcttcgct gaaggcggta ccactaagaa catcaacacc atggccgtct 2580 tccttactct ggcatacgta tacgagaaga cgcaaaaccc tgtctacctg ccctggctgg 2640 acgcatgggc cgaatgggct atgcatgaac tcccacgcac caagcaggga gggatgcagc 2700 acgccacata cctcacggaa aattaccagc agttgtggga tgatacgttg atgatgaccg 2760 tgatgccgtt ggcaaagatt ggaaagttgc tgaatcggcc ggattatgtg gaggaggcca 2820 agcgtcagac gttggtgcac gtcaagtact tggttgatac gagcaccggg ctgtggtttc 2880 atggctggac gttcgaggat ggtggacata actttgctag agcgaggtgg gcgcgcggta 2940 atagttgggt gactatggtt attccagagt ttattgagtt attggatttg aaggaggggg 3000 atcctattcg cctgttcttg ttggatacgt tagaggccca atgcgaggct ctcatgggcc 3060 tgcaggagga atcgggcttt tggcacaccc ttcttgacca tcctgattca tacgtcgagg 3120 cctccgccac agcaggattc gcatatggta tccttaaggc tgttaggaag aggtatctgc 3180 caaagaagta tcgggtagtc gcagagaagg ccattcaggc agtgttgagc gccgttgacg 3240 agaccggaga actgcagcag acgagctttg gtaccggcat gggggattct ctggacttct 3300 ataagaagat tcccttgaca gccatgccat atgggcaggc catggccatc atggcgctgg 3360 gcgagtatct ccggggacac ctatagaact tacttatcct tttttagata gcatatagag 3420 caacagaagc acttttctga ttagggcatg attgaagtgg taaccccata gaaattgaat 3480 gcttgtcatt ctatccttgc acataatcat gcatgtgcga tcccttgtac tcattgatcg 3540 gtccaattgt gggccgtgaa aatgctgtac cagctgaaga ccttcagctc atttgggcca 3600 gcaaatgcga tctcactctt ctttagaaaa gcatgatcca cttccacagg ttgtattcag 3660 tgaaaaaaac tttccccgct tttcggagat gctgctgatg gggtggcgtg tattggcaac 3720 cccaccgcga gactagtgtt agtcttcttg caatagcctc ctggaatgta ttaacccgaa 3780 agtagtcccg ctctgccttt tcaatcttct gaatcggctg gtcctctaat cttatgtcat 3840 tgtaaagctc tatgaagctt gacgacgatc gcttctcggt gaaataagac ctggcatcct 3900 ttccttggcc gtatacatgt tcccacaacg gcaaataaca gactgtagtc atcagttgag 3960 tcaaagttaa gtaaccgtgt caacagcctt gagcatctgc tctgttgtag gatctcaagg 4020 gcaattttat tggttactgt ctgttcatac gcgtgtcttc ggcagcggca gctgcgaatc 4080 cattttggaa ggcttgaacg aggttctcat ccaactcgta gcgcgactgt gacaagcctg 4140 gggaagctat catcagggct gctgggacag ttgaggaaaa tgccgcctcg tccaaacaat 4200 gagcccatct gattaaaccg taattgagac agcttgtaag tcattgtttc tagctcatat 4260 agccctttag ctttcagcga tacagccaat tttggttcgc cagaccctgt tgttttccaa 4320 gcttttgcga gaggccagct gggtgtcttg ctcatcaaga taagcggtat accaatctca 4380 tgttcggtgg tggggcgttc aagtcggcgt cgagtaaata ggatgggcat acgactggtc 4440 tgtaaaggtg aaccgctggc actagaatgt cacttgttca gtttcatata tttcaaggta 4500 gcggcttcac tttcgagcag ttctgagcta agccccatcg atatctcagt gccctttgta 4560 tgtagcgacc gcaggagcta ttagactcca tcatcaaatg taaggaaaac ggccctatta 4620 aagctgccgc tcgcgggatg ttggtcgagg tcgcaaaaac atggcatatc ctgtcgaatg 4680 ttgcttgaaa tgcgacaaag agcctcgaat ttgaatctag catacagaca tatggcaggc 4740 ctctttcaga tagcatggga gtgtctaaaa cattgcacaa tacgtgtcga acatgtactt 4800 cccaaggcgc tggcatgtca gacggcagaa ttcaaaaggc ggtcaaaaaa cacacagaat 4860 ccccagttga cttttggggg actgtatgtt cttaaatccg cttaaatccg aggttttttg 4920 gtcgaggtcg actagtttct gccgcattgg gcggtcgcag gagcggtcac ggtggacagt 4980 atctatatgc tgtgcaggca gaaatgatgt gtgcctgcag agtgtgcgcc tatttgtttg 5040 attcgtatgt acgtacttgg ctgcatcttc gtttaatact atcctagaat ggagctactt 5100 ctttccagct ctcatacacc cttcagcata gtgcagtgcc ccggtttgtg gtcttcttta 5160 cgaatgcaat gatctgtata ttctaccatg tgagtatcct taaatgatgt tgcatagtaa 5220 tagagcacat agatcagcaa agttgtcatt cgacaagcaa aatcttaact accgttccag 5280 tcattgctga ccatcagtct aatacactgg acatatgaaa attcttcata tcaccaacag 5340 gtgttgttct acgcacactt tccatgatat agcgccgatg caaacatcca cacttcacca 5400 cctatcccca cccattctag tacttcatac cattcaacct cccataaacc cttcaacttc 5460 cataaaaata taggtacata aaatgagtaa ggcactccaa cctccagctc tcccgtatag 5520 cctcccactc tttaagccac ctcccaacct cagtcagcca ggggagaccc gcaggccagc 5580 cacattccac gggggcatct actgctgtag acaatcccgt cagcacaaaa tacctcggaa 5640 ctatataagt