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EBI DbfetchID AM270075; SV 1; linear; genomic DNA; STD; FUN; 371827 BP. XX AC AM270075; XX DT 28-JAN-2007 (Rel. 90, Created) DT 24-MAR-2007 (Rel. 91, Last updated, Version 3) XX DE Aspergillus niger contig An04c0140, 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 1-371827 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 1-371827 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 183524-186233 RX DOI; 10.1073/pnas.89.15.7013 RX PUBMED; 1323123. RA Heller L., Orlean P., Adair Jr W.L.; RT "Saccharomyces cerevisiae sec59 cells are deficient in dolichol kinase RT activity"; RL Proc. Natl. Acad. Sci. U.S.A. 89(15):7013-7016(1992). XX RN [4] RP 283359-285593 RX DOI; 10.1007/BF00172186 RX PUBMED; 1368015. RA Orum H., Rasmussen O.F.; RT "Expression in E. coli of the gene encoding phenylalanine ammonia-lyase RT from Rhodosporidium toruloides"; RL Appl. Microbiol. Biotechnol. 36(6):745-747(1992). XX RN [5] RP 48065-49270 RX DOI; 10.1016/0167-4781(92)90164-U RX PUBMED; 1420310. RA Fujita T., Shirasawa T., Uchida K., Maruyama N.; RT "Isolation of cDNA clone encoding rat senescence marker protein-30 (SMP30) RT and its tissue distribution"; RL Biochim. Biophys. Acta 1132(3):297-305(1992). XX RN [6] RP 48065-49270 RX DOI; 10.1016/0304-4165(92)90108-7 RX PUBMED; 1581340. RA Fujita T., Uchida K., Maruyama N.; RT "Purification of senescence marker protein-30 (SMP30) and its RT androgen-independent decrease with age in the rat liver"; RL Biochim. Biophys. Acta 1116(2):122-128(1992). XX RN [7] RP 40605-42228 RX DOI; 10.1016/0378-1119(92)90505-J RX PUBMED; 1644309. RA O'Connell M.J., Kelly J.M.; RT "Cis-acting control elements 5' to aldA, the aldehyde RT dehydrogenase-encoding gene of Aspergillus niger"; RL Gene 117(1):151-156(1992). XX RN [8] RP 283359-285593 RX PUBMED; 1773059. RA Rasmussen O.F., Oerum H.; RT "Analysis of the gene for phenylalanine ammonia-lyase from Rhodosporidium RT toruloides"; RL DNA Seq. 1(3):207-211(1991). XX RN [9] RP 347725-348503 RX DOI; 10.1073/pnas.88.4.1416 RX PUBMED; 1847521. RA Bertocci B., Miggiano V., Da Prada M., Dembic Z., Lahm H.W., Malherbe P.; RT "Human catechol-O-methyltransferase: cloning and expression of the RT membrane-associated form"; RL Proc. Natl. Acad. Sci. U.S.A. 88(4):1416-1420(1991). XX RN [10] RP 361215-364591 RX PUBMED; 2072900. RA Repetto B., Tzagoloff A.; RT "In vivo assembly of yeast mitochondrial alpha-ketoglutarate dehydrogenase RT complex"; RL Mol. Cell. Biol. 11(8):3931-3939(1991). XX RN [11] RP 348721-349512 RX PUBMED; 2108124. RA Honjo M., Nakayama A., Fukazawa K., Kawamura K., Ando K., Hori M., RA Furutani Y.; RT "A novel Bacillus subtilis gene involved in negative control of sporulation RT and degradative-enzyme production"; RL J. Bacteriol. 172(4):1783-1790(1990). XX RN [12] RP 361215-364591 RX PUBMED; 2503710. RA Repetto B., Tzagoloff A.; RT "Structure and regulation of KGD1, the structural gene for yeast RT alpha-ketoglutarate dehydrogenase"; RL Mol. Cell. Biol. 9(6):2695-2705(1989). XX RN [13] RP 40605-42228 RX DOI; 10.1016/0378-1119(89)90152-2 RX PUBMED; 2606357. RA O'Connell M.J., Kelly J.M.; RT "Physical characterization of the aldehyde-dehydrogenase-encoding gene of RT Aspergillus niger"; RL Gene 84(1):173-180(1989). XX RN [14] RP 183524-186233 RX PUBMED; 2657387. RA Bernstein M., Kepes F., Schekman R.; RT "Sec59 encodes a membrane protein required for core glycosylation in RT Saccharomyces cerevisiae"; RL Mol. Cell. Biol. 9(3):1191-1199(1989). XX RN [15] RP 11394-13304 RX PUBMED; 2777793. RA Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., RA Ikeda Y., Kraus J., Tanaka K.; RT "Molecular cloning and nucleotide sequence of cDNAs encoding the precursors RT of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and RT isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of RT the acyl-CoA dehydrogenase family"; RL J. Biol. Chem. 264(27):16321-16331(1989). XX RN [16] RX DOI; 10.1016/0378-1119(95)00272-8 RX PUBMED; 7557402. RA Saupe S., Turcq B., Begueret J.; RT "A gene responsible for vegetative incompatibility in the fungus Podospora RT anserina encodes a protein with a GTP-binding motif and G beta homologous RT domain"; RL Gene 162(1):135-139(1995). XX RN [17] RP 73923-74951 RX DOI; 10.1016/0378-1119(94)00900-D RX PUBMED; 7698655. RA Murray J.S., Wong M.L., Miyada C.G., Switchenko A.C., Goodman T.C., RA Wong B.; RT "Isolation, characterization and expression of the gene that encodes RT D-arabinitol dehydrogenase in Candida tropicalis"; RL Gene 155(1):123-128(1995). XX RN [18] RX PUBMED; 8007987. RA Chang Y.C., Kwon-Chung K.J.; RT "Complementation of a capsule-deficient mutation of Cryptococcus neoformans RT restores its virulence"; RL Mol. Cell. Biol. 14(7):4912-4919(1994). XX RN [19] RP 218034-220381 RX PUBMED; 8035831. RA Mitsui K., Yaguchi S., Tsurugi K.; RT "The GTS1 gene, which contains a Gly-Thr repeat, affects the timing of RT budding and cell size of the yeast Saccharomyces cerevisiae"; RL Mol. Cell. Biol. 14(8):5569-5578(1994). XX RN [20] RP 68447-69500 RX PUBMED; 8175708. RA Kelleher D.J., Gilmore R.; RT "The Saccharomyces cerevisiae oligosaccharyltransferase is a protein RT complex composed of Wbp1p, Swp1p, and four additional polypeptides"; RL J. Biol. Chem. 269(17):12908-12917(1994). XX RN [21] RP 164389-166989 RX PUBMED; 8196608. RA Lockhart S.R., Rymond B.C.; RT "Commitment of yeast pre-mRNA to the splicing pathway requires a novel U1 RT small nuclear ribonucleoprotein polypeptide, Prp39p"; RL Mol. Cell. Biol. 14(6):3623-3633(1994). XX RN [22] RP 283359-285593 RX DOI; 10.1016/0378-1119(94)90598-3 RX PUBMED; 8200528. RA Faulkner J.D., Anson J.G., Tuite M.F., Minton N.P.; RT "High-level expression of the phenylalanine ammonia lyase-encoding gene RT from Rhodosporidium toruloides in Saccharomyces cerevisiae and Escherichia RT coli using a bifunctional expression system"; RL Gene 143(1):13-20(1994). XX RN [23] RP 177781-181059 RX DOI; 10.1016/0014-5793(93)80398-E RX PUBMED; 8224160. RA Tsukada M., Ohsumi Y.; RT "Isolation and characterization of autophagy-defective mutants of RT Saccharomyces cerevisiae"; RL FEBS Lett. 333(1-2):169-174(1993). XX RN [24] RP 11394-13304 RX DOI; 10.1016/0167-4781(93)90015-6 RX PUBMED; 8268228. RA Hainline B.E., Kahlenbeck D.J., Grant J., Strauss A.W.; RT "Tissue specific and developmental expression of rat long-and medium-chain RT acyl-CoA dehydrogenases"; RL Biochim. Biophys. Acta 1216(3):460-468(1993). XX RN [25] RP 270281-272133 RX DOI; 10.1104/pp.102.4.1147 RX PUBMED; 8278545. RA Uhlmann A., Ebel J.; RT "Molecular cloning and expression of 4-coumarate:coenzyme A ligase, an RT enzyme involved in the resistance response of soybean (Glycine max L.) RT against pathogen attack"; RL Plant Physiol. 102(4):1147-1156(1993). XX RN [26] RP 361215-364591 RX DOI; 10.1007/BF00351844 RX PUBMED; 8299151. RA Mockovciakova D., Janitorova V., Zigova M., Kaclikova E., Zagulski M., RA Subik J.; RT "The ogd1 and kgd1 mutants lacking 2-oxoglutarate dehydrogenase activity in RT yeast are allelic and can be differentiated by the cloned amber RT suppressor"; RL Curr. Genet. 24(5):377-381(1993). XX RN [27] RP 350279-351530 RX PUBMED; 8335636. RA Yamagata S., D'Andrea R.J., Fujisaki S., Isaji M., Nakamura K.; RT "Cloning and bacterial expression of the CYS3 gene encoding cystathionine RT gamma-lyase of Saccharomyces cerevisiae and the physicochemical and RT enzymatic properties of the protein"; RL J. Bacteriol. 175(15):4800-4808(1993). XX RN [28] RP 48065-49270 RX DOI; 10.1016/0014-5793(93)80998-A RX PUBMED; 8348951. RA Shimokawa N., Yamaguchi M.; RT "Molecular cloning and sequencing of the cDNA coding for a calcium-binding RT protein regucalcin from rat liver"; RL FEBS Lett. 327(3):251-255(1993). XX RN [29] RP 68447-69500 RX PUBMED; 8428586. RA te Heesen S., Knauer R., Lehle L., Aebi M.; RT "Yeast Wbp1p and Swp1p form a protein complex essential for oligosaccharyl RT transferase activity"; RL EMBO J. 12(1):279-284(1993). XX RN [30] RP 350279-351530 RX DOI; 10.1002/yea.320090409 RX PUBMED; 8511969. RA Ono B., Ishii N., Naito K., Miyoshi S., Shinoda S., Yamamoto S., Ohmori S.; RT "Cystathionine gamma-lyase of Saccharomyces cerevisiae: structural gene and RT cystathionine gamma-synthase activity"; RL Yeast 9(4):389-397(1993). XX RN [31] RP 341567-342945 RX DOI; 10.1016/0378-1119(95)00654-0 RX PUBMED; 8566773. RA Pishko E.J., Kirkland T.N., Cole G.T.; RT "Isolation and characterization of two chitinase-encoding genes (cts1, RT cts2) from the fungus Coccidioides immitis"; RL Gene 167(1-2):173-177(1995). XX RN [32] RP 341567-342945 RX PUBMED; 8675298. RA Yang C., Zhu Y., Magee D.M., Cox R.A.; RT "Molecular cloning and characterization of the Coccidioides immitis RT complement fixation/chitinase antigen"; RL Infect. Immun. 64(6):1992-1997(1996). XX RN [33] RP 345449-347168 RX DOI; 10.1016/0167-4781(96)00042-5 RX PUBMED; 8679704. RA Akiyama M., Nakashima H.; RT "Molecular cloning of the acr-2 gene which controls acriflavine sensitivity RT in Neurospora crassa"; RL Biochim. Biophys. Acta 1307(2):187-192(1996). XX RN [34] RP 356742-359870 RX DOI; 10.1073/pnas.93.16.8419 RX PUBMED; 8710886. RA Lambrechts M.G., Bauer F.F., Marmur J., Pretorius I.S.; RT "Muc1, a mucin-like protein that is regulated by Mss10, is critical for RT pseudohyphal differentiation in yeast"; RL Proc. Natl. Acad. Sci. U.S.A. 93(16):8419-8424(1996). XX RN [35] RP 221088-223743 RX PUBMED; 8861954. RA Takahashi M., Inoue N., Ohishi K., Maeda Y., Nakamura N., Endo Y., RA Fujita T., Takeda J., Kinoshita T.; RT "PIG-B, a membrane protein of the endoplasmic reticulum with a large RT lumenal domain, is involved in transferring the third mannose of the GPI RT anchor"; RL EMBO J. 15(16):4254-4261(1996). XX RN [36] RP 60597-62111 RX PUBMED; 8865587. RA Wodzinski R.J., Ullah A.H.; RT "Phytase"; RL Adv. Appl. Microbiol. 42:263-302(1996). XX RN [37] RP 174426-176352 RX DOI; 10.1006/jmbi.1996.0529 RX PUBMED; 8893857. RA Isnard A.D., Thomas D., Surdin-Kerjan Y.; RT "The study of methionine uptake in Saccharomyces cerevisiae reveals a new RT family of amino acid permeases"; RL J. Mol. Biol. 262(4):473-484(1996). XX RN [38] RP 297026-298750 RX DOI; 10.1016/0378-1119(96)00153-9 RX PUBMED; 8917102. RA Hatamoto O., Watarai T., Kikuchi M., Mizusawa K., Sekine H.; RT "Cloning and sequencing of the gene encoding tannase and a structural study RT of the tannase subunit from Aspergillus oryzae"; RL Gene 175(1-2):215-221(1996). XX RN [39] RP 299170-300783 RX DOI; 10.1016/0378-1119(96)00172-2 RX PUBMED; 8917108. RA August P.R., Rahn J.A., Flickinger M.C., Sherman D.H.; RT "Inducible synthesis of the mitomycin C resistance gene product (MCRA) from RT Streptomyces lavendulae"; RL Gene 175(1-2):261-267(1996). XX RN [40] RP 229353-231053 RX PUBMED; 8955402. RA Wright M.B., Howell E.A., Gaber R.F.; RT "Amino acid substitutions in membrane-spanning domains of Hol1, a member of RT the major facilitator superfamily of transporters, confer nonselective RT cation uptake in Saccharomyces cerevisiae"; RL J. Bacteriol. 178(24):7197-7205(1996). XX RN [41] RP 218034-220381 RX DOI; 10.1002/(SICI)1097-0061(199701)13:1<55::AID-YEA48>3.3.CO;2-0 RX PUBMED; 9046087. RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., Bruschi C.V.; RT "Sequencing of a 40.5 kb fragment located on the left arm of chromosome VII RT from Saccharomyces cerevisiae"; RL Yeast 13(1):55-64(1997). XX RN [42] RP 218034-220381 RX DOI; 10.1002/(SICI)1097-0061(19970630)13:8<717::AID-YEA132>3.0.CO;2-2 RX PUBMED; 9219336. RA Bossier P., Goethals P., Rodrigues-Pousada C.; RT "Constitutive flocculation in Saccharomyces cerevisiae through RT overexpression of the GTS1 gene, coding for a 'Glo'-type RT Zn-finger-containing protein"; RL Yeast 13(8):717-725(1997). XX RN [43] RP 177781-181059 RX DOI; 10.1016/S0378-1119(97)00084-X RX PUBMED; 9224897. RA Matsuura A., Tsukada M., Wada Y., Ohsumi Y.; RT "Apg1p, a novel protein kinase required for the autophagic process in RT Saccharomyces cerevisiae"; RL Gene 192(2):245-250(1997). XX RN [44] RP 336384-337878 RX DOI; 10.1007/s004380050477 RX PUBMED; 9230902. RA Mende K., Homann V., Tudzynski B.; RT "The geranylgeranyl diphosphate synthase gene of Gibberella fujikuroi: RT isolation and expression"; RL Mol. Gen. Genet. 255(1):96-105(1997). XX RN [45] RP 309626-311491 RX DOI; 10.1074/jbc.272.42.26678 RX PUBMED; 9334251. RA Gum Jr J.R., Ho J.J., Pratt W.S., Hicks J.W., Hill A.S., Vinall L.E., RA Roberton A.M., Swallow D.M., Kim Y.S.; RT "MUC3 human intestinal mucin. Analysis of gene structure, the carboxyl RT terminus, and a novel upstream repetitive region"; RL J. Biol. Chem. 272(42):26678-26686(1997). XX RN [46] RP 18345-20736 RX DOI; 10.1006/bbrc.1997.7439 RX PUBMED; 9345280. RA Tsukamoto T., Shibagaki Y., Imajoh-Ohmi S., Murakoshi T., Suzuki M., RA Nakamura A., Gotoh H., Mizumoto K.; RT "Isolation and characterization of the yeast mRNA capping enzyme beta RT subunit gene encoding RNA 5'-triphosphatase, which is essential for cell RT viability"; RL Biochem. Biophys. Res. Commun. 239(1):116-122(1997). XX RN [47] RP 60597-62111 RX DOI; 10.1016/S0167-4781(97)00107-3 RX PUBMED; 9349716. RA Pasamontes L., Haiker M., Henriquez-Huecas M., Mitchell D.B., RA van Loon A.P.; RT "Cloning of the phytases from Emericella nidulans and the thermophilic RT fungus Talaromyces thermophilus"; RL Biochim. Biophys. Acta 1353(3):217-223(1997). XX RN [48] RP 356742-359870 RX PUBMED; 9383611. RA Vivier M.A., Lambrechts M.G., Pretorius I.S.; RT "Coregulation of starch degradation and dimorphism in the yeast RT Saccharomyces cerevisiae"; RL Crit. Rev. Biochem. Mol. Biol. 32(5):405-435(1997). XX RN [49] RP 167330-169916 RX PUBMED; 9409622. RA Teigelkamp S., Mundt C., Achsel T., Will C.L., Luhrmann R.; RT "The human U5 snRNP-specific 100-kD protein is an RS domain-containing, RT putative RNA helicase with significant homology to the yeast splicing RT factor Prp28p"; RL RNA 3(11):1313-1326(1997). XX RN [50] RP 1-3750 RX DOI; 10.1007/s004380050610 RX PUBMED; 9435787. RA Espagne E., Balhadere P., Begueret J., Turcq B.; RT "Reactivity in vegetative incompatibility of the HET-E protein of the RT fungus Podospora anserina is dependent on GTP-binding activity and a WD40 RT repeated domain"; RL Mol. Gen. Genet. 256(6):620-627(1997). XX RN [51] RP 34434-35276 RX PUBMED; 9612290. RA Kim T.S., Dodia C., Chen X., Hennigan B.B., Jain M., Feinstein S.I., RA Fisher A.B.; RT "Cloning and expression of rat lung acidic Ca(2+)-independent PLA2 and its RT organ distribution"; RL Am. J. Physiol. 274(5 Pt 1):L750-L761(1998). XX RN [52] RP 135347-136603 RX PUBMED; 9774652. RA Espinoza F.H., Farrell A., Nourse J.L., Chamberlin H.M., Gileadi O., RA Morgan D.O.; RT "Cak1 is required for Kin28 phosphorylation and activation in vivo"; RL Mol. Cell. Biol. 18(11):6365-6373(1998). XX RN [53] RP 48065-49270 RX PUBMED; 9792046. RA Fujita T., Shirasawa T., Inoue H., Kitamura T., Maruyama N.; RT "Hepatic and renal expression of senescence marker protein-30 and its RT biological significance"; RL J. Gastroenterol. Hepatol. 13(Suppl):S124-S131(1998). XX RN [54] RP 336384-337878 RX DOI; 10.1006/fgbi.1998.1095 RX PUBMED; 9917370. RA Tudzynski B., Holter K.; RT "Gibberellin biosynthetic pathway in Gibberella fujikuroi: evidence for a RT gene cluster"; RL Fungal Genet. Biol. 25(3):157-170(1998). XX RN [55] RP 356742-359870 RX DOI; 10.1046/j.1365-2958.1999.01151.x RX PUBMED; 9987114. RA Gagiano M., van Dyk D., Bauer F.F., Lambrechts M.G., Pretorius I.S.; RT "Msn1p/Mss10p, Mss11p and Muc1p/Flo11p are part of a signal transduction RT pathway downstream of Mep2p regulating invasive growth and pseudohyphal RT differentiation in Saccharomyces cerevisiae"; RL Mol. Microbiol. 31(1):103-116(1999). XX RN [56] RP 60597-62111 RX DOI; 10.1006/abbi.1999.1115 RX PUBMED; 10087168. RA Han Y., Lei X.G.; RT "Role of glycosylation in the functional expression of an Aspergillus niger RT phytase (phyA) in Pichia pastoris"; RL Arch. Biochem. Biophys. 364(1):83-90(1999). XX RN [57] RP 160199-162750 RX DOI; 10.1046/j.1365-2958.1999.01242.x RX PUBMED; 10096075. RA Amrani L., Cecchetto G., Scazzocchio C., Glatigny A.; RT "The hxB gene, necessary for the post-translational activation of purine RT hydroxylases in Aspergillus nidulans, is independently controlled by the RT purine utilization and the nicotinate utilization transcriptional RT activating systems"; RL Mol. Microbiol. 31(4):1065-1073(1999). XX RN [58] RP 60597-62111 RX PUBMED; 10223979. RA Han Y., Wilson D.B., Lei X.G.; RT "Expression of an Aspergillus niger phytase gene (phyA) in Saccharomyces RT cerevisiae"; RL Appl. Environ. Microbiol. 65(5):1915-1918(1999). XX RN [59] RP 190396-192370 RX PUBMED; 10322005. RA Hurtado C.A., Rachubinski R.A.; RT "MHY1 encodes a C2H2-type zinc finger protein that promotes dimorphic RT transition in the yeast Yarrowia lipolytica"; RL J. Bacteriol. 181(10):3051-3057(1999). XX RN [60] RP 60597-62111 RX DOI; 10.1006/abbi.1999.1184 RX PUBMED; 10328821. RA Rodriguez E., Porres J.M., Han Y., Lei X.G.; RT "Different sensitivity of recombinant Aspergillus niger phytase (r-PhyA) RT and Escherichia coli pH 2.5 acid phosphatase (r-AppA) to trypsin and pepsin RT in vitro"; RL Arch. Biochem. Biophys. 365(2):262-267(1999). XX RN [61] RX DOI; 10.1126/science.284.5418.1368 RX PUBMED; 10334994. RA Kennedy J., Auclair K., Kendrew S.G., Park C., Vederas J.C., RA Hutchinson C.R.; RT "Modulation of polyketide synthase activity by accessory proteins during RT lovastatin biosynthesis"; RL Science 284(5418):1368-1372(1999). XX RN [62] RP 135347-136603 RX PUBMED; 10373527. RA Kimmelman J., Kaldis P., Hengartner C.J., Laff G.M., Koh S.S., Young R.A., RA Solomon M.J.; RT "Activating phosphorylation of the Kin28p subunit of yeast TFIIH by Cak1p"; RL Mol. Cell. Biol. 19(7):4774-4787(1999). XX RN [63] RP 22053-23789 RX DOI; 10.1105/tpc.11.7.1337 RX PUBMED; 10402433. RA Walker A.R., Davison P.A., Bolognesi-Winfield A.C., James C.M., RA Srinivasan N., Blundell T.L., Esch J.J., Marks M.D., Gray J.C.; RT "The TRANSPARENT TESTA GLABRA1 locus, which regulates trichome RT differentiation and anthocyanin biosynthesis in Arabidopsis, encodes a WD40 RT repeat protein"; RL Plant Cell 11(7):1337-1350(1999). XX RN [64] RP 78958-80081 RX DOI; 10.1074/jbc.274.33.23185 RX PUBMED; 10438489. RA Nakano M., Morita T., Yamamoto T., Sano H., Ashiuchi M., Masui R., RA Kuramitsu S., Yagi T.; RT "Purification, molecular cloning, and catalytic activity of RT Schizosaccharomyces pombe pyridoxal reductase. A possible additional family RT in the aldo-keto reductase superfamily"; RL J. Biol. Chem. 274(33):23185-23190(1999). XX RN [65] RP 227405-228932 RX DOI; 10.1016/S0969-2126(99)80170-1 RX PUBMED; 10508789. RA Timm D.E., Mueller H.A., Bhanumoorthy P., Harp J.M., Bunick G.J.; RT "Crystal structure and mechanism of a carbon-carbon bond hydrolase"; RL Structure 7(9):1023-1033(1999). XX RN [66] RP 304150-304900 RX DOI; 10.1128/JB.182.6.1472-1480.2000 RX PUBMED; 10692350. RA Nienaber A., Huber A., Gottfert M., Hennecke H., Fischer H.M.; RT "Three new NifA-regulated genes in the Bradyrhizobium japonicum symbiotic RT gene region discovered by competitive DNA-RNA hybridization"; RL J. Bacteriol. 182(6):1472-1480(2000). XX RN [67] RP 11394-13304 RX DOI; 10.1016/S1388-1981(00)00013-5 RX PUBMED; 10760462. RA Hiltunen J.K., Qin Y.; RT "beta-oxidation - strategies for the metabolism of a wide variety of RT acyl-CoA esters"; RL Biochim. Biophys. Acta 1484(2-3):117-128(2000). XX RN [68] RP 48065-49270 RX DOI; 10.1016/S0024-3205(99)00602-5 RX PUBMED; 10809175. RA Yamaguchi M.; RT "Role of regucalcin in calcium signaling"; RL Life Sci. 66(19):1769-1780(2000). XX RN [69] RP 1-3750 RX DOI; 10.1016/S0923-2508(00)00145-5 RX PUBMED; 10875280. RA Loubradou G., Turcq B.; RT "Vegetative incompatibility in filamentous fungi: a roundabout way of RT understanding the phenomenon"; RL Res. Microbiol. 151(4):239-245(2000). XX RN [70] RP 353081-355774 RX DOI; 10.1038/78182 RX PUBMED; 10932196. RA Vervoort R., Lennon A., Bird A.C., Tulloch B., Axton R., Miano M.G., RA Meindl A., Meitinger T., Ciccodicola A., Wright A.F.; RT "Mutational hot spot within a new RPGR exon in X-linked retinitis RT pigmentosa"; RL Nat. Genet. 25(4):462-466(2000). XX RN [71] RP 1-3750 RX DOI; 10.1128/MMBR.64.3.489-502.2000 RX PUBMED; 10974123. RA Saupe S.J.; RT "Molecular genetics of heterokaryon incompatibility in filamentous RT ascomycetes"; RL Microbiol. Mol. Biol. Rev. 64(3):489-502(2000). XX RN [72] RP 135347-136603 RX DOI; 10.1016/S0092-8674(00)00083-0 RX PUBMED; 11007479. RA Chang W.H., Kornberg R.D.; RT "Electron crystal structure of the transcription factor and DNA repair RT complex, core TFIIH"; RL Cell 102(5):609-613(2000). XX RN [73] RP 160199-162750 RX DOI; 10.1046/j.1365-2958.2000.02119.x RX PUBMED; 11029694. RA Amrani L., Primus J., Glatigny A., Arcangeli L., Scazzocchio C., RA Finnerty V.; RT "Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila RT melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a RT mechanism for the insertion of the terminal sulphur atom in the RT molybdopterin cofactor"; RL Mol. Microbiol. 38(1):114-125(2000). XX RN [74] RP 314329-315228 RX DOI; 10.1271/bbb.64.1896 RX PUBMED; 11055393. RA Zhang X.Y., Dai A.L., Zhang X.K., Kuroiwa K., Kodaira R., Shimosaka M., RA Okazaki M.; RT "Purification and characterization of chitosanase and RT Exo-beta-D-glucosaminidase from a Koji mold, Aspergillus oryzae IAM2660"; RL Biosci. Biotechnol. Biochem. 64(9):1896-1902(2000). XX RN [75] RP 307082-309166 RX PUBMED; 11058086. RA Yamada H.Y., Matsumoto S., Matsumoto T.; RT "High dosage expression of a zinc finger protein, Grt1, suppresses a mutant RT of fission yeast slp1(+), a homolog of CDC20/p55CDC/Fizzy"; RL J. Cell Sci. 113(Pt22):3989-3999(2000). XX RN [76] RP 292732-294453 RX DOI; 10.1016/S0960-9822(00)00752-1 RX PUBMED; 11069113. RA Smith S., de Lange T.; RT "Tankyrase promotes telomere elongation in human cells"; RL Curr. Biol. 10(20):1299-1302(2000). XX RN [77] RP 356742-359870 RX DOI; 10.1016/S0168-6445(00)00056-5 RX PUBMED; 11152942. RA Gancedo J.M.; RT "Control of pseudohyphae formation in Saccharomyces cerevisiae"; RL FEMS Microbiol. Rev. 25(1):107-123(2001). XX RN [78] RP 347725-348503 RX DOI; 10.1097/00002826-200009000-00004 RX PUBMED; 11154093. RA Inzelberg R., Carasso R.L., Schechtman E., Nisipeanu P.; RT "A comparison of dopamine agonists and catechol-O-methyltransferase RT inhibitors in Parkinson's disease"; RL Clin. Neuropharmacol. 23(5):262-266(2000). XX RN [79] RP 227405-228932 RX DOI; 10.1074/jbc.M007621200 RX PUBMED; 11154690. RA Bateman R.L., Bhanumoorthy P., Witte J.F., McClard R.W., Grompe M., RA Timm D.E.; RT "Mechanistic inferences from the crystal structure of fumarylacetoacetate RT hydrolase with a bound phosphorus-based inhibitor"; RL J. Biol. Chem. 276(18):15284-15291(2001). XX RN [80] RP 286252-289911 RX DOI; 10.1016/S1074-5521(00)00056-9 RX PUBMED; 11182319. RA Silakowski B., Nordsiek G., Kunze B., Blocker H., Muller R.; RT "Novel features in a combined polyketide synthase/non-ribosomal peptide RT synthetase: the myxalamid biosynthetic gene cluster of the myxobacterium RT Stigmatella aurantiaca Sga15"; RL Chem. Biol. 8(1):59-69(2001). XX RN [81] RP 227405-228932 RX DOI; 10.1073/pnas.98.2.641 RX PUBMED; 11209059. RA Aponte J.L., Sega G.A., Hauser L.J., Dhar M.S., Withrow C.M., RA Carpenter D.A., Rinchik E.M., Culiat C.T., Johnson D.K.; RT "Point mutations in the murine fumarylacetoacetate hydrolase gene: Animal RT models for the human genetic disorder hereditary tyrosinemia type 1"; RL Proc. Natl. Acad. Sci. U.S.A. 98(2):641-645(2001). XX RN [82] RP 227405-228932 RX PUBMED; 11262262. RA Ros Viladoms J., Vilaseca Busca M.A., Lambruschini Ferri N., Mas Comas A., RA Gonzalez Pascual E., Holme E.; RT "Evolution of a case of tyrosinemia type I treated with NTBC"; RL An. Esp. Pediatr. 54(3):305-309(2001). XX RN [83] RP 227405-228932 RX DOI; 10.1074/jbc.M009341200 RX PUBMED; 11278491. RA Bergeron A., D'Astous M., Timm D.E., Tanguay R.M.; RT "Structural and functional analysis of missense mutations in RT fumarylacetoacetate hydrolase, the gene deficient in hereditary tyrosinemia RT type 1"; RL J. Biol. Chem. 276(18):15225-15231(2001). XX RN [84] RP 106960-111188 RX PUBMED; 11294906. RA Losko S., Kopp F., Kranz A., Kolling R.; RT "Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast RT vacuole is blocked in the doa4 Mutant"; RL Mol. Biol. Cell 12(4):1047-1059(2001). XX RN [85] RP 174426-176352 RX DOI; 10.1271/bbb.65.728 RX PUBMED; 11330701. RA Kosugi A., Koizumi Y., Yanagida F., Udaka S.; RT "MUP1, high affinity methionine permease, is involved in cysteine uptake by RT Saccharomyces cerevisiae"; RL Biosci. Biotechnol. Biochem. 65(3):728-731(2001). XX RN [86] RP 291313-291962 RX DOI; 10.1128/JB.183.12.3689-3703.2001 RX PUBMED; 11371533. RA Eaton R.W.; RT "Plasmid-encoded phthalate catabolic pathway in Arthrobacter keyseri 12B"; RL J. Bacteriol. 183(12):3689-3703(2001). XX RN [87] RP 272422-279865 RX DOI; 10.1023/A:1010294330190 RX PUBMED; 11386351. RA Hutchinson C.R., Kennedy J., Park C., Kendrew S., Auclair K., Vederas J.; RT "Aspects of the biosynthesis of non-aromatic fungal polyketides by RT iterative polyketide synthases"; RL Antonie Van Leeuwenhoek 78(3-4):287-295(2000). XX RN [88] RP 314329-315228 RX DOI; 10.1271/bbb.65.977 RX PUBMED; 11388486. RA Zhang X.Y., Dai A.L., Kuroiwa K., Kodaira R., Nogawa M., Shimosaka M., RA Okazaki M.; RT "Cloning and characterization of a chitosanase gene from the koji mold RT Aspergillus oryzae strain IAM 2660"; RL Biosci. Biotechnol. Biochem. 65(4):977-981(2001). XX RN [89] RP 170268-173076 RX PUBMED; 11495983. RA Basten D.E., Visser J., Schaap P.J.; RT "Lysine aminopeptidase of Aspergillus niger"; RL Microbiology 147(Pt8):2045-2050(2001). XX RN [90] RP 311604-312704 RX DOI; 10.1007/s002940100215 RX PUBMED; 11525406. RA Strittmatter A.W., Irniger S., Braus G.H.; RT "Induction of jlbA mRNA synthesis for a putative bZIP protein of RT Aspergillus nidulans by amino acid starvation"; RL Curr. Genet. 39(5-6):327-334(2001). XX DR EMBL-CON; AM270983. DR RFAM; RF00005; tRNA. XX FH Key Location/Qualifiers FH FT source 1..371827 FT /organism="Aspergillus niger" FT /mol_type="genomic DNA" FT /clone="An04c0140" FT /db_xref="taxon:5061" FT CDS complement(join(<1..2192,2257..3304,3361..3750)) FT /locus_tag="An04g03250" FT /note="Function: co-expression of het-e and het-c leads to FT cell death." FT /note="Function: het-e1 of P. anserina is responsible for FT vegetative incompatibility." FT /note="Remark: het-e1 of P. anserina shows two sequence FT motifs, a GTP-binding domain and a repeated region that FT shares similarity with that of the beta-transducin." FT /note="Remark: the reactivity of the HET-E protein depends FT on two functional elements, a GTP-binding domain and FT several WD40 repeats." FT /note="Remark: truncated ORF due to the contig end." FT /note="Title: similarity to beta transducin-like protein FT het-e1 - Podospora anserina [truncated ORF]" FT /db_xref="GOA:A2QIE7" FT /db_xref="InterPro:IPR013026" FT /db_xref="UniProtKB/TrEMBL:A2QIE7" FT /citation=[16] FT /citation=[50] FT /citation=[69] FT /citation=[71] FT /inference="profile:COGS:COG0457" FT /inference="similar to AA sequence:PIR:T18521" FT /protein_id="CAK38591.1" FT /translation="MTITHESHSQFAVTWDLALKRYTAAVGRQLDDPSLPHPSSVEELL FT NRLDSQNGHFSQFRENKRSLFNILTCICNPIERFGSMAASIASNAFPASSVCFSAITYL FT IDAAKDVSASYNAVIELFFTLKASLSDFLVRLAIYDGSRMSDALQAKVVDILVTLLEIF FT GQATKLVRAGLRGRIIQFTKNALLGSDKTLQGLVAKLDRLCQTEHQLVGAETLSETKKA FT NVAVENLSAVLNGASLVLEDNHGRLAQAQADLQRLVEGQNDLRQEVHRDISSLLGSFIG FT SGAKANGDSDYLRTLLQPSLAPSDMYYTFARKRLSGTGEWIEAEVGFRSWLNQEQPLLW FT INGPPGSGKSFLAEYIISNLKTRFPQGVDQGSEISVGYYFFKDNNPQTRGLHQALRDVA FT YQICLNDSVYAGHVAARCRAPGDISSLQSAWMTLFRDYFIEGDAGNRRAYIVLDGLDEC FT MEADRQSLLEFLLELTAEESESKSRVQFVMLGRPHLSADVADAFHESVSSISIDRSKND FT DDIARYVEHSVRRSRNIARAPSSLRKEVTEFLVKHAQGMFLWVDLMTQELGRHNRASSI FT RECLQRPPKGLYEAMRRTLEGLSAYLKGDDPEELNTILGWVACASRPLSLREIEATLTL FT GSSDQDDILDIESLLRLQFASFLALVRDDGLTTSDLQAEVDLSPLQIDDDHDEDVEDFK FT LENDFSSNPETTEVMFCHASIGDFFRDENENKRSAGPEFVAIGVDIVESRISTLKACLQ FT LVCNSTECPHLRNYALVWWHSHVKAVIPHIHRIGGSDLQEIRSLLLKTLRDESVLEAWI FT SLRDADDFWSLDTLDPIAKLLDDKLFVDSLPLDMRNWVLSSIQEPARLLVPAAECIANK FT WLQGYRWDARTCMLIIHRIRCLLEGKLDEEFPDAPAASIVLDSAEWAKLPKTAEWNRRV FT AVCLRDTAHYEEAQAYFEAALELDDQMWLARSGLAYLYSLSGQHEKSLELYKENIEILE FT TAFGNPEKRDKLPHDVEGDDLADTYQSIGEELLSLGDRASALVYLEKALHVTTEGKFLS FT KYIQLLAEENTPEANEKIIQHLKGLDTASGDNGATRLTECLSENSRLVWSSDFYQAIAF FT AAKSTDQLEWLEYAYGTAIEVAKKQRNSVVAFALQVSLADLFISYDNKESRALEIWQMV FT MDFPATFMQGNLLMLYIQSLVSRYYGAYLITKATQAGPGTADAE" FT mRNA complement(join(<1..2192,2257..3304,3361..>3750)) FT /locus_tag="An04g03250" FT exon complement(<1..2192) FT /locus_tag="An04g03250" FT /number=1 FT intron complement(2193..2256) FT /locus_tag="An04g03250" FT /number=1 FT exon complement(2257..3304) FT /locus_tag="An04g03250" FT /number=2 FT intron complement(3305..3360) FT /locus_tag="An04g03250" FT /number=2 FT exon complement(3361..3750) FT /locus_tag="An04g03250" FT /number=3 FT exon complement(4170..5546) FT /locus_tag="An04g03260" FT /number=1 FT CDS complement(4170..5546) FT /locus_tag="An04g03260" FT /note="Remark: general weak similarity to several different FT proteins involved in protein-protein interaction." FT /note="Similarity: weak similarity to desmoplakin I and FT centrosome associated protein CEP250 from H. sapiens." FT /note="Title: weak similarity to myosin heavy chain - Homo FT sapiens" FT /db_xref="UniProtKB/TrEMBL:A2QIE8" FT /inference="similar to AA sequence:PIR:S04090" FT /protein_id="CAK38592.1" FT /translation="MSSILPQAGDKHLPALPIGTSSLHQDPIVYIDRQARQIQRNLQIL FT IDAQSEGLLATLNGSPQNGAISDGTYTPTSDTSSSQRPPTIPIRQPAPEKIGLSAARKG FT IFRSIYDLLRLREEEREILTFRIDERTQALADINGFNIHRAGLEDAISTIQDNRESQHT FT VALRQESRKLEEDIHEMETRLSQMKARHQHILRELSQMENSIESKLSSYRASISLLDSN FT VRKYLQNPPVKPQDSSSKDATFYSLNPNRRTLEMAEEHWQKEQSDLRERQREVDAEIEA FT LEAGGGVWKQVIGEVSGFEKRLKSAMRLSIQSQSQLLNHDGPSGSKSEEDLARTVLEDL FT THTTERVENHLEVAENKDWKLLVCCISAELQALREARQLLLNIFNVAETDISPSADKRT FT SNGIHTHEDHDAHGDPLGVDNPEPPAEFLEDTEEHPHGAVSRSDDEDDEPDPAWLLPES FT " FT mRNA complement(<4170..>5546) FT /locus_tag="An04g03260" FT CDS join(6022..6161,6268..6437,6500..7026,7083..9341, FT 9408..9755) FT /locus_tag="An04g03270" FT /EC_number="3.4.25.1" FT /note="Complex: the 26S proteasome of S. cerevisiae FT contains a 20S catalytic core and a 19S regulatory FT subunit." FT /note="Function: regulatory subunit of the 26S proteasome FT of S. cerevisiae." FT /note="Function: the 26S proteasome degrades ubiquinated FT proteins." FT /note="Title: strong similarity to proteasome 19S FT regulatory particle subunit Rpn2 - Saccharomyces FT cerevisiae" FT /note="nucleus" FT /db_xref="GOA:A2QIE9" FT /db_xref="InterPro:IPR016642" FT /db_xref="UniProtKB/TrEMBL:A2QIE9" FT /inference="profile:COGS:COG5116" FT /inference="profile:PFAM:PF01851" FT /protein_id="CAK38593.1" FT /translation="MVGLASAAGLVGFLSEPDPELRVFALKTLDSQIDLLWTEVVDAVP FT QIEALYEDESFPERELAALVAAKVYYHLQEYNESMVFALGAGKLFQLDSGGEFEETIIA FT KCVDTFVSLSAAQRPVAGDHQANLNTSFPTSGEGATSTSASLTSPITPFSQSALPSKSL FT LSRQEVPGVDAAYPGGEDAGVNHAEETPLVLKRGVQGHLQTVIDRLFEQCFVQKRYRQV FT IGIAIEAKNLDVLRKTILRASEDEKKQNGESRRSEELMEYVLDICMGIVQERGFRNEIL FT KLILELLNEIPAPDYFSIAKCVVYLNEHSMASVILRQLVEKGDARSLAVAYQISFDLYD FT NSTQEFLQKVRQEISELVPENDESEQEAAGGDQEESKESDPLLDSQSRSIGDSRTKISP FT EARTAFKSIRDILDGVKTNQLNVEFLFRNNKADIAIMNKLRDSLEARNSIFHSAVSLSN FT GFMHAGTAHDKFFRDNLDWLSKAVNWSKFTATAALGVIHRGNLSQGQKLLQPYLPKERS FT ITNVAAGGHSGASSIYSQGGSLYAYGLIFANHGGMAVPVIRDYFKKATDEVIQHGGALG FT LGVAGMASGDEGLYEDLRNVLYTDSAINGEAVGLAMGLIMLGTGNMKVLEDMIQYAHDT FT QHEKIVRGLAMGMALIMYGRQEAADELINGLLGDPDPALRYGGIMTIALAYCGSSSNKA FT VRKLLHVAVSDVNDDVRRIAVLSLGFILFRKHQSVPRMVELLSESYNPHVRYGAAMALG FT ISCAGTGLDEAIDLLEPMLKDSTDFVRQGALISLAMVLVQQNEAMNPRVSSLRKVMMKM FT IGDRHEDAMAKFGCAVALGIIDAGGRNCTISLQTQTGNLNMPGIVGAAVFVQYWYWFPL FT THFLSLSFAPTSVIGVDQKLEVPYFKFHSNTRPSLFDYPPEQQVKAEEAPEKVKTAVLS FT TTAQAKRRAQRREKQQRRESMDIDQTPTTPKVSDQADKMDTDETAVKTEEENKEGEKEA FT GEGQKKKVEREKVGYELENMSRVLPAQLKYLTFPDPRYEPVKRPTGGVVVVLDKTPEEP FT RETIEMTASKETSREARQPAPAADVAESLQDRLQATMGAAGLQTPQRGAGRFPFGADLG FT PFAGAAAAAGVLTAVDEDEEGGEEAPVPNEFEYETEPEDE" FT mRNA join(<6022..6161,6268..6437,6500..7026,7083..9341, FT 9408..