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InterPro: IPR011545 DNA/RNA helicase, DEAD/DEAH box type, N-terminal
Protein matches
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UniProtKB Matches: 22338 proteins |
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Accession
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IPR011545 DNA/RNA_helicase_DEAD/DEAH_N |
Secondary
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IPR001410
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Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR014001 DEAD-like helicase, N-terminal
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Found in
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IPR004576 Transcription-repair coupling factor
IPR004589 DNA helicase, ATP-dependent, RecQ type
IPR004609 DNA helicase, ATP-dependent, RecG
IPR005259 Primosomal protein n
IPR005736 Reverse gyrase
IPR006293 DNA helicase, ATP-dependent, RecQ type, bacterial
IPR016438 RNA helicase, ATP-dependent, SK12/DOB1
IPR017170 Lhr-like ATP-dependent RNA helicase, predicted
IPR018329 DNA helicase, ATP-dependent, RecQ type, N-terminal
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Contains
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IPR000629 RNA helicase, ATP-dependent, DEAD-box, conserved site
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GO Term annotation
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Function
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GO:0003676 nucleic acid binding
GO:0005524 ATP binding
GO:0008026 ATP-dependent helicase activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Members of this family include the DEAD and DEAH box helicases. Helicases are involved in unwinding nucleic acids. The DEAD box helicases are involved in various aspects of RNA metabolism, including nuclear transcription, pre mRNA splicing, ribosome biogenesis, nucleocytoplasmic transport, translation, RNA decay and organellar gene expression.
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Structural links
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Database links
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Pfam Clan: CL0008.22
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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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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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Andersen CB, Ballut L, Johansen JS, Chamieh H, Nielsen KH, Oliveira CL, Pedersen JS, Seraphin B, Le Hir H, Andersen GR.
Structure of the exon junction core complex with a trapped DEAD-box ATPase bound to RNA.
Science 313 2006 1968-72
[PubMed: 16931718]
http://dx.doi.org/10.1126/science.1131981
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Bono F, Ebert J, Lorentzen E, Conti E.
The crystal structure of the exon junction complex reveals how it maintains a stable grip on mRNA.
Cell 126 2006 713-25
[PubMed: 16923391]
http://dx.doi.org/10.1016/j.cell.2006.08.006
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de la Cruz J, Kressler D, Linder P.
Unwinding RNA in Saccharomyces cerevisiae: DEAD-box proteins and related families.
Trends Biochem. Sci. 24 1999 192-8
[PubMed: 10322435]
http://dx.doi.org/10.1016/S0968-0004(99)01376-6
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Matsui T, Hogetsu K, Usukura J, Sato T, Kumasaka T, Akao Y, Tanaka N.
Structural insight of human DEAD-box protein rck/p54 into its substrate recognition with conformational changes.
Genes Cells 11 2006 439-52
[PubMed: 16611246]
http://dx.doi.org/10.1111/j.1365-2443.2006.00951.x
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Aubourg S, Kreis M, Lecharny A.
The DEAD box RNA helicase family in Arabidopsis thaliana.
Nucleic Acids Res. 27 1999 628-36
[PubMed: 9862990]
http://dx.doi.org/10.1093/nar/27.2.628
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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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InterPro 23.1
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