gtcacaagta tccagaaatc tccgtagaat tgacaccggc gcgcgacccc 5700 aaggtggatt atgcatagga tagaagatga gaactttttc cactgggaat gagaaacaca 5760 cttggactag cttctctaga tgcttcagtc tcaggactgc gtttgactcg ttagatggta 5820 ccccgccgat gctcaggggt atgagatcgt cactgaccgc cagtgtcggg gctggaggct 5880 ggtggaggag catttctcgc cagctggctt cagggcggag gtaggggtgt tgacgttcta 5940 actctgtggt ggagggatca ctgctctttt gtggtccgaa tcgggagaga taagagctaa 6000 tatctctgtg gaaacttgat ccatggttgc tgacaaagtg tttcaggagc ttgttcatga 6060 gggggtttac agtgcgctta ggtttcaggg ccggtgtcga tgtcgatgag tctttttgag 6120 ggcggaagaa taaggccgtt tggagggatg gggatgtttt gatgagtgag ttccagacgt 6180 ggcagacgcg ttgtgagaag aggagggtgg ttgtgtctag gtttaggagg actggttcca 6240 gtacctcggg gatgaggaat atttggtgtg gtgagtccat tgtttcggct tggtggtgta 6300 gtactgtagt gggtttgtat atcttgcaaa tagagaaatg tttattcaag tgtaagtgtt 6360 gcggaagatg agaaactagt agtgaagtct ttcttttctt gttgtctggg ttgttatgct 6420 caaatgtggt ggacaggtag aagattgcgt gggatggact tctacaaaac tccgaaaaag 6480 tacttacgtg cctaattacg taggggtaaa atgcctcttt cgtgttgatg aggtacacga 6540 ctggcctcat aaagacggaa agacgatgga atgatgagac tcaggcagag aattaccggt 6600 gccatcttca aatactctca ttcatataca ccgagtccca gctccaaaga tatgagcagg 6660 aagttatggt tgacataaat cctgatgaga aaacccatct agagagctag tgattcacag 6720 caatcgcaat tcctgacagt gcttgtttcg tgtcttgtat accacctaca atcgagcctc 6780 cgaagtatca agcccatatt cctctgccag cgcatctcca catgtcaaac cggtgacata 6840 cgcagttgcc tgtgtgtggt tgttcgtcaa aacaggcacc acacccatgt cggcgatccg 6900 cagattctcg acaccaaata cccggaaccg gctgtccacg acagcatcgg catccccgga 6960 cttacccatc ttggtcgttc cagtcatgtg ccaactggat ccgagggtgt tcttccagaa 7020 ctcaagaata tcctcatccg actcggacgg gggcgcaatc aatgcggaca cggtgtcttt 7080 ttggaaagat tcatgcttcg tcacctccag cgcgtgccga tagatctcaa tacatgcgcg 7140 cctgtcaaac gggtgggaca agaactttgg atcaaacagc agcgggtctt cagggttggc 7200 tgactgcaga cgcacttcac cgctggattg ctcgttcatc aaaaacacga gcatgcaaac 7260 gtagctgtaa tctttgaaag gctcgggaga gatgagatgc agcgggaagt gtgtcatgaa 7320 ctcgtagtgt ggcaccgtgt cgcgttgtag gaattcctgc actgtcggag gcagtgcttt 7380 gaattcctca gatgccacca agcggtcgga cttgagccag ccggcgccaa tctggcacga 7440 gtgccgcgcc cacggcccgg tgccatcttt gctccattgt tccagagctg actccatagc 7500 agccgggtta ccgaagaagg catcgcgatc gtttgttgtc gggtttcgtt ggaagcacag 7560 cggtgcgaaa aagtggtccc gaagaccctg gcctaccgca ggcatgtcct tgacgacggg 7620 gatcccgaat tgttgtagtt gtcccgctgg tccaagtccc gaatgcatca gaatcttggg 7680 cgtgtccagt gatccggttg ttagaatcac ttctttggat gcgaagtctg cagcgacaag 7740 ccatggttag ttgaacggtt cagctcgaaa aatagctcga ttacatacat tttgccccct 7800 tggtttccac accaacagtc ttggtgcctt ggagtacgag cctgagcgct ggcgtctccg 7860 ttatgatagt caaattggac ggggcttcgt ccaaaagatc agttgctgtc actcttcgac 7920 cctggtggga tgaattaatg accaacgcca tgccaatcgg gtctcccgag ttgtggtcag 7980 ggttccgagc caggccagcc tgctcgaaga catccatcat caagggaaga tcctgctccc 8040 attcagcagc atagccgacc ttcagactcc cttgggagcc atggtctgag gtcctcgggg 8100 ctgcatattt gctattcttc gggtccacaa tggcaccgtt aaatgtttcc agctgtctga 8160 atcgagcctg catgcgctcc cagcgaaaca ggtcatcacc aacaagccca gcccattggt 8220 tatagtcgtc tcgcgcaccc acggtgtaga caccgaagtt gatggcgctg ctgccgccca 8280 ggaccttgcc ccgagaatag tcgatctgtc ggccattaca gtgttcttgt ggggtggtct 8340 tgtaccccca gttcaggttt ccattcataa aggtctgcca tcgttggccg tccacacgca 8400 gtgatggatc atcgttacga gggccggctt caagcaggag gacctgaggc cgtcgcgctg 8460 accgagcaag ccttgaagca agggcacagc ccgccgggcc acctatagca tcgttaggtg 8520 aggtcctgat cgacgaacga gacttccata ctaaccaccc acaacgacga attcccacgt 8580 ctgatcagtc gaggccattg tatattcaag attaccaccc tgtcggcagc tgtgacacag 8640 cgataagaac agtgtctcac aaggacaaaa ggatcacaag tcagaagagc agatgcccca 8700 attaaaggca gatgacagaa gcttggcgag tgggactctc attgagtcta gtcctgagat 8760 cgacagtgag acacgaaaga