>9755) FT /locus_tag="An04g03270" FT exon 6022..6161 FT /locus_tag="An04g03270" FT /number=1 FT sig_peptide 6022..6072 FT /locus_tag="An04g03270" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(6073..6161,6268..6437,6500..7026,7083..9341, FT 9408..9752) FT /locus_tag="An04g03270" FT intron 6162..6267 FT /locus_tag="An04g03270" FT /number=1 FT exon 6268..6437 FT /locus_tag="An04g03270" FT /number=2 FT intron 6438..6499 FT /locus_tag="An04g03270" FT /number=2 FT exon 6500..7026 FT /locus_tag="An04g03270" FT /number=3 FT intron 7027..7082 FT /locus_tag="An04g03270" FT /number=3 FT exon 7083..9341 FT /locus_tag="An04g03270" FT /number=4 FT intron 9342..9407 FT /locus_tag="An04g03270" FT /number=4 FT exon 9408..9755 FT /locus_tag="An04g03270" FT /number=5 FT CDS join(10391..10629,10875..11094) FT /locus_tag="An04g03280" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIF0" FT /protein_id="CAK38594.1" FT /translation="MLTLPDSRQPNHAAPASQPHDIKHNLEGTDYLGSRRLPRHLLHSV FT SAGARARVPEVSDRPISATRKEDHHPEWPRREWPTYSVGSILLQVCYCGPVVHDSNSVQ FT LDYIFRLVRRHGDPLCSLLLPGPRNIHQKVAFVSYLTRYSYPRLNCLE" FT mRNA join(<10391..10629,10875..>11094) FT /locus_tag="An04g03280" FT exon 10391..10629 FT /locus_tag="An04g03280" FT /number=1 FT intron 10630..10874 FT /locus_tag="An04g03280" FT /number=1 FT exon 10875..11094 FT /locus_tag="An04g03280" FT /number=2 FT CDS join(11394..11508,11581..11592,11654..11925,12011..12755, FT 12811..13304) FT /locus_tag="An04g03290" FT /EC_number="1.3.99.13" FT /note="Catalytic activity: acyl-CoA + ETF <=> FT 2,3-dehydroacyl-CoA + reduced ETF." FT /note="Complex: forms with another flavoprotein (ETF = FT 'Electron-Transferring Flavoprotein') and EC 1. 5. 5. 1 a FT system reducing ubiquinone and other acceptors." FT /note="Localization: mitochondrial matrix in Rattus FT norvegicus." FT /note="Pathway: initial step of the mitochondrial fatty FT acid beta-oxidation system." FT /note="Remark: a number of acyl-CoA dehydrogenases of FT different substrate specifity are present in all FT organisms." FT /note="Remark: closest manual homolog (BLASTP): PIR:A34252 FT long-chain-acyl-CoA dehydrogenase precursor - Rattus FT norvegicus." FT /note="Title: strong similarity to long-chain acyl-CoA FT dehydrogenase - Rattus norvegicus" FT /note="localisation:mitochondrion" FT /db_xref="GOA:A2QIF1" FT /db_xref="InterPro:IPR006092" FT /db_xref="UniProtKB/TrEMBL:A2QIF1" FT /citation=[15] FT /citation=[24] FT /citation=[67] FT /inference="profile:COGS:COG1960" FT /inference="profile:PFAM:PF00173" FT /inference="profile:PFAM:PF00441" FT /inference="profile:PFAM:PF02770" FT /protein_id="CAK38595.1" FT /translation="MAKTFTKGDVASHNKADNLWVVIDDDVYDLTKFQDEHPGGKKILQ FT RVAGKDASKQFWKYHNEGILKKYKGNLQIGSLDSKKAAAPEPPASSAPASQPSKPLAAP FT VDVASAKSSETQDPFGELIPFADPAWYQGYHSPYFNQTHSALREEIRQWVDSEIEPYVT FT EWDEAKKVPDHIYKQMGERGYLAGLLGMKKYPVDYTPHRVQSVAPENWDLFHEMLLTDE FT LSRVGSGGLVWNLIGGFGIGCPPLVKFGKKPLVDRILPGILAGDKRICLAITEPDAGSD FT VANLTCEAKLSPDGKHYIVNGEKKWITNGVWSDYFTTAVRTGDAGMNGVSVLLIERDMG FT GVSTRRMDCQGVWSSGTTYITFEDVKVPVENLIGKENQGFKVIMTNFNHERIGIVIQCV FT RFARVCYEESMKYAHKRRTFGKRLIDHPVIRMKLAHMARQIEATYNWLENIIYQCQSMD FT ETEAMLKLGGAIAGLKAQSTTTFEFCAREASQIFGGLSYSRGGQGGKIERLYRDVRAYA FT IPGGSEEIMLDLSMRQSLRVHQMFGLKL" FT mRNA join(<11394..11508,11581..11592,11654..11925,12011..12755, FT 12811..>13304) FT /locus_tag="An04g03290" FT exon 11394..11508 FT /locus_tag="An04g03290" FT /number=1 FT intron 11509..11580 FT /locus_tag="An04g03290" FT /number=1 FT exon 11581..11592 FT /locus_tag="An04g03290" FT /number=2 FT intron 11593..11653 FT /locus_tag="An04g03290" FT /number=2 FT exon 11654..11925 FT /locus_tag="An04g03290" FT /number=3 FT intron 11926..12010 FT /locus_tag="An04g03290" FT /number=3 FT exon 12011..12755 FT /locus_tag="An04g03290" FT /number=4 FT intron 12756..12810 FT /locus_tag="An04g03290" FT /number=4 FT exon 12811..13304 FT /locus_tag="An04g03290" FT /number=5 FT CDS join(14211..14309,14367..14585,14649..16129,16180..16922, FT 16978..17594) FT /locus_tag="An04g03300" FT /note="Complex: SPT4 and SPT5 from S. cerevisiae form a FT complex that does not contain SPT6." FT /note="Function: STP5 from S. cerevisiae is a transcription FT elongation protein." FT /note="Title: strong similarity to transcription elongation FT protein Spt5 - Saccharomyces cerevisiae" FT /note="nucleus" FT /db_xref="GOA:A2QIF2" FT /db_xref="InterPro:IPR017071" FT /db_xref="UniProtKB/TrEMBL:A2QIF2" FT /inference="profile:COGS:COG5164" FT /inference="profile:PFAM:PF03439" FT /inference="similar to AA sequence:PIR:A40253" FT /protein_id="CAK38596.1" FT /translation="MSRNVLDQDFGSEEEDDDFNPAPADDSGDEDTKAARRAPDDDDDD FT DDEEEVNTGRSGRQRAGSEDNAGRGADDDEEGENDDEEEEGDEEDEDEEEEEEDDDEDA FT NAGRPRKRRRKAGVHSFFEEEAGVDEDEDEAEDDEDELAEFGGEMHPDDMDALPVGAET FT DDRRHRQLDRQRELAASMDAEKQAQMLKERYGRNRAAATDAVVVPKRLLLPSVDDPSIW FT GVRCKAGKEREVVFSIQKRIEERPPGSRNPIKIMSAFERGGAMAGYIYVEARRQADVMD FT ALQDMTNVYPRTKMILVPVREMPDLLRVQKSEELMPGGWVRIKRGKYQGDLAQIEEVET FT NGLAVTVRLIPRLDYGMNEDIGAPISDPKRKRPGMNPAVARPPQRAFSEAEAKKKHAKY FT LSATSGLGGKSWNYLGETYVDGFLIKDLKVQHLITKNVNPRLEEVTMFARGSEDGTSNL FT DLASLAETLKNSAAEDSYLPGDPVEVFRGEQQGLIGRTSSTRGDIVTLLVTEGDLAGQT FT IDAPVKSLRKRFREGDHVKVIGGSRYQDELGMVVQVKDDTVTLLSDMSMQEITVFSKDL FT RLSAETGVDGKLGMFDVHDLVQLDAATVACIVKVDRESLRVLDQNGSIRTILPTQVANK FT ITPRKDAVATDRNGAEIRHGDTVREVYGEQRNGVIIHIHRSFLFLHNKAQAENSGIVVV FT RTTNVVTVSAKGGRSTGPDLTKMNPALMRNGVPGGMMGPPQKSFGRDRMIGKTVMVRKG FT PFKGLVGIVKDSTDMQARVELHSKNKLISIPKDILVVKDPVTGQTIDMGRGRGGPRVPH FT GGSGGPPSAWQGGRTPMGAGDSSRTPAWGGPSSSRTPAWAGMGGSRTPAWKQDGSRTSN FT PYDGSQTAYGGFGSRTPAWNAGARTPYVGSGNSDFDAFAAGSRTPAWGSSNAGNRTPAW FT AGASASNGTKDRGYDAPTPGGYSAPTPGAYGSAPTPGVSAPTPGAWADSAPTPGAFNAP FT TPGDASKRPYDAPTPAAFDNAGGSRPYDAPTPALGGSAATPGAGAYGDGDDGGPRYEEG FT TPSP" FT mRNA join(<14211..14309,14367..14585,14649..16129,16180..16922, FT 16978..>17594) FT /locus_tag="An04g03300" FT exon 14211..14309 FT /locus_tag="An04g03300" FT /number=1 FT intron 14310..14366 FT /locus_tag="An04g03300" FT /number=1 FT exon 14367..14585 FT /locus_tag="An04g03300" FT /number=2 FT intron 14586..14648 FT /locus_tag="An04g03300" FT /number=2 FT exon 14649..16129 FT /locus_tag="An04g03300" FT /number=3 FT intron 16130..16179 FT /locus_tag="An04g03300" FT /number=3 FT exon 16180..16922 FT /locus_tag="An04g03300" FT /number=4 FT intron 16923..16977 FT /locus_tag="An04g03300" FT /number=4 FT exon 16978..17594 FT /locus_tag="An04g03300" FT /number=5 FT CDS complement(join(18345..19073,19174..20736)) FT /locus_tag="An04g03310" FT /note="Remark: high proline and glutamine content is FT indicative for various polynucleotide-binding domains." FT /note="Similarity: N-terminal region with high proline and FT glutamine content shows similarities to different FT DNA-directed RNA polymerases, C-terminal region shows FT similarity to mRNA-capping-enzyme of S. pombe." FT /note="Title: similarity to hypothetical mRNA-capping FT enzyme subunit SPAC644.04 - Schizosaccharomyces pombe" FT /db_xref="GOA:A2QIF3" FT /db_xref="InterPro:IPR004206" FT /db_xref="UniProtKB/TrEMBL:A2QIF3" FT /citation=[46] FT /inference="similar to AA sequence:UniProtKB:SPAC644.4" FT /protein_id="CAK38597.1" FT /translation="MDLRTIMNTESAGNSSAPSQPQPSPSQAPRDSSDPIYPPRDQLPS FT SSSYPSAFPGPPPPQRSHASPERSSSYGSLQSPYQYRPSPAIIPSAPSQRAPTPPPYGA FT SVSRDSFASVAYNQQQQQQQQQSPVAQQRSQSIQSVITPYSHSSNSFHARESSPTGAAQ FT PYPSQHFSPSAQGSLPNTPRGSAAAIYAHQSPQSSVRPQSSGRDSLSNRASSPWVGPDA FT AAAAMHVSPSAAARSSRAESRTFDQTPRKHSSTSERRESDESVSPRTTFLPGSRPEAAT FT ARPDQTAMSQSEHVENGITMKEGQTTQHSPAHQQHINSSPSSRMSITKESSVDDSTAQW FT VQKTRVASDPNITSSPQQPKRKRRRLNELPIYAQKCARSKGRCPPIPKPHPPIPKHARD FT SPANPWIVRQRAVSSAQGAVAAVAPPVKVKGDSTPVNGPSTPQRPSEPPQVGSLGPWEP FT SITGFIPHEEVTKIVADFLFQHVVLRNDAIAAPAGAAAAGQMPIIEVEAKLGQLIDMDR FT GERMFMCDNQSNSAKAQHRAMNNFLNEAVKMSMPQSNQGRIPLSYAHKKERDTFYEVSP FT NELPPVIRQNLNPRHKPKVRVTVDQRTGEVLAKIVKCRIADLDVHSPRTCVDWRISVNL FT EMSYDGDVSNLPVADGRGGRGGDRNKDRMSYRHLAYQIDLTQVAKSEVCTPQQPAPIKK FT KKHDMLTSLPSLQPPVKGEFEHELEVEISAAEIRRQGQMAMTGDPKNQYEELIKGFVDN FT VRVLARAVPP" FT mRNA complement(join(<18345..19073,19174..>20736)) FT /locus_tag="An04g03310" FT exon complement(18345..19073) FT /locus_tag="An04g03310" FT /number=1 FT intron complement(19074..19173) FT /locus_tag="An04g03310" FT /number=1 FT exon complement(19174..20736) FT /locus_tag="An04g03310" FT /number=2 FT CDS complement(join(22053..22480,22538..22612,22673..23273, FT 23343..23789)) FT /locus_tag="An04g03320" FT /note="Function: TTG1 is potentially involved in signal FT transduction to downstream transcription factors in A. FT thaliana." FT /note="Function: protein regulates the trichome FT differentiation and anthocyanin biosynthesis in Arabidopsis FT thaliana." FT /note="Similarity: strong similarity to hypothetical FT protein YPL247 form S. cerevisiae." FT /note="Similarity: strong similarity to putative beta FT transducin from S. pombe." FT /note="Similarity: ttg1 from A. thaliana contains four WD40 FT repeats." FT /note="Title: similarity to transparent testa glabra1 TTG1 FT - Arabidopsis thaliana" FT /db_xref="InterPro:IPR019781" FT /db_xref="UniProtKB/TrEMBL:A2QIF4" FT /citation=[63] FT /inference="profile:COGS:COG2319" FT /inference="profile:COGS:COG5635" FT /inference="profile:PFAM:PF00400" FT /inference="similar to AA sequence:UniProtKB:ATH251523.1" FT /protein_id="CAK38598.1" FT /translation="MQPTSQSGQQPPSAQQQQTPQQQQPNARASMVNSHGHSRSSPAGF FT EQPKYRQPGSSPGSAYPPHTPQGTKYSPLGLADIRPTGDLLGDPITSSGMAPFNGDNPV FT PTNSNYIAPWPIYSMDWCKWPITGSSSSFGGKIALGSYLEDNHNYIQIIDTHWTQPDPD FT TPDAAAGEIKLDYVKTAEATHSYPVTRILWEPPSSQKQSTDLLATSGDHLRLWSLPTAQ FT PVPSSNSITRSASQHAPTAKLSPLALLSNSKSPEHTAPITSLDWNTISPSLIITSSIDT FT TCTIWDIPTLTAKTQLIAHDKEVYDVRFCANSVDVFVSCGADGSVRMFDLRSLEHSTII FT YEPTEKHEKVPTPGNGSPSGQAQPVWPPPLLRIAASPHDSHLLATFSQDSNIVRVLDVR FT QPGQALLELKGHGSSINCVEWSPNRRGVLASGADDCFVLLWDLINQHNAAPVPPMPPVP FT HNAGTPATPSERGPAAVWLCDNEVSNISWSPQGGTTPAGHPRDWLGVCGGRGLWGVAL" FT mRNA complement(join(<22053..22480,22538..22612,22673..23273, FT 23343..>23789)) FT /locus_tag="An04g03320" FT exon complement(22053..22480) FT /locus_tag="An04g03320" FT /number=1 FT intron complement(22481..22537) FT /locus_tag="An04g03320" FT /number=1 FT exon complement(22538..22612) FT /locus_tag="An04g03320" FT /number=2 FT intron complement(22613..22672) FT /locus_tag="An04g03320" FT /number=2 FT exon complement(22673..23273) FT /locus_tag="An04g03320" FT /number=3 FT intron complement(23274..23342) FT /locus_tag="An04g03320" FT /number=3 FT exon complement(23343..23789) FT /locus_tag="An04g03320" FT /number=4 FT exon 24729..25934 FT /locus_tag="An04g03330" FT /number=1 FT CDS 24729..25934 FT /locus_tag="An04g03330" FT /note="Title: strong similarity to hypothetical protein FT SPAC1F12.08 - Schizosaccharomyces pombe" FT /db_xref="GOA:A2QIF5" FT /db_xref="InterPro:IPR004820" FT /db_xref="UniProtKB/TrEMBL:A2QIF5" FT /inference="profile:COGS:COG0615" FT /inference="profile:COGS:COG1019" FT /inference="similar to AA sequence:PIR:S67451" FT /protein_id="CAK38599.1" FT /translation="MASDQLSALLLLPPPPSASFNEFKAAYEPVLLGVCTKLVRELNGA FT NHTAILDIALSLPGLLSPSCRPRTRAFSSLQSLLESIYRLIGIVCVEQGIELDGPGGID FT PRVILLDYDSVQTAVTRDNPCDGPIIDLQTLARSGRLWDYIYYPDNQVGQGLATAFSSF FT YSESRDPNGGSMSAIPDAPNWKAAESLLVMDDNHTSTTHYSVAVGGTFDHFHIGHKLLL FT TATALVLQPAEDVEAGNVRKITVGVTGEGLLAKKKYAEYLESWDERCMSTGSFLSAIMD FT FRLPETSAPRIERESGSGPDDKYIQMQMRPDLVFKLVQITDPFGPTVTDKGISALVVSK FT ETRAGGSAVNEERAKKGWESLEVFEVDVLHTGEVPTDDAESFASKISSTDIRRRRMEMA FT TE" FT mRNA <24729..>25934 FT /locus_tag="An04g03330" FT sig_peptide 24729..24785 FT /locus_tag="An04g03330" FT /inference="protein motif:SignalP:2.0" FT mat_peptide 24786..25931 FT /locus_tag="An04g03330" FT CDS join(27638..27826,27939..29108,29383..29416,29506..29516, FT 29549..29551) FT /locus_tag="An04g03340" FT /note="Title: weak similarity to hypothetical syntaxin 8 FT related protein B13N20.240 - Neurospora crassa" FT /db_xref="UniProtKB/TrEMBL:A2QIF6" FT /protein_id="CAK38600.1" FT /translation="MERPRHIEDLADELISDILSYLLGSEYLSPEPSPTSPQGSSRDSD FT NGTTHAFGEKSELDRFRLPVMSDISRTWCDPSTKEAVPSLKTRPACCEPEADDHIGWSH FT ILDGVDVDNLPVSSIHRRRLDDQKYILDSNLDLRLLRRAIAAFSSLQQVKLLRLQDEAD FT EQLLDHIRERSLGRTTRLDWEPACTRAITSLSISLLESNCNSVRFVGPQISPEATVRLL FT QAPSTSLSALGARLASLDVTFHSAAKLSTYMETLSNVFHDFFLAAKNLTTIHLGFPTNA FT PLDLALEQIFHHVQWKRLRTLSIQGWRLGSEEIIAFIRRHRRQLRNVRLASVYLRPGGR FT WREVLTVLHDEMDLLERIDLRGIDYTSNFDANINTNAHHNADAAGPGTGSSQTPTLAIV FT VQPTPDMAPHKAFLNMDYYSNSGPPGKTRRSFSETTLEQLRGHTSDVLGDNGESRRICN FT ITDRSDGKNI" FT mRNA join(<27638..27826,27939..29108,29383..29416,29506..29516, FT 29549..>29551) FT /locus_tag="An04g03340" FT exon 27638..27826 FT /locus_tag="An04g03340" FT /number=1 FT intron 27827..27938 FT /locus_tag="An04g03340" FT /number=1 FT exon 27939..29108 FT /locus_tag="An04g03340" FT /number=2 FT intron 29109..29382 FT /locus_tag="An04g03340" FT /number=2 FT exon 29383..29416 FT /locus_tag="An04g03340" FT /number=3 FT intron 29417..29505 FT /locus_tag="An04g03340" FT /number=3 FT exon 29506..29516 FT /locus_tag="An04g03340" FT /number=4 FT intron 29517..29548 FT /locus_tag="An04g03340" FT /number=4 FT exon 29549..29551 FT /locus_tag="An04g03340" FT /number=5 FT CDS complement(join(29862..32082,32119..32510)) FT /locus_tag="An04g03350" FT /note="Function: Ral2 from S. pombe probably is a GDP - GTP FT exchange factor for Ras1" FT /note="Phenotype: deletion mutant shows no response to the FT mating pheromone, but their vegetative growth was FT apparently normal in S. pombe." FT /note="Title: similarity to ras1 activating gene ral2p FT -Schizosaccharomyces pombe" FT /db_xref="InterPro:IPR006652" FT /db_xref="UniProtKB/TrEMBL:A2QIF7" FT /inference="profile:PFAM:PF01344" FT /inference="similar to AA sequence:PIR:A33827" FT /protein_id="CAK38601.1" FT /translation="MMSRSQSSLGFMDAGRDDPSAPGAQPGHQAPPSNSGPINLSGLVC FT NVRRTTGREPHPLVGATTTILGDKLYVFGGRVLSKSRPQLTSDIYELDLIRRHWTKIET FT TGDIPRPRYFHSVCALGDHKLVCYGGINGSGGQEAQPEVVVMSDIHIFDVPSRTWTRVP FT ATDSPQGRYAHCATILPSSAHFTSATAPLSAIHHNPASSNPHQGSIGVDIDGFGGAEMV FT VVGGQDSSNHYIEQISVFNLRSLKWTSTTHLGRSCGAYRSVVAPLVGMNVSDIGSAADD FT GEAQEPLEESQVEGCPMLVYSNYNFLDVKLELQVRLPDGRLIEKPMQSQASPPGLRFPN FT GGVINGHFVVSGTYLTSSKQEYALWALDLRTLTWGRIDAGGSVFGHGSWNRGILWPRRN FT TFVILGHRKRSLVEDYNHRRINFSHVCMVELEAFGLYNNACRTTPTSGYISYSSPAVPA FT SMQHKLTKLTSGGRPFTSASDELGRLAQSLPEMADMELQAVGGERIPVNSRILTRRWGP FT YFIQLLRESCDSGIAETATLRPAVAMYPSRNSSITITPSLGQNSTYSNSSTLVSNRSVT FT SKSLLANLEIPSAHSLSPTSRPRVLYLPHTVITLQVLVYYFYTSSLPPAGSPLCTPQIL FT CSLLQLARPYQVDGLLEATVERLHQVLDGRNAAAVFNAAAMAAGGGRGTGFTSGPGGTL FT EALNGAHAGHESSSGTGTTTSQSHLTSDSSDTEHGTSALSVASSASGVMGSRGIPLRIN FT TNIFSRRHRSNAGVDRDREDSMSNASISTSASTNTSFDHSDSEMGGDPTRPSHHRRNTD FT AELRPEREIWTGDLSSVIGLQKRGLRGLMEGRRLRERNNKPAGAADHVATAVAPPPGA" FT mRNA complement(join(<29862..32082,32119..>32510)) FT /locus_tag="An04g03350" FT exon complement(29862..32082) FT /locus_tag="An04g03350" FT /number=1 FT intron complement(32083..32118) FT /locus_tag="An04g03350" FT /number=1 FT exon complement(32119..32510) FT /locus_tag="An04g03350" FT /number=2 FT CDS complement(join(34434..34690,34749..35001,35084..35192, FT 35257..35276)) FT /locus_tag="An04g03360" FT /EC_number="3.1.1.4" FT /note="Catalytic activity: Phosphatidylcholine + H(2)O <=> FT 1-acylglycerophosphocholine + a fatty acid anion." FT /note="Function: aiPLA2 degrades internalized FT phosphatidylcholine in R. norvegicus." FT /note="Localization: in lysosomal fraction of R. norvegicus FT lung epithelium." FT /note="Title: strong similarity to acidic FT Ca(2+)-independent phospholipase A2 aiPLA2 - Rattus FT norvegicus" FT /db_xref="GOA:A2QIF8" FT /db_xref="InterPro:IPR019479" FT /db_xref="UniProtKB/TrEMBL:A2QIF8" FT /citation=[51] FT /inference="profile:COGS:COG0450" FT /inference="profile:PFAM:PF00578" FT /protein_id="CAK38602.1" FT /translation="MAQERAPLRLGSVAPNFEADSSNGPITFHDYIGNSWAILFSHPDD FT FTPICTTELGAFAKLEPEFTARGVKLIGLSANGTESHHAWIKDIDEVNGSNLKFPIISD FT PERKVAYLYDMVDYQDTTNVDAKGMALTIRSVFIIDPSKKIRLIMSYPASTGRNTAEVL FT RVVDALQTTDKHGVTCPINWLPGDDVVIPPPVSTEDAQKKFGDIRIVKP" FT mRNA complement(join(<34434..34690,34749..35001,35084..35192, FT 35257..>35276)) FT /locus_tag="An04g03360" FT exon complement(34434..34690) FT /locus_tag="An04g03360" FT /number=1 FT intron complement(34691..34748) FT /locus_tag="An04g03360" FT /number=1 FT exon complement(34749..35001) FT /locus_tag="An04g03360" FT /number=2 FT intron complement(35002..35083) FT /locus_tag="An04g03360" FT /number=2 FT exon complement(35084..35192) FT /locus_tag="An04g03360" FT /number=3 FT intron complement(35193..35256) FT /locus_tag="An04g03360" FT /number=3 FT exon complement(35257..35276) FT /locus_tag="An04g03360" FT /number=4 FT CDS complement(join(35320..35746,35927..36131,36535..36976, FT 37654..37803,37910..38029)) FT /locus_tag="An04g03370" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIF9" FT /protein_id="CAK38603.1" FT /translation="MKTTKGSASQEPASGEALGELGHEDPGAPRSVEASQSVNPEQLDT FT TRRGSRHALGKNHNRIAMGEALIADEWTGRASRDARWSPLRRSAGFLFRKKSSFPVIGH FT HSPSRDESRRDPLGKLQKYTLMRTVHFEQSKCCTELPLGQTPLLYLFAEHIRIKYSSAG FT EESMRYIGRIELFAGLARYVDCPREIVSRLVPGEESMAILIGRAKLIKLSVESAIFNDQ FT VIFQPSRVRHVRFRTVVDQVVTGKMGKMARTIAPSFNITIGPNRTRLSAEPFSCKVVGR FT QLSGGKRVETLASGRYERTELGTQQSVVRALGNPNLALEFRFLLSKKIPEGEGHFPMRP FT ALNIPPGMSSCGSNQGRSAPWAVADCVIGIACPAAVIRWRGIQAVVRVQCGCCPPLPRS FT SIPVPFTGSSSLGSPTSGLIGVYLVLPASSVAFIFFCFLLILLFYHSN" FT mRNA complement(join(<35320..35746,35927..36131,36535..36976, FT 37654..37803,37910..>38029)) FT /locus_tag="An04g03370" FT exon complement(35320..35746) FT /locus_tag="An04g03370" FT /number=1 FT intron complement(35747..35926) FT /locus_tag="An04g03370" FT /number=1 FT exon complement(35927..36131) FT /locus_tag="An04g03370" FT /number=2 FT intron complement(36132..36534) FT /locus_tag="An04g03370" FT /number=2 FT exon complement(36535..36976) FT /locus_tag="An04g03370" FT /number=3 FT intron complement(36977..37653) FT /locus_tag="An04g03370" FT /number=3 FT exon complement(37654..37803) FT /locus_tag="An04g03370" FT /number=4 FT intron complement(37804..37909) FT /locus_tag="An04g03370" FT /number=4 FT exon complement(37910..38029) FT /locus_tag="An04g03370" FT /number=5 FT CDS join(38154..38231,38459..38594,38733..38978,39035..39052, FT 39108..39224,39289..39608) FT /locus_tag="An04g03380" FT /note="Title: strong similarity to hypothetical protein FT My005 - Homo sapiens" FT /db_xref="GOA:A2QIG0" FT /db_xref="InterPro:IPR017956" FT /db_xref="UniProtKB/TrEMBL:A2QIG0" FT /inference="profile:COGS:COG2947" FT /inference="profile:PFAM:PF04543" FT /inference="similar to AA sequence:UniProtKB:AF059619.1" FT /protein_id="CAK38604.1" FT /translation="MAPQRKRKSESASIAEETESPAAKRVAAPDTPATGEKRKRGRPRK FT YPEGSTPKRPDGPKRGRGRPRKDPNAPTPAKSTTPKQGKRGRPRKNPIENGTEPTSSTT FT KPETIDTTSFEGRSYWLMKAEPESRLEKGVDVKFSIDDLASRKEPEPWDGVRNPVAQKH FT IRDMKKGDLAFFYHSNCKVPGIAGIMEIVQEHSPDESAFDPAHPYYDEKSNRDDPKWQV FT VHVEFRRKFNKMITLNDLKSYAQSERALENMQVLKQSRLSVTPVSVTEWAFIMRVADEN FT EAKANAEASKDDSAEGDEPESSE" FT mRNA join(<38154..38231,38459..38594,38733..38978,39035..39052, FT 39108..39224,39289..>39608) FT /locus_tag="An04g03380" FT exon 38154..38231 FT /locus_tag="An04g03380" FT /number=1 FT intron 38232..38458 FT /locus_tag="An04g03380" FT /number=1 FT exon 38459..38594 FT /locus_tag="An04g03380" FT /number=2 FT intron 38595..38732 FT /locus_tag="An04g03380" FT /number=2 FT exon 38733..38978 FT /locus_tag="An04g03380" FT /number=3 FT intron 38979..39034 FT /locus_tag="An04g03380" FT /number=3 FT exon 39035..39052 FT /locus_tag="An04g03380" FT /number=4 FT intron 39053..39107 FT /locus_tag="An04g03380" FT /number=4 FT exon 39108..39224 FT /locus_tag="An04g03380" FT /number=5 FT intron 39225..39288 FT /locus_tag="An04g03380" FT /number=5 FT exon 39289..39608 FT /locus_tag="An04g03380" FT /number=6 FT CDS join(40605..40732,40789..40988,41048..42228) FT /locus_tag="An04g03400" FT /EC_number="1.2.1.3" FT /EC_number="1.2.1.5" FT /note="Catalytic activity: Aldehyde + NAD+ + H2O = FT Carboxylate + NADH." FT /note="Localization: different aldh isozymes are located in FT the mitochondria and cytoplasm." FT /note="Title: strong similarity to aldehyde dehydrogenase FT aldA - Aspergillus niger" FT /db_xref="GOA:A2QIG1" FT /db_xref="InterPro:IPR016162" FT /db_xref="UniProtKB/TrEMBL:A2QIG1" FT /citation=[13] FT /citation=[7] FT /inference="profile:COGS:COG1012" FT /inference="profile:PFAM:PF00171" FT /inference="similar to AA sequence:SWISSPROT:DHAL.ASPNG" FT /protein_id="CAK38605.1" FT /translation="MSDLSVQLTAPNGRTYAQPVGLFINNEFVASKSGEKFATINPSNE FT AEITSVYAAGEEDVDIAVKAARKALNHPSWKLLPPTERGTLMLKLADLVEQHKETLATI FT ETWDNGKPYSVSLNDDLGEVVGCLRYYAGYADKVHGQTISTTPAKFAYTLRQPIGVVGQ FT IIPWNFPLAMAAWKLGPALACGNTVVLKPAEQTPLSVLYLANLIKEAGFPPGVVNILNG FT LGRVAGSALVTHPGVDKVAFTGSTLTGREVMKLAAGTLKNITLETGGKSPLVVFSDADI FT DQAAKWAHAGIMYNQGQVCTATSRILVHESVYDKFVALFKEAVANTSKVGDPFADDTFQ FT GPQVTKAQYDRVLSYIEAGKSEGATLVAGGEPFKNVGDGKGFFIAPTIFTNVKDNMRIY FT REEVFGPFVVISSFSEEDEAVRRANDTTYGLGAALFTKDIERAHRVASEIEAGMVWINS FT SNDSDIRVPFGGVKQSGIGRELGEAGLEAYSQIKAVHVNLGTKL" FT mRNA join(<40605..40732,40789..40988,41048..>42228) FT /locus_tag="An04g03400" FT exon 40605..40732 FT /locus_tag="An04g03400" FT /number=1 FT intron 40733..40788 FT /locus_tag="An04g03400" FT /number=1 FT exon 40789..40988 FT /locus_tag="An04g03400" FT /number=2 FT intron 40989..41047 FT /locus_tag="An04g03400" FT /number=2 FT exon 41048..42228 FT /locus_tag="An04g03400" FT /number=3 FT CDS complement(join(42845..42876,43023..43243,43367..43390, FT 43495..43519,43554..43629)) FT /locus_tag="An04g03410" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIG2" FT /protein_id="CAK38606.1" FT /translation="MQSDSTTDQSKSTPKNILILHACNATNAHTTYNILIFHKTYFTTC FT TYKTLSSQETTHLPPLLPQHLQVTLSQRFKILTCKQSKRNFYPNCISLWFFVSRPIALI FT SLFHLWDAIKQWYEFETGFGF" FT mRNA complement(join(<42845..42876,43023..43243,43367..43390, FT 43495..43519,43554..>43629)) FT /locus_tag="An04g03410" FT exon complement(42845..42876) FT /locus_tag="An04g03410" FT /number=1 FT intron complement(42877..43022) FT /locus_tag="An04g03410" FT /number=1 FT exon complement(43023..43243) FT /locus_tag="An04g03410" FT /number=2 FT intron complement(43244..43366) FT /locus_tag="An04g03410" FT /number=2 FT exon complement(43367..43390) FT /locus_tag="An04g03410" FT /number=3 FT intron complement(43391..43494) FT /locus_tag="An04g03410" FT /number=3 FT exon complement(43495..43519) FT /locus_tag="An04g03410" FT /number=4 FT intron complement(43520..43553) FT /locus_tag="An04g03410" FT /number=4 FT exon complement(43554..43629) FT /locus_tag="An04g03410" FT /number=5 FT CDS join(48065..48103,48197..48357,48455..48601,48673..49270) FT /locus_tag="An04g03420" FT /note="Function: regucalcin from R. norvegicus has an FT inhibitory effect on the activation of FT Ca2+/calmodulin-dependent enzymes and protein kinaseC and FT regulates nuclear function in liver cells; it can inhibit FT Ca(2+)-activated DNA fragmentation, DNA and RNA FT synthesis,protein kinase and protein phosphatase activities FT in the nuclei." FT /note="Function: regucalcin from R. norvegicus is a FT calcium-binding protein that does not contain the EF-hand FT motif, it is a regulatory protein in Ca2+ FT signaling,maintaining intracellular Ca2+ homeostasis due to FT activating Ca2+ pump enzymes in the plasma membrane and FT microsomal membranes of liver and kidney cells." FT /note="Title: strong similarity to regucalcin also known as FT senescence marker protein-30 SMP30 - Rattus norvegicus" FT /db_xref="InterPro:IPR011042" FT /db_xref="UniProtKB/TrEMBL:A2QIG3" FT /citation=[28] FT /citation=[53] FT /citation=[5] FT /citation=[68] FT /citation=[6] FT /inference="profile:COGS:COG3386" FT /inference="profile:PFAM:PF03758" FT /protein_id="CAK38607.1" FT /translation="MSGFQYQKWTVSEPYVDVPGTLLEGPFHDKTKNEFRFVDIWEQKL FT YVLDLAKGPDSLKIMDTSVSIGVTANIANAGDSRENQIVVAAKHGFALVDRTTGALSYI FT QKVWDDPAKEHRMRFNDGAVDSHGRFWAGAMNDSKVQNPVNEGVIFRLDPDMKLHRMVE FT QVTIPNGIGWNPADDTMYLTDSPTGKIYAFDFDAETGNISNRRVFFDIGEPKEPDGFAI FT DEEGCIWSAIYGGGKVIRISPEGKIIGEITFPTRNITCPAFVGTELFITTAKDDTNDDQ FT FPESVRYGGRLYRVDVGIKGKPKNEFRLEGSPL" FT mRNA join(<48065..48103,48197..48357,48455..48601,48673..>49270) FT /locus_tag="An04g03420" FT exon 48065..48103 FT /locus_tag="An04g03420" FT /number=1 FT intron 48104..48196 FT /locus_tag="An04g03420" FT /number=1 FT exon 48197..48357 FT /locus_tag="An04g03420" FT /number=2 FT intron 48358..48454 FT /locus_tag="An04g03420" FT /number=2 FT exon 48455..48601 FT /locus_tag="An04g03420" FT /number=3 FT intron 48602..48672 FT /locus_tag="An04g03420" FT /number=3 FT exon 48673..49270 FT /locus_tag="An04g03420" FT /number=4 FT CDS complement(join(53041..53147,53212..53338,53439..53504, FT 53768..53901,53984..54411,54752..54913,55143..55263, FT 55453..55497,55596..55657,55744..55823)) FT /locus_tag="An04g03430" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIG4" FT /protein_id="CAK38608.1" FT /translation="MGLYSVNSSGSSSSSIILSRITADERGDSIPSRLLVDKPFTHSTH FT IPRIPRDPFTAPAGRAKPLNWARQHYGSVEALEYLPGTLPILTDSAGYQAVSGSLRYPV FT SPSILPYHDLKLILVKVLALRNSSPRISLASPHLNTDRLQMSLAAPSSLNYIIPSFTLQ FT ATLIRTGLPAHLPKTRCLSPRVAAVPIPPKKLKQGPRLVRIGRWGGWPRFSHSGRPNHD FT VLHACGQHAFAFLPPKNVDDRRVTVVVPMSAADHRCFSPFQFSDCHPSVHTSAVLCPFP FT PYLEVDSSLLLGVLMDLFGSPFVARRQQSRQIIGKTGSSSSYCHLSGPRRMLCVFIRTL FT VSSESPGQGDIHLQAATQPKPMQRVQGVWAGLVEYNGVSEACTMGTRPLSSENIGGRAS FT PDCRDPLMSVSPMLWGLKNAGWDGSPDLCAAYMRLRHDACTFGN" FT mRNA complement(join(<53041..53147,53212..53338,53439..53504, FT 53768..53901,53984..54411,54752..54913,55143..55263, FT 55453..55497,55596..55657,55744..>55823)) FT /locus_tag="An04g03430" FT exon complement(53041..53147) FT /locus_tag="An04g03430" FT /number=1 FT intron complement(53148..53211) FT /locus_tag="An04g03430" FT /number=1 FT exon complement(53212..53338) FT /locus_tag="An04g03430" FT /number=2 FT intron complement(53339..53438) FT /locus_tag="An04g03430" FT /number=2 FT exon complement(53439..53504) FT /locus_tag="An04g03430" FT /number=3 FT intron complement(53505..53767) FT /locus_tag="An04g03430" FT /number=3 FT exon complement(53768..53901) FT /locus_tag="An04g03430" FT /number=4 FT intron complement(53902..53983) FT /locus_tag="An04g03430" FT /number=4 FT exon complement(53984..54411) FT /locus_tag="An04g03430" FT /number=5 FT intron complement(54412..54751) FT /locus_tag="An04g03430" FT /number=5 FT exon complement(54752..54913) FT /locus_tag="An04g03430" FT /number=6 FT intron complement(54914..55142) FT /locus_tag="An04g03430" FT /number=6 FT exon complement(55143..55263) FT /locus_tag="An04g03430" FT /number=7 FT intron complement(55264..55452) FT /locus_tag="An04g03430" FT /number=7 FT exon complement(55453..55497) FT /locus_tag="An04g03430" FT /number=8 FT intron complement(55498..55595) FT /locus_tag="An04g03430" FT /number=8 FT exon complement(55596..55657) FT /locus_tag="An04g03430" FT /number=9 FT intron complement(55658..55743) FT /locus_tag="An04g03430" FT /number=9 FT exon complement(55744..55823) FT /locus_tag="An04g03430" FT /number=10 FT exon 57854..59344 FT /locus_tag="An04g03440" FT /number=1 FT CDS 57854..59344 FT /locus_tag="An04g03440" FT /note="Remark: the blastp hits are due to the serine-rich FT ORF sequence." FT /note="Similarity: the ORF shows strong similarity to the FT A. niger EST an_3444." FT /note="Title: similarity to novel polypeptide sequence SEQ FT ID NO:1786 from patent WO2003029271-A2 - Homo sapiens" FT /db_xref="GOA:A2QIG5" FT /db_xref="InterPro:IPR004827" FT /db_xref="UniProtKB/TrEMBL:A2QIG5" FT /protein_id="CAK38609.1" FT /translation="MSSTLTGPSPDDAHPAEDHGTFGRKRPRSHDDSASSDGPDPVRHR FT PLSWQPSAPVEPSVKSTQLRSIGVESILNPPSKAAVVAAEPGREGLGSQVPTTSSSPSH FT ARLPSSPSVHLPSPSVHPAKRLSASPAMKHHQAIAPASPSARFVPTGGGYAQRLGVSQS FT PLAHPSRLASYSAAPGSPLSVDPFPGQSVSTSTHPAPAPVSMHSTPTFHSRRTSANPTP FT APSSQETSPTTPVSAYSQLGRSSPAVSAAPMQQTTPSFLNATAYGSSEPATRLPSVMAG FT PRSTGEEAATAGAPPENPPYPGMIPCILDLKSGSSSQAEKRKANSDASRRFRNRKRNEM FT QLEQKIAGQLEEIQKKTEELKRRDDQIRSLMQERDFYRSERDFFREHVSRLVPTGQLPA FT RPASPLTLRPPFESTASEREATWHASEARKMVENTSGSGKLAPAPSHLMAGSSTRPPVT FT WSTAPTSYPAAHVERSMLPDEQQARSLPQFPGQWARNS" FT mRNA <57854..>59344 FT /locus_tag="An04g03440" FT CDS complement(join(60099..60290,60369..60473,60528..60557)) FT /locus_tag="An04g03450" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIG6" FT /protein_id="CAK38610.1" FT /translation="MAMAIAPDQPFRLEVHNGGPRAAVGGIFSGRGRMEREVDAGRIYL FT LITDPTHAVGCPDWLNRARGRVDVPLWEKVPGCPRLPSILLPKIYRTLSMAEDSRVHAS FT SIDP" FT mRNA complement(join(<60099..60290,60369..60473,60528..>60557)) FT /locus_tag="An04g03450" FT exon complement(60099..60290) FT /locus_tag="An04g03450" FT /number=1 FT intron complement(60291..60368) FT /locus_tag="An04g03450" FT /number=1 FT exon complement(60369..60473) FT /locus_tag="An04g03450" FT /number=2 FT intron complement(60474..60527) FT /locus_tag="An04g03450" FT /number=2 FT exon complement(60528..60557) FT /locus_tag="An04g03450" FT /number=3 FT CDS join(60597..60640,60752..62111) FT /gene="phyA" FT /locus_tag="An04g03460" FT /product="phytase phyA-Aspergillus niger" FT /EC_number="3.1.3.8" FT /note="Catalytic activity: 3-phytase catalyzes the FT conversion of myo-inositol hexakisphosphate + H2O = FT D-myo-inositol 1,2,4,5,6-pentakisphosphate + FT orthophosphate." FT /note="Function: catalyzes the hydrolysis of phytic acid FT into myo-inositol and inorganic phosphate." FT /note="Gene-ID: phyA" FT /note="Pathway: inositol phosphate metabolism." FT /note="extracellular/secretion proteins" FT /db_xref="GOA:A2QIG7" FT /db_xref="InterPro:IPR016274" FT /db_xref="UniProtKB/TrEMBL:A2QIG7" FT /citation=[36] FT /citation=[47] FT /citation=[56] FT /citation=[58] FT /citation=[60] FT /inference="profile:PFAM:PF00328" FT /inference="similar to AA sequence:UniProtKB:AB022700.1" FT /protein_id="CAK38611.1" FT /translation="MGVSAVLLPLYLLSGVTSGLAVPASRNQSTCDTVDQGYQCFSETS FT HLWGQYAPFFSLANKSAISPDVPAGCHVTFAQVLSRHGARYPTDSKGKKYSALIEEIQQ FT NATTFEGKYAFLKTYNYSLGADDLTPFGEQELVNSGVKFYQRYESLTRNIVPFIRSSGS FT SRVIASGNKFIEGFQSTKLKDPRAQPGQSSPKIDVVISEASTSNNTLDPGTCTVFEDSE FT LADDIEANFTATFVPSIRQRLENDLSGVSLTDTEVTYLMDMCSFDTISTSTVDTKLSPF FT CDLFTHEEWINYDYLQSLNKYYGHGAGNPLGPTQGVGYANELIARLTHSPVHDDTSSNH FT TLDSNPATFPLNSTLYADFSHDNGIISILFALGLYNGTKPLSSTTAENITQTDGFSSAW FT TVPFASRMYVEMMQCQSEQEPLVRVLVNDRVVPLHGCPVDALGRCTRDSFVKGLSFARS FT GGDWGECFA" FT mRNA join(<60597..60640,60752..>62111) FT /gene="phyA" FT /locus_tag="An04g03460" FT sig_peptide join(60597..60640,60752..60770) FT /gene="phyA" FT /locus_tag="An04g03460" FT /inference="protein motif:SignalP:2.0" FT exon 60597..60640 FT /gene="phyA" FT /locus_tag="An04g03460" FT /number=1 FT intron 60641..60751 FT /gene="phyA" FT /locus_tag="An04g03460" FT /number=1 FT exon 60752..62111 FT /gene="phyA" FT /locus_tag="An04g03460" FT /number=2 FT mat_peptide 60771..62108 FT /gene="phyA" FT /locus_tag="An04g03460" FT /product="phytase phyA-Aspergillus niger" FT CDS complement(join(62444..62600,62820..62944)) FT /locus_tag="An04g03470" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIG8" FT /protein_id="CAK38612.1" FT /translation="MDPHHRQPQQTSIPPRGRPAGARAGAIKDIRQTKEYKVAARREGE FT CLLTGVGFVVVAYGDKRPKRLVERSSSASATPSTLTSGSGKVEGEGEK" FT mRNA complement(join(<62444..62600,62820..>62944)) FT /locus_tag="An04g03470" FT exon complement(62444..62600) FT /locus_tag="An04g03470" FT /number=1 FT intron complement(62601..62819) FT /locus_tag="An04g03470" FT /number=1 FT exon complement(62820..62944) FT /locus_tag="An04g03470" FT /number=2 FT CDS complement(join(63358..63369,63621..63766,64150..64278, FT 64402..64501)) FT /locus_tag="An04g03480" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIG9" FT /protein_id="CAK38613.1" FT /translation="MLYEEKVAVQISHISQSVSNLRGIAFLTYQPADHPVRTDHGVCFG FT SLVHDTMAPLYLSNLILVSNLRGISLPYQPAVNSTLCGTHIYIYIIPELLLLSKCNQIG FT IYDRLTLYRQYNKAPPYHSLMDDF" FT mRNA complement(join(<63358..63369,63621..63766,64150..64278, FT 64402..