InterPro : IPR014001

Name  Helicase superfamily 1/2, ATP-binding domain Short Name  Helicase_ATP-bd
Type  Domain Description  Helicases have been classified in 5 superfamilies (SF1-SF5). All of theproteins bind ATP and, consequently, all of them carry the classical Walker A(phosphate-binding loop or P-loop) and Walker B(Mg2+-binding aspartic acid) motifs. For the two largest groups, commonlyreferred to as SF1 and SF2, a total of seven characteristic motifs has beenidentified []. These two superfamilies encompass a large number of DNA and RNA helicases from archaea, eubacteria, eukaryotes and viruses that seem to be active as monomers or dimers. RNA and DNA helicases are considered to be enzymes that catalyse the separation of double-stranded nucleic acids in an energy-dependent manner [].The various structures of SF1 and SF2 helicases present a common core with two alpha-beta RecA-like domains [, ]. Thestructural homology with the RecA recombination protein covers the fivecontiguous parallel beta strands and the tandem alpha helices. ATP binds tothe amino proximal alpha-beta domain, where the Walker A (motif I) and WalkerB (motif II) are found. The N-terminal domain also contains motif III (S-A-T)which was proposed to participate in linking ATPase and helicase activities.The carboxy-terminal alpha-beta domain is structurally very similar to theproximal one even though it is bereft of an ATP-binding site, suggesting thatit may have originally arisen through gene duplication of the first one.This entry represents the DNA-binding domain of classical SF1 and SF2 helicases.
Paste the following link
 Feedback
  Feedback
Object Class
Object ID
Category
Your name:
Your email address:
Lab
Institute
Subject:
Message:
* Evidence
* Attachment size limit is 10 MB
Lists
This ProteinDomain isn't in any lists. Upload a list.

Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

3 Child Features

Id Name Short Name Type
IPR011545 DEAD/DEAH box helicase domain DEAD/DEAH_box_helicase_dom Domain
IPR006935 Helicase/UvrB domain Helicase/UvrB_dom Domain
IPR011492 DEADbox, Flavivirus DEAD_Flavivir Domain

4 Contains

Id Name Short Name Type
IPR010614 DEAD2 DEAD_2 Domain
IPR002464 DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site DNA/RNA_helicase_DEAH_CS Conserved_site
IPR000629 ATP-dependent RNA helicase DEAD-box, conserved site RNA-helicase_DEAD-box_CS Conserved_site
IPR014013 Helicase, superfamily 1/2, ATP-binding domain, DinG/Rad3-type Helic_SF1/SF2_ATP-bd_DinG/Rad3 Domain

14 Found In

Id Name Short Name Type
IPR000330 SNF2-related SNF2_N Domain
IPR004589 DNA helicase, ATP-dependent, RecQ type DNA_helicase_ATP-dep_RecQ Family
IPR004483 Helicase SMUBP-2/Hcs1-like SMUBP-2/Hcs1_like Family
IPR004807 UvrABC system, subunit B UvrB Family
IPR003450 Replication origin-binding protein Replication_origin-bd Domain
IPR006310 DnaQ exonuclease/DinG helicase, predicted DnaQ_DinG Family
IPR006474 Helicase Cas3, CRISPR-associated, core Helicase_Cas3_CRISPR-ass_core Domain
IPR022307 DEAD/DEAH-box helicase, putative, actinobacteria Helicase_put_actinobac Family
IPR006293 DNA helicase, ATP-dependent, RecQ type, bacterial DNA_helicase_ATP-dep_RecQ_bac Family
IPR004473 Restriction endonuclease, type I, HsdR Restrct_endonuc_typeI_HsdR Family
IPR010222 RNA helicase, ATP-dependent DEAH box, HrpA-type RNA_helicase_ATP-dep_DEAH_HrpA Family
IPR010225 RNA helicase, ATP-dependent DEAH box, HrpB-type RNA_helicase_ATP-dep_DEAH_HrpB Family
IPR017575 CRISPR-associated helicase, CYANO-type CRISPR-assoc_helicase_CYANO Family
IPR017548 CRISPR-associated DEAD/DEAH-box helicase Csf4 CRISPR-assoc_helicase_Csf4 Family

0 Parent Features

3 Publications

First Author Title Year Journal Volume Pages
Gorbalenya AE Two related superfamilies of putative helicases involved in replication, recombination, repair and expression of DNA and RNA genomes. 1989 Nucleic Acids Res 17 4713-30
Caruthers JM Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase. 2000 Proc Natl Acad Sci U S A 97 13080-5
Caruthers JM Helicase structure and mechanism. 2002 Curr Opin Struct Biol 12 123-33



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)