caaccccgca acgtttgcgc cataaccatt cccggccaac 8820 ctaaaagacg gaaaaagaga cggttcaaac tgtagtgttg taggctgccg tgtcttgtgt 8880 cgtgtcagcc gtgcggacat attatgggtt attccagacc cacaaagtcg agactaagtg 8940 agttgggagt tcctaggcaa acagttgagg tccactcaac gctgtctcag tgatgatcct 9000 tttgagtttc gcggtgcgag accgacggct cttcttcccc gagaccttcc ctcgagacca 9060 cttctcgcgg tgaagatatg agtggcattg tctcgtgagc caaggagtta gcagcatgca 9120 caagcttgac agggatcatc tccctagcca ccctgctgaa tgctccttcg cccaccactt 9180 gttgtccagc tctttaccat tggtggaagt gaacacgagt gaagaggggt gaagagataa 9240 cattcgtatg cagacctctg taagccggct aaaccagaat tgtcgctgat gcgaccgggg 9300 gtacgtgatc agatactcct cgactgaaaa gctcatgaag agctgcagaa acgtgacgtg 9360 gagaaaatct tgcataatgc attgcagttt gctgcagaat cttaccattt cccgtctcgc 9420 cttgcttttt ctttttattt tctttttcat tctcttcttc accctcttcc ctattaaaca 9480 gatgaatgta ttcctgcgtt ctgtcattgc caagcgtcga ctgtcaggta tcccaaaacc 9540 gatagcttag cgcccgagca gcaatgtcct tgagcacggc gatgcggacg aaaaggaaga 9600 ccgtttcaga gctcaagatc ccggtataag ttccctttcg ggacggaaat agtgctattc 9660 acgtggagaa gacaggacag agaagagctc gtccagcaag actagcgcgg ccacttcaca 9720 agtctccgaa ggttttgcga cagcgccgat cgggacgcga ccgaagtgga gagcatttgt 9780 cggtgatcac aacaggcgta cagtagttca agcacagtct cactagcggt agtacttcgg 9840 agtccggaga aaatcagtga tggcgggtcg ttgcagagct ggactggact ggggacgagt 9900 ggagttgcga attgaagtgt cgcgaagatg aacatgatca ggctccaatt tgcctgaggc 9960 cacactacgg tcaacagagc tggatatcta aatctatgct gctttacttc atattcgcca 10020 atgataattt acaaatacct tgaggtttag tattcttgaa agtaaggtta atagtcccgt 10080 tatgcgcttg tgtatagtgt ataagtttct cctgaaatct atatgtagac cagcaactgc 10140 aaggcaagcg tcataagggg caccttctat caggcgtcaa ttatagctta tccgccgtac 10200 tgccgcttac ctgattgatg gaacatttgt actacttccc cttcctaatg ttactagtgg 10260 gcgattttct tattaagaga agggtgttga taagggcgct ttggggcccg ccttgggtgc 10320 atcctgtccc aagtcatgtc gtagatgtta gcaacgcata caccgcgcaa agcatggtat 10380 cacagcatag aaaaatttcc gcaaataagt gtctggggta tccctatggg cgtcaggact 10440 gtctcagtaa tggggccatg atggttgagc caaaatgagg agagccttgc catggcaatc 10500 tactactagt agtagtagca acacaggaag gaccttccga cccagaaggg ccgttccccg 10560 atacgctcag tgctttggag gtagctccca cccttgtcac tgtcagcgag ttagttgcat 10620 caatcagtac tgatcaataa tgctgataat tctagcattg ctgcttttcc tagtatcgcc 10680 cgtcgtgaga gccagttcgc aatgtcggtg tcaacctggt gacgcatgct ggccttccag 10740 ggatggttgg aaacacttga atgaatccat cagtggtcat ttagttcgag tctaccccat 10800 cggccatgta tgccatgagc ccttcttcga ccaagcctcc tgcaatcagc ttgttcactt 10860 gcagtatgac tctaattggc gcgcagagca accaggtagg atgccattta tgagcaacgc 10920 ctacatgtgt ccgttgtcgc tgacaaatat gcaaacacca caggagctct gcagagcttc 10980 aactgggaga actggccccg ggaaaacgag aattgtacta ttgaggcgaa tccaagctcg 11040 gtgtgcgggc aaggtcgcat accgttatac tctgcagtga tccagtcagt cgatgagatc 11100 tgcgcagtgg tcaaatttgc caagcaaagg aatattcgat tggtcatcaa gaatacaggt 11160 catgactcaa ctggtcgctc cggtgctccc cattctctcc aaatcctcac gaatcgtctg 11220 aaagacataa ccttccatga tgacttcgtg ccttcccaag gggatttggg aatggataac 11280 cccaacgcca gtggggtgcc tgcggtgacg ataggggccg gagtcatggt aggtgagctt 11340 tatgccgccg ctgctgctcg agggcttatt gtggtagccg gagaatgttc cacagtcggg 11400 gttgccggag gatatctcca gggaggtgga gtgtcaacag ttcttagtcc aatgtatgga 11460 ctggcggtcg atcatgttct ggaactggag gttgtgaccg cacaggtaca tggacctttt 11520 tcttaggttc tcatggagct aatgaacgca gggcgagata gtcactgcga atggatacca 11580 acatgacgat ttgttctggg ccctccgggg aggcggagga ggcacttatg gtgttgtcac 11640 caaggccacg atgcgagcat ttccagatat tccagcggtt atcccgaccg ttcacttcat 11700 ctatccacga gcaaatgatg tcttctggca agcagtagcg caggttgtgc gactcacgca 11760 atccatgtcg gttaacggaa attcgggaca gtacatagta ggtcatctgc caaattacca 11820 ttggtatgtg aattggacaa tgtttgtctg ggacgacacc gaatcagaat