>64501)) FT /locus_tag="An04g03480" FT exon complement(63358..63369) FT /locus_tag="An04g03480" FT /number=1 FT intron complement(63370..63620) FT /locus_tag="An04g03480" FT /number=1 FT exon complement(63621..63766) FT /locus_tag="An04g03480" FT /number=2 FT intron complement(63767..64149) FT /locus_tag="An04g03480" FT /number=2 FT exon complement(64150..64278) FT /locus_tag="An04g03480" FT /number=3 FT intron complement(64279..64401) FT /locus_tag="An04g03480" FT /number=3 FT exon complement(64402..64501) FT /locus_tag="An04g03480" FT /number=4 FT CDS complement(join(64627..67347,67409..67498)) FT /locus_tag="An04g03490" FT /note="Title: similarity to hypothetical protein AAN10358.2 FT - Drosophila melanogaster" FT /db_xref="UniProtKB/TrEMBL:A2QIH0" FT /protein_id="CAK38614.1" FT /translation="MEANNTEVVGRASVARELGSPAALSLDLTPRETRRSSSRASRRTT FT REPEAHPSNLSHSSYSLPPTPVTTSFEEQLPSAKRRKTQRSATVDEKTDSTQDSAQTPN FT QKGSGGPSQISNSVSRKRERGRKSALANGETVQPATPAPNPKQQSQSTLHNFLSRKPQD FT RRKSLATQNPSPNPTMSTSNVSNSPVMNPSASNGRKTRKSMPAKLNGVENSEKTSSVDS FT TTSVTSTPQQNAQGGKANKTPASSAASANNAKAAQTQEASTKLATPATQPRSTPRTTTA FT RSRRAERKSRAMAVTQDSKSVQSTPVSAVNANSHKPVNSQVAARTSSRPQRSTRKTAAT FT SASQAVDDGSLETPSAPKTPFSREVADSIESTPAFDSKAGYETMSGYDLDTPGYERSTP FT YGESFPFEYPADMYGNKFGLDGSNDGPGSPTASFSTTTSAARTSGRTRKPTIKAMESLE FT SERRFRRNRAPSSMPESALKEVKGKAAVKKTRANKKASAKTTGTAQAFKAAVDGKWAAV FT ANRLLDLAAAAVAPEFEPSSEAEGWLEELRKEYVKKSEEKKTETPTVQSEAEPVTEAAS FT EAQPQAEIGVEGSSKPFSTSETHRWTDEDGFVFTGKKNKYGEELVLVGEGYSWFRPNNT FT YGDKLLPQPPIRLKSHEQFEKDRIFGYPPRMGERNLPQDNKMPFFFENVDEVKATIKAR FT EEARKRGIAVDRMMPAAYIQTLIAQHDENAPKDGSGEAKETKETKEPTRKRRRGGEASE FT TTQPTKRRRREPEPTPPAEPPKTLRIKLTLKGGAAGATRKRSHSEMEDQPAETKPTETK FT SQQERSSPSKILKLGLRRNYTQEMMKRTTPEDLAKGPPEPPKDKLEALNLAPLPGPPPR FT NYNTAPGGRPRRRAAAALIAEFQNHAEQRARRANARKRNVPSDKSDDPNSQPNGQPNGH FT SNGQPN" FT mRNA complement(join(<64627..67347,67409..>67498)) FT /locus_tag="An04g03490" FT exon complement(64627..67347) FT /locus_tag="An04g03490" FT /number=1 FT intron complement(67348..67408) FT /locus_tag="An04g03490" FT /number=1 FT exon complement(67409..67498) FT /locus_tag="An04g03490" FT /number=2 FT CDS join(68447..68592,68668..68866,68930..69208,69261..69500) FT /locus_tag="An04g03495" FT /note="Complex: Swp1 from S. cerevisiae is a component of FT the oligosaccharyltransferase complex." FT /note="Function: Swp1 from S. cerevisiae interacts FT physically with Wbp1." FT /note="Function: Swp1 from S. cerevisiae was isolated as a FT suppressor of a mutation in wbp1, an essential component of FT the N-oligosaccharyl transferase." FT /note="Title: similarity to oligosaccharyltransferase delta FT subunit Swp1 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIH1" FT /db_xref="InterPro:IPR008814" FT /db_xref="UniProtKB/TrEMBL:A2QIH1" FT /citation=[20] FT /citation=[29] FT /protein_id="CAK38615.1" FT /translation="MQLWHSVLQLSLLASAAIPTAAASAWGFTDATVSVNTKGAGVGAG FT VKEVIPDNKALTKPVALGVADTLKVTLTAQEGRAGKHAHQVYLLLQDPETGLDISYPFN FT VKDNGKSRLDLKDLPIQFLSASEPLEARFLIGSFGESTAYNAAAFQLDVTRNADEPVPT FT VEVSRYGKLPEIHHIFKSDPQSPPVVITLAFVAMVLATLPVLGGVWLFLGVNVNHLPTA FT LKSAPIPHVVFLGSLLSIEGIFFLYYTSWTLFQILPAVAVVGSVAFVSGSRALGEVQGR FT RLAGLR" FT mRNA join(<68447..68592,68668..68866,68930..69208,69261..>69500) FT /locus_tag="An04g03495" FT exon 68447..68592 FT /locus_tag="An04g03495" FT /number=1 FT sig_peptide 68447..68515 FT /locus_tag="An04g03495" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(68516..68592,68668..68866,68930..69208,69261..69497) FT /locus_tag="An04g03495" FT intron 68593..68667 FT /locus_tag="An04g03495" FT /number=1 FT exon 68668..68866 FT /locus_tag="An04g03495" FT /number=2 FT intron 68867..68929 FT /locus_tag="An04g03495" FT /number=2 FT exon 68930..69208 FT /locus_tag="An04g03495" FT /number=3 FT intron 69209..69260 FT /locus_tag="An04g03495" FT /number=3 FT exon 69261..69500 FT /locus_tag="An04g03495" FT /number=4 FT CDS join(69935..70160,70230..70597,70799..70933) FT /locus_tag="An04g03500" FT /note="Title: weak similarity to glycoprotein gpv FT -Varicella-zoster virus" FT /db_xref="UniProtKB/TrEMBL:A2QIH2" FT /protein_id="CAK38616.1" FT /translation="MGASSSKPARSAAQAVSRRQYPKQPVSPPTSSPAQPPPASKPTRQ FT QPQPPRQPSRPPPAGPTYHSKEPPSLERSSAIDLDGRDPDFAAQLRTIGPVTPNPTFSP FT SSTFARQQPAPTVFPPASNPALLVFSARQRLTKAAEQELEAMGRSGFQGREYLDALTIR FT QVLAMRDRQGLSAEEIERLLRLKSGVVGRLGERGVDYIYGLYAAAMLLHYSRARAIMWA FT CGITGELGLALPGHNWYSKD" FT mRNA join(<69935..70160,70230..70597,70799..>70933) FT /locus_tag="An04g03500" FT exon 69935..70160 FT /locus_tag="An04g03500" FT /number=1 FT intron 70161..70229 FT /locus_tag="An04g03500" FT /number=1 FT exon 70230..70597 FT /locus_tag="An04g03500" FT /number=2 FT intron 70598..70798 FT /locus_tag="An04g03500" FT /number=2 FT exon 70799..70933 FT /locus_tag="An04g03500" FT /number=3 FT tRNA complement(71625..71714) FT /gene="tRNA-Asp (GTC)" FT /locus_tag="An04e03510" FT /product="transfer RNA-Asp (GTC)" FT /inference="profile:tRNAscan:1.4" FT CDS join(71740..72002,72279..72390,73178..73351) FT /locus_tag="An04g03520" FT /note="Title: questionable ORF" FT /db_xref="UniProtKB/TrEMBL:A2QIH3" FT /protein_id="CAK38617.1" FT /translation="MLYQLPIVPFKTRAIVLRTSPIATMKPTPPDDDSTSHTINTNHSK FT TGDPGLSSSHFSFQKSSTNIRHTRNNRNRSQETPSSTLLAIAKSHADDPGKYQVTTETA FT SSGEEVYTNEMVMKRRNPEMSSIHQPNVTSTSPTLVQNHSKTYAVMRGSLKWGGGDYPG FT SMGGDGQYDGSWQILGRDP" FT mRNA join(<71740..72002,72279..72390,73178..>73351) FT /locus_tag="An04g03520" FT exon 71740..72002 FT /locus_tag="An04g03520" FT /number=1 FT intron 72003..72278 FT /locus_tag="An04g03520" FT /number=1 FT exon 72279..72390 FT /locus_tag="An04g03520" FT /number=2 FT intron 72391..73177 FT /locus_tag="An04g03520" FT /number=2 FT exon 73178..73351 FT /locus_tag="An04g03520" FT /number=3 FT CDS complement(join(73923..74234,74339..74677,74733..74951)) FT /locus_tag="An04g03530" FT /EC_number="1.1.1.-" FT /note="Function: NAD-dependent D-arabinitol dehydrogenase FT ARD of C. tropicalis interconverts D-arabinitol plus NAD FT with D-ribulose plus NADH." FT /note="Similarity: shows strong similarity to several short FT chain dehydrogenase/reductases with different FT specificities." FT /note="Title: strong similarity to NAD-dependent FT D-arabinitol dehydrogenase ard - Candida tropicalis" FT /db_xref="GOA:A2QIH4" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2QIH4" FT /citation=[17] FT /inference="profile:COGS:COG1028" FT /inference="profile:PFAM:PF00106" FT /inference="similar to AA sequence:PIR:JC4041" FT /protein_id="CAK38618.1" FT /translation="MSVSFDTTDVAPAPVPVVQDGPCLGSKSRMPEFSLAGKVVLVSGA FT ARGLGLTQAEALLEAGAKVYALDRLDEPSPEFAVIQERALQELGTELHYRRIDVRDTEL FT LNTVIETIANTEGRMDGLVAAAGIQQETPALEYTAKDSNTMFEVNVTGVFMTAQAVAKQ FT MIRFGNGGSIALIASMSGTIANRGLICPAYNASKAAVIQLGRNLASEWGQYKIRVNTIS FT PGYIVTAMVEKLFEQYPERRDEWPKQNMLGRLSAPNEYRGAAVFLLSDASSFMTGSDLR FT IDGGHAAW" FT mRNA complement(join(<73923..74234,74339..74677,74733..>74951)) FT /locus_tag="An04g03530" FT exon complement(73923..74234) FT /locus_tag="An04g03530" FT /number=1 FT intron complement(74235..74338) FT /locus_tag="An04g03530" FT /number=1 FT exon complement(74339..74677) FT /locus_tag="An04g03530" FT /number=2 FT intron complement(74678..74732) FT /locus_tag="An04g03530" FT /number=2 FT exon complement(74733..74951) FT /locus_tag="An04g03530" FT /number=3 FT CDS join(75157..75275,75488..75574,75689..76136) FT /locus_tag="An04g03540" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIH5" FT /protein_id="CAK38619.1" FT /translation="MSPWVASSGGMMLAQDGHEGSCEQLEIGTSTQERLAARERVTTVI FT VTALFNQYDISTRSISSFSPAVTGPIMRNSPRSVALTASSKANLRPDRHEQRTTAGHGF FT PLEGPLFVECSAFSFRQSGDGANGGAAGGKKLPSTSNRKTGDGKRMTVRVTVGLSLPLL FT LITGPAWAVLEATFYSVEHSTGWSRVVRRSSRIQCQSSRALVLHIIRHLSGYSM" FT mRNA join(<75157..75275,75488..75574,75689..>76136) FT /locus_tag="An04g03540" FT exon 75157..75275 FT /locus_tag="An04g03540" FT /number=1 FT intron 75276..75487 FT /locus_tag="An04g03540" FT /number=1 FT exon 75488..75574 FT /locus_tag="An04g03540" FT /number=2 FT intron 75575..75688 FT /locus_tag="An04g03540" FT /number=2 FT exon 75689..76136 FT /locus_tag="An04g03540" FT /number=3 FT CDS complement(join(76157..76202,76299..76348,76678..76983)) FT /locus_tag="An04g03550" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIH6" FT /protein_id="CAK38620.1" FT /translation="MLTGPDTAADEDAGAMVAEVRGRNAPNFRQEKATRESQKGKMGTP FT HLVTVHLPGIGMRPFHPAKKNMMVTRQSHGSASGGRSDCLLYIWFRPINHIVGSRDHQL FT ANRIAWTCDKLAVAKYYATVSTEKALSPM" FT mRNA complement(join(<76157..76202,76299..76348,76678..>76983)) FT /locus_tag="An04g03550" FT exon complement(76157..76202) FT /locus_tag="An04g03550" FT /number=1 FT intron complement(76203..76298) FT /locus_tag="An04g03550" FT /number=1 FT exon complement(76299..76348) FT /locus_tag="An04g03550" FT /number=2 FT intron complement(76349..76677) FT /locus_tag="An04g03550" FT /number=2 FT exon complement(76678..76983) FT /locus_tag="An04g03550" FT /number=3 FT CDS join(77149..77235,77380..77498,77538..77671,77813..77837, FT 77969..78065) FT /locus_tag="An04g03560" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIH7" FT /protein_id="CAK38621.1" FT /translation="MKIGLNKHWVQMRPSDMRPASLSNPEDPGNQNAGETAIGSGNDRL FT EGGRLFRDPQVPDSPTDRLESNCWPQRNATGNVEQQPRFQPYYFDLDETTTDAVLEIKE FT LTYIKALTPDETSGPMQRAKEDANIRKVNVIVTEAVADNTVAQRLRVLA" FT mRNA join(<77149..77235,77380..77498,77538..77671,77813..77837, FT 77969..>78065) FT /locus_tag="An04g03560" FT exon 77149..77235 FT /locus_tag="An04g03560" FT /number=1 FT intron 77236..77379 FT /locus_tag="An04g03560" FT /number=1 FT exon 77380..77498 FT /locus_tag="An04g03560" FT /number=2 FT intron 77499..77537 FT /locus_tag="An04g03560" FT /number=2 FT exon 77538..77671 FT /locus_tag="An04g03560" FT /number=3 FT intron 77672..77812 FT /locus_tag="An04g03560" FT /number=3 FT exon 77813..77837 FT /locus_tag="An04g03560" FT /number=4 FT intron 77838..77968 FT /locus_tag="An04g03560" FT /number=4 FT exon 77969..78065 FT /locus_tag="An04g03560" FT /number=5 FT CDS complement(join(78958..79420,79476..79881,79955..80081)) FT /locus_tag="An04g03570" FT /EC_number="1.1.1.65" FT /note="Function: pyridoxine 4-dehydrogenase PLR of S. pombe FT catalyzes the reduction of pyridoxal by NADPH to form FT pyridoxine and NADP+." FT /note="Title: strong similarity to pyridoxine FT 4-dehydrogenase PLR - Schizosaccharomyces pombe" FT /db_xref="GOA:A2QIH8" FT /db_xref="InterPro:IPR001395" FT /db_xref="UniProtKB/TrEMBL:A2QIH8" FT /citation=[64] FT /inference="profile:COGS:COG0667" FT /inference="profile:PFAM:PF00248" FT /inference="similar to AA sequence:PIR:T43436" FT /protein_id="CAK38622.1" FT /translation="MPEIAGKEVGPIGFGLMGLTWRATPPSQEQAFDAMHTAIQKGCTC FT WNGGENYGPLEYNSLVLLEQYLERYPEDADKIVLNIKGGVNPETHQIDASPENTRRSLD FT NCIAQLKSRKKIDMFEFARRDPAVPMHETFALIEKEYVQTGKIEGIALSEVRAETIHEA FT VKYTKVLAVEAELSLFTTDILENGVAAACAQYGIPIIAYSPIGRGMLTGQFKKFDDLPQ FT DSLLRSFDFPRFQRENFEKNMQLVQKVEDIAKRKNCTPAQLAINWTRALSRRPGVPTII FT PIPGATTAERVEENSTQIDITDEEMLEIDEILAKFTPAGERYPGAIPVNT" FT mRNA complement(join(<78958..79420,79476..79881,79955..>80081)) FT /locus_tag="An04g03570" FT exon complement(78958..79420) FT /locus_tag="An04g03570" FT /number=1 FT intron complement(79421..79475) FT /locus_tag="An04g03570" FT /number=1 FT exon complement(79476..79881) FT /locus_tag="An04g03570" FT /number=2 FT intron complement(79882..79954) FT /locus_tag="An04g03570" FT /number=2 FT exon complement(79955..80081) FT /locus_tag="An04g03570" FT /number=3 FT CDS join(80762..80767,80996..81877) FT /locus_tag="An04g03580" FT /note="Title: similarity to hypothetical protein BAA97223.1 FT - Arabidopsis thaliana" FT /db_xref="GOA:A2QIH9" FT /db_xref="InterPro:IPR006620" FT /db_xref="UniProtKB/TrEMBL:A2QIH9" FT /protein_id="CAK38623.1" FT /translation="METKEIYEEPDSTSILYSNTKHAAITFQIPHLSTTCHRINFETSQ FT PPLPEYKNLCAAVIDNAFTEEECAELIRIAESSTIPPGDSTATPTWERAMINIGNGRQA FT LATDTRNCGRIIYDSEDIADKLLARLLPFFKELGIDKIENQPRVTGLGGRNKAYGMTRL FT NERLRFLKYEGGEYFRPHWDALYMTPDGKEKSYYTIQLYLNGNGEQDLGELKREMKRAE FT RGEGEVNMDVKGELLGGATSFLPRYEEKERHLRVFPKTGSVLVFQQMDLLHGGDPVLRG FT TKYTMRTDVMYQQL" FT mRNA join(<80762..80767,80996..>81877) FT /locus_tag="An04g03580" FT exon 80762..80767 FT /locus_tag="An04g03580" FT /number=1 FT intron 80768..80995 FT /locus_tag="An04g03580" FT /number=1 FT exon 80996..81877 FT /locus_tag="An04g03580" FT /number=2 FT CDS join(82797..82842,82928..83591,83643..84834) FT /locus_tag="An04g03590" FT /EC_number="3.1.1.5" FT /note="Catalytic activity: lysophospholipase catalyzes the FT conversion of 2-lysophosphatidylcholine + H2O = FT glycerophosphocholine + a carboxylate." FT /note="Pathway: phospholipid degradation." FT /note="Title: strong similarity to lysophospholipase from FT patent WO0127251 - Aspergillus oryzae" FT /db_xref="GOA:A2QII0" FT /db_xref="InterPro:IPR002642" FT /db_xref="UniProtKB/TrEMBL:A2QII0" FT /inference="profile:PFAM:PF01735" FT /protein_id="CAK38624.1" FT /translation="MQCIAALLAFASILSGVSASFNNEYGRHLMQQRALPNAPDGYTPT FT TVGCSASRPTVRSATALSSNESSWLRTRRNNTLSAMREFFGRVNITDFDAVGYINRISS FT NTSDLPNIGIAVSGGGYRALMNGAGAIKAFDNRTVNSTSNGQLGGLLQSATYLAGLSGG FT AWLVGSIYLNNFSTISSLQTYDPGDVWQFQNSIFEGPDGDSIQIIDSATYYRDIYDAVS FT GKDDAGWQTSITDYWGRALSYQLVNATAGGINYTWSSIALTDSFRRAEMPMPVLVADGR FT YPDELLVSSNATVYEFNPWEFGTFDPTVHGFVPVQYLGSRFVAGSLPSNESCVRGFDNG FT GFIMGTSSTLFNQFLLQINTTSLPSFLKDAFTSILEDLGENSQDIAVYTPNPFYLWANS FT TSPSASQTVLDLVDGGEDLQNIPLHPLIQPERHVDVIFAVDSSADTQYNWPNGTALVAT FT YERSLNSTGIGNGTAFPAIPDQNTFVNEGLNTRPTFFGCNSSNTTGPAPLVVYLPNFPY FT VTFSNVSTFDPSYSESQRDSIILNGYDVATMGNNSRDGEWSSCVACAVLSRSFERTNTT FT VPDQCSRCFERYCWDGTTNSSTPGTYEPSTVFDNAGYAVMPAVFATTMAAATVSAFM" FT mRNA join(<82797..82842,82928..83591,83643..>84834) FT /locus_tag="An04g03590" FT sig_peptide join(82797..82842,82928..82938) FT /locus_tag="An04g03590" FT /inference="protein motif:SignalP:2.0" FT exon 82797..82842 FT /locus_tag="An04g03590" FT /number=1 FT intron 82843..82927 FT /locus_tag="An04g03590" FT /number=1 FT exon 82928..83591 FT /locus_tag="An04g03590" FT /number=2 FT mat_peptide join(82939..83591,83643..84831) FT /locus_tag="An04g03590" FT intron 83592..83642 FT /locus_tag="An04g03590" FT /number=2 FT exon 83643..84834 FT /locus_tag="An04g03590" FT /number=3 FT CDS join(85356..90103,90153..90705) FT /locus_tag="An04g03600" FT /note="Title: strong similarity to hypothetical protein FT EAA64794.1 - Aspergillus nidulans" FT /db_xref="GOA:A2QII1" FT /db_xref="InterPro:IPR017956" FT /db_xref="UniProtKB/TrEMBL:A2QII1" FT /inference="profile:COGS:COG0643" FT /inference="profile:COGS:COG1196" FT /inference="profile:COGS:COG5271" FT /inference="profile:PFAM:PF00533" FT /protein_id="CAK38625.1" FT /translation="MARAAVIPQSPPKRTTRTRTKGSTTTTSAKPAPKTTKARAPSSAT FT EARKRGSRTTAAASKPAEEDADESTDDEIGMFSERKTTTVAKPKGRPPTKSTTSTTGRG FT RKPTPTTNAESGSDNDDELAQSDAPKKRAGRPRTKPATPAKTETAPKTRGRPKGSTTTK FT STKPVDPVKENTRLNAKGFTDIDFSSSREAPKRVYIATNSATARSNMLRGPAKKKKVTF FT QDPSDTAEEEMSEPSPPPTAGRRRGTIGPGLQAGLASKPVRKPAATSAKGRKPGTAKKD FT GPKPLSPKKTTQVAKALSSYVDSDGEDDELSGDKDQVKFVVDSPHKHGSENTGLSSPVK FT KINITGKFRKSLDENGEPLPGPRRSIDFNDTLLMSSPARRPPPSPFNFSLRETPKRGAF FT ALRDDPKSLSQPHLSPTHNSPLKLSPRKAHLETPKRGSVFLDSGRPLSQPNFTPGHNSP FT LKASPRKGLFGASFTSQAHAESTSTPLRHSVSFLQSPAKRIASPFKSSLSASRGPITED FT DEADPREDVEEPATPDVDESPLRMTDFEGAKDFESEDEQVDEELPERVDDNYATKEIDT FT QSPAVAEESDEDTLHEEVDREQTIEYEEDDMGNAAEDVTTHEEHVDSDVPNDQHVEESA FT DELVEATEEPMEEFEEEFEEKLRNDPEEEPADEPVEPMEEPMEEYAEATAEEFAVEPTE FT HIDELVKEPMGEFAEESVEPPMEETEESVEGEATEPTEEPCESPVKELVTEPDVELVRE FT SEAEQTHSTGEDEEIGENRDQNEPQEHTTEYAEDGQELDAEVPSPETREDTVEMEDISA FT SQPEKDLSPAKHSETREPILEGETSVGHDQENAEQPDQEAEEQTESANPATENAPGPAN FT TGLRSSLVEGLEDVFVEHAAAPEPVNDDRDGSETEDDPDMLEASDEENAAEAFDDFDDV FT DDQYTFDDSEPTLVGFEATERIPPNLVPIQPYEVEEAEDPFSPSRQAQNASRRVLSPVR FT ILESHIRQSPIRRSTRNVPTAAAAMGNGTQNNVDLSDPFVEHSHATPRRRSTRGLVFDN FT APRFTPLAQQFRQWKSNSPEKAQARRPRRGIFSLGGRRRSSNVTSTSEVSYPDVSRQAE FT ALSSEPQIPHQEREDVDAPEVAESEEQEPETNDELAHEETPMPVSPVSPAPQEQSEVVD FT VPESNEDQEQEAEPMAEDPNQPSSAELPTPQEDLNDFDMTQPEEQDQDPELVGDEPSPE FT KASLPNSPILEEDSNDADMPAIYEDEPSQPIGDMPSQVEASLAEPDTLQKTDKHADIPQ FT IYEDEDQGSQLAGDTETLEEPLEQPAEVVESSQEAVTDASEDKENMYAVPSVPDNLASE FT AQPGKERELEDIPVLAPSTPVKNRIPEMQTVHTVSKVPLKPEGQISPLKMSRKRGLSLS FT ASSPGRSSRLRMSIAPIAQNAPQLSPRKSPRLQRTVARQSLGQSHTPDTAKKHVEAQRP FT APPKRPSYSPSPKKKTKTPRTSITAPKLALQGSVVYVDVHTTEGEDASGIFIELLQQMG FT ARCVKNWSWNPRASVSPEEGTEPKEGKVGITHVVYKDGGVRTLEKVRHARGLVKCVGVG FT WVLDCERENKWLDEAHYEVDLSIIPRGGAKRRKSMEPRALSNVNGTLVKTDAASASANR FT RRSSLAPPKESTPRDATPSSRDEPSTPDATPKIGAGHTEADQRYCHTPKTPGYTFDMDA FT IGMSPATPFYLSQRTKLVQQTCPPKQTRQGLFTTPAAAREPNQKLRAKLEAARRKSLAY FT KPRVGSPLVE" FT mRNA join(<85356..90103,90153..>90705) FT /locus_tag="An04g03600" FT exon 85356..90103 FT /locus_tag="An04g03600" FT /number=1 FT intron 90104..90152 FT /locus_tag="An04g03600" FT /number=1 FT exon 90153..90705 FT /locus_tag="An04g03600" FT /number=2 FT CDS complement(join(90850..90889,90996..91501)) FT /locus_tag="An04g03610" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QII2" FT /protein_id="CAK38626.1" FT /translation="MSDSIPSAHDDEQHQHQQHHHPTNAEDRKAAAALSALNPSHIAPD FT TPKSASTPSAADQEALGQAMSRLEIASGQSGGAGGRGGVQKPAEAQKRVPVEATKKKAA FT KVAVEDVNLLVCQYLIERFGRRLIGMVGKIEELELNKSTATELLRLHDGNVVEAMRAFV FT SVGPGLKHVDVCCMMNIT" FT mRNA complement(join(<90850..90889,90996..>91501)) FT /locus_tag="An04g03610" FT exon complement(90850..90889) FT /locus_tag="An04g03610" FT /number=1 FT intron complement(90890..90995) FT /locus_tag="An04g03610" FT /number=1 FT exon complement(90996..91501) FT /locus_tag="An04g03610" FT /number=2 FT CDS join(92002..92029,92097..92206,92261..92324,92390..92482, FT 92531..92582,92636..93680) FT /locus_tag="An04g03620" FT /EC_number="2.5.1.54" FT /note="Catalytic activity: FT 2-dehydro-3-deoxyphosphoheptonate aldolase catalyzes the FT conversion of FT 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate + FT orthophosphate = phosphoenolpyruvate + D-erythrose FT 4-phosphate + H2O." FT /note="Pathway: 2-dehydro-3-deoxyphosphoheptonate aldolase FT catalyzes the first step in the biosynthesis from FT chorismate of the aromatic amino acids (the shikimate FT pathway)." FT /note="Title: similarity to FT 2-dehydro-3-deoxyphosphoheptonate aldolase - Arabidopsis FT thaliana" FT /db_xref="GOA:A2QII3" FT /db_xref="InterPro:IPR002480" FT /db_xref="UniProtKB/TrEMBL:A2QII3" FT /inference="profile:COGS:COG3200" FT /inference="profile:PFAM:PF01474" FT /protein_id="CAK38627.1" FT /translation="MAESEWSPSSWASKPIKQDVVYDDAAGVQAALAKLQKLPPLVTTQ FT EVDDLKKSLKNVALGKAFVLQGGDCAELFDYCNMDMIEAKVKLLLQMSLVLIWGANKPV FT VRIARIAGQFAKPRSSPMETIDGVEMPSFRGDNINGFDATPESRKPDPSRLVSAYFHSA FT ATLNYMRASLSSGLADLHSPLDWGLGHVITPSIREKYTRIVNRVKDALRFMQTVGIDTD FT RGVETVDIYTSHEGLLLEYEQSLLRHLKNPDSPSTTHSYYATSSHFLWIGDRTRQLNGA FT HVEFFRGIANPIGIKIGPSMTPAELTSLLDIVNPAREIGKVTLISRYGAAKISQYLPAH FT IAAVQASGHIPVWQCDPMHGNTQATPSGVKTRHFSDILSELKQALEIHRAAGSFLGGMH FT LELTGEAVTECVGGAGGLTEEGLSERYTTFCDPRLNEKQALELAFLVAGFYRELDEELA FT EDESI" FT mRNA join(<92002..92029,92097..92206,92261..92324,92390..92482, FT 92531..92582,92636..>93680) FT /locus_tag="An04g03620" FT exon 92002..92029 FT /locus_tag="An04g03620" FT /number=1 FT intron 92030..92096 FT /locus_tag="An04g03620" FT /number=1 FT exon 92097..92206 FT /locus_tag="An04g03620" FT /number=2 FT intron 92207..92260 FT /locus_tag="An04g03620" FT /number=2 FT exon 92261..92324 FT /locus_tag="An04g03620" FT /number=3 FT intron 92325..92389 FT /locus_tag="An04g03620" FT /number=3 FT exon 92390..92482 FT /locus_tag="An04g03620" FT /number=4 FT intron 92483..92530 FT /locus_tag="An04g03620" FT /number=4 FT exon 92531..92582 FT /locus_tag="An04g03620" FT /number=5 FT intron 92583..92635 FT /locus_tag="An04g03620" FT /number=5 FT exon 92636..93680 FT /locus_tag="An04g03620" FT /number=6 FT CDS complement(join(93915..94008,94084..94997,95068..95314, FT 95382..96085)) FT /locus_tag="An04g03630" FT /note="Title: strong similarity to hypothetical transport FT protein YCR023c - Saccharomyces cerevisiae" FT /db_xref="InterPro:IPR011701" FT /db_xref="UniProtKB/TrEMBL:A2QII4" FT /inference="profile:COGS:COG0477" FT /inference="similar to AA sequence:PIR:S19434" FT /protein_id="CAK38628.1" FT /translation="MSVDSSIDGDKDSVNTAIHDGSSAQTRILAPAPIPESSQWRRLSV FT DDHLVANSSDDDESSFSDSDSDSFSSSEDEEDNNLIANEDDPNHNDTADEKPVTWSSLP FT KKSQLAILTIARLSEPLTQTSLQAYMFYQLKSFDPSLPDSTISGQAGILQGSFTAAQFL FT TAVWWGRLADAEWMGRKRVLLIGSLGTCLSCLGFGFSRSFVAAAVFRTLGGVLNSNVGV FT MRTMIAEIIEEKKYQSRAFLLLPMCFNIGVIIGPVLGGALADPVKNYPQIFGPGTFLGG FT ANGVEWMRKWPFLLPNLLSAVFIFCSLLAVFFGLDETHETARYRSDWGRQLGHRIARAL FT RRTRNKDSKYYQRLNEHPDDESLYIDDNTSHHHRRSISISSRSSRPKPKTHQRPKFREI FT YTRNVLLTLLAQFLLAFHTSAFNAITFTFLPTPRAPPESHRGWFHFSGGLGLPSSRVGL FT ATAIIGIIGLPLQIFIYPWVQGYLGTLRSFRTFLPFSSLAYALMPFLLLLPRAAYIVWP FT AFTVVIALQVVSRTFALPAAVILVNNSVSDAKVLGTINGVSQSISSAARTLGPFLGGWG FT LGEGLRENFVGGVWWGLAVEAVLGWVVLWFIWEGKGIERKKKSSSKYGVYMDGWMNGLG FT WVMIDETAFIDYEYVFS" FT mRNA complement(join(<93915..94008,94084..94997,95068..95314, FT 95382..>96085)) FT /locus_tag="An04g03630" FT exon complement(93915..94008) FT /locus_tag="An04g03630" FT /number=1 FT intron complement(94009..94083) FT /locus_tag="An04g03630" FT /number=1 FT exon complement(94084..94997) FT /locus_tag="An04g03630" FT /number=2 FT intron complement(94998..95067) FT /locus_tag="An04g03630" FT /number=2 FT exon complement(95068..95314) FT /locus_tag="An04g03630" FT /number=3 FT intron complement(95315..95381) FT /locus_tag="An04g03630" FT /number=3 FT exon complement(95382..96085) FT /locus_tag="An04g03630" FT /number=4 FT CDS complement(join(97179..98231,98283..98992,99046..100249)) FT /locus_tag="An04g03640" FT /note="Similarity: the ORF shows weak (but specific) FT similarity to the A. niger protein An17g02290. The FT similarity between the two proteins, however, is restricted FT to a stretch of about 140 amino acids." FT /note="Title: weak similarity to hypothetical protein FT SPAC4H3.11c - Schizosaccharomyces pombe" FT /db_xref="UniProtKB/TrEMBL:A2QII5" FT /inference="profile:COGS:COG3264" FT /inference="profile:COGS:COG5022" FT /protein_id="CAK38629.1" FT /translation="MSREATTNSFASFGSDFDPEHEALASTKELGHGSPRLPSMHTNAR FT KRHEYEEEEPDYAFNTSTFEQYLPDFSPVGTSEEEEEADNDDSISIEAGRGPTKPPRRL FT DDSRNSYMSIENSVRSSSPAVRLDYPTSNTPQKSALRNPARRAVSDSLRKDAQIRRASL FT AHKENVDPHTAKSNRKERRTLSDMHAKVRDTYEGSLIEDERPPAMANSTRPTRFGNPNL FT SHQIADAVEKASQEAYARELRRGKSSTNSRNMAHNAGDTATQQSFLLPDLPNLSELVSG FT VYEDGTPVYARQNRARTTRFVSPPHDATDVSLTREHMPLDAVPIPEDEKALFVSLRLLQ FT DKVAELERSKSDAERRLDDMKRENESLRTNKSRSKDKHGRSRPYESEEDDYRRDQLASD FT NQKLDAANLALQNKLDIIERKAQIQESTLKRLNRERDMAVSQLGVAYLESQDLKSENES FT LRQENADLKSQISKILSAGSRARDDTVESEQSSMTDASDEDSQPDTQHSRHTSRSTREV FT TGKSSRSKTRRQEDSRAKISTQVDKEISRLEQERAEEALFSIDVPRTREKSKSKSGKSK FT SRSESSDVSTRKQSNTGKQRVKRVVVEEVEETEPVESSGEVTGNTKKSNATEQDLTLLS FT FVDEREIAQLRKTLEEERLARKRRQSSTSKEQTANETGNTTRQSLSKSTIPRKSSLKES FT KGLPSRPASAMGDLTANSKASMTEGESNLSVPVERPRRHSDNSVPAASQRRRRRMAEEM FT TSAFILPDITFNPAHVVDNNLAKLPEPAQRALDSATKHNGKNCTVCKQTIPGGSCDHTA FT EAVKIPKPVPVSERMPEPSVYNEEPTMRPAQSPELALATVLKALEDELAHLKMQLVAYQ FT GSYNKLDASLSKRKRKSLGEKIEKLLKDIDMKADQIYALYDVLEGQKQNGREMTEQEME FT VTLQSIGIDTAGRTADVTATTDKSSRKEPDSEDDDELPWEGFESTLEMTGRTGGSRRN" FT mRNA complement(join(<97179..98231,98283..98992,99046..>100249)) FT /locus_tag="An04g03640" FT exon complement(97179..98231) FT /locus_tag="An04g03640" FT /number=1 FT intron complement(98232..98282) FT /locus_tag="An04g03640" FT /number=1 FT exon complement(98283..98992) FT /locus_tag="An04g03640" FT /number=2 FT intron complement(98993..99045) FT /locus_tag="An04g03640" FT /number=2 FT exon complement(99046..100249) FT /locus_tag="An04g03640" FT /number=3 FT CDS complement(join(101252..102544,102608..102766)) FT /locus_tag="An04g03650" FT /product="hypothetical protein" FT /note="Remark: blast matches are due to repetitive FT sequence." FT /db_xref="UniProtKB/TrEMBL:A2QII6" FT /protein_id="CAK38630.1" FT /translation="MHIPANFRQFDIRQDGPGNIINNPNNNNNTDGSQDKNHASGNDNS FT SRNNIIIICVACIIFAVASALMTYFVLRTLRRMNCRPKYLPGKFLKDKWNRWNVGVSYG FT QVPGSNNQNANTTRDTPAEGGSEMRSTTPAANNTSNVRRDTSVRSVITLPAYSPSPKPT FT EQVIAREGERAGMDMVVEFPETAEEEESRREELMESLYQIRLQRREELADREWRRQERR FT EARARGDYIRLEELRQESRARARSSASANGSASNLSAALAESRNRGRDRRISSVSYAEL FT GHVRHDGSRIRATSPDSDRRPLLTDASAPDRSSGSILTGVHSRGESYSSYQSGATNVSD FT ADTLTQVQSHAVSAHSADRPSIAVDEGDVGELNIPPPEYEVLEWGEAPPYTSPVAERNE FT HAPQLRELTPLPTIHIDVASPISNTPTTPTNPLREEEREEQQSTEQHTTANQPISEEHA FT EEEHPASQSAETHLLRDDTHSHQSS" FT mRNA complement(join(<101252..102544,102608..>102766)) FT /locus_tag="An04g03650" FT exon complement(101252..102544) FT /locus_tag="An04g03650" FT /number=1 FT intron complement(102545..102607) FT /locus_tag="An04g03650" FT /number=1 FT exon complement(102608..102766) FT /locus_tag="An04g03650" FT /number=2 FT CDS join(103114..103227,103404..103598,103683..103742, FT 103808..103945) FT /locus_tag="An04g03660" FT /note="Title: weak similarity to hypothetical protein FT YLR094c - Saccharomyces cerevisiae" FT /db_xref="UniProtKB/TrEMBL:A2QII7" FT /protein_id="CAK38631.1" FT /translation="MDKKRHARIHGLKLCDGWEKGPGKNTSRTAARFQRLTGPAEVTDQ FT KYDPWTLPDSGGQFDRDTTRLRIKRDCIQIKKDPIAPSRLIKDDFIVKREAQSKLMLPG FT LGFLSVDLLQTSLYLALSSGWGCHYPVGRKSSRVIITLETSYNGVSLWSLLLNPDPLLI FT YRIEM" FT mRNA join(<103114..103227,103404..103598,103683..103742, FT 103808..>103945) FT /locus_tag="An04g03660" FT exon 103114..103227 FT /locus_tag="An04g03660" FT /number=1 FT intron 103228..103403 FT /locus_tag="An04g03660" FT /number=1 FT exon 103404..103598 FT /locus_tag="An04g03660" FT /number=2 FT intron 103599..103682 FT /locus_tag="An04g03660" FT /number=2 FT exon 103683..103742 FT /locus_tag="An04g03660" FT /number=3 FT intron 103743..103807 FT /locus_tag="An04g03660" FT /number=3 FT exon 103808..103945 FT /locus_tag="An04g03660" FT /number=4 FT CDS complement(join(103947..104001,104080..104178, FT 104225..104346,104574..104754,104865..104978, FT 105346..105460,105654..105714,105740..105805)) FT /locus_tag="An04g03670" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QII8" FT /protein_id="CAK38632.1" FT /translation="MAKINLPKKISFGKSGGTDAYVAKFEDPWHGWVSLGSFGIAGVGG FT VLYAPRFNGWCGMRLDWIGVAGITCVFGSWRPERILANVCYMIPVAHMLVFMMSESSSE FT LCFDAVIAIYSDFRVAGPPQVHQTSYIPVISKKHAALMKVFWRENKKPSTNSFSKTYFD FT IVFTTESEARCNTVSKVLPRRKIFSSPLPGMNCHQFCMGSQGDMALHRVLAVTVIRTYR FT DWVKVMCDNTSDSAQCALRSAKNIPLLIVRQIMGNSRKFVALIARSAI" FT mRNA complement(join(<103947..104001,104080..104178, FT 104225..104346,104574..104754,104865..104978, FT 105346..105460,105654..105714,105740..>105805)) FT /locus_tag="An04g03670" FT exon complement(103947..104001) FT /locus_tag="An04g03670" FT /number=1 FT intron complement(104002..104079) FT /locus_tag="An04g03670" FT /number=1 FT exon complement(104080..104178) FT /locus_tag="An04g03670" FT /number=2 FT intron complement(104179..104224) FT /locus_tag="An04g03670" FT /number=2 FT exon complement(104225..104346) FT /locus_tag="An04g03670" FT /number=3 FT intron complement(104347..104573) FT /locus_tag="An04g03670" FT /number=3 FT exon complement(104574..104754) FT /locus_tag="An04g03670" FT /number=4 FT intron complement(104755..104864) FT /locus_tag="An04g03670" FT /number=4 FT exon complement(104865..104978) FT /locus_tag="An04g03670" FT /number=5 FT intron complement(104979..105345) FT /locus_tag="An04g03670" FT /number=5 FT exon complement(105346..105460) FT /locus_tag="An04g03670" FT /number=6 FT intron complement(105461..105653) FT /locus_tag="An04g03670" FT /number=6 FT exon complement(105654..105714) FT /locus_tag="An04g03670" FT /number=7 FT intron complement(105715..105739) FT /locus_tag="An04g03670" FT /number=7 FT exon complement(105740..105805) FT /locus_tag="An04g03670" FT /number=8 FT CDS join(105894..106137,106247..106328,106387..106906) FT /locus_tag="An04g03680" FT /EC_number="3.2.1.-" FT /note="Title: similarity to glucanase ZmGnsN4 from patent FT WO200073470-A2 - Zea mays" FT /db_xref="GOA:A2QII9" FT /db_xref="InterPro:IPR002925" FT /db_xref="UniProtKB/TrEMBL:A2QII9" FT /inference="profile:COGS:COG0412" FT /protein_id="CAK38633.1" FT /translation="MSCPDCFSGHVHEDATPRGTVTTLHGRDAYVTEPTSTENPIKGII FT VIIPDAFGWEFVNNRILADHYADKGGYKVYLPEFMNGHAAPVWSLKTLSSVFKTSSILD FT WIKKPYHVACAAYAMIPFMYHNKFNTSWPTVKTFFTAVRRNEGANLPIAAAGFCWGGLH FT TVYLAHGEEDDKVNGKPLIDAGFTGHPSNLKIPGDIEKIKIPVSFAVAELDNMLKMPQI FT KQIEKALGEEVGEVKVYYGAGHGFCVRADVMVKDVRVQAEEAEDQAIGWFQKQFAKVSY FT " FT mRNA join(<105894..106137,106247..106328,106387..>106906) FT /locus_tag="An04g03680" FT exon 105894..106137 FT /locus_tag="An04g03680" FT /number=1 FT intron 106138..106246 FT /locus_tag="An04g03680" FT /number=1 FT exon 106247..106328 FT /locus_tag="An04g03680" FT /number=2 FT intron 106329..106386 FT /locus_tag="An04g03680" FT /number=2 FT exon 106387..106906 FT /locus_tag="An04g03680" FT /number=3 FT CDS complement(join(106960..107858,107912..108906, FT 109030..109973,110039..110702,110752..111188)) FT /locus_tag="An04g03690" FT /note="Function: the S. cerevisiae homolog Ste6p is a FT ABC-transporter similar to the human MDR transporter. Ste6p FT is responsible for transport of mating pheromone a-factor FT across the plasma membrane." FT /note="Induction: expression of STE6 is mating type FT dependent." FT /note="Similarity: shows strong similarity to several known FT and hypothetical ABC-type transporter proteins." FT /note="Title: strong similarity to mating pheromone FT transporter Ste6 - Saccharomyces cerevisiae" FT /note="plasma membrane" FT /db_xref="GOA:A2QIJ0" FT /db_xref="InterPro:IPR003593" FT /db_xref="UniProtKB/TrEMBL:A2QIJ0" FT /citation=[84] FT /inference="profile:COGS:COG1132" FT /inference="profile:PFAM:PF00005" FT /inference="profile:PFAM:PF00664" FT /inference="similar to AA sequence:PIR:DVBYS6" FT /protein_id="CAK38634.1" FT /translation="MAALLAGARRFIHRKPRWMSLFSFTTTKHYPVLIGGFTFTAVSSL FT SVPIFSVVLGEIFNTFTLFGGGKIAKQDLTPQISTFAVQLVGLGAINWVCNSVYFILFV FT IFGELQVANARTKLFERLLQKSQEWFETQPDGTRVFLSSLQGQVDDLQKATSQPLGLAL FT QYIFRAIFSLALAFFTSWNLTLVTLAGIPFLSAALSFLSTKTNSCMETQKTELGHLSLI FT VDNATSSIDSVKSFNGQDTEMRNFVISVDNAALHYLKRARFTSLQISILRLMTFGMFVQ FT GFWYGSSLATSGELSAGEVLRTFWACLAAAQSMEFLMPQIVVLAKGKDAALSLAHILSS FT ESEDAVRGEGRGSIYPKFCEGDIEVSNVSFAYPAQPNRPVLNTTSFFFPAGETTFVIGR FT SGSGKSTLGQLLTRFYLPVSGDILIDGVPIQSLSIDWVRNNITLLEQRSVLFKESIFMN FT VAFGSRNYEGLNKVDVRECIDLARLQSTIDDLPKGIDTCVGHGGDFLSGGQKQRVAIAR FT ARLRDTPILIMDEPTSALDATNRVEITKAIREWRRGKTTIIITHDMSQIMDHDFAYIMD FT QGSVIQAGYRHELEESTTCFATSKKLSRDESEHADAHSASDRCSSASSKSSIESTRSQS FT PDSFSQHNELAQHSYAIHGYKTSLQSIRQSADTQRVRPRRESIGMQIKRLLKNAAHLAP FT QERMSLGQIMLTILPNLTRGQKLLLLLGCFSTLGHSMATPLFSYCLSKLLETFYNKQAK FT ASTWSLIVLGIAIGDGVISFLMHYLLELCGQAWVDRLRKRGFHRIHDQPRKWFEEAGNE FT PSQLTSSLNHSAEEMRNLVGHFGGYVLVATSVTVVAIIWCMAVCWKLTLVAVACGPVIY FT AITRGLERTTGIWERRCTGVRTTASEIFIETFSQIRTVRTLTLEPYFHKKHMKAAALCM FT VLGVKKAVYTGFLFGLVESMIIFVSSKQPVYKKPMLAELNCAGLIFYYGAVLVSSLEFT FT VTSLMTVFSVLLFSIGYASTVLSWIPQISVSHIMANQVLRLARLPQGASHEHRGNLKIT FT TAAPVKIKNLNFRYPSRPDAHVLRDVSINIPRNQCTAIVGRSGSGKSTIASLLLSLYEA FT PTSQDRMPPISLNGIDIQRIHTPTLRSLISIVSQRPSIFPGTVADNISYGLEDDSPLRT FT MFHIRAAAEAAGIDEFITSLPKGYFTMIGDGGAGMSGGQAQRLVIARALVRQPQLLILD FT EATSSLDPNNAKIIRRTVQRLVATRLGLTVLIITHARDMMEIADNIIVIDKGRVVEAGK FT YKLLARQQGGKLRALIEDPDSDADEPGI" FT mRNA complement(join(<106960..107858,107912..108906, FT 109030..109973,110039..110702,110752..>111188)) FT /locus_tag="An04g03690" FT exon complement(106960..107858) FT /locus_tag="An04g03690" FT /number=1 FT intron complement(107859..107911) FT /locus_tag="An04g03690" FT /number=1 FT exon complement(107912..108906) FT /locus_tag="An04g03690" FT /number=2 FT intron complement(108907..109029) FT /locus_tag="An04g03690" FT /number=2 FT exon complement(109030..109973) FT /locus_tag="An04g03690" FT /number=3 FT intron complement(109974..110038) FT /locus_tag="An04g03690" FT /number=3 FT exon complement(110039..110702) FT /locus_tag="An04g03690" FT /number=4 FT intron complement(110703..110751) FT /locus_tag="An04g03690" FT /number=4 FT exon complement(110752..111188) FT /locus_tag="An04g03690" FT /number=5 FT CDS complement(join(111854..111911,111970..112006, FT 112069..112353,112407..112431,112499..112543)) FT /locus_tag="An04g03700" FT /note="Title: strong similarity to hypothetical protein FT YPL225w - Saccharomyces cerevisiae" FT /db_xref="InterPro:IPR008476" FT /db_xref="UniProtKB/TrEMBL:A2QIJ1" FT /inference="similar to AA sequence:PIR:S65244" FT /protein_id="CAK38635.1" FT /translation="MSKPFDPETAENFEDMEKQFAVKAVEHLMTYWSILEKVPGSQLRL FT TKMDDDILESFQKEFPDFDPAETLNEDKMKSKEGKEKWRNWINQYEKIIEDFNFGTMLR FT ASPNVEYDRDTTIFAMRMQFYAIEIARNRAGLNDWIYERAQKAKK" FT mRNA complement(join(<111854..111911,111970..112006, FT 112069..112353,112407..112431,112499..