EC 3.6.4.13 - RNA helicase

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IntEnz Enzyme Nomenclature
EC 3.6.4.13

Names

Accepted name:
RNA helicase
Other names:
CSFV NS3 helicase
DBP2
DbpA
DDX17
DDX25
DDX3
DDX3X
DDX3Y
DDX4
DDX5
DEAD-box protein DED1
DEAD-box RNA helicase
DEAH-box protein 2
DEAH-box RNA helicase
DED1
Dex(H/D) RNA helicase
EhDEAD1
EhDEAD1 RNA helicase
eIF4A helicase
KOKV helicase
Mtr4p
nonstructural protein 3 helicase
NPH-II
RHA
RNA helicase A
RNA helicase DDX3
RNA helicase Hera
RNA-dependent ATPase
TGBp1 NTPase/helicase domain
VRH1
GRTH/DDX25
Systematic name:
ATP phosphohydrolase (RNA helix unwinding)

Reaction

Comments:

RNA helicases utilize the energy from ATP hydrolysis to unwind RNA. Some of them unwind RNA with a 3' to 5' polarity [3], other show 5' to 3' polarity [8]. Some helicases unwind DNA as well as RNA [7,8]. May be identical with EC 3.6.4.12 (DNA helicase).

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00039 , PROSITE:PDOC51192
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot: (1685) [show] [UniProt]

References

  1. Cordin, O., Tanner, N. K., Doere, M., Linder, P., Banroques, J.
    The newly discovered Q motif of DEAD-box RNA helicases regulates RNA-binding and helicase activity.
    EMBO J. 23: 2478-2487 (2004). [PMID: 15201868]
  2. 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: 283-286 (2007). [PMID: 17401195]
  3. Lee, C. G., Hurwitz, J.
    A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3' to 5' direction.
    J. Biol. Chem. 267: 4398-4407 (1992). [PMID: 1537828]
  4. Li, S. C., Chung, M. C., Chen, C. S.
    Cloning and characterization of a DEAD box RNA helicase from the viable seedlings of aged mung bean.
    Plant Mol. Biol. 47: 761-770 (2001). [PMID: 11785937]
  5. Wu, J., Bera, A. K., Kuhn, R. J., Smith, J. L.
    Structure of the Flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing.
    J. Virol. 79: 10268-10277 (2005). [PMID: 16051820]
  6. Gross, C. H., Shuman, S.
    The nucleoside triphosphatase and helicase activities of vaccinia virus NPH-II are essential for virus replication.
    J. Virol. 72: 4729-4736 (1998). [PMID: 9573237]
  7. Frick, D. N.
    The hepatitis C virus NS3 protein: a model RNA helicase and potential drug target.
    Curr. Issues Mol. Biol. 9: 1-20 (2007). [PMID: 17263143]

[EC 3.6.4.13 created 2009]