tggttgagga 11880 acagattccg ccctttctga ggtttcttga ctggtttggt atcgagtatc aatatgagtt 11940 ggccgagtac tccaagatca gcgcattcct caccattccc aaacaggtgg acattggcgg 12000 gatcggatac ctgcaaagca gcgtagtgat atccgaatca ttcatgaata gcaccgccgg 12060 cgcttcaaga ctgacagcat ccttttccaa gttgatgttg gaccctgggg cactgatcac 12120 ggtcaatgtg ctaggggggc agattaacct caacgccaag gacgaggacg catctgtcaa 12180 tccgctgtgg cggtcatcgt ccctccttgt agtcctgatg caatcattcc cgcccacacc 12240 cgaagctcaa tcagccgcac atcaaacgct gtcccagacc aatacaccca ttctcgcctc 12300 catcgatccc gagggaggtg gtgtctactt caacgaggca gaccccgatc agagtgactt 12360 ccagaatgct ttctggggtc atcattatgg ccgattgcgt cgaatcaaga gccgatggga 12420 tccggccggg ctgttcgtgg tgcggaatgg agtcggtagc gaggactggg atgttgagag 12480 tatgtgtaga aaggagacaa tggtaccggc ctaggcaaat caaagtatgc gagaggagtt 12540 catgccattg tagtaggctg gcgctctcat ccgaagccaa gttactatag atttaggaaa 12600 accagtggct tcgggtctac aacaatggga tcgatggaat gcggaacttt agcacatggc 12660 ttgaacagct tgttgtggca ctggccagat ttcgttcccg gctgagtccc aactatgcag 12720 atccttgcgc gatctgtgca gatggaggga agtgtactct gtatacgaga agatgctaga 12780 tccatcaaag tttaaagttc caaggggggg ttgtgctctt tggttcgtga tactggaacc 12840 aggaatccgg ggtaaagcaa aagagacagg gaaaggttgg acctcggggt agctcatatc 12900 tattttgggt atctttcgga cgagacggcg gaagaacaag ttcaagacag tcaataggag 12960 acgagggggc aagggagttg aaccgacagt ccagggaaat tagacgagga gagcgggtga 13020 accatgtgac cctcgcaaat accaaatacc agaccaccag ccacagtctt ggctgagttc 13080 ggctattgga agacccgatg aaccagccgg ggagaaccag agcagcgggt tattcggtac 13140 gctaaagtat gcgcccatga ttacttactt agtccagtag gtctggtacc tgctgggaga 13200 cccttaacac cgccccccca cggagtttgt gtctgccggt ccagaggccc aagcctgcaa 13260 aagttgccca gaggcgccgc cgcagcaaat gccaggttcc ccgaacacag gcaggcaggc 13320 aggcgggttc aaccccggac ttcttcctga ctagtcccag cgaagtcttc caaccacttt 13380 cccctccccc catctcccac ccccccgact ccataatcca ataatctagt cccttctctt 13440 ccttcgcttc tcctcttccc ttctctccgc tcgctctctg tcgctcttct ttcgcctccc 13500 cgctcctttc cctatttcat cttcttttct ctctttttag tccctcaatc ttttggaatt 13560 gacaaccaac ccccacgtcc gggtgttaac ggctttcttt cttttactct attctttcct 13620 ctactggccg tcatctttct ttcactgttc gttctgattg ctccttcagc gatacgatta 13680 aaatagacct tcagtggcgc cgctccaaaa ccttccgatc cttccccttg tcgcccttga 13740 agacgtcctc tcccccttca acttgcgacg aacggtgcga acaatcactc aacatcgcca 13800 ccagagtctc ttttcctccc actagcgttc tgcccttgac ttcagtattg agaagttggc 13860 gcttgtgtgc gtttcatggc tgtcctgtaa aacggacgct gcgcctcact tgaagaaggc 13920 taatctggca cctaggaggc tccagagact ccttgcgatc ggctggccag tcattcgatt 13980 gggaagagaa ggatgcaaag gaagacgtgg tttggcttca caagtacttc tgcttcgtct 14040 tatttttttg cttgttggga cgtataggcc gatttgctgg actgcgacac cgatttgaca 14100 tggcgctacc ttctaaaccc gtcgcaatcg gaatctacaa ccggcctact gcccttgtcc 14160 tctgaccatt tcctgggaag gtggatgtaa aactactgtg tcagcctgac cttgtgatcg 14220 aggtcaccga tccccaaaga tgtgggattc tctttccaaa ccgcccgagg gcctcgttgg 14280 aggttatcag ggtggtagca tggccatcaa gattatgatg gcagtcttct gtgcaattgc 14340 tttgtataat gctgtggaac tcgtcattct cattttcctc accttcactc gctacagcgg 14400 tctctatttc tgggccatgt tgctctccgc cgtgcttggc gtcatccccc aagcaatcgg 14460 ctttctgcta tagttcttcg ctatcgggcc tctctggttt gcagtcacct tttctacaat 14520 aggcttttac ttcatggtcc ccggccagtc catcgtcctc tactcccgac tccacttggt 14580 cgtacagagc caaacgctgc tgcggcgggt gctgtacctg attatcttcg acacgattgt 14640 cctacttatt ccgacgactg tgctcaccta ttgcacgatc tatgtccgca ccacgcccgt 14700 gattcggggg ttcaatgtga tggagcgaat gcagctggct tggttttgcg cacaggaaat 14760 tctcatctcg ctcatctaca tcgccgagac tttgaagctg ctacgtttgc ggcccgaaaa 14820 ggacgctgaa cggcataaga ccatgtatga attaatagcc atcaacctgg tgatcattct 14880 cctagatatc gcgctcctgg ttctggagta tgtcggactc tacacactcc agaccacctt 14940 gaaggctgca