>112543)) FT /locus_tag="An04g03700" FT exon complement(111854..111911) FT /locus_tag="An04g03700" FT /number=1 FT intron complement(111912..111969) FT /locus_tag="An04g03700" FT /number=1 FT exon complement(111970..112006) FT /locus_tag="An04g03700" FT /number=2 FT intron complement(112007..112068) FT /locus_tag="An04g03700" FT /number=2 FT exon complement(112069..112353) FT /locus_tag="An04g03700" FT /number=3 FT intron complement(112354..112406) FT /locus_tag="An04g03700" FT /number=3 FT exon complement(112407..112431) FT /locus_tag="An04g03700" FT /number=4 FT intron complement(112432..112498) FT /locus_tag="An04g03700" FT /number=4 FT exon complement(112499..112543) FT /locus_tag="An04g03700" FT /number=5 FT CDS complement(join(113214..113313,113367..114211, FT 114268..114387,114440..114675,114734..114808, FT 114858..114885)) FT /locus_tag="An04g03710" FT /note="Title: similarity to hypothetical protein FT SPBC3E7.03c - Schizosaccharomyces pombe" FT /db_xref="GOA:A2QIJ2" FT /db_xref="InterPro:IPR019318" FT /db_xref="UniProtKB/TrEMBL:A2QIJ2" FT /inference="similar to AA sequence:PIR:T40377" FT /protein_id="CAK38636.1" FT /translation="MDFRPLQGQEKLQRVTKLLDSLRTDLEAKSLTSKERVQTLLELRQ FT HGTNPNHAHPIYSKEGIELLARYGVDGDSPDVRRAALRCVANALLLDGSMRQLFVDTGY FT GGKLAERLKCDSSEDEMVISRILFLSTYDTTMDFDNLIRHHSLGENVNYQIVRHAKQFP FT KSGKKSLSQMDELALTDTLKLIFNVSKIYSDLAATFSASIPHLFKMINRIDIPPKPLEG FT LLSYLLNCLSTLDLENKKGKVFDSSPLFPTFNQNCNVDKLINILDQAVSAYGPDELETK FT AIPLFHTLVVIHEMAPDGPRKYMQWLLLPEDNDRSRPIGQSDTLSSKLLNLSTTPYPNL FT KTAISELMFVLSGKDAENLTKNIGYGFAAGLLASRGMEIPKTAGEAFATNPNGFDPEIN FT PITGQKWAAEKKDEGPPMTKEEKEREAERLFVLFERAKANGILQVENPVTRALHEGRFE FT ELPDSDDSD" FT mRNA complement(join(<113214..113313,113367..114211, FT 114268..114387,114440..114675,114734..114808, FT 114858..>114885)) FT /locus_tag="An04g03710" FT exon complement(113214..113313) FT /locus_tag="An04g03710" FT /number=1 FT intron complement(113314..113366) FT /locus_tag="An04g03710" FT /number=1 FT exon complement(113367..114211) FT /locus_tag="An04g03710" FT /number=2 FT intron complement(114212..114267) FT /locus_tag="An04g03710" FT /number=2 FT exon complement(114268..114387) FT /locus_tag="An04g03710" FT /number=3 FT intron complement(114388..114439) FT /locus_tag="An04g03710" FT /number=3 FT exon complement(114440..114675) FT /locus_tag="An04g03710" FT /number=4 FT intron complement(114676..114733) FT /locus_tag="An04g03710" FT /number=4 FT exon complement(114734..114808) FT /locus_tag="An04g03710" FT /number=5 FT intron complement(114809..114857) FT /locus_tag="An04g03710" FT /number=5 FT exon complement(114858..114885) FT /locus_tag="An04g03710" FT /number=6 FT CDS join(115785..118715,118765..119031,119081..121180) FT /locus_tag="An04g03720" FT /note="Title: strong similarity to hypothetical protein FT SPAC6F6.17 - Schizosaccharomyces pombe" FT /db_xref="InterPro:IPR000276" FT /db_xref="UniProtKB/TrEMBL:A2QIJ3" FT /inference="profile:COGS:COG3468" FT /inference="profile:COGS:COG5271" FT /inference="similar to AA sequence:PIR:T39050" FT /protein_id="CAK38637.1" FT /translation="MVEILGPLSARPPTPPRTSSRMLSENDRTEDSPVVVHTPRDSPFS FT VNGSTGAPSSRQSKRVNFSPWTRYIKPPSFTNSAAKSKSDLKSLPPSNECKPTKSILKP FT TTSHSAANSPSAEPQAPISFAMLLESILQQLAGEAVSSRLDAYMQFFGALRAYDNLPGD FT QEIIARLGLITQFIQRDVSRDLTTGGPLHTNLVIQALKLAVALVWHSEISARLPDDFKT FT FLVDHSVNCLQDVKMPKSVVTHYLSVLSTQNFNAKVMTNTRILRILTVLHELTNRVTGS FT AIVSQRLSIYLRVLNQSKMIFVSNASLWMDHLISGLLHHVKDIRIKAISVGFQTAIACG FT PNPTLSKCVREVFSRPLDERRKLVTEVCERMTRMMALADCGVHIPQIWSVIILLLRSKK FT FNVDQWEHFKEWVLVLQRCFNCSDSAIKAQAIVGWNRFVYVVGPSDTTSPSLLRMLSKP FT IVSQFDRKKQDKQPSQLALCSYYNLLYYAFRPSASFQHLDVVWEEYVVSPASSIFSSVP FT SLSDRVAHVLSNMLWSPQAKVWLENKVNESNKLDPEELPSIDSRWIRSRITSVLSVFEE FT IFKSSVWNPDIERSNIATAWIGLSKALSHASSKEITPTPESMQAVAHVLGLLQRLWNAG FT PSSLNAAIEKDSADAFYDRFSFLSTTMIYSLGSARFTEKLLLKTADETFQAATTPTHRH FT QKANTSLDSPILHFLRFISELPGHSGPSPSYTRLVTRVLEATCSDKLSRSSRLEFLSQC FT ADIHVFDAAAHVGDDRLAETVWKSVAQLSASSLSSFPMETARERDGSVCRDYENIVNIL FT SAGLKFSDVFEVWNPLVDSLIRVVRTEKGDRAIATMAVEPLAGSIIEQGTRNTCTPSAS FT LLRLSLSIPYCHEAETVKGTHETTFPHKLFELVDKTLRQSYESFDPVEPNGIADFIECL FT TSLLGSGVPTFRTAMLTHLQQSLAFYLKDGERKIDAESGVESRILTACRALSSAVLNIL FT QAAEPHDAFCVQKFEPIICSGLESTHASVTKRFLDFWRCSFGSQETVPCPETISLALQD FT IELQMKLQQPRGHRQISQFEAQAGRQDAQDAKVIPVDTSVKSRIAFILDDPFTLGLNSS FT PITGGSERKAMPSSSEKQTGPSAVQVSQADDDSDPDMATDHPIPLPTGSGDPRKRSELF FT SIIESLRSSSPPTNTPRELGFMTPPHLRDLRNADADAGTPQTPTLPPVATDNEYGFLGS FT SPTPGTRSRTQLSEPEIPQSLSTPAAEDSAIENELQSSPPKPKSTSPDPQSNTGNMNTP FT GSANTTSSKNRRSKRRARRSSRQKKAMNAQPRQPEPTGESMTVDSEEPLIKRLRSSTGK FT LPEDKDRSTEVNQPKDLSKIGPHDSEDPRGPTTDSGATEEPIIEPASLEHQASAEQPKD FT SESQQIDGCDYIADSCSDDMETQVASQLEQDLELAVDLDDAASIEYAATAPEQGANKKR FT KREADQSTPSGKERRRSSRLTKTPSVADVEGGRATRSKRPINASQDVESSPAESAPKRR FT KTDSKSDIIGTSKPAEQAASTDSGKTKVQDTQESSQKRRSSRLSGQAAPAIPEESPLPK FT KSPRPSRSRKSTKDKAKDSIQEEAELQHETPTKDVVDQTVKDEKEPKTTVEDKPTEQLP FT EPDSSVQPTTEAQLDEPMDEPVPETKQTAPDDVQMEDAPVTEPIFEKTPSEEKEMEEGK FT KMRAVSRTTQTESQKEPEITEAEITDSLRKVLSDMKLAKLDRNSLKEIDDLLFDIRVET FT HEALRRNTS" FT mRNA join(<115785..118715,118765..119031,119081..>121180) FT /locus_tag="An04g03720" FT exon 115785..118715 FT /locus_tag="An04g03720" FT /number=1 FT intron 118716..118764 FT /locus_tag="An04g03720" FT /number=1 FT exon 118765..119031 FT /locus_tag="An04g03720" FT /number=2 FT intron 119032..119080 FT /locus_tag="An04g03720" FT /number=2 FT exon 119081..121180 FT /locus_tag="An04g03720" FT /number=3 FT CDS complement(join(121355..121472,121612..121622)) FT /locus_tag="An04g03730" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIJ4" FT /protein_id="CAK38638.1" FT /translation="MVGCDSELDSRLNGMLVLQLHSPVLKHDEYIQLPPRSSYDRT" FT mRNA complement(join(<121355..121472,121612..>121622)) FT /locus_tag="An04g03730" FT exon complement(121355..121472) FT /locus_tag="An04g03730" FT /number=1 FT intron complement(121473..121611) FT /locus_tag="An04g03730" FT /number=1 FT exon complement(121612..121622) FT /locus_tag="An04g03730" FT /number=2 FT CDS join(122060..122136,122227..122650,122752..122829) FT /locus_tag="An04g03740" FT /note="Title: weak similarity to ORF1557 polypeptide FT sequence SEQ ID NO:3114 from patent WO200058473-A2 - Homo FT sapiens" FT /db_xref="GOA:A2QIJ5" FT /db_xref="InterPro:IPR001841" FT /db_xref="UniProtKB/TrEMBL:A2QIJ5" FT /protein_id="CAK38639.1" FT /translation="MVQVSSLALVGYLAPVLVTFLLFVTWLILGARRRRRRHRRYGPQH FT PYPDAEMAAPEGHTRIVISQQLIEELYPQLRYKDWFKENHIQQQQQHLSSGAISRARST FT SGNNSGESPDKSNINTSQDRDKDTDDIDTDTDRDNHRTCAICMDEFADDDEIRSLPCRH FT IFHMEELALEKRIAEGECQGDFGTGGGGY" FT mRNA join(<122060..122136,122227..122650,122752..>122829) FT /locus_tag="An04g03740" FT exon 122060..122136 FT /locus_tag="An04g03740" FT /number=1 FT intron 122137..122226 FT /locus_tag="An04g03740" FT /number=1 FT exon 122227..122650 FT /locus_tag="An04g03740" FT /number=2 FT intron 122651..122751 FT /locus_tag="An04g03740" FT /number=2 FT exon 122752..122829 FT /locus_tag="An04g03740" FT /number=3 FT CDS complement(join(123076..123462,123515..123844, FT 123956..124201)) FT /locus_tag="An04g03750" FT /note="Title: strong similarity to hypothetical protein FT YMR099c - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIJ6" FT /db_xref="InterPro:IPR014718" FT /db_xref="UniProtKB/TrEMBL:A2QIJ6" FT /inference="profile:COGS:COG0676" FT /inference="profile:PFAM:PF01263" FT /inference="similar to AA sequence:PIR:S55085" FT /protein_id="CAK38640.1" FT /translation="MDRSNKPAAIGVGASLPQPTISLRDNTVEATLPTGESVTVHLYGA FT TVTSWKLANGKEQLFVSEKAHLDGSKPIRGGIPVVFPVFGPPPSNHATSALPQHGFARN FT SNWEFLGKSSSEAFGRDRKEGEDAVKLDFGLSHPMLSEEFQKAWPYQFGLVYSVTLTKG FT SLETSLQVQNQGEQNFDFQVLMHTYLSVEDISNIRVKNLQQKEYLDKTQGGAAITETSE FT AVEINKETDRVYKALDPKVPIIVSTASDDQPLFSITREALTDVVVWNPWIEKAKGMADF FT GPDEAYKNMLCVEAGSVAGWQTLEAGESWEGGQTIRPRL" FT mRNA complement(join(<123076..123462,123515..123844, FT 123956..>124201)) FT /locus_tag="An04g03750" FT exon complement(123076..123462) FT /locus_tag="An04g03750" FT /number=1 FT intron complement(123463..123514) FT /locus_tag="An04g03750" FT /number=1 FT exon complement(123515..123844) FT /locus_tag="An04g03750" FT /number=2 FT intron complement(123845..123955) FT /locus_tag="An04g03750" FT /number=2 FT exon complement(123956..124201) FT /locus_tag="An04g03750" FT /number=3 FT tRNA 126073..126160 FT /gene="tRNA-Gly (CCC)" FT /locus_tag="An04e03760" FT /product="transfer RNA-Gly (CCC)" FT /inference="profile:tRNAscan:1.4" FT CDS complement(join(126308..126351,126583..127063, FT 127117..127636,127686..127886,127945..128030, FT 128080..128310)) FT /locus_tag="An04g03770" FT /note="Title: strong similarity to hypothetical protein FT AAD34558.1 - Aspergillus terreus" FT /db_xref="InterPro:IPR011701" FT /db_xref="UniProtKB/TrEMBL:A2QIJ7" FT /inference="profile:COGS:COG0477" FT /protein_id="CAK38641.1" FT /translation="MAMNPEAIELSEAPQSGANSMKLQQALVNRVSGTSILQSHEAKPE FT AESEPDETLYPHGMQFVLISMSLCFCVFLVGLDATILTTAVPRITDEFGSVADVGWYDA FT AFRLTSCMSQLSQGKLYDNYPVKWVFLVNLLLFEGGILLSGLAPSSMIFIIGRAITGLG FT FSGISQGCMVIIAISTPLRRRPTFVGLISASEYTAIAIAPILGGILTSDLSWRWCFYIN FT VPAAALPSAVLLLLKLPNITPRGSKTHIQKLRELDLLGFFLFAPAVLCLLLALQWGGDT FT YSWTNGRIIALLVLSPIIFTGFCLLQHRKQDTAMLPPRVLRKRIIITGAAFSLCLSACR FT AIVQYYLSIWFQTVRNATPLQSGLNTLPLVISVLVSAITGGWLISRTRTYTPILLPASL FT LVIAGIALMTTFTPTTPAKLWIPSLILLGLGSGSAVGVPFIAVQAILPMKDISIGMALM FT TFSQDIGEAVFISVAQAIFLNRLTGDLAKSVPGLDPVMVTHLGATSLEVSAAAAQLGII FT APT" FT mRNA complement(join(<126308..126351,126583..127063, FT 127117..127636,127686..127886,127945..128030, FT 128080..>128310)) FT /locus_tag="An04g03770" FT exon complement(126308..126351) FT /locus_tag="An04g03770" FT /number=1 FT intron complement(126352..126582) FT /locus_tag="An04g03770" FT /number=1 FT exon complement(126583..127063) FT /locus_tag="An04g03770" FT /number=2 FT intron complement(127064..127116) FT /locus_tag="An04g03770" FT /number=2 FT exon complement(127117..127636) FT /locus_tag="An04g03770" FT /number=3 FT intron complement(127637..127685) FT /locus_tag="An04g03770" FT /number=3 FT exon complement(127686..127886) FT /locus_tag="An04g03770" FT /number=4 FT intron complement(127887..127944) FT /locus_tag="An04g03770" FT /number=4 FT exon complement(127945..128030) FT /locus_tag="An04g03770" FT /number=5 FT intron complement(128031..128079) FT /locus_tag="An04g03770" FT /number=5 FT exon complement(128080..128310) FT /locus_tag="An04g03770" FT /number=6 FT CDS complement(join(128772..130806,130905..130963)) FT /locus_tag="An04g03780" FT /note="Title: strong similarity to hypothetical membrane FT protein YJL057c - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIJ8" FT /db_xref="InterPro:IPR000792" FT /db_xref="UniProtKB/TrEMBL:A2QIJ8" FT /inference="profile:COGS:COG0515" FT /inference="profile:PFAM:PF00069" FT /inference="similar to AA sequence:PIR:S56829" FT /protein_id="CAK38642.1" FT /translation="MADEGMSIVPYGSGNLDVVLRHNDSVVVFDRDSQQLVLRHAAESD FT DGNLELADCPYCHRPLRDSSSAQDDHHGGTQPEFINPHYFRMLHNSLPSSVSSSSPPSP FT RRRLVPPALADGPTSEPSYSGSGIQSTQGISSAAFTQDYFKKFFVEETVLGKGGKGVVL FT LVKHVLDGVSLGQYACKRVPVGDDHEWLEKVLAEVQLLQHLTHQNLVSYRHVWLENAKI FT STFGPSVPCAFILQQYCNAGDLHNYICGSVETPTTTEQLKERLRRKSRGGPEPPSEAGG FT PRKLNFEEIYSFFKDITSGLRYLHANGYIHRDLKPNNCLLHKTSDGIRVLVSDFGEVQA FT QDSMRRSTGATGTVSFCAPEVLRREYPGGPFGNFTFKSDIFSLGMILYFLCFAQLPYTH FT ADLIHEEKEDLDQLREEISHWAGFDDAQFIRPDLPGQLYTFLKRLLSLDPDGRPSADEV FT LSGLQAGANVNESFRSRRTSPTSPDIRPSARIHPVESTETPSFRPSTSPNKSLTRSPVA FT VRRTPLYEPDGAETGLSPVVEETSPLSERNTSLSPECDMMVRPWFSGAQSHSPPQAEHR FT EVPQEQPQPVQQLLPPPPGRFSLARVFPSAASLIDSQIPVTALQLAAFLLKVVSIFQPC FT SPLAVNPWVVYPLLLLAAVNFPATGLWTQIVSLLLHLLVVNLSMRMEALCWRASHSAIL FT FSR" FT mRNA complement(join(<128772..130806,130905..>130963)) FT /locus_tag="An04g03780" FT exon complement(128772..130806) FT /locus_tag="An04g03780" FT /number=1 FT intron complement(130807..130904) FT /locus_tag="An04g03780" FT /number=1 FT exon complement(130905..130963) FT /locus_tag="An04g03780" FT /number=2 FT CDS complement(join(131639..132475,132908..133655, FT 133711..133808)) FT /locus_tag="An04g03790" FT /note="Title: strong similarity to hypothetical protein FT YNR053c - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIJ9" FT /db_xref="InterPro:IPR012971" FT /db_xref="UniProtKB/TrEMBL:A2QIJ9" FT /inference="profile:COGS:COG1161" FT /inference="profile:PFAM:PF01926" FT /inference="similar to AA sequence:PIR:S63384" FT /protein_id="CAK38643.1" FT /translation="MGTFKKEASRKERQGKTGDGMGNVRVKGENFYRDAKKLRTLNMLK FT DGKPQRNAEGKITKAASYQSRDAPVARIEPNRKWFGNTRVISQEALSSFREAVAERASD FT PYSVLLKTNKLPMSLIRDDKGVNGLKQHQAKMAIETNPFSDTFGPKAQRKRVKLGVSSL FT ADLAGESAKMHDAYVEKSDHATHEDGTMVVNGDDVAVEEDSSVAPIAKEAVFLKGQSKR FT IWNELYKVIDSSDVVIHLLDARDPEGTRCRSIEKYIREEAPHKHLIFVLNKCDLVPTGV FT AAAWVRHLSTDYPTLAFHASINNSFGKGSLIQLLRQFSSLHSDRKQISVGFIGYPNTGK FT SSVINTLRKKKVCTVAPIPGETKVWQYVTLMKRIYLIDCPGVVPPNPNDSPEDILLRGV FT VRVENVENPEQYIPAILKRVQPKHLERTYGIKSTEDPVEFLSLLARKGGRLLRGGEPDL FT DGVAKMVINDFLRGKIPWFTAPPHNSGEEGEKIEGREGRLGEMSRKRKLDETAPEAADT FT TEAAEKQESGSGDEFEGFDEEDDDDDSIANLEVSDEESGAEED" FT mRNA complement(join(<131639..132475,132908..133655, FT 133711..>133808)) FT /locus_tag="An04g03790" FT exon complement(131639..132475) FT /locus_tag="An04g03790" FT /number=1 FT intron complement(132476..132907) FT /locus_tag="An04g03790" FT /number=1 FT exon complement(132908..133655) FT /locus_tag="An04g03790" FT /number=2 FT intron complement(133656..133710) FT /locus_tag="An04g03790" FT /number=2 FT exon complement(133711..133808) FT /locus_tag="An04g03790" FT /number=3 FT exon 134190..135053 FT /locus_tag="An04g03800" FT /number=1 FT CDS 134190..135053 FT /locus_tag="An04g03800" FT /note="Title: weak similarity to hypothetical protein FT CAB51071.1 - Homo sapiens" FT /db_xref="UniProtKB/TrEMBL:A2QIK0" FT /protein_id="CAK38644.1" FT /translation="MSLFRNCRAATVQFRGFTSSSCLRVGPESPNFVDIPQPIQPDLPS FT KPRVKGTLPVPRELFPARRKDKPTEAYINAATPLPTKETKLDPNDPNTEYIEWKKRMAE FT MRRKNLREGLLELHTRKQRTDKTMMQRSLEKQKRRDRILRQPEREDQRLTRNSVIQDML FT PKHTAVLPDPDRETRLAESKARLEYQQAVKEAERQDNLQELYMNARNFITTEAQLLAEI FT ERVFPEGENEAWRSDHQEGENIWNLGVPPTVQGIVNETRKSETARWDVIQDRVKQLGEQ FT ITGGKL" FT mRNA <134190..>135053 FT /locus_tag="An04g03800" FT CDS complement(join(135347..136214,136270..136510, FT 136558..136603)) FT /locus_tag="An04g03810" FT /note="Complex: TFB3 of S. cerevisiae is a subunit of the FT RNA polymerase II basal transcription factor TFIIH FT complex,that is composed also by the subunits TFB1, TFB2, FT TFB4,KIN28, RAD3, SSL1, SSL2, and CCL1." FT /note="Function: TFIIH is essential for transcription by FT RNA polymerase II and nucleotide excision DNA repair." FT /note="Title: strong similarity to subunit of transcription FT initiation factor TFIIH Tfb3 - Saccharomyces cerevisiae" FT /note="nucleus" FT /db_xref="GOA:A2QIK1" FT /db_xref="InterPro:IPR017907" FT /db_xref="UniProtKB/TrEMBL:A2QIK1" FT /citation=[52] FT /citation=[62] FT /citation=[72] FT /inference="profile:COGS:COG5220" FT /inference="similar to AA sequence:UniProtKB:SCU62805.1" FT /protein_id="CAK38645.1" FT /translation="MPPARDIMAHRGDDDEVCPVCKSSRYLNPDMRFLINPECYHKMCE FT SCVDRIFSSGPANCPVAGCHKTLRKNRFRKQTFEDINVEREVDIRRRVMQILNRREEEF FT DSKRAYDDFLEQREEIIANLVHGTDVAKTESDLQRYAADNMRSIRANQALEAQEASSFR FT EQQTHEQELARLRREAARLEYENERKEMLAGREDVLSRLAAGRPGDAAAIAREGHKVLL FT KKSSARRSEEDRIRQKQAALRSSDARKAGQGALTTADRADDSGDSGLIKGLKKIVTPEP FT EKPYDPFGGLVPNKRDYYTLRDYYPNSYLDPIRQDTRMQAGGYDLQEYYSRTLMEAFAG FT LGCFIDEEVSKREVTSTMGISRPVATEGAALAAVSSAGAPEASS" FT mRNA complement(join(<135347..136214,136270..136510, FT 136558..>136603)) FT /locus_tag="An04g03810" FT exon complement(135347..136214) FT /locus_tag="An04g03810" FT /number=1 FT intron complement(136215..136269) FT /locus_tag="An04g03810" FT /number=1 FT exon complement(136270..136510) FT /locus_tag="An04g03810" FT /number=2 FT intron complement(136511..136557) FT /locus_tag="An04g03810" FT /number=2 FT exon complement(136558..136603) FT /locus_tag="An04g03810" FT /number=3 FT CDS join(136893..138697,138778..138865) FT /locus_tag="An04g03820" FT /note="Remark: The lamprey is considered the most primitive FT living vertebrate and its neurofilaments (NFs) are unique FT in being homopolymers of a single 180 kDa subunit (NF-180)" FT /note="Title: weak similarity to NF-180 - Petromyzon FT marinus" FT /db_xref="UniProtKB/TrEMBL:A2QIK2" FT /protein_id="CAK38646.1" FT /translation="MGVPNNSLHELERQRLELEGNISKLQDSLYHWRTWEAEYDGLKDE FT LNELDDDATMDDYLRVGRDFGGSLVNEAEVKVILGEKQGVTRTKQQAVDLVTRRIDYVK FT QNASTIEKRLRAAEDQLYALDSQDRLPVEPTADFPMTEIFEELDENGEVISSKTTTPGS FT EATDLLEVLKKAGVNDIPDVAKADTPVSSSSQQVTQPTEEASFADSLKKDDTSASEEHP FT VKSSGSEAKETSSELDPTVEVHGERPVMEVDESPEDAKLRREMLQYSLNEVGSVVAELE FT LDEDASDISVDEDYDAYDYDDDEDEEEDEYGRSTRRVLSEDYHRQMRELEEKLNARGMW FT NAGKDTQSLPNEIKQDLDQPSVVRVENNADASSEPVKEKKPKKKVAFADELDIAPASKP FT PTLEKKIAPVRESNVPVLQDAVVERTEPAGKQPVQNDAPKKVSRFKSARKTHNAAEDAT FT ASTTQSSNTSRPAEPRSALRKSEASTTGSSLPLFPAKPAEPKPFSQPITDIVEKEDPTP FT RGPEGKVLADTLVERETPAGPAVAPEPDELDEQLHKKEIASEFYKIRNRMIQQNGGFVG FT EEPEIVPIETEDAPKRVSRFRAARMSLLSFRRMDRKQGSLYLGMAIPLSHGIVI" FT mRNA join(<136893..138697,138778..>138865) FT /locus_tag="An04g03820" FT exon 136893..138697 FT /locus_tag="An04g03820" FT /number=1 FT intron 138698..138777 FT /locus_tag="An04g03820" FT /number=1 FT exon 138778..138865 FT /locus_tag="An04g03820" FT /number=2 FT CDS join(142474..142702,142760..144089,144141..144168) FT /locus_tag="An04g03830" FT /note="Title: similarity to phorbol activated nuclear FT factor-like protein PNF1 from patent WO200162790-A2 - Homo FT sapiens" FT /db_xref="InterPro:IPR018620" FT /db_xref="UniProtKB/TrEMBL:A2QIK3" FT /inference="profile:COGS:COG0532" FT /inference="profile:COGS:COG3468" FT /inference="profile:COGS:COG4775" FT /protein_id="CAK38647.1" FT /translation="MKNVATLAAFAAGANALVGRSDSCCFHLTASGDASGTIGQLGDGQ FT NRIGGGLPATQFCIDSNGGITDSSGRGCVVTSDTTQFQCDLGKSPMSGFSITSSGELEY FT NGDADFVACQTGDNNELNLYTTENSSVTGCENIKLTADSCAGSGAGSVGSSSAPASTPA FT PQSSTPAPAPSSSAPGVPGAGASTGWVPGGPASSASVPYGPGPQSSGAVQVTTVYVTET FT YCGAETTPVVSVPGESTVPLVPVGPGSSAPAGSQPAPSGSPAPQPSETPSYPQSSESPA FT PQPSETPSYPQSSETPAPQPSETPAPQPSGSPAPQPSGSPAPQPSSYPQTSGTPAPQPS FT GTPSYPQTSASPSSAQPSGTATQSSSASCPTDLSGDYEYPHLIVPINSSTPDTAYGTQY FT FGTVSSTVSTIFNFDIPSSDSGKTCSLIFLFPTKDQLETSDYTFSGDGKIDFSQLESAA FT SESTTYNNAPGVKQDYGDFTVSPGNSYLISTFSCPAGQTVSYEMKEAGSTYLNFFEDYN FT PSPLGLYITVC" FT mRNA join(<142474..142702,142760..144089,144141..>144168) FT /locus_tag="An04g03830" FT exon 142474..142702 FT /locus_tag="An04g03830" FT /number=1 FT sig_peptide 142474..142521 FT /locus_tag="An04g03830" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(142522..142702,142760..144089,144141..144165) FT /locus_tag="An04g03830" FT intron 142703..142759 FT /locus_tag="An04g03830" FT /number=1 FT exon 142760..144089 FT /locus_tag="An04g03830" FT /number=2 FT intron 144090..144140 FT /locus_tag="An04g03830" FT /number=2 FT exon 144141..144168 FT /locus_tag="An04g03830" FT /number=3 FT exon complement(145587..146888) FT /locus_tag="An04g03840" FT /number=1 FT CDS complement(145587..146888) FT /locus_tag="An04g03840" FT /note="Title: similarity to microtubule binding protein FT D-CLIP-190 - Drosophila melanogaster" FT /note="cytoskeleton" FT /db_xref="UniProtKB/TrEMBL:A2QIK4" FT /inference="profile:COGS:COG0840" FT /protein_id="CAK38648.1" FT /translation="MTTTLWDPDRILQITKGPHERGMFCLGRARSRYDSRCRWDIPYTK FT YQIVRETLDEIAAKLPHEIYDDELKVLAKWGLCDYHSGQVHEVVSGWHYALASLANLYS FT AYKERAETSHTVHQILQAEVKRCRDLLPPDEDNPQKNLSVLLKRHMRKYSELVEAGKAN FT SALANKLQEERRGEEDKMREMSDLQAKLETSEKKCQALREENAGLVVEVRAKGEECERL FT QEQLGEATAEFSDMQRANEKLRDVNEEMRKEVDDKQGQLNEITAELSVVRCNNSNLRDA FT NEEMRRKIERKQERLNEIRGDLFDMGFAKDSLEDANEKMRREVDSKQEQIETITAQLAS FT VSADLDSTKNELSVACETKTQVQNDLREAVEEISNLQAQLTEIHEQQSTTIWCKIKRWI FT REKASCLSRYRRRYGMRDKEEEVALAPVKPINVG" FT mRNA complement(<145587..>146888) FT /locus_tag="An04g03840" FT CDS complement(join(147741..149876,149933..151885, FT 151942..152514)) FT /locus_tag="An04g03850" FT /note="Title: strong similarity to hypothetical beta FT transducin-like protein het-e1 - Podospora anserina" FT /db_xref="GOA:A2QIK5" FT /db_xref="InterPro:IPR019781" FT /db_xref="UniProtKB/TrEMBL:A2QIK5" FT /inference="profile:COGS:COG5635" FT /inference="profile:PFAM:PF00400" FT /protein_id="CAK38649.1" FT /translation="MGCPKLRNPFRKRHSKKQPRKETTDSSDNPSKLSSNALSGTCSTL FT EPVAQPKSQTDALPAEDNQVPLSSETTLPRRDGKARRRNLWQEAYDTLDEKQRQYMKPV FT REHEQSSDNHENADTNHVYKTLDEVIQTVKAQYQIRMSKREDSKLRDAANKILTATLSC FT KDIISAIVALDPTGHASSAWTVVSLGLTMTQNYRDQQMAWFQSSAILTDILARYAVMEK FT LYRDDGSELNDKIEDAILRVYIAVLKYAAEAMTIYRSNTGKRLMQSVVALANLPLTDIE FT SSIATEEEHLGKWLQMHQEMQRKQEANSILLGIDRLLDDVRNVAQKIELDKLPIAEGAH FT FDSHMDENQVECLKNTRVELLDGIMDWVDDTQGKTIFWLRGVAGTGKSTISRTVARKLQ FT ERELLGASFFFKRGEGDRGNASRFITTIAKQFMIALPQLRKEIATAMEDDLIVSKSLKE FT QFDHLLLKPLLEMKMSNGQRLPIVIVVDALDECEERSIETIIQLLPRLQESEAIYLKVF FT VTSRPEHPILEGFEQIEGEHKDVALHEIERCTVERDMAVFFEDRLSRIRKKRKLEDTWP FT GEIKTQALVDMAMPLFIFAATVCRLLEDYRWDPDDSLNNIMKRQYNNSQLDKTYLPVLD FT RLLGGQDQQAQSELVKQFQQVVGIIVVLESPLSIASLSNLINMKENLIRIRLDSLHSVL FT NIPSDNNKPVRMFHLSFREFLLHPATRETTKLSVDGQSTHRDLAYKCIAVMMDPRHGLR FT QNICGLPGHGTSRDDIGAERIERYFPAELRYATRYWVHHLTQGALNISDQDGVHEFLET FT HFLHWLEAMSVLAHLPETIGSVNMLLSIVQRSHANLISRFLYDAKRFTLKNISIAKEFP FT LQLYSSALLFAPEKCTIRNTFFHCVPPYFSQLPRVPEYWGAELQTVETGSDMVESLEFS FT PDGRMFLTLGESLKLWETSTGDLRNTLVPRTPFGGECAFSPDGKLVAALIFDKILLWDS FT LYGTLKHTLKVQSNWGSAMAFLSNEHLVSTSTDKTLEIWSTISGKLQKTAPFGNNEKFM FT SGGQTTINLSPDGSLLVRTLKDGTTKLWDTAKAEPRHILRSPGEEVQTLAFSPDGQLLA FT TGSRYGILELWDLCEGTLQHTLRCHATRCHINSIAFSHDGRLLALACARGLNIWDIGHS FT PILSTFVSHNMGSNLVRFSPDDKLVALVRNDKVTLWDTARLEKMHALGGHPDGVTVVRP FT SPTGSFLASGSSDTTVRVWDIFTGTVQRVLQGHSNAITNISISPNGHLLAASSEDGLIK FT IWDVSNGDLQHTLSSDNSGGMVCMLFSPDGNLFLAISRHKTRLWDVVTGLCKWTVEQKV FT RGHRLRTHATFSLDSQLISYAVPLEATLRNTADGSLHETLTIPFDDVDEVALSPSGNLL FT ATSHIGGNVDVRLWNTSTGRVEHVLTGCSTEELQFSPDGKLFSSGDPWMGVKVWNVTDG FT TLRQTLGAKKTDRYSWLLDTNRKEYKIHHEAQGYIIPLNDDWIRLGEDKILWLPPEYRG FT INGNISTRVGNTYIVGCETGDVIFIGLRSPSED" FT mRNA complement(join(<147741..149876,149933..151885, FT 151942..>152514)) FT /locus_tag="An04g03850" FT exon complement(147741..149876) FT /locus_tag="An04g03850" FT /number=1 FT intron complement(149877..149932) FT /locus_tag="An04g03850" FT /number=1 FT exon complement(149933..151885) FT /locus_tag="An04g03850" FT /number=2 FT intron complement(151886..151941) FT /locus_tag="An04g03850" FT /number=2 FT exon complement(151942..152514) FT /locus_tag="An04g03850" FT /number=3 FT exon 153893..154645 FT /locus_tag="An04g03860" FT /number=1 FT CDS 153893..154645 FT /locus_tag="An04g03860" FT /note="Catalytic activity: R-CHOH-R' + NADP(+) <=> R-CO-R' FT + NADPH" FT /note="Function: Acts on a wide range of carbonyl compounds FT , including quinones, aromatic aldehydes, FT ketoaldehydes,daunorubicin, and prostaglandins E and F, FT reducing them to the corresponding alcohol." FT /note="Title: similarity to carbonyl reductase NADPH FT -Rattus norvegicus" FT /db_xref="GOA:A2QIK6" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2QIK6" FT /inference="profile:COGS:COG1028" FT /inference="profile:PFAM:PF00106" FT /protein_id="CAK38650.1" FT /translation="MTVMKPLILITGANRGLGYATAKQLTRTGKYRLLIGARTQEKAEE FT AIKELSSSSDDLTPVSLDLNSDESIKAAATFVRERFGSLDILVNNGGINRSSDPNATLR FT ETYRAVFETNVFGVAVVIEAFLPLLRASQYPDRRIVNVTSGLGQIGIAYSPTSEYSARV FT WELPVYRSSKSALNMMNAVDAVRLQKENILSVVVCPGHCRTDFGGGRGVKSAEEGARPI FT VRAATEGSPDEMFGKVVEDEGYFVEFGW" FT mRNA <153893..>154645 FT /locus_tag="An04g03860" FT CDS join(156391..156556,156666..157396) FT /locus_tag="An04g03870" FT /note="Similarity: the ORF shows similarity to the A. niger FT protein An11g05330. The similarity between the two FT proteins, however, is restricted to a stretch of about 100 FT amino acids." FT /note="Title: weak similarity to phosphatidic acid FT phosphatase ATPAP2 from patent WO200005385-A1 - Arabidopsis FT thaliana" FT /db_xref="GOA:A2QIK7" FT /db_xref="InterPro:IPR000326" FT /db_xref="UniProtKB/TrEMBL:A2QIK7" FT /inference="profile:COGS:COG0671" FT /inference="profile:PFAM:PF01569" FT /protein_id="CAK38651.1" FT /translation="MLVESPGLTSLIGVSLAQEVRTRYPDCRTPLSVLANMHLSKTASD FT HGLQVGQRFKTSFAGLFYLTLWLSGKLHIMDNRGEAWKTLLVMIPSLAATLVAVSRIMD FT ARHHPFDVITGSLLGIICACISYRQYFPSLNEPWKKGRAYPIRTWGRDPVGPVETVRLV FT GTDGSTAALRNPEEERLNEAPQSKTTGSDAGRPLYLPESNPYTTNMYGYSRRDEDDNWS FT SSSEDVAGGYEMQPGYARTQNPALNGPTARLDVDTAYHSQTPQVVLGAATTHETPGAIP FT THADRGRDLTDMPYREV" FT mRNA join(<156391..156556,156666..>157396) FT /locus_tag="An04g03870" FT exon 156391..156556 FT /locus_tag="An04g03870" FT /number=1 FT sig_peptide 156391..156441 FT /locus_tag="An04g03870" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(156442..156556,156666..157393) FT /locus_tag="An04g03870" FT intron 156557..156665 FT /locus_tag="An04g03870" FT /number=1 FT exon 156666..157396 FT /locus_tag="An04g03870" FT /number=2 FT exon 158680..159066 FT /locus_tag="An04g03880" FT /number=1 FT CDS 158680..159066 FT /locus_tag="An04g03880" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIK8" FT /protein_id="CAK38652.1" FT /translation="MFVAFIDLLFFGAFIAGVYELRFIAGANCSHWDGGSVYISLGPFG FT YYGYRTDNPLSFHIDKTCAMLKASFALGIIEVVFFFWTAILALAIYKRPEVVVKETTVR FT RRSHSSRRGHRRHSSSGRRQQYVV" FT mRNA <158680..>159066 FT /locus_tag="An04g03880" FT sig_peptide 158680..158766 FT /locus_tag="An04g03880" FT /inference="protein motif:SignalP:2.0" FT mat_peptide 158767..159063 FT /locus_tag="An04g03880" FT /product="hypothetical protein" FT CDS join(160199..160274,160355..162750) FT /locus_tag="An04g03890" FT /note="Function: HxB is responsible for the insertion of FT the terminal sulphur atom in the molybdopterin cofactor." FT /note="Induction: HxB is independently controlled by the FT purine utilization and the nicotinate utilization FT transcriptional activating systems." FT /note="Remark: the xanthine oxidase class of molybdoenzymes FT requires the molybdopterin cofactor (MoCF) to have a FT terminal, cyanolysable sulphur ligand." FT /note="Title: strong similarity to transulphurylase hxB FT -Aspergillus nidulans" FT /db_xref="GOA:A2QIK9" FT /db_xref="InterPro:IPR015421" FT /db_xref="UniProtKB/Swiss-Prot:A2QIK9" FT /citation=[57] FT /citation=[73] FT /inference="profile:COGS:COG3217" FT /inference="profile:PFAM:PF03473" FT /inference="profile:PFAM:PF03476" FT /inference="similar to AA sequence:UniProtKB:AF128114.1" FT /protein_id="CAK38653.1" FT /translation="MSDRGKCQYPDDVDVIREREYPLLKDTTYLDHAGTTLYAKSLIES FT FSRDLTSNLYGNPHSMSAPSQLSTQRVDDIRLRALRFFSADPEEFDLVFVANATAAIKL FT VADSFRESTPQGFWYGYHVDSHTSLVGARELAGIGSRCFVTDAEVESWISQLDTEPVQG FT PRLFAYPAQSNMNGRRFPRGWCGRIRESAKDTYTLLDVASLVSTSPFDLSDASAAPDFA FT VLSFYKIFGFPDLGALIVRKSAGHIFDKRKFFGGGTVDMVLTQGTQWHAKKQSSIHERL FT EDGTLPFHNIIALGSAFDTHERLFGSMDNISSHTRFLAKRLYDRMTTLRHYNGESVCHV FT YKPSHSDYTDPSTQGPILAFNLRSSQGAWIGKSEVEKMASVRNIQIRSGTLCNPGGTAA FT SLNWSGADMLRHFGAGMRCGDDHDIMDGRPTGILRVSLGAMSNLTDIDTFMGFIEEFYV FT EKSPNVCALVPPLEANLTHRSGFHVESLSVYPIKSCGAFKVPDGKRWEIRREGLVWDRE FT WCLIHQGTGTALNQKRYPRMALIRPFIDLSHGVLRVTCGSIRSPSQKTLEIPLDRENSN FT LTTTSLCQNSSKPSTVCGDQVIVQAYSSPTVSAFFSDFLGVPCTLARFPPQSSTRLAEP FT RRGLGSRKSPLRPAMPGAFPQDTPTPEAERNPILLSNESPILLISRSSVNRLNETIKSS FT PTTTNSTGRKKAVAADVFRANIVVAEDFPQPVSAGRPYIEDHWESLRIGPDNLHFNVLG FT SCQRCQMVCVDQLTGVRGEEPYSTLAKTRKSGNKIYFGRHLAISSNGDGNSVNSRTVMV FT GDVVTPSYYGP" FT mRNA join(<160199..160274,160355..>162750) FT /locus_tag="An04g03890" FT exon 160199..160274 FT /locus_tag="An04g03890" FT /number=1 FT intron 160275..160354 FT /locus_tag="An04g03890" FT /number=1 FT exon 160355..162750 FT /locus_tag="An04g03890" FT /number=2 FT CDS complement(join(163025..163531,163570..163683)) FT /locus_tag="An04g03900" FT /note="Remark: alternate names in S. cerevisiae = FT YmL25,YGR076c." FT /note="Title: similarity to mitochondrial ribosomal protein FT of the large subunit Ymr26 - Saccharomyces cerevisiae" FT /note="localisation:mitochondrion" FT /db_xref="UniProtKB/TrEMBL:A2QIL0" FT /protein_id="CAK38654.1" FT /translation="MRRASSVPTLKRSLPPRPSCTPTPSTPTRSCRARTSAPAELVKLA FT IKYNVEALLPPGRKSTEFKETRRAERGLAIKGTGIGQKVKGHKWERTMEARLEDRRKAM FT MEMPEMIRLWKQVSFPSLFLSFVRYAGWCTDLISLNSTERSRSWLEVVAQAVKAYASGC FT IIFFYSPRVEWIRGLHNVASVLFYTSRRAAANQPSIQLGESFD" FT mRNA complement(join(<163025..163531,163570..>163683)) FT /locus_tag="An04g03900" FT exon complement(163025..163531) FT /locus_tag="An04g03900" FT /number=1 FT intron complement(163532..163569) FT /locus_tag="An04g03900" FT /number=1 FT exon complement(163570..163683) FT /locus_tag="An04g03900" FT /number=2 FT CDS join(164389..164457,164540..164755,164823..164926, FT 165440..166804,166968..166989) FT /locus_tag="An04g03910" FT /note="Complex: Prp39p is uniquely associated with the U1 FT snRNP and is recruited with the U1 snRNP into splicing FT complexes." FT /note="Function: Prp39p is necessary for the stable FT interaction of mRNA precursors with the snRNP components of FT the pre-mRNA splicing machinery." FT /note="Title: strong similarity to pre-mRNA splicing factor FT Prp39 - Saccharomyces cerevisiae" FT /note="nucleus" FT /db_xref="GOA:A2QIL1" FT /db_xref="InterPro:IPR003107" FT /db_xref="UniProtKB/TrEMBL:A2QIL1" FT /citation=[21] FT /inference="profile:COGS:COG0457" FT /inference="similar to AA sequence:PIR:S47920" FT /protein_id="CAK38655.1" FT /translation="MADYNYGGSEEENAELKKLETELLDDPDNFETWEKLVRAGEALEG FT GINRNSNPQAITTVRNVYDRFLAKFPLLFGYWKKYADLEFSITGTEAADMVYERGVASI FT SPSVDLWTNYCSFKAETSHDADVIRELFERGATSVGLDFLAHPFWDKYIEFEERLEAFD FT KIFAILGRVIHIPMHQYARYFERYRQLAQTRPVVELASPETLTQFRAELDAAAGHVAPG FT AKAEAEVERDLRLRVDSYHLEIFSKTQTETTKRWTYESEIKRPYFHVTELDEGQLNNWK FT KYLDFEESEGSYLRTQFLYERCLVTCAHYDEFWQRYARWMAGQPGKEEEVRNIYQRASC FT LYVPIANPATRLQYAYFEEMSGRVDVAKEIHDAILINLPNHIETIVSLANMSRRHGGLE FT AAIEVYKSQLDSPQSDLATKAALVAEWARLLWKIKGSAEDARQVFQTNQQYYMDSRPFW FT TSYLNFELDQPTSSSTENVQYERIKQVIEDIRSKSTLPADVVRELVQIYMVYLLERGTK FT DAAKEYMTLDREVHGPASVSKMKAAEAVQLPPAQPVPSATPVAEVVVPTPPQANPYAYY FT QQTPVNGGIFQRMAC" FT mRNA join(<164389..164457,164540..164755,164823..164926, FT 165440..166804,166968..>166989) FT /locus_tag="An04g03910" FT exon 164389..164457 FT /locus_tag="An04g03910" FT /number=1 FT intron 164458..164539 FT /locus_tag="An04g03910" FT /number=1 FT exon 164540..164755 FT /locus_tag="An04g03910" FT /number=2 FT intron 164756..164822 FT /locus_tag="An04g03910" FT /number=2 FT exon 164823..164926 FT /locus_tag="An04g03910" FT /number=3 FT intron 164927..165439 FT /locus_tag="An04g03910" FT /number=3 FT exon 165440..166804 FT /locus_tag="An04g03910" FT /number=4 FT intron 166805..166967 FT /locus_tag="An04g03910" FT /number=4 FT exon 166968..166989 FT /locus_tag="An04g03910" FT /number=5 FT CDS join(167330..167629,167694..169672,169763..169916) FT /locus_tag="An04g03920" FT /note="Complex: U5-100kD is tightly associated with the U5 FT snRNP." FT /note="Function: U5-100kD is an RS domain-containing FT putative RNA helicase." FT /note="Function: U5-100kD potentially facilitates FT conformational changes in the spliceosome during nuclear FT pre-mRNA splicing." FT /note="Similarity: the C-terminal domain of U5-100kD shows FT significant homology to the S. cerevisiae splicing factor FT Prp28p." FT /note="Title: strong similarity to U5 snRNP 100 kD protein FT U5-100kD - Homo sapiens" FT /note="nucleus" FT /db_xref="GOA:A2QIL2" FT /db_xref="InterPro:IPR014014" FT /db_xref="UniProtKB/Swiss-Prot:A2QIL2" FT /citation=[49] FT /inference="profile:COGS:COG0513" FT /inference="profile:COGS:COG1197" FT /inference="profile:PFAM:PF00270" FT /inference="profile:PFAM:PF00271" FT /inference="similar to AA sequence:UniProtKB:AF026402.1" FT /protein_id="CAK38656.1" FT /translation="MDGIMTNGSSEAHPPMPPPEPIERPPTPPPPPPEDSALPPPPPDT FT SAPPPPPEDLPPAPPPETEPKKKKVGWGTKRPAPTPLSVEELVRKKREADAAAAKPKFL FT SKKEREKLALEKRAQEVAATRRLKSEHASNGVDRSATHSPSVSSEGPNGDARSIPTGPR FT AMRNSDAAPTAPAAMRHSQSHNKNYDLAPPPPPKSMSFGLTSGKGDSRFVDEDEAAAQA FT ALVKQRYMGADQTSNFSAKKKRKRTTDRKFNFEWNAEEDTSGDYNPLYQHRHETNFFGR FT GRLAGFGDDVAESVAHKYARALEDRDREAGSIRAREILEMERRRREESTRNQLDKHWSE FT KKLEHMRERDWRIFKEDFNISTKGGSVPNPMRSWDESNLPKRLMELINRVGYKEPTPIQ FT RAAIPIAMQNRDLIGVAVTGSGKTAAFLLPLLCYIAELPRIDEFEWRKADGPYAIVLAP FT TRELAQQIEIEAKKFTGPLGFNVVSIVGGHSLEEQAYSLRDGAEIIIATPGRLVDCIER FT RILVLSQCCYVIMDEADRMIDLGFEEPVNKILDALPVSNEKPDSEDAENPLAMSRHINH FT DQHRYRQTMMYTATMPTAVERIARKYLRRPAIVTIGSAGEAVDTVEQRVEMIAGEDKRK FT KRLGDILSSGEFRAPIIVFVNIKRNCDAIAREIKQWGFSSVTLHGSKTQDQREAALASV FT RNGTTDVLVATDLAGRGIDVPDVSLVVNFNMATSIESYTHRIGRTGRAGKSGVAITFLG FT NEDADVMYDLKQMLMKSPISRVPEELRKHEAAQSKPTRGFSSKKNNEEGGGGGKVGW" FT mRNA join(<167330..167629,167694..169672,169763..