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InterPro: IPR001650 DNA/RNA helicase, C-terminal
Protein matches
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UniProtKB Matches: 42251 proteins |
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Accession
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IPR001650 DNA/RNA_helicase_C |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Found in
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IPR000185 SecA protein
IPR004576 Transcription-repair coupling factor
IPR004589 DNA helicase, ATP-dependent, RecQ type
IPR004609 DNA helicase, ATP-dependent, RecG
IPR004807 Excinuclease ABC, B subunit
IPR005259 Primosomal protein n
IPR006293 DNA helicase, ATP-dependent, RecQ type, bacterial
IPR006474 Helicase Cas3, CRISPR-associated, core
IPR010222 RNA helicase, ATP-dependent DEAH box, HrpA type
IPR010225 RNA helicase, ATP-dependent DEAH box, HrpB type
IPR013444 Helicase Cas3, CRISPR-associated, Anaes-subtype
IPR014018 SecA motor DEAD
IPR014412 Genome polyprotein, Flavivirus type
IPR016438 RNA helicase, ATP-dependent, SK12/DOB1
IPR017170 Lhr-like ATP-dependent RNA helicase, predicted
IPR017575 CRISPR-associated helicase, Cyano-type
IPR018329 DNA helicase, ATP-dependent, RecQ type, N-terminal
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GO Term annotation
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Function
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GO:0003676 nucleic acid binding
GO:0004386 helicase activity
GO:0005524 ATP binding
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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The domain, which defines this group of proteins is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase.
The eukaryotic translation initiation factor 4A (eIF4A) is a member of the DEA(D/H)-box RNA helicase family This is a diverse group of proteins that couples an ATPase activity to RNA binding and unwinding. The structure of the carboxyl-terminal domain of eIF4A has been determined to 1.75 A resolution; it has a parallel alpha-beta topology that superimposes, with minor variations, on the structures and conserved motifs of the equivalent domain in other, distantly related helicases [1].
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Structural links
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Database links
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Interactions
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This domain has been experimentally proven to be involved in Protein:Protein interactions. Representative
data is shown with the following
example proteins:
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Example proteins
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O00571 ATP-dependent RNA helicase DDX3X
O01836 ATP-dependent RNA helicase glh-3
O09053 Werner syndrome ATP-dependent helicase homolog
P09052 ATP-dependent RNA helicase vasa
P10081 ATP-dependent RNA helicase eIF4A
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR018982 |
RQC domain |
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| IPR018329 |
DNA helicase, ATP-dependent, RecQ type, N-terminal |
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| IPR004589 |
DNA helicase, ATP-dependent, RecQ type |
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| IPR014021 |
Helicase, superfamily 1/2, ATP-binding domain |
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| IPR012337 |
Polynucleotidyl transferase, ribonuclease H fold |
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| IPR013084 |
Zinc finger, CCHC retroviral-type |
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| IPR002121 |
Helicase/RNase D C-terminal, HRDC domain |
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| IPR001650 |
DNA/RNA helicase, C-terminal |
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| IPR001878 |
Zinc finger, CCHC-type |
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| IPR002562 |
3'-5' exonuclease |
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| IPR000629 |
RNA helicase, ATP-dependent, DEAD-box, conserved site |
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| IPR011545 |
DNA/RNA helicase, DEAD/DEAH box type, N-terminal |
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| IPR014014 |
RNA helicase, DEAD-box type, Q motif |
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| IPR014001 |
DEAD-like helicase, N-terminal |
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PDB Chain |
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ModBase |
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CATH Domain |
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SWISS-MODEL |
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SCOP Domain |
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Additional Reading
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Rodamilans B, Montoya G.
Expression, purification, crystallization and preliminary X-ray diffraction analysis of the DDX3 RNA helicase domain.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 283-6
[PubMed: 17401195]
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Assenmacher N, Wenig K, Lammens A, Hopfner KP.
Structural basis for transcription-coupled repair: the N terminus of Mfd resembles UvrB with degenerate ATPase motifs.
J. Mol. Biol. 355 2006 675-83
[PubMed: 16309703]
http://dx.doi.org/10.1016/j.jmb.2005.10.033
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Truglio JJ, Karakas E, Rhau B, Wang H, DellaVecchia MJ, Van Houten B, Kisker C.
Structural basis for DNA recognition and processing by UvrB.
Nat. Struct. Mol. Biol. 13 2006 360-4
[PubMed: 16532007]
http://dx.doi.org/10.1038/nsmb1072
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Caruthers JM, McKay DB.
Helicase structure and mechanism.
Curr. Opin. Struct. Biol. 12 2002 123-33
[PubMed: 11839499]
http://dx.doi.org/10.1016/S0959-440X(02)00298-1
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Tanner NK, Linder P.
DExD/H box RNA helicases: from generic motors to specific dissociation functions.
Mol. Cell 8 2001 251-62
[PubMed: 11545728]
http://dx.doi.org/10.1016/S1097-2765(01)00329-X
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Gorbalenya AE, Koonin EV, Donchenko AP, Blinov VM.
Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes.
Nucleic Acids Res. 17 1989 4713-30
[PubMed: 2546125]
http://dx.doi.org/10.1093/nar/17.12.4713
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Koonin EV.
Escherichia coli dinG gene encodes a putative DNA helicase related to a group of eukaryotic helicases including Rad3 protein.
Nucleic Acids Res. 21 1993 1497
[PubMed: 8385320]
http://dx.doi.org/10.1093/nar/21.6.1497
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Deaconescu AM, Chambers AL, Smith AJ, Nickels BE, Hochschild A, Savery NJ, Darst SA.
Structural basis for bacterial transcription-coupled DNA repair.
Cell 124 2006 507-20
[PubMed: 16469698]
http://dx.doi.org/10.1016/j.cell.2005.11.045
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Mackintosh SG, Lu JZ, Jordan JB, Harrison MK, Sikora B, Sharma SD, Cameron CE, Raney KD, Sakon J.
Structural and biological identification of residues on the surface of NS3 helicase required for optimal replication of the hepatitis C virus.
J. Biol. Chem. 281 2006 3528-35
[PubMed: 16306038]
http://dx.doi.org/10.1074/jbc.M512100200
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Lillard-Wetherell K, Machwe A, Langland GT, Combs KA, Behbehani GK, Schonberg SA, German J, Turchi JJ, Orren DK, Groden J.
Association and regulation of the BLM helicase by the telomere proteins TRF1 and TRF2.
Hum. Mol. Genet. 13 2004 1919-32
[PubMed: 15229185]
http://dx.doi.org/10.1093/hmg/ddh193
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