gtctacagtg tgaagctgaa gctggaattc ggcgtcctga ggaaactggt 15000 ttcactggtc catgcccgcc cggcggagtc gagctcctcg gatcaggaca cctacccgac 15060 atttgttgat cccaaccaga tcacgggaga tgtgacacgt gctgcccccg cctacagtcg 15120 acggcagtcg cagtacccgt ggaccgccat ctccatggac agcctggtcc tatccgatcg 15180 ccgaagtcag catgtcacct catcggaaat agaacggcct tcctgacctt cgaattcatc 15240 tccgtgccgc aaaccttggc tgcatgtata tacaatctca ggctgtgata tatctcacac 15300 cagggctaca ccgatactga tatcgggtac cagtccgcag agaacggcct ctgccctggt 15360 gaagggcccg ccacccaagc aggtttcccg tgcattgtac agcaaatggc cgggaatgcg 15420 ggaaatgtgg ctgcagcgat ggctaggttc gcccatacat ggctgcccgg accagagtct 15480 tgtcactccg atcccatgta aaaaccatgt atacgtcatg accattattc ctgtatatac 15540 tacatctgta cataaactat tatcatgcta cgatagatga tcactcatgt gtacgtatac 15600 cttgttcgga cgtaggtgga tgaccgggcg gctcgaaggt tcagatgatg gcaagacaag 15660 cacagtaagt agtagtgccc cgtagatccc cgtagacagc catagagcgt gtccgcaggg 15720 ccctgaacga gcccggccga aagagaaaat cgcctctggt gggtcggaac tagtccgacg 15780 tcccggaaaa ttggaactat cgtcacccgc agcactggcc aagcaaccgg gcgattcgtg 15840 agatagctcg gacccgtgca tgagataggt gcggtacgtc ggcaagctag tggttatggg 15900 cgtggaccag tccgagccaa atggagtcca gagaggagcc cttaatgagg tatcatatag 15960 tctagttccg gtatccgtca tgagaagcgg agtccagtgg ctcgccaggg gcgtcacctg 16020 cgtaatgggg gaactcttgg gtccagtaaa tggggaagcc tgtatcctgc ttattggggg 16080 tttcttatgc ggcctgacgg tcaatgtgcg aatcatggaa gggcgcatac accgaaggat 16140 agcccaagcc gacagggccg attattgaat cggactgata gggggaaagg gagtctccac 16200 ctggcagctg cgacggggtt aaccttacat gcagtcaaat acttttctta gaaagaaaga 16260 ctcttcgaag aaagaatcgt acctgattcc tgggagtcgg atgcaatggt acgtggcgct 16320 gtcactgcca gtgccactga actttccgac caggatgaat tcattgttgt cattgttgtt 16380 gaacggttgc ttaaagctac ccaattattt gggatgaaca tgactaactg gcctgtaacc 16440 ctggaggact gcgatgatgt catcaacagg tcaacttcaa tctctggaac gagacgttca 16500 cggagaggtt gtctgaaggt ttcatctcac tctaaattat tatccgggtc gataagtttg 16560 ggaggtgtgg taggtgaacc ctggccccaa tgctgtcaca cttttgtact ttcatcatta 16620 ctgactcgga agatactgtg atcataggct gactgactga gttagccatc caggtactgt 16680 gctaacttga tgaggaatgc agagatcaac tggcaaaatg caaggctagc ctggaaacgg 16740 cactcgtcac gggttttgca gggctgtgat tggcagggac actacccgat cgtggtgaat 16800 cgcgggctgg aattcatctt ttttcccagt cgggcgggac gtccagtgga gggatcaccc 16860 gcgctgctga ttggtccctg ccaacttttg gccaccaacg gctggccgct aaccccaaag 16920 aaggcatccg gccatcgctt acccgctcca tctggcagtc caacccatgg ggaacgacag 16980 agagtccgtc cctcatgaaa ttgattcttt ttcctcctcc tctgactgct ccatctgcct 17040 gtttcttcgc tagaaaccct cgcttaaggg gcgtttggat tcccgaatac cttacctctc 17100 ggtcggtaac cgggctccat ctgactgttc gggcattgcg acaaactaaa tcacctttcg 17160 ccgctgcgac catctatata gtggtagtat attactcctt actatcagcc cgcctgccac 17220 cacacccctc cgccccccgg gtctcagcct ccccgtcttc acctactgtt agtatgtgtt 17280 ttggtttatc ttccccgtct ggtcgagtat agtggcaact actagctact acattgatcc 17340 agcctgccaa gtcaccgcta acccctcgtc agtatactcc agactcatcc ccatatcctc 17400 cgctttgtcc taccccgcgt catcttgtgc gtcgagtatc ccattgcggt tccgttcccc 17460 ctatcgagca gttcagcccc gcaagctatc tagagccacc gaccttgata tctcttcaca 17520 gtcacttggg agagcgtcct tttattcgga tgggaatcat acgtttcaca tcgcccatgt 17580 cacccagttg aaacgattca caccaatgtc cccttgacac tggtggagaa tacacagttt 17640 cctaccggac cactgttcct ctccccccct agtccgaaaa tggattcgca caatgccccc 17700 gcctcctcgg cgggccgggg cacggatttt gatcctcgca ctcctggagc tcacgaagga 17760 accccggttt cagatcaagg ccacaatacc tccatggatg gtgcaactgt aggcggcacg 17820 gaccgagtat atcctattcg gtcaatcatt tccttcaacc ccgctgctac ggatcccaat 17880 cagcaaggta taccgaatga aatccgttcg ccgcgaagtg gtgctcgctc ttattcaatc 17940 atcgacgccg atacctggga ccaattgagt tcgcagccca ctagttcgcc gcataccaac 18000 ccttctccta atgcgcctgt tcatacgccc