>169916) FT /locus_tag="An04g03920" FT exon 167330..167629 FT /locus_tag="An04g03920" FT /number=1 FT intron 167630..167693 FT /locus_tag="An04g03920" FT /number=1 FT exon 167694..169672 FT /locus_tag="An04g03920" FT /number=2 FT intron 169673..169762 FT /locus_tag="An04g03920" FT /number=2 FT exon 169763..169916 FT /locus_tag="An04g03920" FT /number=3 FT CDS complement(join(170268..170390,170467..172837, FT 172925..173076)) FT /gene="apsA" FT /locus_tag="An04g03930" FT /product="lysine aminopeptidase apsA-Aspergillus niger" FT /EC_number="3.4.11.-" FT /note="Function: the aminopeptidase apsA from A. niger was FT found to be active towards a number of amino acid FT p-nitroanilide (pNA) substrates, viz. K-pNA, R-pNA, FT L-pNA,M-pNA, A-pNA and F-pNA." FT /note="Gene-ID: apsA" FT /note="Remark: the most preferred N-terminal amino acid is FT lysine and not leucine,arginine or alanine, the N-terminal FT amino acids preferred by the yeast homologues." FT /db_xref="GOA:A2QIL3" FT /db_xref="InterPro:IPR006025" FT /db_xref="UniProtKB/TrEMBL:A2QIL3" FT /citation=[89] FT /inference="profile:COGS:COG0308" FT /inference="profile:PFAM:PF01433" FT /inference="similar to AA sequence:UniProtKB:ANI292570.1" FT /protein_id="CAK38657.1" FT /translation="MCGARRGEVTGSTNVPGGREVLPTNVKPLHYDLTLEPNFANFSYD FT GTVVIDLDVAEDTTSISLNSNEIKIHNAVVSSQGAVVASNPEITLNQDQQVATIKFADT FT IPAGSSAQLKLTFTGELNDNMAGFYRSSYKAADGQTKYIATTQMEPTDARRAFPCFDEP FT ALKAKFTVTLVADKSMTCLSNMDVASETEVAGGKKAVKFNTSPVMSTYLLAFIVGHLNY FT IETKAFRVPIRVYATPDQDIEHGRFSLDLAARTLAFYEKAFDNEFPLPKMDMVAVPDFS FT AGAMENWGLITYRVVDVLLDEKTSGAARKERIAETVQHELAHQWFGNLVTMDFWDGLWL FT NEGFATWMSWYSCNSFFPEWKVWQTYVIDTLQGALSLDSLRSSHPIEVPVKRADEINQI FT FDAISYSKGSSVLRMISKYMGEDVFIQGVRDYIKKHAYGNTQTGDLWAALANASGKPVE FT EVMDIWTKKVGFPVVTVSENPSNSTIKLKQNRFLRTGDVRPDEDTTLYPVMLGLRTKNG FT IDEDTMLTEREGEFKVPDLDFFKLNADHSAIYRTSYTPERLSKLGEAAKGGLLSVEDRA FT GMIADAGALAASGFQSTSGLLSLLKGFDSEAEFIVWNEILTRVGSLRAAWLFEDVSTRD FT ALKAFQRSLVSHKAHELGWEFSEKDGHILQQFKALMFGSAGMAEDPVVVKAAQDMFQQF FT AAGDENAIHPNIRGSVFSIVLKNGGEKEYNVVLDRFRNAPTSDEKTTALRCLGAAEDPA FT LIQRTLDLASGDEVKNQDIYMPLGGLRSHPAGIEARWSWLKNNWDAIYKRLPPSLGMLG FT TVVQLSTASFCTEEQLKDVQDFFQSKDTKGFDRAVEQSLDSIRAKVNWVKRDRADVESW FT LKANSYNGKL" FT mRNA complement(join(<170268..170390,170467..172837, FT 172925..>173076)) FT /gene="apsA" FT /locus_tag="An04g03930" FT exon complement(170268..170390) FT /gene="apsA" FT /locus_tag="An04g03930" FT /number=1 FT intron complement(170391..170466) FT /gene="apsA" FT /locus_tag="An04g03930" FT /number=1 FT exon complement(170467..172837) FT /gene="apsA" FT /locus_tag="An04g03930" FT /number=2 FT intron complement(172838..172924) FT /gene="apsA" FT /locus_tag="An04g03930" FT /number=2 FT exon complement(172925..173076) FT /gene="apsA" FT /locus_tag="An04g03930" FT /number=3 FT CDS complement(join(174426..175024,175094..175358, FT 175418..175868,175928..176159,176250..176352)) FT /locus_tag="An04g03940" FT /note="Function: MUP1 encodes the high affinity methionine FT permease from S. cerevisiae." FT /note="Function: MUP1 has also be shown to be a major FT permease in cysteine uptake." FT /note="Remark: MUP1 encodes an integral membrane protein FT with 13 putative membrane-spanning regions." FT /note="Title: strong similarity to high affinity methionine FT permease Mup1 - Saccharomyces cerevisiae" FT /note="plasma membrane" FT /db_xref="GOA:A2QIL4" FT /db_xref="InterPro:IPR004841" FT /db_xref="UniProtKB/TrEMBL:A2QIL4" FT /citation=[37] FT /citation=[85] FT /inference="profile:COGS:COG0833" FT /inference="similar to AA sequence:PIR:S61943" FT /protein_id="CAK38658.1" FT /translation="MTDPVVESAYQKGILPDAKAVEEGPRRTDGVSGLYEGNVFEATPD FT DRRQIGVISASFLIFNRVIGTGIFATPSTILSLSGSVGLSLIMWVIGTLIAMAGTAVYL FT EWGTAIPKNGGEKNYLEYVFKKPKFLMTAMYAAYAVLLGWAASNSVVFGEYILNAADIE FT VDRWNQRGIGLACITAAFLIHSFAVKWGLMLQNFLGVVKLVIILFVIVAGWVALGGHMK FT IDPPHNFTNAFEGTTDTGYGIVMALYNVIWSFIGYSNANYALSETKNPTRTLKIAAPIA FT IISVGIMYMLCNIAYFAAVPKEQFLSSGQTVAAAFFGNMFGARAEKVMSVFVALSAFGN FT VLSVIFSQGRIVQALGREGVLPLSKIWASNRPFNSPAAGLFEHWVVSVIIMLAPPPGDA FT YNFLVNLISYPLSIVNVFVSGGLIYIYLTKEKNFPDWSPGIRATLPVTIFFCLSNMYLV FT VAPYVPPSAGQSVYNSLPYYLHCVVALGIFALGAIYYLVWAVLMPRFGRYILVKESVVD FT ADGWSRSVFTKMPIEQAEALRHEGQQQGEHHF" FT mRNA complement(join(<174426..175024,175094..175358, FT 175418..175868,175928..176159,176250..>176352)) FT /locus_tag="An04g03940" FT exon complement(174426..175024) FT /locus_tag="An04g03940" FT /number=1 FT intron complement(175025..175093) FT /locus_tag="An04g03940" FT /number=1 FT exon complement(175094..175358) FT /locus_tag="An04g03940" FT /number=2 FT intron complement(175359..175417) FT /locus_tag="An04g03940" FT /number=2 FT exon complement(175418..175868) FT /locus_tag="An04g03940" FT /number=3 FT intron complement(175869..175927) FT /locus_tag="An04g03940" FT /number=3 FT exon complement(175928..176159) FT /locus_tag="An04g03940" FT /number=4 FT intron complement(176160..176249) FT /locus_tag="An04g03940" FT /number=4 FT exon complement(176250..176352) FT /locus_tag="An04g03940" FT /number=5 FT CDS complement(join(177781..178073,178112..180692, FT 180821..180926,181016..181059)) FT /locus_tag="An04g03950" FT /EC_number="2.7.1.-" FT /note="Function: APG1 is a serine/threonine protein kinase FT involved in induction of autophagy after nutrient FT limitation." FT /note="Remark: S. cerevisiae imports cytosolic components FT into the vacuole non-selectively by autophagy and degrades FT them by vacuolar hydrolases under nutrient starvation FT conditions." FT /note="Remark: at least 15 APG genes are involved in FT autophagy in yeast." FT /note="Title: strong similarity to serine/threonine protein FT kinase Apg1 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIL5" FT /db_xref="InterPro:IPR002290" FT /db_xref="UniProtKB/Swiss-Prot:A2QIL5" FT /citation=[23] FT /citation=[43] FT /inference="profile:COGS:COG0515" FT /inference="profile:PFAM:PF00069" FT /inference="similar to AA sequence:PIR:S61137" FT /protein_id="CAK38659.1" FT /translation="MGLFHHSTLFLPLLRRSNEGPHGEMPIGHYTRLSEIGRGSFAVVY FT KGVHTRSRTYVAIKSVTMTKLSRKLKENLASEISILKQLHHPHIVALLDCHDTTSNIHL FT VMEFCALGDLSHFIKGRNTLQDSPYTRELIAKYPNPGEGAGLNEVIVRHFLKQLSSALR FT FLRDRDLIHRDIKPQNLLLCPAPSSYRSGAADVVPFKSSEDSFSPKTGLESLPMLKLAD FT FGFARSLPATSLAETLCGSPLYMAPEILRYEKYDAKADLWSVGTVLYEMVVGRAPFRAV FT NHIELIKKIEQNKDQISFPSKNRVSEDIRELIRGLLKQHPMDRMNFDVYFAHKVLTEPI FT PGLVADDAPLGRSPADPTPRPGSGSRRSTPVQMKRENALSGGVRDEPATYPAAQRAMTQ FT SPRPETPSTPMRRTGSAGTPHAAPNEPTPPASHPTRPSPVSLATAPGRQEHVDRPPTTT FT VVEQQRRRTASSGVPQVDKPVEKAKDEKEHAAQEVAFERDYVLVEKRAVEMNAFADELA FT YNPRMQGGQAGAVSRRSGAAPGTPPAGGSSPHASPSKAMQIISGRSRADSAHVRQNSYD FT RRYGQSPTSATSAISKALNMASGRLFGMSFSPPLTITKGGRSPPLAYNPFPAYPSAQTS FT LIVHADGGKPGANLDEDSKTVHDLEECATRSDVVYGFAEVKYKQLIPLAPSAATGYPGD FT PGSDAVDSADGGLTVDAIVTLSEEALVLYVKALSLLAKSMDIARVWWTRKSRGDTLSRA FT DTGSTVAGNRINNVVQWVRNRFNEVLEKAEFVRLKLVEAQKRLPSDHPSHPSNLSVGSS FT LGSGTSADVVVSPDVTAEKLMYERALEMSRVAAINEITGEDLAGCEISYVTAIRMLEAI FT LDDVEVSRPGQSGGADRADARRDNEDGGQNEPQAVILAKSANAWHSDIENPESPGVAPE FT EAGAAVESVHAPVQWTGQNAAVESGASLPCSGSHAAEIRTLTVRSMQDHAHFAPLLFSI FT FISSYSSSISCPSSCGHC" FT mRNA complement(join(<177781..178073,178112..180692, FT 180821..180926,181016..>181059)) FT /locus_tag="An04g03950" FT exon complement(177781..178073) FT /locus_tag="An04g03950" FT /number=1 FT intron complement(178074..178111) FT /locus_tag="An04g03950" FT /number=1 FT exon complement(178112..180692) FT /locus_tag="An04g03950" FT /number=2 FT intron complement(180693..180820) FT /locus_tag="An04g03950" FT /number=2 FT exon complement(180821..180926) FT /locus_tag="An04g03950" FT /number=3 FT intron complement(180927..181015) FT /locus_tag="An04g03950" FT /number=3 FT exon complement(181016..181059) FT /locus_tag="An04g03950" FT /number=4 FT CDS complement(join(183524..185616,185681..186233)) FT /locus_tag="An04g03960" FT /EC_number="2.7.1.108" FT /note="Catalytic activity: SEC59 catalyzes the transfer of FT mannose to dolichol-linked oligosaccharide." FT /note="Function: SEC59 encodes a membrane protein required FT for core glycosylation in S. cerevisiae." FT /note="Phenotype: SEC59 mutants accumulate inactive and FT incompletely glycosylated forms of secretory proteins." FT /note="Title: similarity to dolichol kinase Sec59 FT -Saccharomyces cerevisiae" FT /note="endoplasmatic reticulum" FT /db_xref="GOA:A2QIL6" FT /db_xref="InterPro:IPR000374" FT /db_xref="UniProtKB/TrEMBL:A2QIL6" FT /citation=[14] FT /citation=[3] FT /inference="profile:COGS:COG0170" FT /inference="profile:COGS:COG4589" FT /inference="similar to AA sequence:PIR:JQ0124" FT /protein_id="CAK38660.1" FT /translation="MAVSLSQEEDESLPVNGSALDIELSDTPRQPSRSPHPYRRKGSHS FT SSLPADTGGRSTRLHWPRTSSDSGTEADDESTGILRGLPAAPLRPRKGLRSGRHAVGED FT DQWFPLLRPWPSITRSTSRSSRRSSGEEAEASATGLREQEARKRRTGVLQRLLEAALLL FT SVGGVVLGQENTRAVAWAWRKELLAHALLVIGLYAAYPFHRDGRFRFSRLRSFVIPTSF FT DPAPLLYPILIPIYVALSLAQHTPSLILPNVLLSLSSLPPAVIPLHDCVHGHSIVHWMI FT TLLPIILSEQLSAGISPPRPLSLLGLNSESLALLFPLHQALIPTLDFLLTTSVLPAELQ FT LLTSALINLLLFASSPQAEILKALLWLGGLCIFISCRDVLRWEVALARIPSWKFRRAPS FT NSQSPRSIFNVLDHKLCQRLSRTGTSEDNLSDSDSPEGQFSLVSRKTMVESRDRTKAGE FT PIRTVEAEVTEGVRQPTLTHRRRHTISSVSEVARTGKVRTTPSGRRKRSMAPGLASFLS FT LTVPQAQVRKWLYALFIYVTVLLIILGPVRKYVGERALHGEDPFGWALSYLLGNVSWFR FT FWVIMWNLEYWIPIPARLDPDLLNASCGLGWVEHLRRDVFGEANSRLLVAAYCIVVLVT FT GLAVVLQLSSVAEVDTRRKVFHGMMVLMFLPTVYVDPTFCALALSLVLSVFLLLDLFRA FT SQLPPISRPLTYFLAPYVDGRDHRGPVIVSHIFLLIGCSIPLWLSLADIPRTGDHPWIG FT WSALTRDVSMVSGIVCVGMGDAAASLVGRRFGRRKWFWGGGKSLEGSVAFAVAVTCGLL FT FARIWLVVGEWPVSGGSDGPHQNFPWVKAMVKVILAAGGTSATEAILTGCNDNVVVPIV FT LWLLVRGLGV" FT mRNA complement(join(<183524..185616,185681..>186233)) FT /locus_tag="An04g03960" FT exon complement(183524..185616) FT /locus_tag="An04g03960" FT /number=1 FT intron complement(185617..185680) FT /locus_tag="An04g03960" FT /number=1 FT exon complement(185681..186233) FT /locus_tag="An04g03960" FT /number=2 FT exon complement(186755..189109) FT /locus_tag="An04g03970" FT /number=1 FT CDS complement(186755..189109) FT /locus_tag="An04g03970" FT /note="Remark: The EST sequence of EMBLEST:BE759313 is from FT Aspergillus niger but deviates in several positions from FT the sequence of the genomic DNA." FT /note="Title: strong similarity to hypothetical protein FT SPAC577.12 - Schizosaccharomyces pombe" FT /db_xref="InterPro:IPR006175" FT /db_xref="UniProtKB/TrEMBL:A2QIL7" FT /inference="profile:COGS:COG0251" FT /inference="profile:COGS:COG2102" FT /inference="profile:PFAM:PF01902" FT /inference="similar to AA sequence:PIR:T40556" FT /protein_id="CAK38661.1" FT /translation="MATSTPSLPLPTSPTSLNVIALISGGKDSLYSILHCIRNGHKVVA FT LGNLYPPTTTTTPHEEGKPQDEEEQDEEEDIDSFMYQTIGHSIIPHYESALGIPLYRQP FT ITGSAVDTGRVYRDSSSSASSGGEGKEGEGGTDETESLIPLLQRIKAAHPEANAISAGA FT ILSTYQRTRIENVAARMGLVPLAWLWQYPVLPAPEERFGLGSGEAGLLEDMAAVGCEAR FT IIKVASGGLDAGFLWGDVSGRNAMVRRRIVNGMKRFVLDGGDVRGAVLGEGGEYESLAL FT DGPSFLWKRRIEVPRWEEGAGEGGVAFVRVRGARCVDKDAEGDGVVPGDVRRPVLLDEG FT FKGVLEEVLGGEEVMGKREESSVVSSQRQMEMSQSTNGGTWVVANITAPEAGPGAAEQM FT EAIAQKIEAILASTRHEDGSAPRTTADIVFTTVLLRSMADFALMNGIYVSLFKKPNPPA FT RATVACGESLPEGVKVMVSAVVDLGPREQRQGLHVQSRSYWAPANIGPYSQAMSVPVQG FT SEHMVYIAGQIPLEPASMEMMSASGEALTRPWIENYTTRAVLSLQHLWRIGHAMEVDWW FT LGAVAFLTGGEHIETQARLAWNIWERMHARQEQEDDEDGESGLDVWDIKYGGRAHEQAT FT GPSTPNLPNFGVVQSDALVPAFFAVQIEELPRGSDIEWQGLGYRCGGLRMAAEETDYGR FT KTTVSTEQNLSYIGIEIDMGQLGSDLDSYLQDKLQKLPELVEGSHAIIYTSQPLSKPAF FT PAQIVPCKSVWGPKGRELAAGVIIQRHAPAL" FT mRNA complement(<186755..>189109) FT /locus_tag="An04g03970" FT CDS complement(join(190396..191660,191797..192370)) FT /locus_tag="An04g03980" FT /note="Function: MHY1 encodes a C(2)H(2)-type zinc finger FT protein with the ability to bind putative stress response FT elements and whose activity is essential for both hyphal FT and pseudohyphal growth in Y. lipolytica." FT /note="Function: Mhy1p may act as a transcription factor." FT /note="Induction: transcription of MHY1 is dramatically FT increased during the yeast-to-hypha transition in Yarrowia FT lipolytica." FT /note="Phenotype: Deletion of MHY1 is viable and has no FT effect on mating, but it does result in a complete FT inability of cells to undergo mycelial growth." FT /note="Title: similarity to C2H2-type zinc finger protein FT Mhy1p - Yarrowia lipolytica" FT /note="nucleus" FT /db_xref="GOA:A2QIL8" FT /db_xref="InterPro:IPR015880" FT /db_xref="UniProtKB/TrEMBL:A2QIL8" FT /citation=[59] FT /inference="profile:COGS:COG5048" FT /inference="profile:PFAM:PF00096" FT /protein_id="CAK38662.1" FT /translation="MDGTYTMAPTSVQGQPSFAYYADSQQRQHFTSHPSDMQSYYGQVQ FT AFQQQPQHCMPEQQTLYTAPLMNMHQMATTNAFRGAMNMTPIASPQPSHLKPTIVVQQG FT SPALMPLDTRFVGNDYYAFPSTPPLSTAGSSISSPPSTSGTLHTPINDSFFAFEKVEGV FT KEGCEGDVHAEILANADWARSDSPPLTPVFIHPPSLTASQTSELLSAHSSCPSLSPSPS FT PVVPTFVAQPQGLPTEQSSSDFCDPRQLTVESSINATPAELPPLPTLSCDDEEPRVVLG FT SEAVTLPVHETLSPAFTCSSSEDPLSSLPTFDSFSDLDSEDEFVNRLVDFPPSGNAYYL FT GEKRQRVGTTYPLEEEEFFSEQSFDESDEQDLSQSSLPYLGSHDFTGVQTNINEASEEM FT GNKKRNNRKSLKRASTSDSETDSISKKSQPSINSRATSTETNASTPQTVQARHNSDAHS FT SCASEAPAAPVSVNRRGRKQSLTDDPSKTFVCTLCSRRFRRQEHLKRHYRSLHTQDKPF FT ECNECGKKFSRSDNLAQHARTHAGGSVVMGVIDTGNATPPTPYEERDPSTLGNVLYEAA FT NAAATKSTTSESDESSSDSPVADRRAPKKRKRDSDA" FT mRNA complement(join(<190396..191660,191797..>192370)) FT /locus_tag="An04g03980" FT exon complement(190396..191660) FT /locus_tag="An04g03980" FT /number=1 FT intron complement(191661..191796) FT /locus_tag="An04g03980" FT /number=1 FT exon complement(191797..192370) FT /locus_tag="An04g03980" FT /number=2 FT CDS join(192597..192643,192735..192889,193091..193197) FT /locus_tag="An04g03990" FT /product="hypothetical protein" FT /db_xref="InterPro:IPR002345" FT /db_xref="UniProtKB/TrEMBL:A2QIL9" FT /protein_id="CAK38663.1" FT /translation="MTGGRTDDNPGTALNQLNGGWWYLGLYLTTMPQVYEGRTGTLCVE FT TSQTKKDEYGSGRSRFKETGRDWPIWKEESRPEGWAVDKRATDLLVLRAGSAVSSEQ" FT mRNA join(<192597..192643,192735..192889,193091..>193197) FT /locus_tag="An04g03990" FT exon 192597..192643 FT /locus_tag="An04g03990" FT /number=1 FT intron 192644..192734 FT /locus_tag="An04g03990" FT /number=1 FT exon 192735..192889 FT /locus_tag="An04g03990" FT /number=2 FT intron 192890..193090 FT /locus_tag="An04g03990" FT /number=2 FT exon 193091..193197 FT /locus_tag="An04g03990" FT /number=3 FT CDS complement(join(193668..193779,194072..194170, FT 194240..194340,194389..194455,194722..194829, FT 194952..195027,195220..195271)) FT /locus_tag="An04g04000" FT /note="Title: strong similarity to EST an_2710 -Aspergillus FT niger" FT /db_xref="UniProtKB/TrEMBL:A2QIM0" FT /protein_id="CAK38664.1" FT /translation="MSPPAGPGLLSVADMLIAADKPDRLRDDAGPNGNGTIIQQRSEAE FT QGKGSIVTGREEDGQSQKVGYYFGSNNTYGLGLGGVGLKWPFGPPRVGIERRQSHLEPG FT ILWHFSHTLMPSRPPIGTWSSPHLPGHYGKTAANVPTRAHVPHALTPFLGSAADVVGPG FT FWLVRPPRRAPPPVGLRSQVSHSVGTEMCTGANLLFFAAPD" FT mRNA complement(join(<193668..193779,194072..194170, FT 194240..194340,194389..194455,194722..194829, FT 194952..195027,195220..>195271)) FT /locus_tag="An04g04000" FT exon complement(193668..193779) FT /locus_tag="An04g04000" FT /number=1 FT intron complement(193780..194071) FT /locus_tag="An04g04000" FT /number=1 FT exon complement(194072..194170) FT /locus_tag="An04g04000" FT /number=2 FT intron complement(194171..194239) FT /locus_tag="An04g04000" FT /number=2 FT exon complement(194240..194340) FT /locus_tag="An04g04000" FT /number=3 FT intron complement(194341..194388) FT /locus_tag="An04g04000" FT /number=3 FT exon complement(194389..194455) FT /locus_tag="An04g04000" FT /number=4 FT intron complement(194456..194721) FT /locus_tag="An04g04000" FT /number=4 FT exon complement(194722..194829) FT /locus_tag="An04g04000" FT /number=5 FT intron complement(194830..194951) FT /locus_tag="An04g04000" FT /number=5 FT exon complement(194952..195027) FT /locus_tag="An04g04000" FT /number=6 FT intron complement(195028..195219) FT /locus_tag="An04g04000" FT /number=6 FT exon complement(195220..195271) FT /locus_tag="An04g04000" FT /number=7 FT CDS join(200990..201202,201264..201407,202045..202536) FT /locus_tag="An04g04010" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIM1" FT /protein_id="CAK38665.1" FT /translation="MRVRIHPENGSGRQDWNLLSQQFSAPNRCETITERPGLAYIVQSQ FT NQQIFNFVPSPYTDWRREPYYSTHSKGNGTSPSVRALLRQTVQQEVRRQTELLSVDYLY FT LPSTSSTDVERLIKAASEPLYEPRIKRGGVIINYGSHTVSTHSATYFRVISLHDSGSFR FT MENLPRRQTMPYASYATTLPSSAVDHGLVYSPKMYSPTETEVMFPHTHERMHAVRPNGV FT MATVELAVVANPSSRQAVLVPAGRAGTGASRPSIAGMKLPHFLRGPSTTTACTTACSTA FT D" FT mRNA join(<200990..201202,201264..201407,202045..>202536) FT /locus_tag="An04g04010" FT exon 200990..201202 FT /locus_tag="An04g04010" FT /number=1 FT intron 201203..201263 FT /locus_tag="An04g04010" FT /number=1 FT exon 201264..201407 FT /locus_tag="An04g04010" FT /number=2 FT intron 201408..202044 FT /locus_tag="An04g04010" FT /number=2 FT exon 202045..202536 FT /locus_tag="An04g04010" FT /number=3 FT CDS complement(join(202733..203017,203088..203210)) FT /locus_tag="An04g04020" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIM2" FT /protein_id="CAK38666.1" FT /translation="MAGGANHSPPLASTGSLPKFSTNGAIRNHSIDTPEYDAVQSWLLR FT SATLVHDLPCTNPGTELNEHATWMSSRLPAGFDSILECRDEHAVIIGISTRWNNHTSKK FT GAPSPTSIGRWAVQAVKHIKVTRGLARFKLS" FT mRNA complement(join(<202733..203017,203088..>203210)) FT /locus_tag="An04g04020" FT exon complement(202733..203017) FT /locus_tag="An04g04020" FT /number=1 FT intron complement(203018..203087) FT /locus_tag="An04g04020" FT /number=1 FT exon complement(203088..203210) FT /locus_tag="An04g04020" FT /number=2 FT CDS join(203221..203348,203441..203570,203987..204044, FT 204163..204342,204410..204576,204629..204738, FT 204788..204878) FT /locus_tag="An04g04030" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIM3" FT /protein_id="CAK38667.1" FT /translation="MSISYSTPSQRCSILDRVVGAFGGMRSGRPRALAVRPEPSPVRTQ FT DVAAPSMMIVRDSMGNGVTGEIKDTEITQTEGKLTVRPRESGGPAPSAGMRLEVPILER FT AGKPAQNSARPRCLRVNFIAGGIASMAHYSTFRPASASRKALSHAETFGGDPIAPSASW FT VANGCVDQCPNMIDARPSLGPSKALGLPSAHCTLQVGESGRGKDRPLSASINHDNNSYW FT DLGQTKRIAVSTEHPEKNNARSAGSASLVSPLPHGPPQGPDVRGARARRGAGCRTCEWD FT GTMGPF" FT mRNA join(<203221..203348,203441..203570,203987..204044, FT 204163..204342,204410..204576,204629..204738, FT 204788..>204878) FT /locus_tag="An04g04030" FT exon 203221..203348 FT /locus_tag="An04g04030" FT /number=1 FT intron 203349..203440 FT /locus_tag="An04g04030" FT /number=1 FT exon 203441..203570 FT /locus_tag="An04g04030" FT /number=2 FT intron 203571..203986 FT /locus_tag="An04g04030" FT /number=2 FT exon 203987..204044 FT /locus_tag="An04g04030" FT /number=3 FT intron 204045..204162 FT /locus_tag="An04g04030" FT /number=3 FT exon 204163..204342 FT /locus_tag="An04g04030" FT /number=4 FT intron 204343..204409 FT /locus_tag="An04g04030" FT /number=4 FT exon 204410..204576 FT /locus_tag="An04g04030" FT /number=5 FT intron 204577..204628 FT /locus_tag="An04g04030" FT /number=5 FT exon 204629..204738 FT /locus_tag="An04g04030" FT /number=6 FT intron 204739..204787 FT /locus_tag="An04g04030" FT /number=6 FT exon 204788..204878 FT /locus_tag="An04g04030" FT /number=7 FT exon 205795..206004 FT /locus_tag="An04g04035" FT /number=1 FT CDS 205795..206004 FT /locus_tag="An04g04035" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIM4" FT /protein_id="CAK38668.1" FT /translation="MSSHTYQPFPIPFFKSRLTPEQQIIHLPTNQPYKYFTTPYTLLES FT FFSFFSSCGDATIFTRVAWTSVSP" FT mRNA <205795..>206004 FT /locus_tag="An04g04035" FT CDS complement(join(206295..206371,206455..207218, FT 207291..207438,207574..207652)) FT /locus_tag="An04g04040" FT /note="Title: strong similarity to hypothetical thioredoxin FT SPAC577.08c - Schizosaccharomyces pombe" FT /db_xref="GOA:A2QIM5" FT /db_xref="InterPro:IPR013766" FT /db_xref="UniProtKB/TrEMBL:A2QIM5" FT /inference="profile:COGS:COG0526" FT /inference="profile:COGS:COG3118" FT /inference="profile:PFAM:PF00085" FT /inference="similar to AA sequence:PIR:T40552" FT /protein_id="CAK38669.1" FT /translation="MSTLVQINSREQFSSLLSSSTFVVADFYADWCGPCKAIAPAYEQL FT ASQLSRPNKITFTKVNVDKNQDIARQYGITAMPTFVLFERGRPTSTVRGANAKELNDLV FT RKLATEAEKAPEGNDAGSSSGVGWIGAPAPKNYSDISDQYDPKGLELLNRASEFGTAKT FT LFDSSKPSSLNNAKGKAGAAPDWVESDTDEQLMLFIPFQSTLKVHSLQITSLPPSADEE FT VEDEDERPMRPRTVSLYTNRSHVLGFDEADDIPAVQTVTIQPEDWDPKTGTAKVDLRFV FT KFQSVTSLVIFFVDGDGDSEKLRVDRVRIFGEAGEKREMGKLEKIGDEPEKPSLCSYMD FT SRHIHTYNDIHIQYQ" FT mRNA complement(join(<206295..206371,206455..207218, FT 207291..207438,207574..>207652)) FT /locus_tag="An04g04040" FT exon complement(206295..206371) FT /locus_tag="An04g04040" FT /number=1 FT intron complement(206372..206454) FT /locus_tag="An04g04040" FT /number=1 FT exon complement(206455..207218) FT /locus_tag="An04g04040" FT /number=2 FT intron complement(207219..207290) FT /locus_tag="An04g04040" FT /number=2 FT exon complement(207291..207438) FT /locus_tag="An04g04040" FT /number=3 FT intron complement(207439..207573) FT /locus_tag="An04g04040" FT /number=3 FT exon complement(207574..207652) FT /locus_tag="An04g04040" FT /number=4 FT exon complement(208379..208963) FT /locus_tag="An04g04050" FT /number=1 FT CDS complement(208379..208963) FT /locus_tag="An04g04050" FT /note="Title: similarity to hypothetical protein dnajp FT -Schizosaccharomyces pombe" FT /db_xref="GOA:A2QIM6" FT /db_xref="InterPro:IPR015609" FT /db_xref="UniProtKB/TrEMBL:A2QIM6" FT /inference="profile:COGS:COG0484" FT /inference="profile:PFAM:PF00226" FT /inference="similar to AA sequence:PIR:T39203" FT /protein_id="CAK38670.1" FT /translation="MTRSNHPLTQDYYEVLNLPFTETPTALSKQQLKAAYHKALLKYHP FT DKAPGAIADTSSLPTSDTNSSSHTSHRYTIDEITTAYKTLSDPYLRAEYDRSLRLDRAR FT VAEREKTGTVFHTGLEVVDLEDLACDESDADAALWYRGCRCGDERGFLVTEQDLEREAD FT HGEIVVGCRGCSLWMKVLFAVEDGDGDEQNT" FT mRNA complement(<208379..>208963) FT /locus_tag="An04g04050" FT CDS complement(join(209694..210431,210504..210860)) FT /locus_tag="An04g04060" FT /EC_number="1.11.1.5" FT /note="Catalytic activity: 2 ferrocytochrome c + H(2)O(2) FT <=> 2 ferricytochrome c + 2 H(2)O." FT /note="Cofactor: heme" FT /note="Function: protection against toxic peroxides." FT /note="Title: strong similarity to cytochrome-c peroxidase FT precursor Ccp1 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIM7" FT /db_xref="InterPro:IPR019794" FT /db_xref="UniProtKB/TrEMBL:A2QIM7" FT /inference="profile:COGS:COG0376" FT /inference="profile:PFAM:PF00141" FT /protein_id="CAK38671.1" FT /translation="MASAARTASRAFLRSTPATSSFRPAARSARFALPSQGFRAASRRG FT YTSEAGEAKSSNSLLWAGIAAAGGVGAYFYLKGGDASVTSKDFVPTKEDYQKVYDAVAH FT RLANETDYDDGSYGPVLVRLAWHASGTYDKETGTGGSNGATMRFAPESDHGANAGLKHA FT RDFLEPIKAQFPWITYSDLWTLAGACAIQELGGPAIPWRPGREDKDVAACTPDGRLPDA FT TKEQSHIRDIFYRMGFNDQEIVALVGAHSLGRAHTDRSGFDGPWDFSPTVFTNEFFRLL FT VEEKWQQRKWNGPKQFTDKTTGTLMMMPADLALTKDKAFRKYVELYAKDSDLFFKDFSN FT VFVKLLELGVPFKTEDRYVFKTSE" FT mRNA complement(join(<209694..210431,210504..>210860)) FT /locus_tag="An04g04060" FT exon complement(209694..210431) FT /locus_tag="An04g04060" FT /number=1 FT intron complement(210432..210503) FT /locus_tag="An04g04060" FT /number=1 FT exon complement(210504..210860) FT /locus_tag="An04g04060" FT /number=2 FT CDS complement(join(211160..211277,211425..211577, FT 211846..212029,212300..212427,213092..213650, FT 213916..214069)) FT /locus_tag="An04g04070" FT /note="Similarity: the ORF shows weak similarity to anohter FT A. niger protein: An11g09200. The similarity between the FT two proteins, however, is restricted to a stretch of about FT 60 amino acids." FT /note="Title: weak similarity to hypothetical protein FT encoded by An11g09200 - Aspergillus niger" FT /db_xref="UniProtKB/TrEMBL:A2QIM8" FT /protein_id="CAK38672.1" FT /translation="MAVNYRHGLSILELIVYLPSLFISLYMGFRHGFQRNAGWILLIIF FT SLARIVAGMVLCIVGSSMSSSLQGITNSIEAKVGDVLYVIAWACLCVLLLVVGSKYASI FT EDGEHRLLLAVGISVPLLLVRLIYSLLSVFTHNPTFNMLTGNVTVFLVMAVLEEIVIVG FT ICLGVGMTLEVRQRPTEYEACEAPAQGGSELESQQRPDITSYNPKKQERRQKKRRGGPI FT SQLIGLAIDEIRSRRHTTKTTQCASSLFNGIEAYFFFKFVQWKIKTKQFLAELRLLHPD FT IWGMIVAAALEINQRGTEAMVDYRACCFVAVANVSYHIGDVNITATENDRHQGLIISYQ FT KRNERLTSRIGYDRCMEMVVVAPPESSQLSQWTHITDNRHNNGSVNSMLCGTLDSRRQK FT CGERLAESKDSAQSSSICVLPLVRRAWTTDSA" FT mRNA complement(join(<211160..211277,211425..211577, FT 211846..212029,212300..212427,213092..213650, FT 213916..>214069)) FT /locus_tag="An04g04070" FT exon complement(211160..211277) FT /locus_tag="An04g04070" FT /number=1 FT intron complement(211278..211424) FT /locus_tag="An04g04070" FT /number=1 FT exon complement(211425..211577) FT /locus_tag="An04g04070" FT /number=2 FT intron complement(211578..211845) FT /locus_tag="An04g04070" FT /number=2 FT exon complement(211846..212029) FT /locus_tag="An04g04070" FT /number=3 FT intron complement(212030..212299) FT /locus_tag="An04g04070" FT /number=3 FT exon complement(212300..212427) FT /locus_tag="An04g04070" FT /number=4 FT intron complement(212428..213091) FT /locus_tag="An04g04070" FT /number=4 FT exon complement(213092..213650) FT /locus_tag="An04g04070" FT /number=5 FT intron complement(213651..213915) FT /locus_tag="An04g04070" FT /number=5 FT exon complement(213916..214069) FT /locus_tag="An04g04070" FT /number=6 FT CDS join(214704..214754,214854..215426,215479..215622, FT 215675..216514) FT /locus_tag="An04g04080" FT /note="Title: similarity to hypothetical negative acting FT factor related protein - Neurospora crassa" FT /db_xref="GOA:A2QIM9" FT /db_xref="InterPro:IPR001138" FT /db_xref="UniProtKB/TrEMBL:A2QIM9" FT /inference="similar to AA sequence:UniProtKB:NCB3E4.9" FT /protein_id="CAK38673.1" FT /translation="MGKPSGGCGTCRARRVKCDETRPVCRRCRKARRTCSGYRDPHSVW FT FRDESDAVARRVKGSATLDTGSSSAESPILTLARRNTSSEYYPGQHTLRFPLAIVNFAL FT DHTFQATCFFLDAYTWFNASKIVETSFKHGAGPAESLGQKAMMASIASVGLANLASMQR FT SSSMRLSARHEYTTALQLTNAALCDPNLVTADTTLTAIVCLSLFEIIACHKNESLDSWI FT EHSQGVATVLELRGRDQLRREGGFWMFQALRNEVVLGCLQKKTRLPSVLVDMPDQVAAD FT LPPYPFPPDGDRLVKIMAKFTGLQADVREGILLDSSEIVKMAMAIDLELGHFASHASAD FT FTYKVETQPGSVTSCEHDEGNFCHYQGTYHIYQSIWSCNIWNNYRYTRILVNSMILTHL FT RSMASSGHQVLDYGLFKDHCIRIRDLMRQLATDICCSIPFKFGVAGFDKKDVFDSLHTH FT AGTGFTLLLPLAMAALVGGVSSPMHNWAMRCFHVIGRGMGIGTASTLVTVLGNEPGGLH FT WIDAMESGHTVCSRAVLQ" FT mRNA join(<214704..214754,214854..215426,215479..215622, FT 215675..>216514) FT /locus_tag="An04g04080" FT exon 214704..214754 FT /locus_tag="An04g04080" FT /number=1 FT intron 214755..214853 FT /locus_tag="An04g04080" FT /number=1 FT exon 214854..215426 FT /locus_tag="An04g04080" FT /number=2 FT intron 215427..215478 FT /locus_tag="An04g04080" FT /number=2 FT exon 215479..215622 FT /locus_tag="An04g04080" FT /number=3 FT intron 215623..215674 FT /locus_tag="An04g04080" FT /number=3 FT exon 215675..216514 FT /locus_tag="An04g04080" FT /number=4 FT CDS complement(join(216917..217079,217163..217276, FT 217352..217467,217676..217916,218006..218013)) FT /locus_tag="An04g04090" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIN0" FT /protein_id="CAK38674.1" FT /translation="MAGWGKKVSSSNSTSRASGTGIRENLQAERQSIFTPGKRPSMRPS FT KLMHNKSSKEGGGGGNWAGKPASQQKERPGMRREELAESKQLYMKDRRKSSVRVASGAA FT APNGCKQLLTFDPNRPGCHANETPLLRSNNVMEASQAPFHSACLPRGDFLHGSRDAVAD FT PALAGASGSILFYVYDLKSHSIPNLSMGMFEQQVTPTTIAQTSSGRNSVR" FT mRNA complement(join(<216917..217079,217163..217276, FT 217352..217467,217676..217916,218006..>218013)) FT /locus_tag="An04g04090" FT exon complement(216917..217079) FT /locus_tag="An04g04090" FT /number=1 FT intron complement(217080..217162) FT /locus_tag="An04g04090" FT /number=1 FT exon complement(217163..217276) FT /locus_tag="An04g04090" FT /number=2 FT intron complement(217277..217351) FT /locus_tag="An04g04090" FT /number=2 FT exon complement(217352..217467) FT /locus_tag="An04g04090" FT /number=3 FT intron complement(217468..217675) FT /locus_tag="An04g04090" FT /number=3 FT exon complement(217676..217916) FT /locus_tag="An04g04090" FT /number=4 FT intron complement(217917..218005) FT /locus_tag="An04g04090" FT /number=4 FT exon complement(218006..218013) FT /locus_tag="An04g04090" FT /number=5 FT CDS join(218034..218148,218216..218236,218327..218433, FT 218507..218675,218835..220381) FT /locus_tag="An04g04100" FT /note="Function: GTS1 gene product of S. cerevisiae appears FT to modulate the timing of budding to obtain an appropriate FT cell size independent of the DNA replication cycle. a FT loss-of-function mutation results in a shortened unbudded FT period and smaller cell size, whereas overexpression of the FT GTS1 gene product extends the unbudded period and results FT in larger cells." FT /note="Title: strong similarity to Lsr1 - Saccharomyces FT cerevisiae" FT /db_xref="GOA:A2QIN1" FT /db_xref="InterPro:IPR000449" FT /db_xref="UniProtKB/TrEMBL:A2QIN1" FT /citation=[19] FT /citation=[41] FT /citation=[42] FT /inference="profile:COGS:COG2319" FT /inference="profile:COGS:COG5347" FT /inference="profile:PFAM:PF01412" FT /inference="similar to AA sequence:PIR:S58223" FT /protein_id="CAK38675.1" FT /translation="MVAGISKRQQFRNERALQDLIRSVPGNDRCADCQALNPGWASWNV FT RIFICMRCASLHRKLGTHISKVKSLSMDTWTDDQVDNMKSHGNNIMNKIYNPKNVKPPV FT PTDVDESDACMERFIRQKYQHRSLDEAKAKPPSLSPQSDSFGASGISVRKGSGDASFDA FT KLATLRDMGFANERRNAIALRELDGNLEKTIETLVRLGEGNGSVSLAKSPAAQPTPDAG FT KSSNPFDQLDARPATRQASGSYNPFDAPVQSQPQAQQAPVQSLEQSFQNLQVAQPLFPH FT STGGYPMRQVSLPQPLYQQTATPPVPTNFAQSAYVSSPQPLDGGNNPFFQTGAQPQASM FT TPPASNIAQNNPFFSQVAPQPTGMQQPPQSQAASNSPFGPLRHANTMPAMPSTSPFGQP FT SPFQSQLQSQSQLQPQPQAQPQPQYQMQQHLQQPQGSLNPYQAMTAPATPQSAGYLAQP FT QYGYQASAQHLAPQPTGRVDKNSILSLYQFSPQPSAIPEQPQYRPSTAVNPPTQTGQPS FT PFNTMPQQQQSQPFNTMPQQQQQQQQPQQQQQQQSNPLTDPLSASGNRNPFFTTAPQPG FT ASALAPTTTAQATPYLTTTAPPQQQQQQTVNVYGGMPNKPAGFPRGHMSQQSVDINGFQ FT SGRHSPDAFASLSARYG" FT mRNA join(<218034..218148,218216..218236,218327..218433, FT 218507..218675,218835..>220381) FT /locus_tag="An04g04100" FT exon 218034..218148 FT /locus_tag="An04g04100" FT /number=1 FT intron 218149..218215 FT /locus_tag="An04g04100" FT /number=1 FT exon 218216..218236 FT /locus_tag="An04g04100" FT /number=2 FT intron 218237..218326 FT /locus_tag="An04g04100" FT /number=2 FT exon 218327..218433 FT /locus_tag="An04g04100" FT /number=3 FT intron 218434..218506 FT /locus_tag="An04g04100" FT /number=3 FT exon 218507..218675 FT /locus_tag="An04g04100" FT /number=4 FT intron 218676..218834 FT /locus_tag="An04g04100" FT /number=4 FT exon 218835..220381 FT /locus_tag="An04g04100" FT /number=5 FT CDS complement(join(221088..222450,222511..222657, FT 222822..222934,222992..223222,223363..223743)) FT /locus_tag="An04g04110" FT /note="Title: strong similarity to protein PIG-B - Mus FT musculus" FT /db_xref="GOA:A2QIN2" FT /db_xref="InterPro:IPR005599" FT /db_xref="UniProtKB/TrEMBL:A2QIN2" FT /citation=[35] FT /inference="profile:PFAM:PF03901" FT /inference="similar to AA sequence:UniProtKB:D84436.1" FT /protein_id="CAK38676.1" FT /translation="MSGVRRRRRASSTTSFSSPSSLSDSDYIADADATDPDASLLYDSF FT SRSGHLRPSSWSSSFFSSSSSSSSTFLSTPPSSLRIFLFLIAFRLVNALTVRTFFQPDE FT FFQSLEPAWRAAFGDDHAPWITWEWRHQLRSSLHPLLFTAVYATTDLLTRLLRLSPAWQ FT AECLVAAPKVAQAVIAAVGDLFTWRLACRVYDPMSHEAWAALALTIISPWQWFCSTRTL FT SNCLETSLTIVALYMWPWVWFRQCLVLAAVACILRPTNLLIWMVLASLLLYRSTPLRRA FT TLVREALLCGSAVLAVSTTADRFFYGFWTFPPLRFLYFNLAQSLAVFYGKNDWHYYLSQ FT GLPLLLTTALPFAAAGLYHSLTRPRSGGLSELQTSIQVQLASVCLTMIFGLSLISHKEV FT RFIYPLLPSLHVLTAPVLVKFFRPAVTGGSQRHTPRRLTLVFLLLANAVIALYTTVIHA FT SGPAAVLSYLRDQRQIHGSNDMTDTSQPGITAGFLMPCHSTPWRSHLVYPTISAWALSC FT EPPVGLDASEKATYLDEADQFYADPEQFLRTNMIGGLRRFPRRPSYDKYNRKSSQLPTE FT YQSKTPHEWPDYLVFFAQLEPTLRSLLRFSAYKECHRTWNTAWHDDWRRRGDIVVWCVD FT PSEQAARDSLYIQRQRESRDLHFDRIVQTFTKPTHKQRLTRLWKSIFSSKSQSGSWSWA FT WPWQRRKRTTIFGFELPAWPFSRSSRKSSSWTFPAWEELNRRMNDRANWA" FT mRNA complement(join(<221088..222450,222511..222657, FT 222822..222934,222992..223222,223363..>223743)) FT /locus_tag="An04g04110" FT exon complement(221088..222450) FT /locus_tag="An04g04110" FT /number=1 FT intron complement(222451..222510) FT /locus_tag="An04g04110" FT /number=1 FT exon complement(222511..222657) FT /locus_tag="An04g04110" FT /number=2 FT intron complement(222658..222821) FT /locus_tag="An04g04110" FT /number=2 FT exon complement(222822..222934) FT /locus_tag="An04g04110" FT /number=3 FT intron complement(222935..222991) FT /locus_tag="An04g04110" FT /number=3 FT exon complement(222992..223222) FT /locus_tag="An04g04110" FT /number=4 FT intron complement(223223..223362) FT /locus_tag="An04g04110" FT /number=4 FT exon complement(223363..223743) FT /locus_tag="An04g04110" FT /number=5 FT CDS complement(join(224388..224493,224586..224668)) FT /locus_tag="An04g04120" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIN3" FT /protein_id="CAK38677.1" FT /translation="MRGYKRLVWGTRKRDMRAGGEEEEGLRGGEESAAVTGRLLPIWLA FT NTRIVVDRKFARPKLHR" FT mRNA complement(join(<224388..224493,224586..>224668)) FT /locus_tag="An04g04120" FT exon complement(224388..224493) FT /locus_tag="An04g04120" FT /number=1 FT intron complement(224494..224585) FT /locus_tag="An04g04120" FT /number=1 FT exon complement(224586..224668) FT /locus_tag="An04g04120" FT /number=2 FT CDS join(224721..225212,225283..225984,226039..226224) FT /locus_tag="An04g04130" FT /EC_number="2.6.1.13" FT /note="Catalytic activity: L-ornithine + a 2-oxo acid <=> FT L-glutamate 5-semialdehyde + an L-amino acid." FT /note="Cofactor: Pyridoxal-phosphate." FT /note="Title: strong similarity to ornithine-2-oxo-acid FT transaminase YLR438w - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIN4" FT /db_xref="InterPro:IPR015421" FT /db_xref="UniProtKB/TrEMBL:A2QIN4" FT /inference="profile:COGS:COG4992" FT /inference="profile:PFAM:PF00202" FT /inference="similar to AA sequence:PIR:XNBYO" FT /protein_id="CAK38678.1" FT /translation="MASNGTNGTNGHNGVSSYHASTTQEAIQAEKDFAAHNYHPLPIVF FT ARAQGTTVWDPEGRQYLDFLSAYSAVNQGHCHPKLVAALVDQASRLTLSSRAFYNDVFP FT RFAEFVTKYFGFDMVLPMNTGAEAVETGIKIARKWGYKVKGIPENQAVVLSAENNFHGR FT TFAAISLSSDPESRENYGPYLPGIGCTIPGTEKPIAYNDKAALREAFEKAGPNLAAFLV FT EPIQGEAGIVVPDEDYLQEARALCDKHNVLLICDEIQTGIARTGKLLCHEWSGIKPDMV FT LLGKAISGGMYPVSCVLGRKDVMLTIEPGTHGSTYGGNPLACAVAIRALEVVQEENMVE FT RAEKLGHVFRDGLQAIKSPIIQTVRGKGLLNAIVIDESKTNGHSAWDLCMLLKTKGLLA FT KPTHENIIRLAPPLVITDDEVQKALDIIKEAVNELPTLTGAAEDEVIPPPEKKVKVSLE FT N" FT mRNA join(<224721..225212,225283..225984,226039..>226224) FT /locus_tag="An04g04130" FT exon 224721..225212 FT /locus_tag="An04g04130" FT /number=1 FT intron 225213..225282 FT /locus_tag="An04g04130" FT /number=1 FT exon 225283..225984 FT /locus_tag="An04g04130" FT /number=2 FT intron 225985..226038 FT /locus_tag="An04g04130" FT /number=2 FT exon 226039..226224 FT /locus_tag="An04g04130" FT /number=3 FT CDS complement(join(226323..226493,226634..226780)) FT /locus_tag="An04g04140" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIN5" FT /protein_id="CAK38679.1" FT /translation="MAAETGKMRGIKWGAIGGRGTGRKEEGEKRGGGHMHHQQTSRVLF FT NYNHGISLEVAETVCNRITHAWASDHGSTITMSQKPRARTSPLLDTTSHRLWSEQAILR FT C" FT mRNA complement(join(<226323..226493,226634..>226780)) FT /locus_tag="An04g04140" FT exon complement(226323..226493) FT /locus_tag="An04g04140" FT /number=1 FT intron complement(226494..226633) FT /locus_tag="An04g04140" FT /number=1 FT exon complement(226634..226780) FT /locus_tag="An04g04140" FT /number=2 FT CDS complement(join(227405..227616,227709..227855, FT 227936..228415,228492..228687,228750..228932)) FT /locus_tag="An04g04150" FT /EC_number="3.7.1.2" FT /note="Remark: Hereditary tyrosinemia type 1 (HT1) is an FT autosomal recessive disease caused by a deficiency of the FT enzyme involved in the last step of tyrosine FT degradation,fumarylacetoacetate hydrolase (FAH). Thus far, FT 34 mutations in the FAH gene have been reported in various FT HT1 patients." FT /note="Title: strong similarity to fumarylacetoacetase FT -Homo sapiens" FT /db_xref="GOA:A2QIN6" FT /db_xref="InterPro:IPR011234" FT /db_xref="UniProtKB/TrEMBL:A2QIN6" FT /citation=[65] FT /citation=[79] FT /citation=[81] FT /citation=[82] FT /citation=[83] FT /inference="profile:COGS:COG0179" FT /inference="profile:PFAM:PF01557" FT /inference="similar to AA sequence:PIR:A37926" FT /protein_id="CAK38680.1" FT /translation="MTLTETPFTIDNLPYGVISTAETPTPRCATVLEDDVIDLSALEKD FT GYFKSIPGLKGDVFSMPTLNKFASLPKETHVRTRAALVDLLSDNDIRKKYAIPLSTVQN FT HLPMETKNFSDFYCSFEHTRNVPSWFVIPSVYNGRQSSLRISGTPIRRPWGVTLDSNKP FT NDPPAFRPSARFDFELEMGVYLSHPLPPGEILNINNAKDHIFGLVILNDWSARDIQTYE FT MAPLGPFHSKGSGTSISPWIVPIEALEGSQCNARVQDPAPLKHLAWKGKEDEATFDIEL FT KARVIRDGKSYTVTETNLKELYWTPYQQVTHLCSAGEGLSTGDIFGTGTITSDVREEIG FT VACLLERKLERNILSEASKDGLDFLADRDEVIMEGWCVNRLTGGKFGFGECRSVILPAL FT KEGSWE" FT mRNA complement(join(<227405..227616,227709..227855, FT 227936..228415,228492..228687,228750..>228932)) FT /locus_tag="An04g04150" FT exon complement(227405..227616) FT /locus_tag="An04g04150" FT /number=1 FT intron complement(227617..227708) FT /locus_tag="An04g04150" FT /number=1 FT exon complement(227709..227855) FT /locus_tag="An04g04150" FT /number=2 FT intron complement(227856..227935) FT /locus_tag="An04g04150" FT /number=2 FT exon complement(227936..228415) FT /locus_tag="An04g04150" FT /number=3 FT intron complement(228416..228491) FT /locus_tag="An04g04150" FT /number=3 FT exon complement(228492..228687) FT /locus_tag="An04g04150" FT /number=4 FT intron complement(228688..228749) FT /locus_tag="An04g04150" FT /number=4 FT exon complement(228750..228932) FT /locus_tag="An04g04150" FT /number=5 FT CDS join(229353..229457,229504..229650,229697..230230, FT 230364..231053) FT /locus_tag="An04g04160" FT /note="Phenotype: mutations in S. cerevisiae Hol I are FT resposible for nonselective cation/histindiol uptake in S. FT cerevisiae." FT /note="Remark: Hol I is a member of the major facilitator FT superfamily (drug resistance subfamily) of transporters." FT /note="Title: similarity to multidrug resistance protein FT Hol1 - Saccharomyces cerevisiae" FT /db_xref="InterPro:IPR011701" FT /db_xref="UniProtKB/TrEMBL:A2QIN7" FT /citation=[40] FT /inference="profile:COGS:COG0477" FT /protein_id="CAK38681.1" FT /translation="MIDEEKTQEVVHGLKTTPDGLILDPQPSDDPKDPLNWKSSRKARI FT LSIWAIACFSSQATCMTNMQGSYLQAPLYHKTATQISLSVSCGLIGIMVGSILVVPLSR FT RYGSCFCLFWSTIGILFAAVWSAMMTSSSDYIPFLISRLFAGLCAGVPLILGSEFVMRA FT FFRHQRGKCLHILHIPFLMGVSIGPTLGAYIDARASWTVSFWYTVPLNGVLALVILIFL FT EEAIYAEGEQKRQSFLQRKWNMYVRGRAIPPQLRASWKNMTLALRQWLLCSVSTSLKPL FT ETMVDTQCQRFRWPHVLPQYSLLFTLAVNLNTTVTLTQAIGTALAELYGHFISDRLPLY FT LSHRKSKTQDIEPTEWRPEYRLHCLWIPVIMLPVGLGLFGASLEYHYHWVLLALGFLLL FT TFGAISLLPVAMTYLCDCFPNYVSEVSAGMGVWRLILGLLSTVFITPWNDRVGPGWLFG FT SAGLITLPAFGGVMFLMVFGRQVRQMGFRRLRS" FT mRNA join(<229353..229457,229504..229650,229697..230230, FT 230364..>231053) FT /locus_tag="An04g04160" FT exon 229353..229457 FT /locus_tag="An04g04160" FT /number=1 FT intron 229458..229503 FT /locus_tag="An04g04160" FT /number=1 FT exon 229504..229650 FT /locus_tag="An04g04160" FT /number=2 FT intron 229651..229696 FT /locus_tag="An04g04160" FT /number=2 FT exon 229697..230230 FT /locus_tag="An04g04160" FT /number=3 FT intron 230231..230363 FT /locus_tag="An04g04160" FT /number=3 FT exon 230364..231053 FT /locus_tag="An04g04160" FT /number=4 FT CDS complement(join(231433..231753,231806..232131, FT 232199..232309,232357..232492)) FT /locus_tag="An04g04170" FT /EC_number="1.1.1.250" FT /note="Catalytic activity: D-arabinitol + NAD(+) <=> FT D-ribulose + NADH." FT /note="Title: strong similarity to NAD-dependent FT D-arabinitol dehydrogenase ard - Candida tropicalis" FT /db_xref="GOA:A2QIN8" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2QIN8" FT /inference="profile:COGS:COG1028" FT /inference="profile:PFAM:PF00106" FT /inference="similar to AA sequence:PIR:JC4041" FT /protein_id="CAK38682.1" FT /translation="MATRSDCNVHGLEFREAKPSQGDPARPVADLFRLDNRTIISISPE FT ITGATGFLGTTLAIAILESGGDIVCLDLASAPNSPDWNKVEAAAQKHARQLSYYPLDVT FT DESGVEKTFTQFIPTLRYPLKGVVACAGLSRNGPATEFPVSSFRRMLDINVTGTFLVAQ FT AAAREMLRTNTTGSMVFVASMSGYVSNKGVDTAGYNASKAAVHQLTRSLAAEWGSRVGM FT PLIRVNSLSPGYIRTAATAEALQKPGMESQWVGDNMLFRLSTADEFRAPVLFMLGDGSS FT FMTGADLRVDGGHCAW" FT mRNA complement(join(<231433..231753,231806..232131, FT 232199..232309,232357..>232492)) FT /locus_tag="An04g04170" FT exon complement(231433..231753) FT /locus_tag="An04g04170" FT /number=1 FT intron complement(231754..231805) FT /locus_tag="An04g04170" FT /number=1 FT exon complement(231806..232131) FT /locus_tag="An04g04170" FT /number=2 FT intron complement(232132..232198) FT /locus_tag="An04g04170" FT /number=2 FT exon complement(232199..232309) FT /locus_tag="An04g04170" FT /number=3 FT intron complement(232310..232356) FT /locus_tag="An04g04170" FT /number=3 FT exon complement(232357..232492) FT /locus_tag="An04g04170" FT /number=4 FT CDS complement(join(233369..233866,233933..234046, FT 234078..234089)) FT /locus_tag="An04g04180" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIN9" FT /protein_id="CAK38683.1" FT /translation="MPPRLITNSGSYSHQRSYKKRYEADQTDRPKQRIENMTMAEAGRE FT LQRLTRNIMLAKRNIKRWESEHEELIARFYNSEGKIVVPPAVDEKTSVTSVQGESTGED FT CSLKGATNEHGQTPHVSENDEVLGEGNMDLDEDAQCEKSSDIRGDADGRLQEVATTATA FT GCDDQLLPDAGDVGFLEDLMDSTDEPKGEEDCLKTALGSLTINV" FT mRNA complement(join(<233369..233866,233933..234046, FT 234078..>234089)) FT /locus_tag="An04g04180" FT exon complement(233369..233866) FT /locus_tag="An04g04180" FT /number=1 FT intron complement(233867..233932) FT /locus_tag="An04g04180" FT /number=1 FT exon complement(233933..234046) FT /locus_tag="An04g04180" FT /number=2 FT intron complement(234047..234077) FT /locus_tag="An04g04180" FT /number=2 FT exon complement(234078..234089) FT /locus_tag="An04g04180" FT /number=3 FT CDS join(234598..234684,234912..235034,235125..235178, FT 235299..235358,235491..235727) FT /locus_tag="An04g04190" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIP0" FT /protein_id="CAK38684.1" FT /translation="MRFTTGCSSGTDVHLSTSSRRSRESEIAPSVDIPDRSGSSDEFIT FT VPIIGCDLYFSQRYGSAKALRIADKCVLGEVDLYPTHRSFFPQAICQPTLETAIYALLV FT ALYTEQGDADMRRLVKLKDKVEACDICRHHRMPKPWSPDLFVLFLYTDFRESCFMLPRE FT LQLEDPTAVLLAQPTAKKPTYYD" FT mRNA join(<234598..234684,234912..235034,235125..235178, FT 235299..235358,235491..>235727) FT /locus_tag="An04g04190" FT exon 234598..234684 FT /locus_tag="An04g04190" FT /number=1 FT intron 234685..234911 FT /locus_tag="An04g04190" FT /number=1 FT exon 234912..235034 FT /locus_tag="An04g04190" FT /number=2 FT intron 235035..235124 FT /locus_tag="An04g04190" FT /number=2 FT exon 235125..235178 FT /locus_tag="An04g04190" FT /number=3 FT intron 235179..235298 FT /locus_tag="An04g04190" FT /number=3 FT exon 235299..235358 FT /locus_tag="An04g04190" FT /number=4 FT intron 235359..235490 FT /locus_tag="An04g04190" FT /number=4 FT exon 235491..235727 FT /locus_tag="An04g04190" FT /number=5 FT CDS complement(join(236083..236212,236307..236525, FT 236864..236995,237081..237258,237341..237432, FT 237483..237842,238274..238354,238448..238474, FT 238668..238761,238845..238962)) FT /locus_tag="An04g04200" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIP1" FT /protein_id="CAK38685.1" FT /translation="MGDARWFWLRCLGFCLWRITATTTLTTAAGSSPLRNQPPYYRPWN FT ESRVCRPHHGPLPPSDHQSYFDATGMSWVAAHFSGAISSLVYTPSPSPFVYLFLARQAV FT SIARLLAGSGNSPRLGLSTRASAPPAPRSSARISVKLFNSLVRWSSVSVSPGSGSSPFV FT PLVFCVRHCLAEISPILLTLLATSRVPRIGVCGTRRQFLVHGVAYGSVLTDRLCRHQLV FT ETCSKEIGMFSVPASRPGILAREISSYLPHVAWIDGQSGNDVAGLAWPFTTPVILARAG FT AAQWSDLFFVSRASCRHGSSHALILRGTTGSGGCLPTHFAPLLLRLYPHRGSHTNSITR FT GRESMLSLSLARSPGSPKIDNQIFSLYYPTTGYITAGRLEKASAKIILELQISCSPAPP FT GGDCFGGKSSIIRSVGCGREGRWWTSWWDCPRGYRAVWIQGPSYYSDGLGPSTTLLTPS FT HLCFVPTVDPICACIDPA" FT mRNA complement(join(<236083..236212,236307..236525, FT 236864..236995,237081..237258,237341..237432, FT 237483..237842,238274..238354,238448..238474, FT 238668..238761,238845..>238962)) FT /locus_tag="An04g04200" FT exon complement(236083..236212) FT /locus_tag="An04g04200" FT /number=1 FT mat_peptide complement(join(236086..236212,236307..236525, FT 236864..236995,237081..237258,237341..237432, FT 237483..237842,238274..238354,238448..238474, FT 238668..238761,238845..238878)) FT /locus_tag="An04g04200" FT /product="hypothetical protein" FT intron complement(236213..236306) FT /locus_tag="An04g04200" FT /number=1 FT exon complement(236307..236525) FT /locus_tag="An04g04200" FT /number=2 FT intron complement(236526..236863) FT /locus_tag="An04g04200" FT /number=2 FT exon complement(236864..236995) FT /locus_tag="An04g04200" FT /number=3 FT intron complement(236996..237080) FT /locus_tag="An04g04200" FT /number=3 FT exon complement(237081..237258) FT /locus_tag="An04g04200" FT /number=4 FT intron complement(237259..237340) FT /locus_tag="An04g04200" FT /number=4 FT exon complement(237341..237432) FT /locus_tag="An04g04200" FT /number=5 FT intron complement(237433..237482) FT /locus_tag="An04g04200" FT /number=5 FT exon complement(237483..237842) FT /locus_tag="An04g04200" FT /number=6 FT intron complement(237843..238273) FT /locus_tag="An04g04200" FT /number=6 FT exon complement(238274..238354) FT /locus_tag="An04g04200" FT /number=7 FT intron complement(238355..238447) FT /locus_tag="An04g04200" FT /number=7 FT exon complement(238448..238474) FT /locus_tag="An04g04200" FT /number=8 FT intron complement(238475..238667) FT /locus_tag="An04g04200" FT /number=8 FT exon complement(238668..238761) FT /locus_tag="An04g04200" FT /number=9 FT intron complement(238762..238844) FT /locus_tag="An04g04200" FT /number=9 FT exon complement(238845..238962) FT /locus_tag="An04g04200" FT /number=10 FT sig_peptide complement(238879..238962) FT /locus_tag="An04g04200" FT /inference="protein motif:SignalP:2.0" FT exon 239518..240681 FT /locus_tag="An04g04210" FT /number=1 FT CDS 239518..240681 FT /locus_tag="An04g04210" FT /EC_number="2.1.1.41" FT /note="Catalytic activity: S-adenosyl-L-methionine + FT 5-alpha-cholest-8,24-dien-3-beta-ol <=> FT S-adenosyl-L-homocysteine + FT 24-methylene-5-alpha-cholest-8-en-3-beta-ol." FT /note="Cofactor: Glutathione." FT /note="Title: strong similarity to FT S-adenosyl-L-methionine:delta24-sterol-C-methyltransferase FT - Glycine max" FT /db_xref="GOA:A2QIP2" FT /db_xref="InterPro:IPR013216" FT /db_xref="UniProtKB/TrEMBL:A2QIP2" FT /inference="profile:COGS:COG2230" FT /inference="similar to AA sequence:PIR:T06780" FT /protein_id="CAK38686.1" FT /translation="MDTQTTVLASRQSGRSSESSSLDAVEKQKLANKELPQTRPDLHNS FT ASPKRWKTFWKAFRYLNNLTPKQVDDFMASYVIYNLDWSDEKAMIETLGPDYQAKVGDC FT LKAYYGVLNHLCALGDVEKMYIPPFMSKKATVLENQLLYEESIAQDIGLSAGDHVLDLG FT CGRGRVAAHMTQYSGAKVTGLNIDPNQIGQAKTYNEKLGFTNNSFVVQDFNSLPLPFED FT ASFDAFYQIQALSLCKDLPSLFREIYRVVKPGAKISLLDWVSLPDYDPSNPEHAELMRR FT VKPLIGAVGTPTPESLEKALTDAGFSVVRSDNASVGGLQAPLIDKVDFYFRSMRQVILG FT LVKTHVLPRHFKTLINRLCLDGEAFIKMDTMRLVTTSYRIIAQKPPQ" FT mRNA <239518..>240681 FT /locus_tag="An04g04210" FT CDS complement(join(240935..241081,241159..241284, FT 241375..241471,241570..241661)) FT /locus_tag="An04g04220" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIP3" FT /protein_id="CAK38687.1" FT /translation="MNAGQKPMACMKAEACCRIVWPWHPRQPAVMRMWVHWLPLTIIAE FT EKVVLVYVLLYGQPYLHGEDATQLTRKNASERALVTKNCRGALPWGRKMGMIRKAARDY FT RMNALYSEDQRAVLGHKQALTLWTETRRGHRTGKDAAIKSTRRTHMCPS" FT mRNA complement(join(<240935..241081,241159..241284, FT 241375..241471,241570..>241661)) FT /locus_tag="An04g04220" FT exon complement(240935..241081) FT /locus_tag="An04g04220" FT /number=1 FT intron complement(241082..241158) FT /locus_tag="An04g04220" FT /number=1 FT exon complement(241159..241284) FT /locus_tag="An04g04220" FT /number=2 FT intron complement(241285..241374) FT /locus_tag="An04g04220" FT /number=2 FT exon complement(241375..241471) FT /locus_tag="An04g04220" FT /number=3 FT intron complement(241472..241569) FT /locus_tag="An04g04220" FT /number=3 FT exon complement(241570..241661) FT /locus_tag="An04g04220" FT /number=4 FT CDS join(242362..242603,242659..242792,242872..243003, FT 243059..243385,243550..243716) FT /locus_tag="An04g04230" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIP4" FT /protein_id="CAK38688.1" FT /translation="MSHPAAHSEAEDWPLPLSVSRPDSIVSSSTSSSGPSYATSPIFPP FT PLSRTASSIGSRSRQASCFSLYEDICRLPLNHSVTISFVRSSKLFKLRFTCIDIRKDAT FT GSLKSLELGGGPGQQTPLIHTFPHLEHPKLPNESSLRVSFMDEQTVQSAHNVFLTQISY FT IFEDWHDCVQFQELVLGSKLVFIAGIAEAKSKGRGEECISQNLRILRNHNGKQVMLFFA FT NSQRKELKRYVSIPINCIDSFNPGKKAGKPVVLQLQPNFDILSQMRTLSIQFLDELAST FT NITSWILVVYESAARSLDGVGYSGTLHKFSFHFFLAPLRPRVSFSSNNIPLL" FT mRNA join(<242362..242603,242659..242792,242872..243003, FT 243059..243385,243550..>243716) FT /locus_tag="An04g04230" FT exon 242362..242603 FT /locus_tag="An04g04230" FT /number=1 FT intron 242604..242658 FT /locus_tag="An04g04230" FT /number=1 FT exon 242659..242792 FT /locus_tag="An04g04230" FT /number=2 FT intron 242793..242871 FT /locus_tag="An04g04230" FT /number=2 FT exon 242872..243003 FT /locus_tag="An04g04230" FT /number=3 FT intron 243004..243058 FT /locus_tag="An04g04230" FT /number=3 FT exon 243059..243385 FT /locus_tag="An04g04230" FT /number=4 FT intron 243386..243549 FT /locus_tag="An04g04230" FT /number=4 FT exon 243550..243716 FT /locus_tag="An04g04230" FT /number=5 FT CDS join(244380..244442,244508..245852,245913..246301) FT /locus_tag="An04g04240" FT /note="Title: strong similarity to phosphate transport FT protein GvPT - Glomus versiforme" FT /db_xref="GOA:A2QIP5" FT /db_xref="InterPro:IPR005828" FT /db_xref="UniProtKB/TrEMBL:A2QIP5" FT /inference="profile:COGS:COG0477" FT /inference="profile:PFAM:PF00083" FT /inference="similar to AA sequence:PIR:S67491" FT /protein_id="CAK38689.1" FT /translation="MGKFRTRWYKTDRAQDFEHEQDRDVRARQVYDTIDRQGFQYLIVF FT VAGVGFFLDGYTLFASNMALPMISYVYWKKEVSSIKITLFNIATLGGTLLGQVLFGYLA FT DRNGRKKMYGLELILMITSTLGVVMASRGENDSMSIYAWLIWWRIVVGIGVGADYPLSS FT VITSEFAPTKHRARMMASVFFMQPLGQIWANLVSLIVIATSRSDTNDLTMSVDRMWRYV FT IGIGVIPAAIATCFRFFVPESPRFLMEIDDDPVKVEFDATALFTEPNAVSSSPTLETES FT WHNFPGQAYSLTTITAEDRSSTSQTGILQPATLNSHWRLTWKDIVQYFWVEGNWRTLAG FT TAMSWFFLDFGFYGISLSSPQFLAKTWGSIHLSAPAPYWETNDSPGASVYDMFFASCTH FT ALVILNVGSFAGGLLLILVIHKLDRVALQKYSFLALSALFIALGCMLITIQKEGPVAVV FT LYVIGQALFNFGPNATTYIIPAEIFPTRYRATCHGLSAGAGKIGSIVVQVFSAYYNFGG FT GFGEEPVKRHGYIMIVFAGCMLFGAIVTCWIPPIQRKPDGSGRGKLWGGKTETLETLAL FT GRLGLDSRYANQGRRRRRDVVT" FT mRNA join(<244380..244442,244508..245852,245913..>246301) FT /locus_tag="An04g04240" FT exon 244380..244442 FT /locus_tag="An04g04240" FT /number=1 FT intron 244443..244507 FT /locus_tag="An04g04240" FT /number=1 FT exon 244508..245852 FT /locus_tag="An04g04240" FT /number=2 FT intron 245853..245912 FT /locus_tag="An04g04240" FT /number=2 FT exon 245913..246301 FT /locus_tag="An04g04240" FT /number=3 FT tRNA complement(246710..246780) FT /gene="tRNA-Gly (GCC)" FT /locus_tag="An04e04250" FT /product="transfer RNA-Gly (GCC)" FT /inference="profile:tRNAscan:1.4" FT CDS join(247285..247509,247672..247715,247826..247967) FT /locus_tag="An04g04260" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIP6" FT /protein_id="CAK38690.1" FT /translation="MGRSASALPHHYVEWFTLEALKSTMIDNSAPLDDSSPLVDSTWSS FT IMSIEEKLIGRLSRATQAITIPPADAPFGGWLAEWAGQDIHLGGYGRFAHGCSLHAYHT FT GKCSVGSCGSYARVVGCDGLILEETISVGSFG" FT mRNA join(<247285..247509,247672..247715,247826..>247967) FT /locus_tag="An04g04260" FT exon 247285..247509 FT /locus_tag="An04g04260" FT /number=1 FT intron 247510..247671 FT /locus_tag="An04g04260" FT /number=1 FT exon 247672..247715 FT /locus_tag="An04g04260" FT /number=2 FT intron 247716..247825 FT /locus_tag="An04g04260" FT /number=2 FT exon 247826..247967 FT /locus_tag="An04g04260" FT /number=3 FT CDS join(248840..249449,249502..250739) FT /locus_tag="An04g04270" FT /note="Title: similarity to hypothetical protein mlr1435 FT -Mesorhizobium loti" FT /db_xref="InterPro:IPR013027" FT /db_xref="UniProtKB/TrEMBL:A2QIP7" FT /inference="profile:COGS:COG2072" FT /protein_id="CAK38691.1" FT /translation="MPSEDVSTGSVNVPIGTFPQTCSSTDVNADQVASQLVEKINTALS FT KGDVQSLSDLFLEDAYWRDHLCLTWDFYTAKGRENIQSFLKSGRLPSKVEIDRSTAFRG FT PYVGPIDAFGDVTGILFYITLSSPLITGQGIVRLAEKDGEWKIFTFYTSMESFVDHPEA FT VNFRRPLGAQHGESLDRKNWKDRRTAEIEAKDRSPTVVVVGAGQSGLIIAARLKMLNID FT VLIIDREENIGDNWRQRYHQLVLHDPVWFDHFPYIPFPPNWPIFTPKDKIAEWFDCYAK FT LLELNVWTKTNIKGSSWDDKEKQWTLDLQRRKEDGTVENRTLNPRYIIQATGHSGKKNV FT PDFKGMDSFQGDLICHSSEFRGAKPGSKGKKAVVVGACNSANDIAQDYYENGYDVTMVQ FT RSSTCVVSSESIVEIGLKGLYEEAGPGTEEADLYLWSIPAELFKAQQIKVTKRQNENDR FT ATLEGLARAGFKVDHGPDGAGLLIKYLQRGGGYYIDVGASQLIIDGKVKVKQGQEITEV FT LPHGLRFADGSELQADEIILATGYQNMATQAQLVFGKEGAKVKDVWGFDETGEMRMWRR FT TGHPGLWFMGGNLAVCRYFSRLLALQIKALELGVTSYDG" FT mRNA join(<248840..249449,249502..>250739) FT /locus_tag="An04g04270" FT exon 248840..249449 FT /locus_tag="An04g04270" FT /number=1 FT intron 249450..249501 FT /locus_tag="An04g04270" FT /number=1 FT exon 249502..250739 FT /locus_tag="An04g04270" FT /number=2 FT CDS join(254250..254328,254387..254853) FT /locus_tag="An04g04280" FT /note="Remark: there is homology to a 5' EST an_3603 from FT A. niger." FT /note="Title: similarity to hypothetical protein FT SPBC800.14c - Schizosaccharomyces pombe" FT /db_xref="InterPro:IPR013901" FT /db_xref="UniProtKB/TrEMBL:A2QIP8" FT /inference="similar to AA sequence:UniProtKB:SPBC800.10" FT /protein_id="CAK38692.1" FT /translation="MYTTDTLPTSFCIAQAIGLSGAAWLSGNIFSLSLMTVPALLQSHR FT EHNIPLSTIAKQWAVVYETGKNRAPPIALFTATTLLYLSWATRAESTLAAIAPRGATTT FT YAISAALTIAIVPWTILAMKGTNNALMEKAKVGVQEEKDPQEGERVLGLLNRWALLNGA FT RAVWPLAGFLVGLSAVVP" FT mRNA join(<254250..254328,254387..>254853) FT /locus_tag="An04g04280" FT exon 254250..254328 FT /locus_tag="An04g04280" FT /number=1 FT sig_peptide 254250..254315 FT /locus_tag="An04g04280" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(254316..254328,254387..254850) FT /locus_tag="An04g04280" FT intron 254329..254386 FT /locus_tag="An04g04280" FT /number=1 FT exon 254387..254853 FT /locus_tag="An04g04280" FT /number=2 FT CDS join(255072..255304,255823..256129,256191..256457, FT 256841..257117,257156..257556) FT /locus_tag="An04g04290" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIP9" FT /protein_id="CAK38693.1" FT /translation="MNTPESSRPGRYRSGFLDIIEYRTVNFRETCKGSGNYHPTIGNRM FT MLAPPVPTGIICFQQGKNIHIHNFESHSICNSIPELRNLRWLLDSTTSTAPSVIMMDSP FT VVASYRHMNIVYRSLEVYIHQYSIPHNNLLHREKVATHAGLDIFWIFGDTCGTKSYAMD FT SWLSPTNLPTPIAWFGEGAYLPPQRLKMLAELRLFGAICEKEIVKSFRIKKDRRGLPAL FT DATKGAWIGLQMMESFFMTPPYQARGAADKLRLDMRTDKCPCFCCLTQILYDSEDHWQS FT RAPLHPPCHRHYYYSPNILESPRDLKYIGEQDIIDISMPHARQDARGVYIRISGIETDC FT YNWESLLFNSWTLTSLFYDRSDIQIISTPRQKASNACGLASRGTGPVGKKQIKRDEQGL FT CSQDWRRQSIFGSRYQKQVLCSRAPRAVYQRLADFALQKPYIKLWVIPPFMRSLWLMQS FT GHSSKKQATKEWMFAKRDSNEAKLSELETNEAYYKD" FT mRNA join(<255072..255304,255823..256129,256191..256457, FT 256841..257117,257156..>257556) FT /locus_tag="An04g04290" FT exon 255072..255304 FT /locus_tag="An04g04290" FT /number=1 FT intron 255305..255822 FT /locus_tag="An04g04290" FT /number=1 FT exon 255823..256129 FT /locus_tag="An04g04290" FT /number=2 FT intron 256130..256190 FT /locus_tag="An04g04290" FT /number=2 FT exon 256191..256457 FT /locus_tag="An04g04290" FT /number=3 FT intron 256458..256840 FT /locus_tag="An04g04290" FT /number=3 FT exon 256841..257117 FT /locus_tag="An04g04290" FT /number=4 FT intron 257118..257155 FT /locus_tag="An04g04290" FT /number=4 FT exon 257156..257556 FT /locus_tag="An04g04290" FT /number=5 FT CDS complement(join(258890..259034,259071..259254, FT 259332..259380)) FT /locus_tag="An04g04300" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIQ0" FT /protein_id="CAK38694.1" FT /translation="MCPIICHLLPATIDPQTKKSMPQFVAYATALYFSSGGEHALGNLL FT LIASTRTNDCTLSRSHISTLGHSLISSQWMYSNSRMLTSSTSCTENPAVLGSIFIHITI FT KLVQSITHRRHNAGQSCVHAA" FT mRNA complement(join(<258890..259034,259071..259254, FT 259332..>259380)) FT /locus_tag="An04g04300" FT exon complement(258890..259034) FT /locus_tag="An04g04300" FT /number=1 FT intron complement(259035..259070) FT /locus_tag="An04g04300" FT /number=1 FT exon complement(259071..259254) FT /locus_tag="An04g04300" FT /number=2 FT intron complement(259255..259331) FT /locus_tag="An04g04300" FT /number=2 FT exon complement(259332..259380) FT /locus_tag="An04g04300" FT /number=3 FT CDS join(260625..260726,260798..260854,260972..261004, FT 261074..261305,261649..261720,262906..263147, FT 263459..263593,263668..263748) FT /locus_tag="An04g04310" FT /product="hypothetical protein" FT /note="Remark: the ORF has an unusual exon/intron structure FT for A. niger." FT /db_xref="UniProtKB/TrEMBL:A2QIQ1" FT /protein_id="CAK38695.1" FT /translation="MGTDSALARGNWEAEKDAGVLIAEASPTLAIASLDGAWESAWLDG FT LLAGLVDLDTVASNASASEMSWATGLLGAGFDGAVGILNGYSSAILSEELQMRGLGVVG FT GSEESGFSRMCGVPGTSLSAWRSSISIRWRGRAFWSGIEFKRQLLAAQKIQPPDCQCPS FT EAGGDRGTKDSNSLRLPIPRENLDLRVIAVAKTYGLNSPRAVIGITYVGGIGLSDRYSN FT LRFALADAYKLARGGDKWHPIKCKQEQQDASKLDTTPSFTDNPESQITADINKSEPACD FT SQPTTTEPREERMFMSFDTPCSLSVKRHEDPEEEAL" FT mRNA join(<260625..260726,260798..260854,260972..261004, FT 261074..261305,261649..261720,262906..263147, FT 263459..263593,263668..>263748) FT /locus_tag="An04g04310" FT exon 260625..260726 FT /locus_tag="An04g04310" FT /number=1 FT intron 260727..260797 FT /locus_tag="An04g04310" FT /number=1 FT exon 260798..260854 FT /locus_tag="An04g04310" FT /number=2 FT intron 260855..260971 FT /locus_tag="An04g04310" FT /number=2 FT exon 260972..261004 FT /locus_tag="An04g04310" FT /number=3 FT intron 261005..261073 FT /locus_tag="An04g04310" FT /number=3 FT exon 261074..261305 FT /locus_tag="An04g04310" FT /number=4 FT intron 261306..261648 FT /locus_tag="An04g04310" FT /number=4 FT exon 261649..261720 FT /locus_tag="An04g04310" FT /number=5 FT intron 261721..262905 FT /locus_tag="An04g04310" FT /number=5 FT exon 262906..263147 FT /locus_tag="An04g04310" FT /number=6 FT intron 263148..263458 FT /locus_tag="An04g04310" FT /number=6 FT exon 263459..263593 FT /locus_tag="An04g04310" FT /number=7 FT intron 263594..263667 FT /locus_tag="An04g04310" FT /number=7 FT exon 263668..263748 FT /locus_tag="An04g04310" FT /number=8 FT CDS join(264593..265093,265166..266921,266987..267498, FT 267564..269015) FT /locus_tag="An04g04320" FT /note="Title: strong similarity to hypothetical protein FT encoded by An04g03250 - Aspergillus niger" FT /db_xref="InterPro:IPR018208" FT /db_xref="UniProtKB/TrEMBL:A2QIQ2" FT /protein_id="CAK38696.1" FT /translation="MAIFSKFKRKKAFPLEQSVGKDQTKETPPYATVAEQPRSTLPAPV FT SEKQEQPKPFQSQSPARSPQPNGHPTHEVEVPTSNASNVVAKPTDMPVDDEYAQAWLDA FT HNMVKELAKQRGQPIDGSLGIADVLKNLNEAPSSRKDKIWNGFQHVLGAIQKIGGAAAS FT VASKVFAPATDCYNVVNFVIDTFKGYQGAYDALDSLFDQCADYLTRLGYYEGRMDKNLR FT ALCAQSLKLFIEVCRKAVALRGSVAGKLKVFTRVMFLSDNGISSLLNEMDKLTNKEKLL FT VLAQTFKNAHDGYRATLRVEGLVSERHALDMEANREKVIIKALGLACEPTPTWRSRYRE FT YLNQRLPDTGQWILREPVFANWEKGQSQANILAIEGGSGSGKSFLASAIIHHLLHKKSA FT NETDPRASTAYYFFEGTAREAVKNAMNLETSAKSIVWQFTQMERLYKKSVARICEERRE FT LDPANISSELLFENSDLHEMNVQFYIVIDGLTGQMGEGMLRFLKRASALKSGRRVRVLL FT TVDAQCFQHLAKMEDISFDSIPISPKNRPDVENVIRWRMDSMPAFKDATRPRISQLRTK FT VCNELYQATQGDYFRINLALDDISKREYESDIENALTNARKGRITQVRSEIEGLNKHCS FT ETEILEINEIGLWIRRYREPLTVKAMTAALYVKGGKLSLLTLPDKIKHKYTLFKIIKGE FT IDFRADEVDEAIPSKCRSQSKAEEEEDEQLQGAGTVSPGEMPWSNISSPRSVHRRRTTN FT DPNIEEAKMALTCLRLLTEEVGQPSDLVSYARSNLAEHMSAVNLALVQVDYKTTFGPYL FT VKLFTVDSSIDTLLNNNGLSGPSPSQRREVRQLLFNNATTDIILQWLNDEAVILNVNNE FT ARGWITGPIRNEGRRALLMPAAMRMARHLVHEPHFVPFIRHAFEFLEGFLNKFENPSEQ FT EKLDSISRIASVERWCEKVLKGPKDALWHTQIGSLLNSHGHKELAEARARQALALNAAD FT WRASTLLAEVVEGSRGIETLKPAIERLASSDEWKQNALVRLGLAKMLFITAELSWKEGQ FT ADTAISYWSRAVDVDFTDNVRVIRCLKSYANGERWGEFIAVLRKMDERSTEQQQGTSEL FT IAARSFPHDMFLQAALHTSELAFAVGAYERSIQLIEERGERATLSLLRYRFGRAINAQQ FT NGSSRAIKQWRQALDGADSYTMSTLISCIAPYYVQQAMAAGPDTEAVSAYLEKIETLLP FT EGVPEAEVILPPRVYIARYYKKQGNLSEAKRIARHVVQLSLEILSDDDEGNDLPAYNQL FT LSIFIAFGDIKNALATRALIAVHFMEQQIDCDGDCNRSMNIAEEMKWCQDCILVHLDEE FT CRRKVEQNRLPYSTCNASHELLRAPRMEESLRNMPKDSVPFGDDWVSFTDWLGLIEKDY FT VSFE" FT mRNA join(<264593..265093,265166..266921,266987..267498, FT 267564..>269015) FT /locus_tag="An04g04320" FT exon 264593..265093 FT /locus_tag="An04g04320" FT /number=1 FT intron 265094..265165 FT /locus_tag="An04g04320" FT /number=1 FT exon 265166..266921 FT /locus_tag="An04g04320" FT /number=2 FT intron 266922..266986 FT /locus_tag="An04g04320" FT /number=2 FT exon 266987..267498 FT /locus_tag="An04g04320" FT /number=3 FT intron 267499..267563 FT /locus_tag="An04g04320" FT /number=3 FT exon 267564..269015 FT /locus_tag="An04g04320" FT /number=4 FT CDS complement(join(270281..270659,270739..271856, FT 271921..272133)) FT /locus_tag="An04g04330" FT /EC_number="6.2.1.12" FT /note="Catalytic activity: ATP + 4-coumarate + CoA = AMP + FT pyrophosphate + 4-coumaroyl-CoA." FT /note="Pathway: flavonoids, stilbene and lignin FT biosynthesis." FT /note="Remark: In soybean, 4CL isoenzymes possessing FT different substrate affinities for substituted cinnamic FT acids, and showing differential regulation to environmental FT stress, may play a pivotal role in distributing substituted FT cinnamate intermediates at a branch point of general FT phenylpropanoid metabolism into subsequent specific FT pathways." FT /note="Title: strong similarity to 4-coumarate-CoA ligase 4 FT 4CL4 - Glycine max" FT /db_xref="GOA:A2QIQ3" FT /db_xref="InterPro:IPR000873" FT /db_xref="UniProtKB/TrEMBL:A2QIQ3" FT /citation=[25] FT /inference="profile:COGS:COG0318" FT /inference="profile:COGS:COG0365" FT /inference="profile:PFAM:PF00501" FT /inference="similar to AA sequence:UniProtKB:GM4CL16.1" FT /protein_id="CAK38697.1" FT /translation="MESSHSHDVVTFSLDAQIEYDPCKPLFIDPQEPCRFLNATQFRFL FT VHTLIAGLKAHGLDRGDCVLLHTGNNVLYTALFLAIIGAGGVYMGSNPHSQLQELNHTV FT SLTHPKWIITEPEGSSTVLTIANKHNLPDDHVLLLDDATITETIRFVHDPSIPPPQNTD FT KPNLLTLLSHGTSAPLAIPDAATAASTPAALYSTSGTTGLPKAAVLSHASLMAQHTSIA FT HSPPYPVTRLISLPIFHLFSSLWTHLFPIRYGEPLYLLREFQLPVFLSTVHQYQITETY FT LVPAMVHMLNQAPATLDVKTRLSSLRYIGVAGAPIDRDSMSAFQDMLHPDACAGQVWGM FT TECGVVFQQCYPANGRSGQGDLGSIGTVTAGCEARLVSGAEVVKDDEVPGQLYVRGAGL FT FTGYLGRNESMVDAEGWFDTGDVAYVKNGEYFIVGRTKELIKVRGYQVCPAEIEAVLLQ FT HPLIADVAVIGTCLSDGSSEAPRAYVVRARAPGARVSSDEVYDFARQRLAAYKALDGGV FT FFVDRIPRTVSGKIQRGKLASMNERRDALAGLLARFKAKDVGGLKGRASVVV" FT mRNA complement(join(<270281..270659,270739..271856, FT 271921..>272133)) FT /locus_tag="An04g04330" FT exon complement(270281..270659) FT /locus_tag="An04g04330" FT /number=1 FT intron complement(270660..270738) FT /locus_tag="An04g04330" FT /number=1 FT exon complement(270739..271856) FT /locus_tag="An04g04330" FT /number=2 FT intron complement(271857..271920) FT /locus_tag="An04g04330" FT /number=2 FT exon complement(271921..272133) FT /locus_tag="An04g04330" FT /number=3 FT CDS complement(join(272422..273370,273423..279865)) FT /locus_tag="An04g04340" FT /EC_number="2.1.1.