gagtcgaccg atcggctctc gcagcagcaa 18060 tctcctaacg tcttctcacc ggcctcgagc gctgccgagc gagacgctcc gccggacgaa 18120 agctccacgt acaggaaggt ggcaccggaa gagggccatg cgagccttgt tacttcgcga 18180 ttccagcacg tggttacggc ggcgggtcat gctgtcatca caggcaatac acctgattcc 18240 tttcgggcct gtgaagacga accaatccac atcccgggcg ccgtgcaaac ctttggcgtc 18300 atgctcgttt tgcgcgagac acccgagggt tctttagcgg tccatgtagc gagtgagaac 18360 tcagaagcta ttctgggtca ctcgccaagc aacctttttg cgctggagag tttcactgac 18420 ctcctgcaag atgatcagac cgacatcctc ctcgatcaca ttgacttcat tcgagacgat 18480 ggatatgatc ccgttagtga tggcccggag gttttcattc tggctgtcaa agaccgattc 18540 gggcggcctc ggcgcttttg gtgtgccatt catgttaata ccgctcaccg ggatgtgatc 18600 atttgtgagt tcgaattgga agacgaccgc atcaatcctc tcaacgttgc tggacgcacg 18660 acacctacat ccccgacagt gactctgggc tttgagccaa ccccagatca attagcaagc 18720 agcactgtga acattagcca gccgttacga gtgcttcgga atgcacgcag aaggaggggt 18780 gaagcagccg ccatggaggt gttcagtatt gttagtcaga tccaggatca gcttggtgat 18840 gcccaaaata tggacgcctt gctcaacatc acgattggca tagttaaaga gttgactgga 18900 tttcaccgcg tgatgatata tcagtttgat agtgaggcca acggagatgt ggtggcagaa 18960 ttagtcgaca caagaatgac caaggacttg tataagggat tacatttccc gtcaacggat 19020 atcccaaagc aagcccgcga cttgtatcgt ctcaacaaag tgcgcatact ctacgaccgt 19080 gaccagatga gctcacggtt ggtgtgtcga ggcatcgagg atctcaagac acctctggac 19140 atgacacatg cctacttgcg tgcaatgtcg cctatccaca tcaagtactt ggcgaacatg 19200 ggggtccgtg cgtccatgtc gatcagtatc aacaacacgc atgatctttg gggtctgatc 19260 tcctgtcact cctatggaga caccggcatg agggtacctt tcccaattcg gaaaatgtgt 19320 cggttgatcg gcgatacact ctcacggaac attgagcgtc tctcttacgc atcacgtctt 19380 caggctcgca agcttctcaa cactattcct acggatgcca acccctcggg ttatataatt 19440 gcctcatcgg atgacttgct gaagcttttt gatgcggact atggcgcatt gtcaattaga 19500 ggggagacta aaatcctcgg gaagtcaacc gagtcacaag agatgctggc tttgttggag 19560 tttctcaaga tccgccagct caattccgtc gttgcgtcgc atcacgtgaa gaaggatttt 19620 ccagacctgc gttatccgcc gggcttcaag gagatctcgg gcatgttata tgtgcctcta 19680 tcggccgatg gcaaggactt tatagtcttc ttccggaagg gcgagctgac gcagatcaaa 19740 tggggtggca atccttatac gaaacttctg cagaatggtc acctcgagcc tcgcgcaagt 19800 ttccaggtgt ggactgagac agtgatggac cgggctcgtg aatggtccga atcggaagta 19860 gagactgcag ccgtcttatg cctggtctat ggcaagttca ttaaagtgtg gagacaacaa 19920 gaggctgctc tggaaggttc gcagttgacg aagctgcttc tggccaattc ggcccatgaa 19980 gtccgaactc cgctgaatgc cattgtcaat tatctggaaa ttgctctaga aggtgccttg 20040 gacacggaga ctcgcgacaa tcttactaaa tcatactccg cctccaaatc attgatatat 20100 gtcatcaacg acctattgga cctgaccaac accgaaaagg gacacaatct gattaaagat 20160 gaaccctttg atctgccctt gtgtttcaag gaagcgaccg ccatgttttc cggcgaggcg 20220 caccggaaag gaattgagta tactgttcac gcccatcccg gtctcccaaa gaccgttttg 20280 ggcgatgaac ggcgcgttcg gcaagcaatt tcaaatctaa tctcgaatgc cattcagcat 20340 acatctacgg gtggcgtcac tgtcgaaatg tggcgggctc ctggcaatcc ggagcctggg 20400 tttgcaacca tacacatgac agtgcttgat acggggactg gaatgtctga cgctatgctg 20460 gagacgatgt tccaggaact ggagcaggtc tcctcggagg acgacagcta ctttttcgac 20520 cgaggtccga acaatgactc gcagcatacc gaggttgaac gcgggaaagg tgtcctcgga 20580 ctggggctcg ctttggtgtc tcgcatcgta cggaataccc acggtcagct cacggtgcgg 20640 tcggaggagg gcaagggtag ccgcttccag atctcgctac agttttctac tccagacgat 20700 acgggttccg accaacccga aaccccacag ccgtccacgc aggagggtga tgccactcct 20760 tttgaggcca aggaagagtt tattttagtc gacagcagct cgtctgcacc aagtgatgga 20820 tggcgacgta gtggtagcca tcgcggcacg attagcccgt ctgcagatga actggacgcc 20880 aaactggtag cagaggattc tattgatcgt acgaaagacg aagctgctgg tctgcttccc 20940 tcttcagatc gccgaaaact cgtcacgctg ccttcaaccc ctgaaaggtt ggatgatgtc 21000 acacgtgcct tgcagcagaa cgtgcagaat ctcgccatat ccgacaaacc agcaattact 21060 agtgcaggcc ctgcaggacc cgctccaacg agtgctcccc ctgccgaatc