-" FT /note="Function: polyketide synthases catalyze the assembly FT of complex natural products from simple precursors such as FT propionyl-CoA and methylmalonyl-CoA in a biosynthetic FT process that closely parallels fatty acid biosynthesis." FT /note="Remark: the lovF gene encodes an enzyme that is FT responsible for the biosynthesis of the FT (2R)-2-methylbutyryl side chain of lovastatin." FT /note="Title: strong similarity to nonaketide synthase lovB FT - Aspergillus terreus" FT /db_xref="GOA:A2QIQ4" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2QIQ4" FT /citation=[61] FT /citation=[87] FT /inference="profile:COGS:COG3321" FT /inference="profile:PFAM:PF00109" FT /inference="profile:PFAM:PF00698" FT /inference="profile:PFAM:PF02801" FT /inference="similar to AA sequence:UniProtKB:AF151722.1" FT /protein_id="CAK38698.1" FT /translation="MTRTEPIAIIGTGCRFPGSATSPSRLWELLSNPRDVASKPPSERF FT NADAFYQAGKARPGMTNAPESYFLQQDVRTFDAPFFKISPAEAASMDPQQRLLMEVVYE FT SLERAGLPLQRLQGSSTGVYCGSMNNDYGQLLGADTDCLRPFSLTGGATSILANRLSYF FT FDWRGPSFVLDTACSSSLIALHLAVEALRNDDCSLAVVAGSNLILSPDPYIGESQAHML FT SPTGRSYMWDVRADGYARGEGVAALVLKRLQDAVADGDPIECVVRSTGVNSDGRTEALT FT MPNGEAQRDLIRSTYARAGLNPLRREDRCQFFEAHGTGTQAGDPQEAFGISAAFFNDDS FT PSDDILYVGSIKSVLGHAEGAAGIAGVIKASLAIQRGAIPPNLLFNELSPKVAPYASHL FT RIPTQALPWPDLPSGTPRRVSVNSFGFGGANAHVILESFSGAASSSSHCQTAVPAILPF FT VFSAASEVSLTAVLRQYIDYLEYHPTVNLLELAASLLGKRSSLSHRLVLTADSLENLQE FT ALKGEVQRRSTDTSSTVTRRLTPEPKRILGVFTGQGAQWPQMGLDVISQCPQALAWLQE FT LQEALDTLPTEYRPDFTLLDELSAPEATSRLNSAAVSLPLRTALQIIQVNILRSLGIEF FT AAVVGHSSGEIAAAYAAGRLTLKDAIRIAYLRGVAAQHAGSQGKSGAMVALSVPWEQAD FT AIRSEASYSGTIAVAAFNSPISVTFSGDSDLITELEWVTESLGYSPRRLRVDTAYHSHH FT MIPCAEPYVQSMRQCQVQTRQGSSDTKWFSSVFEDKIMEELDIQYWSDNMLRPVLFAQA FT LTAAINHLPGLDAIIEVGPHAALQGPTMQTLSAIKPDEADVPYVGMSNRKSGGIEALAL FT AVGSFWANLGAETLDVPSYIRLFSPSLEVSYIPDLPSYPFDHNQKHWAVSRLAAARISR FT RLPIHPLLGALTPETGEAEWRWRNFLRVQDLDWMDGHQVQSQVVFPATGYLVMALEAAR FT IIADQRPLQLVEIRDLTIDRAITVPDNASGVEMLFTFYRTDNDNHKFTGAFTCQSSHDN FT DAFRGCASGRLEVTFGESDATLLPSLGPTASGLRSVDSGEFYQKLDVLGYGYSGIFRTL FT HDIRRRKDIAFARIPALDVGSELLIHPATLDTGLQVMMAAMGDPNDGQLSGLYLPTRIA FT STTINPSFYRVASPSPYEVVATLSWADFSGTRGDIDIFNHQGHGVVQIEGVEIAALARP FT NVDDVRSFGEQAWGPLLPNAALLSPPDLPNCYLELNHLALLYLRDTQQQLVTEDRQQLD FT WHRGRYVAWMDRLLARVRAGDHPIYPPQWLEGEYTWSLPEDWKEVVKYHLAALEAGGPK FT LIEWLRGQASIMEELRRDDLLTRFYQDRAFRAMTRGLADVVGQLAFRYPRMKILEVGAG FT TGSATREVLDRIGRDYHSYTYTDISAAFFEEAQSMFVADKDRFIYQVLDLERDPTEQGF FT PEHEYDLIVASNVLHATRSLSKTMTHLRRLLKPGGRAIVLEIAEPEDVAVSTIFGAFEG FT WWLGENDSRPWGPIVSSDTWDQVLQNSGFGGFETLSPRAVIDKTGLMVFSAQAVDDRIA FT KLQRPLSVPATEQYPDLVIVGGVSARTEHLVAKVRNRVAPYFARVSHVVTLEAFVPPPD FT ALLMAVLVLSDMDTPCLQDISVERLHGMQELFRKTGKLLWTATGKPGENPYQVMTKGIL FT RNLASEIPHALIQHLTISEPCADDSETLATALMRLVHTDFYNDYSLADGTENPEWELRL FT ENGIMMIPRLLASRTINRRLFTSRGFFNKESVEPQLVPVKVVPDKAGLTLASLPERIPS FT NQTDLENGKDIISIQVHYATLYAVYVESVGFLHLVLGRDRKTRTRIAALSVNHGSVVST FT PASWSLDVPSWLPEEHEAAFLSGVTTAIVSRYLVNKTPSNTVLIVDEAPASIQQSVAVM FT ASIKGVRVRFTTSTAVSHKSPTTLFIPPRSSSRAISRLLPAGVSAFVSFRPETDSTIAR FT LKSSLSHVVATYSLHSFYGGSSLLNAEGEGISCADILETSCLFAEQQLGSHTAVVTIKP FT EDIQTYSLSSDRSAIVDWLHSGPVLAYPLAASSLVNLKAHKTYLLVGMTGDLGRSVCHW FT MISRGARHLVLTSRSPNVDPGWLEEMSALGARVVVMAMDVSDRTSVMRVHNHILADLPP FT VGGVVNGAMVARDCAFTETSFEDVNTVLKPKIDGSKILDELYQDEGLDFFILMGSLAGM FT IGSFNQSIYAATAVFMEDLVLQRRLRGQVGSIIHPAEVRGVGYVTRMGSQFSSNVVKLF FT GECILSERDLLEQFAEGILASRPGSGLNPVISCGLAMTDPTVYPDVIWFKNPTLWSHVH FT YFRHSESLGSRKEQVPIKTQLQSANSLSEAAGIIATGFSQKVQRKLQLPSNSDLPGTTL FT LSDLGIDSLIAVDLRVWFVKELGVDMPVLKLLGGSSIDAVAQDAAEKLDPALLPQLQA" FT mRNA complement(join(<272422..273370,273423..>279865)) FT /locus_tag="An04g04340" FT exon complement(272422..273370) FT /locus_tag="An04g04340" FT /number=1 FT intron complement(273371..273422) FT /locus_tag="An04g04340" FT /number=1 FT exon complement(273423..279865) FT /locus_tag="An04g04340" FT /number=2 FT CDS join(280330..280360,280749..281022,281040..281262) FT /locus_tag="An04g04350" FT /note="Title: similarity to hypothetical protein encoded by FT prophage CP-933X Z1925 - Escherichia coli" FT /db_xref="UniProtKB/TrEMBL:A2QIQ5" FT /inference="profile:COGS:COG0500" FT /protein_id="CAK38699.1" FT /translation="MASIRYLLFLVLSAFFAANTGPHQMDIGVGVGLFPAQHRKQMRQR FT HQEWPQNLALVGMNPSCLQKSATRIDYPGKTAYLRCTCCIVCSANRTQDHCICESKTDS FT AWCHYPGYGAQHYLLGRLTMRLHNWRGIFGNADDSSEIFVKALEDEFEEVETHIVDVAL FT LFRACKPRLALA" FT mRNA join(<280330..280360,280749..281022,281040..>281262) FT /locus_tag="An04g04350" FT sig_peptide join(280330..280360,280749..280777) FT /locus_tag="An04g04350" FT /inference="protein motif:SignalP:2.0" FT exon 280330..280360 FT /locus_tag="An04g04350" FT /number=1 FT intron 280361..280748 FT /locus_tag="An04g04350" FT /number=1 FT exon 280749..281022 FT /locus_tag="An04g04350" FT /number=2 FT mat_peptide join(280778..281022,281040..281259) FT /locus_tag="An04g04350" FT intron 281023..281039 FT /locus_tag="An04g04350" FT /number=2 FT exon 281040..281262 FT /locus_tag="An04g04350" FT /number=3 FT CDS join(281975..282230,282298..282749,282797..282871) FT /locus_tag="An04g04360" FT /note="Title: similarity to hypothetical protein 104H10.250 FT - Neurospora crassa" FT /db_xref="GOA:A2QIQ6" FT /db_xref="InterPro:IPR001031" FT /db_xref="UniProtKB/TrEMBL:A2QIQ6" FT /inference="profile:COGS:COG0596" FT /inference="profile:COGS:COG3319" FT /inference="profile:PFAM:PF00975" FT /inference="similar to AA sequence:UniProtKB:NC104H10.24" FT /protein_id="CAK38700.1" FT /translation="MEENPCQIQSGLGTNDLSTPLILFHDAGGTVFPYFCLGDLHRPLY FT GISNSHFDQGGKWDHGIRQMGVVYSHLLRSVIKSGDVILGGWSLGGCVALEVASRLMKL FT PQYTVQGVIMIDSVFPTSKVTDRYPRTIAEVAASFQLPTRMSDARRVQAQQCILYAHEM FT QRDWRPPLFPSGLPPTVLIRAADPVHLDPDAKPHYLDLIRNWTYLGWEEYDRSFIQSCL FT VIPGNHFTIFDDPHCHQTTTKIREACAILARPQQPNPE" FT mRNA join(<281975..282230,282298..282749,282797..>282871) FT /locus_tag="An04g04360" FT exon 281975..282230 FT /locus_tag="An04g04360" FT /number=1 FT intron 282231..282297 FT /locus_tag="An04g04360" FT /number=1 FT exon 282298..282749 FT /locus_tag="An04g04360" FT /number=2 FT intron 282750..282796 FT /locus_tag="An04g04360" FT /number=2 FT exon 282797..282871 FT /locus_tag="An04g04360" FT /number=3 FT CDS join(283359..283498,283560..283666,283729..285593) FT /locus_tag="An04g04370" FT /EC_number="4.3.1.5" FT /note="Catalytic activity: L-phenylalanine = FT trans-cinnamate + NH3." FT /note="Pathway: tyrosine metabolism; phenylalanine FT metabolism; nitrogen metabolism; alkaloid biosynthesis II." FT /note="Remark: the active sites of the enzyme phenylalanine FT ammonia-lyase (Pal) from Rhodosporidium toruloides contains FT a dehydroalanine residue that is believed to be essential FT for catalytic activity." FT /note="Similarity: belongs to the histidine FT ammonia-lyases." FT /note="Title: strong similarity to phenylalanine FT ammonia-lyase Pal - Rhodosporidium toruloides" FT /db_xref="GOA:A2QIQ7" FT /db_xref="InterPro:IPR005922" FT /db_xref="UniProtKB/TrEMBL:A2QIQ7" FT /citation=[22] FT /citation=[4] FT /citation=[8] FT /inference="profile:COGS:COG2986" FT /inference="profile:PFAM:PF00221" FT /inference="similar to AA sequence:PIR:A56628" FT /protein_id="CAK38701.1" FT /translation="MLDKHIPDGHLETTSAHWRDLNQVVQNGELSIDGYSLSLADVVAV FT AKYGCQPRLTDKPETIDAINGSVIALAECLRDGHHIYGVNTGFGGSADSRTNQTTTLQS FT SLLQLLQSGILTASDTTNEGLQLNLQGQSSHSMPSEWVKATMLVRSNSVARGHSAVSLP FT AISAILRLIREDIVPVIPLRGTISASGDLMPLAYVVGAIEGSPGIYVRVKDGSEHQVVT FT AQKALQTIGAKGVTLGPKEGLGLVNGTAASGALAGLVLYEAHQLAVLAQAVTALTVEAI FT QGSTESFHPFIAQVRPHEGQIEAAENILSLLKGSLLARGSSTTQTRTGLVQDRYSLRTA FT SQWIGPQLEDLLLADRQVQVELNSTSDNPLIDTGSKTFYTGGNFQATSITSAMEKTRLA FT LQMFGKMLFVQCNEMIDPNLNNGLPTNLVADDPSLSFTMKGVDINMAAYMSELAYLANP FT VSSHVQTAEMQNQALNSLAFVSARYTMKAVDIVSMMGACALYVACQALDLRVLQLRFFQ FT RVQGVAKEIAHGAFGKALEPFEIDQVADHLSEAIQNSWPSTSRLDLRDRCKRVAEMFIP FT VLFGALLQIIPQNRQTSDLFTAISACKMISVFKLEGVYREVFAEFCTSQPTADFLGTGT FT KEIYTFIRHDLRVPFHQGFVEHPSASQTDLPETINGRVKKTVGGWISVVYEALRNGTLS FT GTILNSFQQ" FT mRNA join(<283359..283498,283560..283666,283729..>285593) FT /locus_tag="An04g04370" FT exon 283359..283498 FT /locus_tag="An04g04370" FT /number=1 FT intron 283499..283559 FT /locus_tag="An04g04370" FT /number=1 FT exon 283560..283666 FT /locus_tag="An04g04370" FT /number=2 FT intron 283667..283728 FT /locus_tag="An04g04370" FT /number=2 FT exon 283729..285593 FT /locus_tag="An04g04370" FT /number=3 FT CDS complement(join(286252..289362,289641..289727, FT 289798..289852,289883..289911)) FT /locus_tag="An04g04380" FT /note="Remark: the terminal NRPS (non-ribosomal peptide FT synthetases) MxaA extends the assembled polyketide chain of FT the myxalamids with alanine. MxaA contains an N-terminal FT domain with homology to NAD binding proteins, which is FT responsible during the biogenesis for a novel type of FT reductive chain release giving rise to the 2-amino-propanol FT moiety of the myxalamids." FT /note="Similarity: belongs to the non-ribosomal peptide FT synthetase modules and related proteins." FT /note="Title: strong similarity to nonribosomal peptide FT synthase MxaA - Stigmatella aurantiaca" FT /db_xref="GOA:A2QIQ8" FT /db_xref="InterPro:IPR016040" FT /db_xref="UniProtKB/TrEMBL:A2QIQ8" FT /citation=[80] FT /inference="profile:COGS:COG1020" FT /inference="profile:PFAM:PF00501" FT /inference="similar to AA sequence:UniProtKB:AF319998.3" FT /protein_id="CAK38702.1" FT /translation="MTIVMASQLTNDLQMNSNDSMTFSPAFERGVSLFDLLYKDLRINS FT VIPLEYHSAILKLSKLLASFIATTNLYILQMEAILIKKANAAPDAVAVEDSDRSVSYRE FT LIARADMIADQLDQGSLKLGSPVCILADTGLHQVMAQVAVLRAGGSCVPIDPAAPEDRI FT KSILEDLNTRHLIADKSNIDRVQQQSAILIESGLEAKIDLDTKAEITVRTNCPDSHRSH FT IIFTSGSTGRPKPIQVLSSSILHALNHFPFGPLLSSDRMTTLIAPGFDMSVCEMWLTLL FT AGATVVRVPDLVRADPPSLEDFVRKHKITVMIVPTALFQVVALIAPSTFGGLRHVVVGG FT EAVSSSALRKVLEAAPPENLWNGYGPAEATIFATVGRLDKEEMRRPRVSIGRAVGDTKI FT YLLDEDLNPVNETGHIGEICIAGPQLSPGYLNRAEENEKKFISVPATRLGGSSDKHIRV FT YRSGDFAQWRDERGVLEFIGRADDQVKISGYRVELGDISCCVEEHRKIHACVVKYIPES FT SDGFLEAYAVPSNWDSQVSSEELIDWVKVRLPSYMVPKMIHMKRNFPLSHSGKVDKKAL FT QPDNDGEQPCHRKERNHLQNDTTDTTKMNDGGEVGDMTQWLLSTLQGFLPRSKITPSDD FT FFSCGLTSLQAARLVGKIKRDHKSSITLAQLHQNPTVEQLTKSMASSDNDSSQVSLERC FT VEDSKNLDPDLLPPDWQAKDEGRVFLTGATGFLGAHILHQLLIMPSVQKVACLIRGQDA FT VDSSTRLQQTLEKYNLWDDRVETTQKIMVLHGDMADPTLGIGEKQFKWLINWASVVFHV FT GARVNWCQPYEAHHVPNVVGTRNVIRAAMLGRRKALHYVSSIDVWTVTGFINKVDRVYE FT DESLDPHLNALPYDTGYAASQFVAEQIVRRARASGLPTAIYRPGFIIGHSKSALANEKD FT YFSRLIMGSIQCGCFPHLPDQFLDYVTVDYVAEAILHIASSRENLGRSYHIVPPDRSLS FT VGHDQKYEMLREIGYPVEMVDYKEWVEKIRDSPGNALEPMMPLLDEPVYEGLSRLQTSK FT NTPVYDPTNTTRALRDRPDIKYVALDGPLLKRFIENWEKRKAFIS" FT mRNA complement(join(<286252..289362,289641..289727, FT 289798..289852,289883..>289911)) FT /locus_tag="An04g04380" FT exon complement(286252..289362) FT /locus_tag="An04g04380" FT /number=1 FT intron complement(289363..289640) FT /locus_tag="An04g04380" FT /number=1 FT exon complement(289641..289727) FT /locus_tag="An04g04380" FT /number=2 FT intron complement(289728..289797) FT /locus_tag="An04g04380" FT /number=2 FT exon complement(289798..289852) FT /locus_tag="An04g04380" FT /number=3 FT intron complement(289853..289882) FT /locus_tag="An04g04380" FT /number=3 FT exon complement(289883..289911) FT /locus_tag="An04g04380" FT /number=4 FT CDS join(291313..291601,291664..291962) FT /locus_tag="An04g04390" FT /note="Remark: activitie of pehA and of the eight enzymes FT involved in the catabolism of phthalate in Arthrobacter FT keyseri through protocatechuate to pyruvate and FT oxaloacetate were demonstrated in cells or cell extracts of FT recombinant E. coli strains." FT /note="Title: similarity to phthalate ester hydrolase pehA FT - Arthrobacter keyseri" FT /db_xref="GOA:A2QIQ9" FT /db_xref="InterPro:IPR000868" FT /db_xref="UniProtKB/TrEMBL:A2QIQ9" FT /citation=[86] FT /inference="profile:COGS:COG1335" FT /protein_id="CAK38703.1" FT /translation="MPRTAIFVIDIQNHLAVDSTSRVPQADRVIKASEEILQTARSITD FT SNGNSSSPLIVFIQHEESPNDGALVKGTEPWELVFHPRADAEGEILVAKKTGDTFKSNR FT DLAQRLRNANVTEIVAFGLQSDACVEATCTGALAAGFHVTVLAGAHSTYDADGKTAQEI FT EREVELRLSTRGARVVRWEKAIAKWVEKQQVV" FT mRNA join(<291313..291601,291664..>291962) FT /locus_tag="An04g04390" FT exon 291313..291601 FT /locus_tag="An04g04390" FT /number=1 FT intron 291602..291663 FT /locus_tag="An04g04390" FT /number=1 FT exon 291664..291962 FT /locus_tag="An04g04390" FT /number=2 FT exon complement(292732..294453) FT /locus_tag="An04g04400" FT /number=1 FT CDS complement(292732..294453) FT /locus_tag="An04g04400" FT /note="Remark: human telomeres are maintained by telomerase FT , a reverse transcriptase that adds telomeric repeats to FT chromosome ends. In human tumors and immortalized FT cells,telomeres are often maintained at a constant length FT setting , indicating that telomerase-mediated telomere FT elongation is tightly regulated. Tankyrase, a telomeric FT poly(ADP-ribose) polymerase (PARP), was identified through FT its interaction with TRF1, a negative regulator of telomere FT extension by telomerase." FT /note="Remark: similarity to Human tankyrase2 patent FT WO200100849-A1." FT /note="Title: similarity to tankyrase2 TANK2 from patent FT WO200100849-A1 - Homo sapiens" FT /db_xref="InterPro:IPR002110" FT /db_xref="UniProtKB/TrEMBL:A2QIR0" FT /citation=[76] FT /inference="profile:COGS:COG0666" FT /inference="profile:PFAM:PF00023" FT /protein_id="CAK38704.1" FT /translation="MERPSPEADVIWWDSSSYYVRCPFCEGVHRHTVNWQTSLFRVSDC FT EKGETYQSCFPINDQGEVAYEIDKKRERYVNICVSNDSDTEADDNEDEDDVDRLATEMA FT HKATIAAEREERHLSITRDAKETIIHTIDGEKSFEYRLIYDAITDCFNGKTRAVQGYLK FT TSSEAELFVRGQHPDGKTMLISAASEKTPEMLSLLIEHGADVNAVDNHGRSALMEAALF FT GRVGNVKVLLEHGADPNIRDDENRRAVYFARESRKNRKERNVRTQDTYEMLVGRQEIVR FT LLSGEIPKSKNAFGKPPTPSLSRPYRFLSSNGGYTKVLHGPIEEYPMTKCGKTVARLER FT GGKFPSVGAMSGWSHTPAQPLRVDARQWTDDVFYIAEIVGHHLASHACDQGICGQYNAC FT HAEKQLIAYFIDRHVFLPRDGLPDPKLEEEITRVEDELERITSCTEIGRVVASLRKEKQ FT ELDDELFDGDEKLVGKDDEIKKLESKRRDVKTALNQLIASPRARRLRMLECKLEILGVQ FT RQRHEDLTEMAEAPPPPASLSEAAILVSSVPCDDCKAFTERVNKHFGLCIQLFASV" FT mRNA complement(<292732..>294453) FT /locus_tag="An04g04400" FT CDS complement(join(295111..295272,295359..295505)) FT /locus_tag="An04g04410" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIR1" FT /protein_id="CAK38705.1" FT /translation="MATWSLASFHLTEGSGRGCVQASDPTLGVNHHGRKAAPAITSRSH FT NPMHQKPVVWYLALLKLASSQSSRTSSHLPPQSVLHVVRVAEINSSGVKRERTVRIC" FT mRNA complement(join(<295111..295272,295359..>295505)) FT /locus_tag="An04g04410" FT exon complement(295111..295272) FT /locus_tag="An04g04410" FT /number=1 FT mat_peptide complement(join(295114..295272,295359..295457)) FT /locus_tag="An04g04410" FT /product="hypothetical protein" FT intron complement(295273..295358) FT /locus_tag="An04g04410" FT /number=1 FT exon complement(295359..295505) FT /locus_tag="An04g04410" FT /number=2 FT sig_peptide complement(295458..295505) FT /locus_tag="An04g04410" FT /inference="protein motif:SignalP:2.0" FT CDS complement(join(295845..296011,296195..296280, FT 296372..296455,296524..296741)) FT /locus_tag="An04g04420" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIR2" FT /protein_id="CAK38706.1" FT /translation="MPGRLDPRTFPHYCGGLPEYMSSKGVQDRAGDVSLRAMTGCDRTM FT IFCNYFSSSAFPIQVFVAFGIQRTAFEGIDDQSNTSVYTHGAKIGRTSFSREHCSGSSV FT IGSKLAIKDRVVMFAKLPTPEMKDQDWEFVGKRRGKLLGLDPVPVVIRRADKTSSGEEL FT SRSQQHAVFGLGTVSILMRAI" FT mRNA complement(join(<295845..296011,296195..296280, FT 296372..296455,296524..>296741)) FT /locus_tag="An04g04420" FT exon complement(295845..296011) FT /locus_tag="An04g04420" FT /number=1 FT intron complement(296012..296194) FT /locus_tag="An04g04420" FT /number=1 FT exon complement(296195..296280) FT /locus_tag="An04g04420" FT /number=2 FT intron complement(296281..296371) FT /locus_tag="An04g04420" FT /number=2 FT exon complement(296372..296455) FT /locus_tag="An04g04420" FT /number=3 FT intron complement(296456..296523) FT /locus_tag="An04g04420" FT /number=3 FT exon complement(296524..296741) FT /locus_tag="An04g04420" FT /number=4 FT exon 297026..298750 FT /locus_tag="An04g04430" FT /number=1 FT CDS 297026..298750 FT /locus_tag="An04g04430" FT /EC_number="3.1.1.20" FT /note="Catalytic activity: digallate + H2O = 2 Gallate." FT /note="Remark: tannase consisted of two kinds of FT subunits,linked by a disulfide bond(s) with molecular FT weights of about 30,000 and 33,000, respectively." FT /note="Remark: the tannase gene product is translated as a FT single polypeptide that is cleaved by post-translational FT modification into two tannase subunits linked by a FT disulfide bond(s)." FT /note="Remark: this enzyme hydrolyzes the ester bonds of FT tannic acid to produce gallic acid and glucose." FT /note="Title: strong similarity to precursor of tannase FT -Aspergillus oryzae" FT /db_xref="GOA:A2QIR3" FT /db_xref="InterPro:IPR003016" FT /db_xref="UniProtKB/TrEMBL:A2QIR3" FT /citation=[38] FT /inference="similar to AA sequence:PIR:JC5087" FT /protein_id="CAK38707.1" FT /translation="MRSPAWAPIATTAFAALANAATPSTLAELCTDSIVKAALPPSEFI FT QGITIDSDSVTTEVVTNSSVSSEFYPSATINYCNVTFAYSHDGIDGDQVLLEIWLPAPT FT DFQNRWLSTGGGGYAINSGDQSLPGGVMYGAASGMTDGGFGGFSNNADTAMLLANGTLD FT YETLYMFAYKAHRELSLIGKALTRNVYGMSDSDKLYAYYQGCSEGGREGWSQVQRFGDE FT WDGAIIGAPAFRWSFQQTQHLYSNVVEKTLDYYPPPCELDKIVNETIAACDAMDGKVDW FT VVARTDLCLLDFDISTIEGKPYSCAASRGTPAQNGTVSAKGIEVAKTIINGLHDSQGRR FT VYFSYQPTAAFDDAETQYNSTTGQWGLDIDQLGGEYIALLVDKNGTTLDSLDGVTYDTL FT KDWMISGLQEYYSTLQTTWPDLTPFHEAGGKVIHFHGDADFSIPTAASIRYWESVRSIM FT YPNQDYNSSAEALNEWYRLYTVPGAGHCATNDAMPNGPFPQTNMAVMIDWVENGVVPTT FT LNATVLQGENEGQNQQLCAWPLRPLWTNNGTTMECVYNQRSIDSWHYDLDAVPMPVY" FT mRNA <297026..>298750 FT /locus_tag="An04g04430" FT sig_peptide 297026..297106 FT /locus_tag="An04g04430" FT /inference="protein motif:SignalP:2.0" FT mat_peptide 297107..298747 FT /locus_tag="An04g04430" FT CDS complement(join(299170..299732,299778..300266, FT 300336..300783)) FT /locus_tag="An04g04440" FT /note="Remark: the mcr locus from Streptomyces lavendulae FT confers high level resistance (> 100 micrograms/ml) to FT mitomycin C (MC) and related mitomycins." FT /note="Remark: the predicted ORF shows similarity to FT oxidoreductases with different specificity." FT /note="Title: strong similarity to mcrA - Streptomyces FT lavendulae" FT /db_xref="GOA:A2QIR4" FT /db_xref="InterPro:IPR016166" FT /db_xref="UniProtKB/TrEMBL:A2QIR4" FT /citation=[39] FT /inference="profile:COGS:COG0277" FT /inference="profile:PFAM:PF01565" FT /protein_id="CAK38708.1" FT /translation="MTVFLLRTALKAIFSEEYVFTPGQPGYETLNNSYSSATESDFKPA FT CVFCPRDTTDVSRFLSIVKPFTDREEIRFAVRSGGQQTTHACANLDNGITVDLNLLRGI FT ELQDGIVRIWAGERWGRVYDFLASQGLAVTGPLSPESGIGGVVLGGGLSLFSSREGFVC FT DNVLNFEVVLANGEIVNANPKTNSDLWEALRGGGNNFGIVTRYDMRTFPQGSLFGGSLW FT YECFGFPHQIEELVKVLQTSQHMSDMYLRATIVYQRKWGYLCENKLYYTRAEAVPKAFR FT PFMEMSYEVQDYRRVGMVSVTEAVASVQQRRNVKEKDQRQTRCAYMNTTVKADEDTLLR FT AFYEFFAVVDPVRFTKGLRLSMSFQPYPVSLMRKSKELGGNMLGLHRRDGPLVGILLLA FT YWDNKEQDGVVLDSMKLMLGRVEDEAVRRGTGSRFKLMNYSSDFQDPIGSYGPRNKQRL FT QQISRKYDPNGMFQRAVPGGFKLMDHYWGGGEPYCQLPYLA" FT mRNA complement(join(<299170..299732,299778..300266, FT 300336..>300783)) FT /locus_tag="An04g04440" FT exon complement(299170..299732) FT /locus_tag="An04g04440" FT /number=1 FT intron complement(299733..299777) FT /locus_tag="An04g04440" FT /number=1 FT exon complement(299778..300266) FT /locus_tag="An04g04440" FT /number=2 FT intron complement(300267..300335) FT /locus_tag="An04g04440" FT /number=2 FT exon complement(300336..300783) FT /locus_tag="An04g04440" FT /number=3 FT exon complement(302056..302385) FT /locus_tag="An04g04450" FT /number=1 FT CDS complement(302056..302385) FT /locus_tag="An04g04450" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIR5" FT /protein_id="CAK38709.1" FT /translation="MMLLLTCYHLQLKPPLCRVHPLVESGLPLLLTKLPSAVTGPEHDH FT SAWATERDDIFINKLSGQFVKEMGVTPPLIIAGPKLSARQPVTTGCCSKAPWANSTCFV FT RLLRR" FT mRNA complement(<302056..>302385) FT /locus_tag="An04g04450" FT CDS join(303033..303147,303207..303385) FT /locus_tag="An04g04460" FT /note="Title: strong similarity to hypothetical protein FT CAE47852.1/AfA24A6.020c - Aspergillus fumigatus" FT /db_xref="UniProtKB/TrEMBL:A2QIR6" FT /protein_id="CAK38710.1" FT /translation="MVKTALFPLALLAAMAPFAAARNCKTGLNYCGWNLLSIGKYGAQV FT NGALEAAGQPTDDAHIRESLFHCNGGGNGDISFTTFCDGGCKDGGTDRSDYC" FT mRNA join(<303033..303147,303207..>303385) FT /locus_tag="An04g04460" FT exon 303033..303147 FT /locus_tag="An04g04460" FT /number=1 FT sig_peptide 303033..303095 FT /locus_tag="An04g04460" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(303096..303147,303207..303382) FT /locus_tag="An04g04460" FT intron 303148..303206 FT /locus_tag="An04g04460" FT /number=1 FT exon 303207..303385 FT /locus_tag="An04g04460" FT /number=2 FT CDS join(304150..304561,304641..304900) FT /locus_tag="An04g04470" FT /note="Remark: a splice site was detected upstream of the FT START codon." FT /note="Title: weak similarity to NifA-regulated gene NrgA FT -Bradyrhizobium japonicum" FT /db_xref="GOA:A2QIR7" FT /db_xref="InterPro:IPR016181" FT /db_xref="UniProtKB/TrEMBL:A2QIR7" FT /citation=[66] FT /inference="profile:COGS:COG0454" FT /inference="profile:COGS:COG0456" FT /inference="profile:PFAM:PF00583" FT /protein_id="CAK38711.1" FT /translation="MTFTIRYATEQDAPHLANINVVSFNHQAFWAALFPNVAVPGTLPL FT KTARCLDKLRSPQVHVVAAVDDDSGKIIGYSRWLFPKDYETSVVDLSSEGVDALAAHED FT GKAYPEGINMGIYQAFKDLLAEMHRLHFEEGDIMLEFLATLPEAQGKGVGTALLQWGIE FT RADAMNARVYLEATEDGYPLYWKHGWRDLQVARLDFTEYGSTGSQEWVVMRRDRRVPVA FT E" FT mRNA join(<304150..304561,304641..>304900) FT /locus_tag="An04g04470" FT exon 304150..304561 FT /locus_tag="An04g04470" FT /number=1 FT intron 304562..304640 FT /locus_tag="An04g04470" FT /number=1 FT exon 304641..304900 FT /locus_tag="An04g04470" FT /number=2 FT exon complement(305654..306688) FT /locus_tag="An04g04480" FT /number=1 FT CDS complement(305654..306688) FT /locus_tag="An04g04480" FT /EC_number="1.3.1.-" FT /note="Remark: LovC Aspergillus terreus interacts with FT lovastatin nonaketide synthase (LNKS) and is necessary for FT the correct processing of the growing polyketide chain and FT production of dihydromonacolin L." FT /note="Remark: putative part of the lovastatin biosynthesis FT gene cluster as seen in Aspergillus terreus." FT /note="Title: strong similarity to enoyl reductase of the FT lovastatin biosynthesis lovC - Aspergillus terreus" FT /db_xref="GOA:A2QIR8" FT /db_xref="InterPro:IPR013154" FT /db_xref="UniProtKB/TrEMBL:A2QIR8" FT /citation=[61] FT /inference="profile:COGS:COG0604" FT /inference="profile:COGS:COG1063" FT /inference="profile:COGS:COG1064" FT /inference="profile:PFAM:PF00107" FT /inference="similar to AA sequence:UniProtKB:AF141925.2" FT /protein_id="CAK38712.1" FT /translation="MPKALVITAPGSRDVVDRPIPTLPDDCLLVKTVSVALNPTDWKSA FT DRKPPGQVIGNDYSGVVEEVGKGVKKAFRKGDRVCGWVQGCNSNNPESGAFAEYCIPKA FT DLQIAIPDRLSFEEASTLGLGTITVGQGLYQSLKLAPPDAPLAQPELVLIYGGSTATGT FT LAIQFAKLSGYTVLTTCSAQNFDLVKSLGADAVFDYKDANAVQAVKDYAQDKLSLVFDT FT VAVESSAKFCGEVISSKGGDYSALLKVAVPRDDVRSLFTIGYTAFGEDFDFGGGIIPAK FT PEDREFAGQFMSKAATFLAEGKVKPHPVKLGPRGLQGVVEGLQDMKDGKVSGQKLVYNV FT ADTP" FT mRNA complement(<305654..>306688) FT /locus_tag="An04g04480" FT CDS join(307082..307520,307567..308078,308144..309166) FT /locus_tag="An04g04490" FT /note="Remark: grt1(+) defines an independent pathway that FT facilitates the function of Slp1." FT /note="Title: strong similarity to zinc-finger protein FT grt1p - Schizosaccharomyces pombe" FT /db_xref="GOA:A2QIR9" FT /db_xref="InterPro:IPR007219" FT /db_xref="UniProtKB/TrEMBL:A2QIR9" FT /citation=[75] FT /inference="profile:PFAM:PF04082" FT /inference="similar to AA sequence:UniProtKB:AF236387.1" FT /protein_id="CAK38713.1" FT /translation="MSARPNDIRRVANFVSAQPSPTDSPSTAPPAGMTPPPRERVPRAC FT EHCRARKIKCNGQQPCNACARHPERCLYRTGSIRQRKNRRTKEAPRPPATLLPLPTTDS FT PTTPSDWSHTSLSDGPAQYKRHHELRAGIGVQNPETGAFQFYGPSSGFCFIHRVYQRIK FT QGSSSEPLLARRSCSIPDAIHRFGLERFMFARPGDSDPRRTHFPSQMFLPRELGDQFIE FT AYFRIMHPQIPILIKSEIDDAWNQMWESPVRDHSVKNQDILFMVLAIGARVANLKGKQP FT ESSVAAWADYFSSRVSEGPIFLQEPSIRGVHLMLLKLMRQNDAYLYLGHATRTCLVLGL FT HRAQVTDGRDPTVHRLRLTFWTTFFCERISSLYMGRPSSLSDRQIDTAYPEDLPPNPYD FT STCAPMQECAFIRAMGEIAKLADRISIEIYSPASIKNPTDLDKLNQISVECDHALQAVT FT PTLPSYLHFFDDSVPIGEPWQEIQRLSLGFCYYVVRMLLSRPALVLTTFFSSVQEAQIA FT TGCTELQSFINSSTSAARNLIHLAHDVYFRRFPDIRYDGALASFLLSASLTLLYDVLNL FT GTDPDRARQTFTVVEKAIKCLDEIEHTGYTSGKALSLDLMRVAKQAVQAADPVVDTNQV FT LMDAFPWLEYVSPSCCQTMLTE" FT mRNA join(<307082..307520,307567..308078,308144..>309166) FT /locus_tag="An04g04490" FT exon 307082..307520 FT /locus_tag="An04g04490" FT /number=1 FT intron 307521..307566 FT /locus_tag="An04g04490" FT /number=1 FT exon 307567..308078 FT /locus_tag="An04g04490" FT /number=2 FT intron 308079..308143 FT /locus_tag="An04g04490" FT /number=2 FT exon 308144..309166 FT /locus_tag="An04g04490" FT /number=3 FT CDS join(309626..310608,310672..311491) FT /locus_tag="An04g04500" FT /note="Remark: the human MUC3 is a large mucin glycoprotein FT expressed by the human intestine and gall bladder." FT /note="Similarity: the similarities of the ORF encoded FT protein to Muc1 from S. cerevisiae and the other proteins FT are mainly based on repetitive structures." FT /note="Title: similarity to ntestinal mucin MUC3 - Homo FT sapiens" FT /db_xref="UniProtKB/TrEMBL:A2QIS0" FT /citation=[45] FT /protein_id="CAK38714.1" FT /translation="MSKANTRAVPWTSHLIYLLLTLPTALSITLLLSDSQHWTLTGDLY FT TFINRYRTTVQTALQVLATLLGAIQIYSICRLINHATRIFFKHSTHHTTLNDLALWSAL FT STPTTNFTLPLPQILLTLLLANLSAVLSALWTGALTPTSTTTTANTTILIPSYANRSFI FT KEYPSQIDTTGPSLRTSLGYFTYSVGVGLLTSLVSSASTASPLTGSLRARSHAKLDSTG FT YSYSGRSYGVGSPVGLADENVISFYPYAANYTYHERGYLAHVSCLYNSSSLFLLEDTYD FT TALYVAKGPLPDSNVSSGEYSTYTGWSTDTIVALGVASQPAAYTKESFVPSWFIVNVGI FT QEKVVDVVPLNNTTSYPEEDTDIDIDPTNKTIHVAMRQLELISNDLTSFYRSTLGDAFN FT TSIADHATNTNTTATISSNFTTTTTSNSTDNETTTLTAIQNTYISLIDDILAAYASAQL FT IVGNFSRPATATVTIDALRLGSRVYIVAVFVVNVLVVLGVGFEMGRTGAWKALPGFDYL FT DARMLVLGGANGGRGIAERAADVGWKGLETGKIGVRLVGVGGARGVGWGLVYGNRSRSK FT GDGGGEKGREGRRASQETLVEGWI" FT mRNA join(<309626..310608,310672..>311491) FT /locus_tag="An04g04500" FT exon 309626..310608 FT /locus_tag="An04g04500" FT /number=1 FT sig_peptide 309626..309706 FT /locus_tag="An04g04500" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(309707..310608,310672..311488) FT /locus_tag="An04g04500" FT intron 310609..310671 FT /locus_tag="An04g04500" FT /number=1 FT exon 310672..311491 FT /locus_tag="An04g04500" FT /number=2 FT CDS complement(join(311604..311878,311951..312704)) FT /locus_tag="An04g04510" FT /note="Remark: The jlbA mRNA formation in A. nidulans is FT elevated up to 40-fold upon amino acid starvation induced FT by the addition of the false feedback inhibitor 3-amino-1,2 FT ,4-triazole." FT /note="Similarity: the ORF shows strong similarity to the FT A. niger EST an_2580." FT /note="Title: similarity to transcription factor jlbA FT -Aspergillus nidulans" FT /note="nucleus" FT /db_xref="GOA:A2QIS1" FT /db_xref="InterPro:IPR011616" FT /db_xref="UniProtKB/TrEMBL:A2QIS1" FT /citation=[90] FT /inference="profile:PFAM:PF00170" FT /inference="similar to AA sequence:UniProtKB:AF361222.1" FT /protein_id="CAK38715.1" FT /translation="MNKSHPTSTRPKRTRPTRRTKPKTKPASSIRSGLINRASPRPTSS FT SPPPSHPPSPRRKRPLLPSLRTGSPGSKDPALSIEEWLSLQLPTCLSPARPSRSSAQNE FT TSPPPPYNSSHFYQDLSQYPDSFYLPPEFHNNPTFDFSSAAFPPVDTTSLFYDDSPPDT FT SLTAGSNSTINTALSSLSDSSYQDQIIGYPDPTTQHTSCATRLHPHPHSLVPVTAAGPD FT LDPIDSLLSSPELSEELNLLASPGVNSLPEPELEYPPMPAVSSTTSSRAAAPPKEAPNR FT VKKRELNTLAARRYRQRRVDRMNQLEEELEAIKRERDELKMRVSKLEGETEALRSMVRS FT QK" FT mRNA complement(join(<311604..311878,311951..>312704)) FT /locus_tag="An04g04510" FT exon complement(311604..311878) FT /locus_tag="An04g04510" FT /number=1 FT intron complement(311879..311950) FT /locus_tag="An04g04510" FT /number=1 FT exon complement(311951..312704) FT /locus_tag="An04g04510" FT /number=2 FT CDS complement(join(313246..313651,314139..314206)) FT /locus_tag="An04g04520" FT /note="Title: questionable ORF" FT /db_xref="UniProtKB/TrEMBL:A2QIS2" FT /protein_id="CAK38716.1" FT /translation="MPSLGVYDSKRKSISVDTDFYKWALRHFHDKNNSATSHSGNTTYL FT MCKHNGPCQGRRENPRYQHNRDSQSRHRCMSGASRSDWVARVEVEGGVNSKWGNLAMSE FT NDSCSMAPSVFTWRVQFSCLSAVLILHHLDSQRLMIDHAELMLDSSWWTLTIT" FT mRNA complement(join(<313246..313651,314139..>314206)) FT /locus_tag="An04g04520" FT exon complement(313246..313651) FT /locus_tag="An04g04520" FT /number=1 FT intron complement(313652..314138) FT /locus_tag="An04g04520" FT /number=1 FT exon complement(314139..314206) FT /locus_tag="An04g04520" FT /number=2 FT CDS join(314329..314439,314514..314882,314974..315228) FT /locus_tag="An04g04530" FT /EC_number="3.2.1.132" FT /note="Catalytic activity: endohydrolysis of FT beta-1,4-linkages between N-acetyl-D-glucosamine and FT D-glucosamine residues in a partly acetylated chitosan." FT /note="Pathway: aminosugars metabolism." FT /note="Remark: by endo-splitting activity, the chitosanase FT hydrolysed chitosan to form chitosan oligomers with FT chitotriose, chitotetraose and chitopentaose as the major FT products. The enzyme hydrolyses chitohexaose to form FT chitotriose, while the chitopentaose and shorter oligomers FT remain intact." FT /note="Title: strong similarity to chitosanase csnA FT -Aspergillus oryzae" FT /db_xref="GOA:A2QIS3" FT /db_xref="InterPro:IPR009939" FT /db_xref="UniProtKB/TrEMBL:A2QIS3" FT /citation=[74] FT /citation=[88] FT /inference="similar to AA sequence:PIR:JC7659" FT /protein_id="CAK38717.1" FT /translation="MHLLTTLLLSTTTTITTLLATAYSIPPNLSALYNKHKSKPCLHPL FT ATGFHDGQNPTDSTFTYCSDLSNKSIFLHSPTLGGRYDNMDIDCDGANSHGGNCGYDES FT IQDQTSFKDLVSSQYGIPDLDANIHPYVVFGNTDYDPQRDGMWPLSVMVVVCGNQLFYG FT IWGDTAGGSWTGEASIALAKLCFPGDGMSGDNGHVGDDVLYIGFVGKEAVPGGRANWKA FT GSTWEFEESIRGLGERLVATLT" FT mRNA join(<314329..314439,314514..314882,314974..>315228) FT /locus_tag="An04g04530" FT exon 314329..314439 FT /locus_tag="An04g04530" FT /number=1 FT sig_peptide 314329..314400 FT /locus_tag="An04g04530" FT /inference="protein motif:SignalP:2.0" FT mat_peptide join(314401..314439,314514..314882,314974..315225) FT /locus_tag="An04g04530" FT intron 314440..314513 FT /locus_tag="An04g04530" FT /number=1 FT exon 314514..314882 FT /locus_tag="An04g04530" FT /number=2 FT intron 314883..314973 FT /locus_tag="An04g04530" FT /number=2 FT exon 314974..315228 FT /locus_tag="An04g04530" FT /number=3 FT CDS complement(join(315652..317048,317096..317449, FT 317511..317709)) FT /locus_tag="An04g04540" FT /note="Title: similarity to hypothetical protein YLR352w FT -Saccharomyces cerevisiae" FT /db_xref="UniProtKB/TrEMBL:A2QIS4" FT /inference="similar to AA sequence:PIR:S51460" FT /protein_id="CAK38718.1" FT /translation="MSAATTVPLSLHKTSQPRYSPAVSGNTSPTEGSRNASPHPSTCSS FT QNSRSSSRRRESFGSIKEDVDGIAQSFVDTHIEHSPQEPTKRNPIEMQPDFCCPCGGFL FT GWKQIRLGGKSLSRSYSDLRSLGNLHARGWAWDTPDVTPPSKPLPVEEQKLQVPEVKEV FT EVEQKPPAGTSALERLPPEVLDHLISMLALDVPPNGYTPRNVDLISCLLTSKTLHAATL FT SVLYRNMTFPHSIIFSKALNHISRYPALGTLVRRLDFSHFTSVGLGRTKQMNAEIQNLT FT SKTLLQCLELLPNLKECLLQEHVEGDISLDVLRKLFTGLPNLSAVDFCGCSSQSFSTLF FT LEALISGPGLPMTLPNLRRVSLHECSSLPAAAFEILLPRLVNLTHLDVTHTQISEEALF FT SIPETAKITHLSISRCSRLRGSRVVEFLSTHPAVCDSLVFLNVLTDPTRSRLLEEEDVQ FT ALLPRLPSTLRSLNLGGAKVTSAHTQALLPLTKHLEELGLSSCELNGQDLNTFFVPPKP FT VEGEPITPWVPSTLCYLDLNKANQLTIGTIFNPNACVILSPQSYPLQVIEFSDKLIAPL FT RERARNTRTSPDWTVRELGRRGWYVRDPASMPEVMLDDGARSWKMGARWWGMRKIPVAV FT GDVGGLYGHYMFKK" FT mRNA complement(join(<315652..317048,317096..317449, FT 317511..>317709)) FT /locus_tag="An04g04540" FT exon complement(315652..317048) FT /locus_tag="An04g04540" FT /number=1 FT intron complement(317049..317095) FT /locus_tag="An04g04540" FT /number=1 FT exon complement(317096..317449) FT /locus_tag="An04g04540" FT /number=2 FT intron complement(317450..317510) FT /locus_tag="An04g04540" FT /number=2 FT exon complement(317511..317709) FT /locus_tag="An04g04540" FT /number=3 FT CDS join(318302..318306,318383..318751,319074..319299, FT 319352..319783) FT /locus_tag="An04g04550" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIS5" FT /protein_id="CAK38719.1" FT /translation="MMEKVERESGKKLQVDVKFPLSKANRPGLPTSQKPTNNGDTGTVL FT VIFFTEGLPAEWRRKAKLSAEKKEKPMDPADDSVGLTQLTTWGPPSLPAANPVVRKEQR FT QKEVPFGCSILYFLPKYFAALLPARFPLVDKSDDSMADLLAPWPSLARSGSPPAFYDIM FT ENRRWWPRDLPDGAGSSRGRVPHSSDHRDFPPLLGTLDERAILVRVIGCVSSSFPMNSQ FT DIIPYSIDRYSFSKVMSPSTPDLHAPLMQYSLPNNYYSPALHLLRAGSRDPAENASPVT FT PPFLPLLLFPLFVIHSHVSLDPEIRRTQSLTVFISSKEKLMKPGHMSKLRPSKFLNQPD FT SGH" FT mRNA join(<318302..318306,318383..318751,319074..319299, FT 319352..>319783) FT /locus_tag="An04g04550" FT exon 318302..318306 FT /locus_tag="An04g04550" FT /number=1 FT intron 318307..318382 FT /locus_tag="An04g04550" FT /number=1 FT exon 318383..318751 FT /locus_tag="An04g04550" FT /number=2 FT intron 318752..319073 FT /locus_tag="An04g04550" FT /number=2 FT exon 319074..319299 FT /locus_tag="An04g04550" FT /number=3 FT intron 319300..319351 FT /locus_tag="An04g04550" FT /number=3 FT exon 319352..319783 FT /locus_tag="An04g04550" FT /number=4 FT CDS complement(join(320396..320485,320539..320652, FT 320708..320794,321043..321179,321360..321476, FT 322018..322083,322176..322349,322448..322558, FT 322686..322764)) FT /locus_tag="An04g04560" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIS6" FT /protein_id="CAK38720.1" FT /translation="MVDTIAEKVIFCRLAVKVCADRITREVESPDLLGSQRYIVLAYLA FT QIADLTESTYGTQTTSLFNDLGSLVYLYEGRLFLPNCLLSIFTRVPLCGGCNVLMKWAV FT RLRVRQAATISGALGTTVLWTLHAYNKAAGLVMNNIIVGTGMGDAACVRRCQVVSCWRE FT RPGSLPNMSRDQGIRGYLPGTNRSSESVRQFVSSTRLLEVSSGAQKPDYERPRPIEGGE FT CELAWEAWAGVGVNFRQTARGSQDGDDLAMGTMSSDGPELGVQAVLKVSGIMLARIPFH FT CLVLGLSTSFGLFQPPPHSVDIICATVSSRQEAWVWSGHTGVP" FT mRNA complement(join(<320396..320485,320539..320652, FT 320708..320794,321043..321179,321360..321476, FT 322018..322083,322176..322349,322448..322558, FT 322686..