agacgccaaa 21120 gccccacctg gcaagtaccg cgttcttgtg gctgaagacg accctatcaa tggcaagatt 21180 gtacagaaga ggcttggaaa gctaggccac accgttcaac tgacagtaaa cggcgaagaa 21240 tgcgcagctg cataccgggc cgattctgcg caatttgacg tcgtcttgat ggacatccag 21300 gtgagttccc tgccaagttt ttatcattat aggcgcgcta atgtgggcta gatgccgatc 21360 gtggatggta tcaactcgac caagatgatc cgcgaatttg agacttcgtc tgattcgacc 21420 gcgctctctt cggtcgcaaa gttgaacaat cggatcccta tatttgcagt ttctgcttct 21480 cttctagaga aggacatgtc cttatatgtc gatgcaggct tcgacgggtg ggtcatgaag 21540 cccatcaact tcaaccggct caatgtcctt ttggaaggcc tccaaacggg ggatacaaga 21600 aattctgcca cgtatcatcc tggctgtgac tgggaacaag gcggctggtt cacgcctatt 21660 cctgaagaaa agcagtagta cacgcttttc tgccttccgc ttatcatcat ccatcgctcc 21720 cctcccttct catccgcaaa ataacgaatc tccacaccag agaaattctg ttgtgtcttt 21780 cttgtcatgc attttgagcg catgattatc tccacctagc ttacagaagc acacaaaagt 21840 cacgaccgcg acatgacgaa agaaaatgaa tgatcggcat tttacgtgtg ttcgacctga 21900 ttgaagcctt gtcttgtgaa aattctacat tactttgtcc atgtataccc cattagttga 21960 tttgtctagg ctcatatctt tgtgttttga actcatggga tctgcgtcct tcatctatca 22020 tggcctggtt ggttggtctg gttttatgca ttttatgtta tctctaatgg tctatgagca 22080 cacgtacagc catatagcaa ttggttcggt ttactatcta tttatttctt acaaggattt 22140 tctgttttgg ttctactggg tagggttcgg gtttatcctg gtatcttttg agcgactttc 22200 ttgctggatg tcgatcagac ttcgacctgt tcattactgt tgtatatcaa atcacaaaca 22260 cacgtattat gactcttact agaatgacta ctacgtaagt agtactataa tatgtacgag 22320 ggcttaagaa gaattaccgc aaacatccaa tgtaaaactc cttaatagta tcacaatata 22380 tctagcaaag atgctagtac ttgacatgac atcattcatc acgcaatcat acccaaaaaa 22440 aaacagccaa agcagttccc aagtcattaa actgatccct atctatacca ccgacatccg 22500 ccgactaaca ccaaacacca ctaccaccct ctaaatccgg catctcctgc accaaatgcc 22560 ccaccgaatg agccagcggc ggctccgcca cagacacaat cgtatcaaca gacccaatcc 22620 tgttcctagt ataccactct ttatccctcc cctggacacc caccggactt tcatcccggt 22680 cactaccaca atccttcgtc tccacagccc caagaccccc agacatagtc gacgcagaag 22740 aataagtaga agtaataagc ggctgcgcac tccccctcct cgagtcacca ccaccaccac 22800 ccccatgaat cgaatacaca cacctcggct gtcgcgacgc accaacaaac ccaacgagcc 22860 tccccaccgc cacaccctca acgaggacct tggtactaac cacgaatggg aagaaagcca 22920 tcgccgcggc gttgtgaaca gtatacacgg ccacgatgtt ggctatgttg aggatgaggg 22980 agatgcagcc tgctacgagg agggtggagc agattcgttg tctgtcttgg tgggttgatt 23040 catagtggaa gtggtgtata acaggtcgga ggtatttgat cacaccccag gtatagacag 23100 ccaggaggag tatttctcgc gtgcagtacg ccgtgacgga gatccgtgag aggattgtga 23160 ctgcgtgcgt ccagtggccg tctttgtaga gggtggctgc ggcgggagcg acgatcacgt 23220 gggggagttg gaagagtagg atggttgcta ttatggtgga gaggaggatt cgttgaatcc 23280 ggagctggaa gtgggcttga gggcgttggt ggattgttat tagtgggagg gagaagtaga 23340 ggaggagggt gttggtgatg ctggctgctg tggtggtgag gacgaagagg atggctgagg 23400 cgatgcgggt gggtgtgtgg gtgtggtgga agaggaggag gatgcagaag gtgctggaga 23460 ggagggtggt ggtggtggtt gttaggaggg tggtggttgg gactgttaga gggcggggtt 23520 tcgtggatgt ggatgtggat gttgttgtga agaaggagag gtcgaagatg aggtagtaga 23580 ggaggagaca ggtgaaggtg gagatggaga tgagggatat cgcggtgtag ctgtctgcgc 23640 gggggagggt gtagtaggat gctatagctg tggtggtggt ggtggtgttc atggcggttg 23700 tttggtcatt gcgtggttca aggataaggg gtagggttcc atggagagat gtgataggaa 23760 gtatataagg tatgggtttg atgtgaggtc tatgctatgg gtttgagtat aacaaagact 23820 cgacttgaat gtgtgtagtt caacagatga agttgaaagt cctatatccg aaccagatgt 23880 ggatggagga gaaaacatct ccggggctgc atagaactaa ccctcaacct cagataaagt 23940 tctgatatgt tcatcgtcgg atccttggtt gagagcggca cctgcaaggg tctggagccg 24000 ccgctgcgga gctgcagagc tacaaacaaa gcaaggattc tcgaggccca cgggagatcg 24060 tcgtgttggt ttgcagcaac aaaagtgggg gacagctgag agcagttcat ccacttgttg 24120 atcagttggt cgcaaggtgg aatattttgg tcaggagatg taagccgaac tagtagttgc 24180 ttgtgcatca cggagtgaac tgatgcttgt tttgtgctga ctgtcggcgg catactagta 24240 ccttgatgct atagtccccg agaaaccatg atactcctct atagagctat tagatgtatt 24300 gtggaggcag ttccatgagt ctggggatgc gcacagacaa atttgaacag agtcaccctc 24360 ggttgagcaa cggaggagat gtccggggac tcggatccgg agacggacag gaaagtcatg 24420 gccctcggat gacttgggcc gccagataag gtttcttgtg ggcctgctgt catttcttga 24480 agaacaactt caatatactc tgctattgac tgtctccttg gcaaggcaat tagggtgact 24540 tctactgcat tgtgatggca tctactggaa cagctacagg ccctacttat catggaacgc 24600 aggatattca cttcattgta tgtatgtatg tatatcgaca tgagtaaccc gaaattcctg 24660 gcattagccc tctcataaat ctccatcgtc tttgacccct ccgaccaata tgacccagac 24720 atctatcccc tcacatcaga atccaaggtg atatgccact agaaatagcg cctagacagt 24780 gcacttgacg ctggcagcac tcagatccac cggctgcgca gcactcgggt ttccatccaa 24840 gtccacatag gtgttccggg agttcagggt ggccagaacc gatccgtatt tcgtgatcac 24900 gcagttggtg ttcgcctgga agttggtcaa ttgcgccgac gaggccttga tgactccacc 24960 ggaaccgact ccggtacctc cgtacagtgc ggagatgctc tgttcgctgc cgtcggcggg 25020 gatggcggca cttccctggg caccagtttg gtcgttggcc agggcaatgg tcacggtggt 25080 aacgacgggg cccgcagaga cagaggcagc cagaagggca atgaggacgg cactgatcga 25140 cttcatcttg agggatggtg gtgtttgttt agaagaaggt agtagtagat ggttgattga 25200 tggtgatggt ccggagacaa gtaggaatgg aatgctgctg tgttgctgga atggtccttg 25260 aaatgtcgag ggagaaggcc tgctttatac ctttgccttt cgctccttgt actgaagggc 25320 atgaatatct tgtcgaggct gtcatggggt ctctggcact tcgtatctgt cttacatcct 25380 gccgggtcgt agacaccctg ccacggcttc aggcgttcca tgactttggt tgacgtcgac 25440 tggattcacg atctgtcgca tacagccgag tgtagactaa ttcaagccga cgtcatgaga 25500 cagggtttcg ataaaagtcc ttcccggcgc cgccgagagt cgaataagag gcatccgaat 25560 ggtggattac caaatcggga cggatattta tgacatcgca tggtgggcac gtgagggtga 25620 gatgcaggtc tcaaaccttc agcatcgagt cgatgcgatg gcgagcctgg agatccttga 25680 ctctccaatc gtagaaacag cgcggcggag agctcgtgtt gttgcgtgaa tacgagaagc 25740 ccatgtcaac aggcattgca ggccgcattc gatgccggtg atggtcccta cacagtggca 25800 tgttgtcttg cggtcagtat aatgctcata atgtatgatg cttatgatct tcactggcaa 25860 tggcggattg aatgatttgc cagcccaggg aagtcgaacg attgggaagg cggagtctag 25920 gaatacgagc tggtgccgta aggcggatgc caaataaaga cgacgggaag gatgatatac 25980 tttccccgat gtaacatccc tgcgacatcg ctcaacttcc ccggacaccc cagcaattca 26040 tgcgacgggg atcgacgccg atcctaaaca tgcgtcatct tggatctcca gttcggatgg 26100 ttcggaggca tcggtgttac ccggatgttg aaagatgaac gaacgccaga aggcaaggaa 26160 ccttgcaaga tctgatgttc tctaccatat ccaagttcac tgcgacaaca tctgaacaat 26220 tactttcgcc atgggcccgg aacgatgagg cttatggttg tgggagaatc tgcgaccaga 26280 atcttaggct ggtctgtcgg acgatttggg cgcgcttacg ggcattgaag gcttggcagg 26340 ttggtacata gccaagaaaa cgacccagaa agaggaaggc cgtggggatt caatggcagc 26400 agccttgcgg cagcgtgcga gccacctggg gcagtgtcat atccgggctt ccgggctaga 26460 agatgtgtct atacagaaag ccgtatccga catagccttc cttgcgtgac tagatgactg 26520 cggcttcaac ggtgggatga tcatgattgt gtacattacc aggagttgct agaagctaca 26580 gggctgccat gacgcttcac gagaactggg tctgagacgt cgacgagtag tggtgatggg 26640 tcttgaatta cgcgaggcct ggtccaatac ctaccagatt gtcggtaatg cactagtagg 26700 tatctggggt cttctggcca gagagtggcg agctcgatga tgatattgca ggtagggaga 26760 cctccgaaga cccttgctta gatgcaccga gggtgaacat ccacacgcta tgttgcggaa 26820 cagaaccggg gatattcccg taccagagtg actagcttca tgatagtctt gaaggcaaaa 26880 ctataagact tgcaaaaagg aaggttcgcg gaagtactag gccgtgtgtc cgtcacgaga 26940 ccgaatactt tttgtagata tccgacatca gtctgactcc gaacgggtta attaacgtgt 27000 ccgcaagaag ttttggcaac tccctactca agtgtagaat ggagctgagt tctgaaacaa 27060 gcaatgagac cctgcgagtc acgtggccag cgtgactgga tgaccggacg ggagctgtga 27120 ggtccctggg caggtatgga agttattgcg cgcacactta aacacctaat ttgatcagat 27180 ccaccccggt tggccttgga tttatatgaa tgaggtgtcg tccagcgttg gatgcggaga 27240 ctatcagaac ggcgatggag |