>322764)) FT /locus_tag="An04g04560" FT exon complement(320396..320485) FT /locus_tag="An04g04560" FT /number=1 FT intron complement(320486..320538) FT /locus_tag="An04g04560" FT /number=1 FT exon complement(320539..320652) FT /locus_tag="An04g04560" FT /number=2 FT intron complement(320653..320707) FT /locus_tag="An04g04560" FT /number=2 FT exon complement(320708..320794) FT /locus_tag="An04g04560" FT /number=3 FT intron complement(320795..321042) FT /locus_tag="An04g04560" FT /number=3 FT exon complement(321043..321179) FT /locus_tag="An04g04560" FT /number=4 FT intron complement(321180..321359) FT /locus_tag="An04g04560" FT /number=4 FT exon complement(321360..321476) FT /locus_tag="An04g04560" FT /number=5 FT intron complement(321477..322017) FT /locus_tag="An04g04560" FT /number=5 FT exon complement(322018..322083) FT /locus_tag="An04g04560" FT /number=6 FT intron complement(322084..322175) FT /locus_tag="An04g04560" FT /number=6 FT exon complement(322176..322349) FT /locus_tag="An04g04560" FT /number=7 FT intron complement(322350..322447) FT /locus_tag="An04g04560" FT /number=7 FT exon complement(322448..322558) FT /locus_tag="An04g04560" FT /number=8 FT intron complement(322559..322685) FT /locus_tag="An04g04560" FT /number=8 FT exon complement(322686..322764) FT /locus_tag="An04g04560" FT /number=9 FT exon 323038..325116 FT /locus_tag="An04g04570" FT /number=1 FT CDS 323038..325116 FT /locus_tag="An04g04570" FT /note="Function: co-expression of het-e and het-c lead to FT cell death." FT /note="Function: het-e1 of P. anserina is responsible for FT vegetative incompatibility." FT /note="Remark: het-e1 of P. anserina shows also two FT sequence motifs, a GTP-binding domain and a repeated region FT that shares similarity with that of the beta-transducin." FT /note="Remark: the reactivity of the HET-E protein depends FT on two functional elements, a GTP-binding domain and FT several WD40 repeats." FT /note="Title: similarity to beta transducin-like protein FT het-e1 - Podospora anserina" FT /db_xref="InterPro:IPR010730" FT /db_xref="UniProtKB/TrEMBL:A2QIS7" FT /citation=[16] FT /inference="profile:COGS:COG0666" FT /inference="profile:PFAM:PF00023" FT /protein_id="CAK38721.1" FT /translation="MRLLNTCLSDTGDFVIQNFLDYELPPYAILSHTWGKEEVTYQEIN FT AASAKTKSGYKKITKCCSVARSNGYKYVWIDTCCIDKTSSAELSEAINSMYLWYQKAEV FT CYAILADVRSEDEISQSKWLTRGWTLQELIAPSRVIFLNERWEVLGDRATLRDQLCEYT FT GIPAGILSGNDDLETSSVAQRMSWAAKRQTSRVEDRAYSLMGIFNVNMPLIYGEGENAF FT IRLQEEIMRISDDQSLFAWTSSDDRGGLLATSPAAFAQSYNIVRFNPYGSLDNPFAVNS FT RGVHLDIGFAGLSADGEGVGILNCVERTCTERTQQDKVIAIYLEDLTFTLHLFKRVKSR FT VLRRIDLGTFRPTRYPVRRICVRGGRTMLIQKRTAVEQDVIPPEMIQLLEELRLPMRYR FT EPAALLMITKAGIRGGVWLLLTQSDVRLEITDQNGQTPLSLAAENGQEDIVQMLLERGA FT SVETKNSDSQTPLSLAAANGHERIVQMLLKKGATTETRSSKDQTPLSLAAENGHEKIVQ FT MLLEVGAAIEARGQWGERTPLSLAAANGHEGIVQILLARGAANKYSDQWLQMPLWKATE FT NGHEGIVKMLLERCDDTENQDTWRWESLLSLATENGHEGIVKMLLERCDDTDNQNTWRW FT DSLLSLATENGHGGIVNMLLERGAKIKTTHPNGWEDIATWLQRMAMRLLPASSHAAT" FT mRNA <323038..>325116 FT /locus_tag="An04g04570" FT CDS complement(join(326299..326331,326485..326538, FT 326614..327504)) FT /locus_tag="An04g04580" FT /note="Similarity: the ORF shows strong similarity to the FT A. niger protein An11g05870. An11g05870, however, is much FT longer than the ORF (853 compared to 325 amino acids)." FT /note="Title: strong similarity to hypothetical protein FT encoded by An11g05870 - Aspergillus niger" FT /db_xref="UniProtKB/TrEMBL:A2QIS8" FT /protein_id="CAK38722.1" FT /translation="MAPISIKVFQNTLRAAATQHRHNYTNIHSITVRWEKDHTKADKVS FT QYFQNLLKTLNIPPAAEHIIRHNSPNPDIPFQQAFHDILEESQPKTNSDHKLLIFHYAG FT HGFIKNGQLTFAETATAEKTLNAGNCLFEDTGLIPDSVHLDILLIFDCCYIGHIATRAP FT IISNRVVEILAATSTQIPRNRILPENAFTAKIAEEITRRKRSGHQYVEFADVFQTLRSR FT GERDKLRPTHALLVGVGSVILPLNNSRTVDPVTIAPMCTALFSVSVAKEMTAEELRQLS FT SWMKNLPCFAGLEVDKGYSLIAEDVRAPIDLDNLSTGYEKYHNE" FT mRNA complement(join(<326299..326331,326485..326538, FT 326614..>327504)) FT /locus_tag="An04g04580" FT exon complement(326299..326331) FT /locus_tag="An04g04580" FT /number=1 FT intron complement(326332..326484) FT /locus_tag="An04g04580" FT /number=1 FT exon complement(326485..326538) FT /locus_tag="An04g04580" FT /number=2 FT intron complement(326539..326613) FT /locus_tag="An04g04580" FT /number=2 FT exon complement(326614..327504) FT /locus_tag="An04g04580" FT /number=3 FT exon complement(328858..329664) FT /locus_tag="An04g04590" FT /number=1 FT CDS complement(328858..329664) FT /locus_tag="An04g04590" FT /note="Title: strong similarity to hypothetical protein FT AAP25659.1 - Bacillus anthracis" FT /db_xref="UniProtKB/TrEMBL:A2QIS9" FT /protein_id="CAK38723.1" FT /translation="MAATVVSSTEPMPNMTPDYEVRLLLNPAKVLSSEHELTDNVRSAL FT NLAPTAIKLNVQFLDTCAKEIYTAGWSARIRKADNEDDLELTYKKRYAVTDGNIDSALT FT ATKNDGFNAGDTKYKAQIEWGYERQILSISRKKTVADAVAGNDNMDLPGTSDSRQMLID FT EAPDKFKNWRPNKWGTSVLAMSRIYGPVFVKRFVGTWGRIPLYVEIWPLINSQRTGIEY FT IVEASFKTENIMTASDERSNLITDLQSKGWLLLKELLKTQLIMERY" FT mRNA complement(<328858..>329664) FT /locus_tag="An04g04590" FT CDS complement(join(329848..329948,330160..330216, FT 330280..330376)) FT /locus_tag="An04g04600" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIT0" FT /protein_id="CAK38724.1" FT /translation="MPHDARRSSDCNPVPASVVQPSVVPPRCKPYPHAKKSVFRIWEIK FT AYSFYPGSLLPSYNKAMGILDELSPGYSTLRRTGTGSIR" FT mRNA complement(join(<329848..329948,330160..330216, FT 330280..>330376)) FT /locus_tag="An04g04600" FT exon complement(329848..329948) FT /locus_tag="An04g04600" FT /number=1 FT intron complement(329949..330159) FT /locus_tag="An04g04600" FT /number=1 FT exon complement(330160..330216) FT /locus_tag="An04g04600" FT /number=2 FT intron complement(330217..330279) FT /locus_tag="An04g04600" FT /number=2 FT exon complement(330280..330376) FT /locus_tag="An04g04600" FT /number=3 FT CDS complement(join(331275..331321,331418..331514)) FT /locus_tag="An04g04610" FT /product="hypothetical protein" FT /note="Remark: the ORF is short in length (47 amino FT acids)." FT /db_xref="UniProtKB/TrEMBL:A2QIT1" FT /protein_id="CAK38725.1" FT /translation="MYHVSTLYLILFLPYTLGKDIQTRSKDCRTLRALRVHHTARAETL FT VD" FT mRNA complement(join(<331275..331321,331418..>331514)) FT /locus_tag="An04g04610" FT exon complement(331275..331321) FT /locus_tag="An04g04610" FT /number=1 FT mat_peptide complement(join(331278..331321,331418..331460)) FT /locus_tag="An04g04610" FT /product="hypothetical protein" FT intron complement(331322..331417) FT /locus_tag="An04g04610" FT /number=1 FT exon complement(331418..331514) FT /locus_tag="An04g04610" FT /number=2 FT sig_peptide complement(331461..331514) FT /locus_tag="An04g04610" FT /inference="protein motif:SignalP:2.0" FT exon complement(332161..333318) FT /locus_tag="An04g04620" FT /number=1 FT CDS complement(332161..333318) FT /locus_tag="An04g04620" FT /note="Title: strong similarity to hypothetical protein FT encoded by An14g05440 - Aspergillus niger" FT /db_xref="InterPro:IPR001810" FT /db_xref="UniProtKB/TrEMBL:A2QIT2" FT /protein_id="CAK38726.1" FT /translation="MANNDVLPEGAIEADVIRATSYHRRDFDMSVIRIKPVDSESVGPG FT ITHAFNRPFQPAKPGLLDYLPVEILLKFIPDLDIQTLFNLRHVNARTRDVVSSLETYQQ FT VTTYAADLICALLRTTLAQWYTLQDVLEVLHTRECSICHAEFGGFVFLFPPKLSRCCFP FT CIRSKSDLRRPVIDPHTHRFHYDREYELITLAEAHNFYGISPAVLRAESVPILKTVRGF FT YTMKETQRKIRHSLVHDKRVRELSTAHQHGIPWSDTFRRGRVMLLRWCMATTAVPYVDR FT ETGEIERGVSCRGCQGRFEQVSSDWRRVGELSAPRDKVYSKAAFMVHFRECQWAKKLWE FT DSKGGTVVVGESEFVRRGGFMEDRKDDHGSEVVAAKKKRPHSTVG" FT mRNA complement(<332161..>333318) FT /locus_tag="An04g04620" FT exon complement(333810..335168) FT /locus_tag="An04g04630" FT /number=1 FT CDS complement(333810..335168) FT /locus_tag="An04g04630" FT /note="Remark: the CAP59 gene is required for capsule FT formation. Capsule formation plays a significant role in FT the pathogenicity of Cryptococcus neoformans." FT /note="Title: strong similarity to capsule-associated FT protein CAP59 - Cryptococcus neoformans" FT /db_xref="UniProtKB/TrEMBL:A2QIT3" FT /citation=[18] FT /inference="similar to AA sequence:PIR:A56055" FT /protein_id="CAK38727.1" FT /translation="MNFNVRQVQTHLFRLTISTASFCFLLFLYISFEWSPSASDPSGFS FT ASSYEDDLDAAIPAISACNGFNPATVADVLDATLTAKLPINGSAVDDFVCSIMTHDMNL FT SAKLDCPATISPRYADLPVRASNSFFSKPKIKYFFALDLYQSAHIMLPLMGTIVETMRF FT LGPEYCALSIVEGRSTDGTYDILNRLKSEMAAMGVRYYLSTSDLNPKAIWADRIKHLST FT LRNQALAPLVSAGAGKFKPYAADATILFINDVVLCVEDLLELLYQHRQQDARMTCAFDW FT NAAGGPFYDSWVSRSMSGNLFFEITHDARYWLTQDMFFDDQPNQQRYGRKLPVQVYSCW FT GGMVILDAAPFVQRKLEFRNHKEGECHMGEPTLLAKDMWGQGLGKILAVPSVNVAYEYK FT ATREAKNGQGYVHNVIESADYKAGKELVVWDKEPPVRIKCMPLFNQQSWVKST" FT mRNA complement(<333810..>335168) FT /locus_tag="An04g04630" FT mat_peptide complement(333813..335051) FT /locus_tag="An04g04630" FT sig_peptide complement(335052..335168) FT /locus_tag="An04g04630" FT /inference="protein motif:SignalP:2.0" FT CDS complement(join(336384..336704,336769..336862, FT 336915..336978,337035..337136,337186..337504, FT 337573..337878)) FT /locus_tag="An04g04640" FT /EC_number="2.5.1.10" FT /note="Catalytic activity: geranyl diphosphate + FT isopentenyl diphosphate = pyrophosphate + FT trans,trans-farnesyl diphosphate" FT /note="Pathway: sterol biosynthesis; terpenoid FT biosynthesis." FT /note="Remark: the rice pathogen, Gibberella FT fujikuroi,produces large amounts of gibberellins, a group FT of natural plant hormones, which induce the superelongation FT (bakanae) disease of rice. Gibberellins are diterpenoid FT compounds which are synthesized via the isoprenoid FT pathway." FT /note="Similarity: belongs to the geranylgeranyl FT pyrophosphate synthases." FT /note="Title: strong similarity to geranylgeranyl FT diphosphate synthase GGSII - Gibberella fujikuroi" FT /db_xref="GOA:A2QIT4" FT /db_xref="InterPro:IPR017446" FT /db_xref="UniProtKB/TrEMBL:A2QIT4" FT /citation=[44] FT /citation=[54] FT /inference="profile:COGS:COG0142" FT /inference="profile:PFAM:PF00348" FT /inference="similar to AA sequence:UniProtKB:GFGGSII.1" FT /protein_id="CAK38728.1" FT /translation="MTRKAEYLANMNPMTPNSGDIIYFLEMVGLGLSGNWYWHAIADRF FT HRWAEYLQLPPAKLFDYDEATATCATFLNSQSLRARPSRIVDSFEGPQTMTDDPYYKVL FT QQPINYLRSVPSKNIRGTIIQALNLWLNAPESVATQVEDLIGHLHDSSLLLDDIQDNSE FT LRRGRPTAYRVFGVAQTINAATHALTQAFEKVVPLMKPGTSHGFFDELRNLHVGQAMDL FT HWTRSGYRPSIADYLEMNRLKTGALFCLASNLLYIQGSFSAEAIKQTDLSDLMISLGQY FT FQARDDYINLASTKYQEQKGFAQDLDEGKLSLPLIHLLTQSPNAALIENIQQERARHGK FT LSADLKQLILDEMRNEKILQLTEETLNGLEAKVFRHLERLEVSSGIKNFTFRFLLDRLR FT EM" FT mRNA complement(join(<336384..336704,336769..336862, FT 336915..336978,337035..337136,337186..337504, FT 337573..>337878)) FT /locus_tag="An04g04640" FT exon complement(336384..336704) FT /locus_tag="An04g04640" FT /number=1 FT intron complement(336705..336768) FT /locus_tag="An04g04640" FT /number=1 FT exon complement(336769..336862) FT /locus_tag="An04g04640" FT /number=2 FT intron complement(336863..336914) FT /locus_tag="An04g04640" FT /number=2 FT exon complement(336915..336978) FT /locus_tag="An04g04640" FT /number=3 FT intron complement(336979..337034) FT /locus_tag="An04g04640" FT /number=3 FT exon complement(337035..337136) FT /locus_tag="An04g04640" FT /number=4 FT intron complement(337137..337185) FT /locus_tag="An04g04640" FT /number=4 FT exon complement(337186..337504) FT /locus_tag="An04g04640" FT /number=5 FT intron complement(337505..337572) FT /locus_tag="An04g04640" FT /number=5 FT exon complement(337573..337878) FT /locus_tag="An04g04640" FT /number=6 FT CDS complement(join(338223..338480,338545..338573, FT 338672..338954)) FT /locus_tag="An04g04650" FT /note="Similarity: the ORF shows weak similarity to the A. FT niger protein An16g00260. An16g00260, however, is much FT longer than the ORF (619 compared to 189 amino acids)." FT /note="Title: weak similarity to hypothetical protein FT encoded by An16g00260 - Aspergillus niger" FT /db_xref="InterPro:IPR008949" FT /db_xref="UniProtKB/TrEMBL:A2QIT5" FT /protein_id="CAK38729.1" FT /translation="MSPVDIPFIHSELVDSEEIARVCATTLPVRKSKYSHLAEKAVSDF FT QQQWQQEVRFAYCGGSSPQGPVTAFFPPESKPDRVEVFTKLIEYFFAHDDVLGVSGSVE FT VDRTESPDAIGWGIRRGTISSARTSAMKQIQSEVFLRLVEIDRPRGNLILHAINKLSRV FT HETIDSRDLKTWDDLLQYRVQDFGAE" FT mRNA complement(join(<338223..338480,338545..338573, FT 338672..>338954)) FT /locus_tag="An04g04650" FT exon complement(338223..338480) FT /locus_tag="An04g04650" FT /number=1 FT intron complement(338481..338544) FT /locus_tag="An04g04650" FT /number=1 FT exon complement(338545..338573) FT /locus_tag="An04g04650" FT /number=2 FT intron complement(338574..338671) FT /locus_tag="An04g04650" FT /number=2 FT exon complement(338672..338954) FT /locus_tag="An04g04650" FT /number=3 FT CDS join(338991..339071,339159..339374) FT /locus_tag="An04g04660" FT /product="hypothetical protein" FT /db_xref="UniProtKB/TrEMBL:A2QIT6" FT /protein_id="CAK38730.1" FT /translation="MYLWRVSNGVYDPKSSGKCAIYILSELGWLEFPQGKPFQSGYKNR FT VWPECRMARNVRLASSVSNEAPQLVPFDWPLIHHCLEWSAGICSVGEGGVGAV" FT mRNA join(<338991..339071,339159..>339374) FT /locus_tag="An04g04660" FT exon 338991..339071 FT /locus_tag="An04g04660" FT /number=1 FT intron 339072..339158 FT /locus_tag="An04g04660" FT /number=1 FT exon 339159..339374 FT /locus_tag="An04g04660" FT /number=2 FT CDS join(341567..341641,341696..341759,341807..341840, FT 341898..342945) FT /locus_tag="An04g04670" FT /EC_number="3.2.1.14" FT /note="Catalytic activity: random hydrolysis of FT N-acetyl-beta-D-glucosaminide 1,4-beta-linkages in chitin FT and chitodextrins." FT /note="Pathway: aminosugars metabolism." FT /note="Remark: expression of the CF/chitinase cDNA insert FT by using the pGEX-4T-3 vector yields a fusion peptide that FT bears CF-specific epitopes and shows chitinase activity." FT /note="Similarity: belongs to the chitinase family." FT /note="Title: strong similarity to chitinase cts1 FT -Coccidioides immitis" FT /db_xref="GOA:A2QIT7" FT /db_xref="InterPro:IPR013781" FT /db_xref="UniProtKB/TrEMBL:A2QIT7" FT /citation=[31] FT /citation=[32] FT /inference="profile:COGS:COG3325" FT /inference="profile:PFAM:PF00704" FT /inference="similar to AA sequence:UniProtKB:CIU60807.1" FT /protein_id="CAK38731.1" FT /translation="MARPPPPWINAGRPGYKTVGYFTNWGVYGRNYQPQDIPAEYITHI FT LYSFANIRPTGEVFLTDTYSDLEKHYPTDSWSEPGTNAYGCIKQLYLLKQQHRHLKTLL FT SIGGWTYSPNFAAPASTPRGRETFARSAVHLLADLGFDGIDIDWEYPADSSQAMDFVHL FT LRDVRRVLDEYSATHLGGKRLLLTIAAPCGPDNIQKLRIGDMDPYLDFWNLMCYDFSGS FT WDKCSGHMANVFHSGRGEITPFCADGAVTMYLRGGVRDARKLIFGLPLYGRAFEGTDGP FT GSGFQGVGEGSWENGVWDYKALPLQGSQEVVDGRLMASWCFDPAKRKMVSYDTPEVAGM FT KTEYIAGRRLGGAMWWELSGDHHVSHERSLVKGTAERLGRLGGLDGTENTLYYPLSRFE FT NLRRGCV" FT mRNA join(<341567..341641,341696..341759,341807..341840, FT 341898..>342945) FT /locus_tag="An04g04670" FT exon 341567..341641 FT /locus_tag="An04g04670" FT /number=1 FT intron 341642..341695 FT /locus_tag="An04g04670" FT /number=1 FT exon 341696..341759 FT /locus_tag="An04g04670" FT /number=2 FT intron 341760..341806 FT /locus_tag="An04g04670" FT /number=2 FT exon 341807..341840 FT /locus_tag="An04g04670" FT /number=3 FT intron 341841..341897 FT /locus_tag="An04g04670" FT /number=3 FT exon 341898..342945 FT /locus_tag="An04g04670" FT /number=4 FT CDS complement(join(343166..343210,343371..343863, FT 343912..344109,344160..344303,344361..344586, FT 344676..344913)) FT /locus_tag="An04g04680" FT /EC_number="1.14.13.7" FT /note="Remark: this ORF represents an putative FAD FT dependent monooxygenase." FT /note="Similarity: belongs to the tetracycline FT 6-hydroxylase family." FT /note="Title: strong similarity to sequence 29 from patent FT WO0100842-A - Corynebacterium glutamicum" FT /db_xref="GOA:A2QIT8" FT /db_xref="InterPro:IPR003042" FT /db_xref="UniProtKB/TrEMBL:A2QIT8" FT /inference="profile:COGS:COG0654" FT /inference="profile:PFAM:PF01360" FT /protein_id="CAK38732.1" FT /translation="MPSPETYDVTIIGGGPVGLLLAYQLSRFELSVCVVEKQDKNSPEG FT RYGRAITLFPRTLELLDQLDLVHAMLQQGFACRSRKVWTFMENIQGTVFDFALVLRQMY FT TEGILRKRLDKEKVTYHGSMECVAFEIGLDGSEYPVTVHCSGPGGMMTAKSKYLVGADG FT GHSLVRRYANIPFDGDSSEDQWIRIDGIVETNMPINRAYGAIETTTHGNVLWAPLDHGA FT TRIGYAYTPEIAAKYPEGVTEEVAVNEAIACLRPFNLKFKEVHWWTLYKIGQRMARTFA FT THNNRVFICGDAAHTHSSGAAQGLNTGIHDAVNLAWKLALEVHGLSHPEVLNTYTTERQ FT SAVQRLLNYDRDISLLMTHKWPVWYDGDRSADPNVLLGEIFQDAAQFNTGLGISYEANV FT INQPLEPSTEVAVGVQPGSRAPDTELTMPGTFQSCAAQPAARRTRCSG" FT mRNA complement(join(<343166..343210,343371..343863, FT 343912..344109,344160..344303,344361..344586, FT 344676..>344913)) FT /locus_tag="An04g04680" FT exon complement(343166..343210) FT /locus_tag="An04g04680" FT /number=1 FT intron complement(343211..343370) FT /locus_tag="An04g04680" FT /number=1 FT exon complement(343371..343863) FT /locus_tag="An04g04680" FT /number=2 FT intron complement(343864..343911) FT /locus_tag="An04g04680" FT /number=2 FT exon complement(343912..344109) FT /locus_tag="An04g04680" FT /number=3 FT intron complement(344110..344159) FT /locus_tag="An04g04680" FT /number=3 FT exon complement(344160..344303) FT /locus_tag="An04g04680" FT /number=4 FT intron complement(344304..344360) FT /locus_tag="An04g04680" FT /number=4 FT exon complement(344361..344586) FT /locus_tag="An04g04680" FT /number=5 FT intron complement(344587..344675) FT /locus_tag="An04g04680" FT /number=5 FT exon complement(344676..344913) FT /locus_tag="An04g04680" FT /number=6 FT CDS complement(join(345449..346142,346202..346673, FT 346723..346818,346880..347168)) FT /locus_tag="An04g04690" FT /note="Remark: acr-2 gene controls acriflavine sensitivity FT in N. crassa. The acr-2 mutation, which confers acriflavine FT resistance, substitutes the amino acid residue at position FT 303 of the encoded protein from asparagine to lysine. FT Progeny that were hypersensitive to acriflavine were FT obtained by disruption of the acr-2 gene by repeat induced FT point mutation (RIP)." FT /note="Similarity: belongs to the GAL4 zinc binuclear FT cluster proteins." FT /note="Title: strong similarity to transcription factor FT involved in acriflavine resistance acr-2 - Neurospora FT crassa" FT /note="nucleus" FT /db_xref="GOA:A2QIT9" FT /db_xref="InterPro:IPR001138" FT /db_xref="UniProtKB/TrEMBL:A2QIT9" FT /citation=[33] FT /inference="profile:PFAM:PF00172" FT /protein_id="CAK38733.1" FT /translation="MEEPCYTCRRRRIRCDQSQSPCVKCATSGYQCFASRPLRWVEGLA FT IRGKLRGVSLATNSASSAKKAKSRKESDSRDSSLAPATESALSVVRSSEGHVAPSKPLI FT SIPSTIGDFAASNLDAVSRYYLDYYNESICGLFIVYDSDRNPLRALMSLALLDHTLLKS FT VLALAARHRVNRHCSFHDLTIKASSDQMIANADALRFKYQAIQGIAQALGDATSRNKDT FT TVASIFLLVFLDLLESGSDRWNVHLEGAKRLMEPSTPDSQAVSRHDSGQTIEDLRNFLA FT SQIYSIETLGGTFVRPKLLSQFNLLEGPQFQETVEQSFLGCPEYLLDAIRYLSARRDTI FT ASSECHDDSTWSYFIQDTMSMIDFIQQFDCSVWASSLPYLGTVPPRGTSSLCTLAQSYK FT IGALIYGKRVLGALTKEYLPLDDLIQELLATIESLQNNETLYKCILWPIIIAGLECQRQ FT EQRESVRTYMESFWEHTKCVNVINASKIIEDRWQRCDSTEPSHWIFSIGNLGRDWLLI" FT mRNA complement(join(<345449..346142,346202..346673, FT 346723..346818,346880..>347168)) FT /locus_tag="An04g04690" FT exon complement(345449..346142) FT /locus_tag="An04g04690" FT /number=1 FT intron complement(346143..346201) FT /locus_tag="An04g04690" FT /number=1 FT exon complement(346202..346673) FT /locus_tag="An04g04690" FT /number=2 FT intron complement(346674..346722) FT /locus_tag="An04g04690" FT /number=2 FT exon complement(346723..346818) FT /locus_tag="An04g04690" FT /number=3 FT intron complement(346819..346879) FT /locus_tag="An04g04690" FT /number=3 FT exon complement(346880..347168) FT /locus_tag="An04g04690" FT /number=4 FT CDS join(347725..348414,348474..348503) FT /locus_tag="An04g04700" FT /EC_number="2.1.1.6" FT /note="Catalytic activity: S-adenosyl-L-methionine + FT catechol = S-adenosyl-L-homocysteine + guaiacol." FT /note="Pathway: tyrosine metabolism." FT /note="Remark: strong similarity to human FT catechol-O-methyltransferase patent WO9111513-A." FT /note="Remark: the mammalian enzyme acts more rapidly on FT catecholamines such as adrenaline or noradrenaline than on FT catechols." FT /note="Similarity: belongs to the SAM-dependent FT methyltransferases." FT /note="Title: strong similarity to FT catechol-O-methyltransferase COMT from patent WO9111513-A FT -Homo sapiens" FT /db_xref="GOA:A2QIU0" FT /db_xref="InterPro:IPR002935" FT /db_xref="UniProtKB/TrEMBL:A2QIU0" FT /citation=[78] FT /citation=[9] FT /inference="profile:COGS:COG2230" FT /protein_id="CAK38734.1" FT /translation="MAPVDEKPASLCRSEPHDTLEVSLLKYIYSHPSLAQIRGCPSALL FT ALIDEFAAKQAFFISLGPDKAKKLSTLFADEKPKVVVELGTYVGYSAIMFADAMRQAAG FT GSSTGLRLWSLEADPLIASIAMNFIELAGLSDIVKVVVGPASDSLKRLSAEGKLSSVDL FT MFIDHIKELYVPDLELSEQLGFLHSGSLVLADNVVHPGAPAYREFVRGSSKYESWGLKC FT LLFPEDIVDEIEISRVK" FT mRNA join(<347725..348414,348474..>348503) FT /locus_tag="An04g04700" FT exon 347725..348414 FT /locus_tag="An04g04700" FT /number=1 FT intron 348415..348473 FT /locus_tag="An04g04700" FT /number=1 FT exon 348474..348503 FT /locus_tag="An04g04700" FT /number=2 FT exon complement(348721..349512) FT /locus_tag="An04g04710" FT /number=1 FT CDS complement(348721..349512) FT /locus_tag="An04g04710" FT /note="Remark: paiB from B. subtilis is essential for FT growth." FT /note="Title: similarity to transcription regulator 2 of FT pai operon paiB - Bacillus subtilis" FT /db_xref="InterPro:IPR007396" FT /db_xref="UniProtKB/TrEMBL:A2QIU1" FT /citation=[11] FT /inference="profile:COGS:COG2808" FT /inference="profile:PFAM:PF04299" FT /protein_id="CAK38735.1" FT /translation="MYLRAIHAESHIPALHQLIRQNPLGILTTAIKSPLYPLLQSSHIP FT FIIDVPSSEDSSDGTIPNGTLRGHMAKQNPQAKALMEALAAQQQQTGNNTSLELEDEVL FT VLFTSEHHHYVTPKFYTETKPATGKVVPTWNYAAAQAYGKIRVYCDSKSEETGTFLQKA FT VEDLTKQSEGSIMGYTGTEGRPGPWKVSDAPVPYVEILKKNIIGIEIRIERLQGKFKMS FT QEMGKGDREGVVSGFEALESDVGKGVAQMVRERGEIKDAQK" FT mRNA complement(<348721..>349512) FT /locus_tag="An04g04710" FT CDS join(350279..350434,350502..351530) FT /locus_tag="An04g04720" FT /EC_number="4.4.1.1" FT /note="Catalytic activity: L-cystathionine + H2O = FT L-cysteine + NH3 + 2-oxobutanoate." FT /note="Pathway: methionine metabolism; cysteine metabolism; FT selenoamino acid metabolism; nitrogen metabolism." FT /note="Remark: CYS3 is the structural gene for FT gamma-CTLase." FT /note="Similarity: similarity to other cystathionine FT gamma-lyases." FT /note="Title: strong similarity to cystathionine FT gamma-lyase - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIU2" FT /db_xref="InterPro:IPR015422" FT /db_xref="UniProtKB/TrEMBL:A2QIU2" FT /citation=[27] FT /citation=[30] FT /inference="profile:COGS:COG0626" FT /inference="profile:PFAM:PF01053" FT /protein_id="CAK38736.1" FT /translation="MAPSNLHHPSTRALHADDHLNRVTDVAPPIHLSTTFRFPDNPDDL FT IPSVDPVEEFDGKNYIYSREFAPNATRFEAVVSSLLNGRAISYSTGLAALQAALVLLNP FT RRISVGEGYHGSHEVISVVSRLSGLQKLPLDCPADALDKGDVILLETPVNPLGTSFSID FT EFAKKAHSRGAYLVVDSTFGPPGLQDPFRWGADLVLHSGSKYFGGHSDLLCGVLATQRK FT DWEKQLLEDRIALGNVIGNLEAWLGLRSLRTLEVRVQRASQGCGSLVSWLHKALSTPST FT AAGSDEQIVQSVVKKIYHTSLQEEPWIQEQMPNGFGPVFSIVLQSEKYAQRLPSKLAFF FT QHATSLGGVESLIEWRALSDSRVDWKLLRLSIGLENWVDLKNDLLEGFKALLQE" FT mRNA join(<350279..350434,350502..>351530) FT /locus_tag="An04g04720" FT exon 350279..350434 FT /locus_tag="An04g04720" FT /number=1 FT intron 350435..350501 FT /locus_tag="An04g04720" FT /number=1 FT exon 350502..351530 FT /locus_tag="An04g04720" FT /number=2 FT exon 353081..355774 FT /locus_tag="An04g04730" FT /number=1 FT CDS 353081..355774 FT /locus_tag="An04g04730" FT /note="Title: weak similarity to retinitis pigmentosa FT GTPase regulator-like protein RPGR - Takifugu rubripes" FT /db_xref="UniProtKB/TrEMBL:A2QIU3" FT /citation=[70] FT /protein_id="CAK38737.1" FT /translation="MAYNAVSQADHEVASNATDSDHSRSPSPHSQHNGHFQQLPLDADH FT IGAGSYLQPAKSNEDSGVKRLGSMIRSMTSTSYDIVEEDDYELPADPSADQSSNSPRYV FT PPLRTVPQTSSTTTTATDAHTPEPALRTPVTDQPVPLSHPTPDLQSLQGAYINNVERLE FT RSAERMSLSSNIGDEIRKMDQEQKRRSSSASNSTHASNYDGLKTSLSSRHGSIQSSRLA FT QVAEHAPTRFYGDSTTRVPAMPYLPPPPAPAAHSEHDFVQQDYYDQELGEELERTYTAA FT STDTYQQARVLFNDFDGVHYVPNENHLGRRVSLTRPPLASRSEAYKEPQAGENMVYYPA FT PVPRMLNLPPRLSQKNDQPRGKRRSQLLGVLAAKNRKSTQLAAGQDLGDGSESSHNNQP FT TSVPPQLRASMFFEQPARAVDVEVTQASAVATLDNILDASTTAPVSAFTGQLDPKGFSQ FT ASRKLSSRDLTEQRKTLNSTSMLGLDHRLSDPDLKDVPLGSSRLHNQTEGEAADVHEGT FT SLRDDNQDALGGPDAPEADGEEHNHEEPEADFTGPPNTLLAELEYRKSELKQRLRSAPE FT TTALHSTLLQLEAVAQKQSEHRRQRPVTLAWEAPDAHPQEGDDDDDVPLGMLFPDKANA FT VTEVRPLGLVERRELEESEPLSRRRARLRGEPAPRSPERRPATMYSTGAPDSQPQEDSG FT DEGETLAQRLKRLKEKDQPSAPADSDFANEILAEIKQVGDDEEATQEKETPPEDETLAQ FT RRARLQKEAEAEARQNSTLKIPRYRRSMADILHARRPTTVGRQSTMRTAAPQPMPQRTL FT DHRMSLQQFPSNYGPMPGAGYAQYQGPAGTVPYGPGMVHPNTFYSDALLGMNHLSYAVP FT PKAKMVRPVNEPGQREIIDRWRQSIV" FT mRNA <353081..>355774 FT /locus_tag="An04g04730" FT exon 356742..359870 FT /locus_tag="An04g04740" FT /number=1 FT CDS 356742..359870 FT /locus_tag="An04g04740" FT /note="Function: MUC1 of yeast is a cell surface flocculin FT involved in pseudohyphal differentiation and invasive FT growth in response to nitrogen starvation." FT /note="Localization: MUC1 of yeast is thought to be an FT integral membrane protein." FT /note="Phenotype: deletion of MUC1 in yeast abolishes FT pseudohyphal differentiation and invasive growth." FT /note="Remark: MUC1 of yeast is a component of a signal FT transduction pathway downstream of MEP2 regulating FT pseudohyphal differentiation and invasive growth." FT /note="Remark: MUC1 of yeast is also known as FLO11, STA4 FT and has a systematic name of YIR019C." FT /note="Remark: there are no hints for any MUC1 FT 1,4-alpha-glucosidase activity in the literature." FT /note="Similarity: blast hits result from repetitive FT stretches in the sequence." FT /note="Title: weak similarity to mucin-like protein Muc1 FT -Saccharomyces cerevisiae" FT /db_xref="UniProtKB/TrEMBL:A2QIU4" FT /citation=[34] FT /citation=[48] FT /citation=[55] FT /citation=[77] FT /protein_id="CAK38738.1" FT /translation="MPPSTVFAYWRREHRRSSASPVSPSLQPTSKAPVTSNPPQLPGLS FT STRPNNLTALGASSVESSSPQVPNNPHEDYYDATKKTIAVSVAPANAPGSSSANLAIPS FT SSSDSHTRPLSISDEQDVTTTTSQSNYSQSSIAPPRSDQSDGDSPKPSSPFRLSLGKSL FT LNSHNLTSDHYNKRSSTPGLSSSGHFRFRTSPDISPGDRMALSHKDKDKEYKYEGAGNR FT RSADRDGSSEQAHHKSGRTRLHLLNPMSLLARRRSSNLASLRTEDTRVGARNIVPAIPD FT DYDPRIRGNIVHDFSAPRPRRNLSTAPVLMHDVNNQSSSADVTYNGTGNFAHGNDQSAQ FT SGEQRKRHTQYSPVFREHFEDDQKVLQVESKAYLQSSLLTAQTNAENDPHTLPVFARKL FT PSKIPEQEVSPEVPSDQTTLKQDSQHSPPNNSRELAQEDTDTIEVIPHQPSGLPKHLKS FT NASRFSFDMNGVESSAQEKLLEEKHKEKEAARRAKARMEGTSFSDGEDDFDEDLLDDMD FT DLEEKIPGVNVDADEDDDFSGFSGPGNALNKPWLAPELSPIIASPLPTGSTNSQNVQEL FT AQGPLAGISAPLPVSDPAVSDVTTNFQALSVATIAPNNAPQVAMGSHPPAPQPIEDDDD FT LYFDDGEFGDLSTEDMGEKFDESIFDDETSHLYERKPVVQQPVPAPVPPPDNGTGSTNP FT LDVTAEHDEFTPEPDYDGGLRHVPSMASDYRKGSIRVYGQTRESLANLGSAKAQGGVLS FT EHNLEAFHNALAKAASEAAASDRFGREASISEQSLGQESTAQTMDTPSGLVSDDSRLSQ FT TVDMAAFEEVFEDFSYDDNDDALFDDPIIAAANAEALENDDEGFYGQEFGFYAQAHGGC FT NGELTNGGYFGPRGVEGVNRSFSSRGKFREPSLTPITERSEWSTRNSVISLTAHGAAHS FT NPIASPGLAQLVDLGAMDDEMSLSALMKLRRGAWGGSNGSLRSSSGSPPLLHSTSNRAS FT FISDASPTVYTAPPDAFGGSATESPIRESDKFRWSLNNTEQRVGQSAAGEREP" FT mRNA <356742..>359870 FT /locus_tag="An04g04740" FT CDS join(361215..361418,361524..363574,363625..363998, FT 364053..364591) FT /locus_tag="An04g04750" FT /EC_number="1.2.4.2" FT /note="Catalytic activity: 2-oxoglutarate + lipoamide = FT S-succinyldihydrolipoamide + CO2." FT /note="Function: the 2-oxoglutarate dehydrogenase complex FT catalyzes the overall conversion of 2-oxoglutarate to FT succinyl-Coa & CO(2). it contains multiple copies of 3 FT enzymatic components: 2-oxoglutarate dehydrogenase FT (E1),dihydrolipoamide succinyltransferase (E2) and FT lipoamide dehydrogenase (E3)." FT /note="Pathway: citrate cycle (TCA cycle); lysine FT degradation; tryptophan metabolism." FT /note="Similarity: similarity to other oxoglutarate FT dehydrogenases." FT /note="Title: strong similarity to oxoglutarate FT dehydrogenase (lipoamide) Kgd1 - Saccharomyces cerevisiae" FT /db_xref="GOA:A2QIU5" FT /db_xref="InterPro:IPR011603" FT /db_xref="UniProtKB/TrEMBL:A2QIU5" FT /citation=[10] FT /citation=[12] FT /citation=[26] FT /inference="profile:COGS:COG0567" FT /inference="profile:PFAM:PF00676" FT /inference="profile:PFAM:PF02779" FT /inference="similar to AA sequence:PIR:DEBY" FT /protein_id="CAK38739.1" FT /translation="MFRSTAVKATSGLRSPACSSCRRSLSLASTARSAANRSSKLGLTT FT RRPLALVDRLSNKRHYAAPAEGVDANDSFLSGNTANYVDEMYVAWKRDPSSVHISWQTY FT FKNMEEGNMPVSQAFQPPPTLVPTPTGGVPQEMPGAGLSFAAGTDVTNHLKVQLLVRAY FT QARGHHKAKIDPLGIRGEAEAFGYNKPKELELDHYGFTERDLDQEFNLGPGILPRFATE FT GRKKMTLREIISTCEKIYCGSYGVEYIHIPDRKPCDWIRDRFEVPEPYKYSVDDKRRIL FT DRLIWSHSFESFLATKFPNDKRFGLEGCETLVPGMKALIDRSVDYGIKDIVIGMPHRGR FT LNVLSNVVRKPNESIFSEFAGSAEPSDEGSGDVKYHLGMNFERPTPSGKRVQLSLVANP FT SHLEAEDPVVLGKTRSIQHYNKDEQNFDSAMGVLLHGDAAFAAQGIVYETMGFHSLPAY FT STGGTIHIVVNNQIGFTTDPRFARSTPYCSDIAKSIDAPVFHVNADDVEAVNYVCQVAA FT DWRAEFKRDVVIDIVCYRKQGHNETDQPSFTQPLMYKRIAQQKSQLDKYVNKLIEEGTF FT TKEDIDEHKKWVWGMLNDSFDRSKDYQPTSKEWLTSAWNGFKTPKELATEVLPHLPTGV FT EGPLLKDVADKISGGGSPEGFTLHKNLKRILANRKKAVDEGQGIDWATAEALAFGSLVS FT EGYHVRVSGQDVERGTFSQRHAVLHDQENEGTYTPLQNISENQGSFVISNSSLSEFGAL FT GFEYGYSLTSPNALVMWEAQFGDFANNAQCIIDQFIAAGESKWLQRSGLVVSLPHGYDG FT QGPEHSSGRMERWLQLCNEEPRVFPEGDKLDRQHQDCNMQIVCMTSPANLFHVLRRQIH FT RQFRKPLVIFFSKSLLRHPLARSDIESFTGDSHFQWIIPDPAHGKEIDEPEKIERVILC FT SGQVYAALTKHREAHGIRNTAITRVEQLHPFPWAQLKENLDSYPNARNIVWAQEEPLNA FT GAWSYTQPRIETLLNETEHHNRRHVLYAGRAPSASVATGLKSVHLKEEQEFLQDAFTVH FT QERLKGE" FT mRNA join(<361215..361418,361524..363574,363625..363998, FT 364053..>364591) FT /locus_tag="An04g04750" FT exon 361215..361418 FT /locus_tag="An04g04750" FT /number=1 FT intron 361419..361523 FT /locus_tag="An04g04750" FT /number=1 FT exon 361524..363574 FT /locus_tag="An04g04750" FT /number=2 FT intron 363575..363624 FT /locus_tag="An04g04750" FT /number=2 FT exon 363625..363998 FT /locus_tag="An04g04750" FT /number=3 FT intron 363999..364052 FT /locus_tag="An04g04750" FT /number=3 FT exon 364053..364591 FT /locus_tag="An04g04750" FT /number=4 FT tRNA 364953..365025 FT /gene="tRNA-Phe (GAA)" FT /locus_tag="An04e04760" FT /product="transfer RNA-Phe (GAA)" FT /inference="profile:tRNAscan:1.4" FT CDS join(365405..365755,365867..366537,366588..366793, FT 366851..367405,367468..367526) FT /locus_tag="An04g04770" FT /note="Title: similarity to hypothetical protein CG6632 FT -Drosophila melanogaster" FT /db_xref="GOA:A2QIU6" FT /db_xref="InterPro:IPR019787" FT /db_xref="UniProtKB/TrEMBL:A2QIU6" FT /inference="profile:COGS:COG5034" FT /inference="profile:PFAM:PF00628" FT /inference="similar to AA sequence:UniProtKB:AE003509.26" FT /protein_id="CAK38740.1" FT /translation="MSAVASSAVNSQGQSARQSTRQTRTNPSRTSKTLGRSSFAYGHGS FT MTDTPSATPVAHGFYPALTHFTDAITALPREFRRHNSLLKEVDAKAWALEDNLLQLLKS FT ASESQPVPYPSTPIPESQESKDRRILFHRVRHTLTDLMMTADEKNHVISNANDELDRQL FT TRLDSIFPFIAGEISDEARLGSLTHWAYTNRNAPKTNTNERPRREAASTKELAHAIHEA FT EAASRSEARREAVIARRQRRTHADSDLDDVRAGGARKGQSSKSRGGAGAGDQAGHGQGN FT TGSGQAKRRKVERPPPVEAGAAMERTASSASTSRQAASKDPAEATKKRRAPNANAAARK FT RNNTNASAVDSPVLAPSPVVAAAAIPRSAVSPGPGAVRPQTSRAQQNSGQANNGRQRPS FT SSASNRVTSNGKATEPKTTTKETTSKTEATPTSNPDTQRETEEPTADISKLPPPISTKR FT EDTDGKPAPSIEPGEVPVPPVSNPPPKGRSSKTSTPVLPTFSEPTQRVRPTRSTDPAPA FT KRSHKKTTSVPVVQARAVSEEEESLHEGDDEDEDGEPRYCYCNEISFGEMVACDNDACP FT REWFHLSCVGLTKPPGKNVKWYCNECKESMRRSRSGR" FT mRNA join(<365405..365755,365867..366537,366588..366793, FT 366851..367405,367468..>367526) FT /locus_tag="An04g04770" FT exon 365405..365755 FT /locus_tag="An04g04770" FT /number=1 FT intron 365756..365866 FT /locus_tag="An04g04770" FT /number=1 FT exon 365867..366537 FT /locus_tag="An04g04770" FT /number=2 FT intron 366538..366587 FT /locus_tag="An04g04770" FT /number=2 FT exon 366588..366793 FT /locus_tag="An04g04770" FT /number=3 FT intron 366794..366850 FT /locus_tag="An04g04770" FT /number=3 FT exon 366851..367405 FT /locus_tag="An04g04770" FT /number=4 FT intron 367406..367467 FT /locus_tag="An04g04770" FT /number=4 FT |