EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR014001 DEAD-like helicase, N-terminal

Protein matches Help

UniProtKB

Matches:

42724 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR014001 DEAD-like_N

Secondary

IPR001410 , IPR011545

Type

Domain

Signatures Help

Database	ID	Name	Proteins
SMART	SM00487	DEXDc	42724
Signatures in BioMart

InterPro Relationships Help

Parent

IPR014021 Helicase, superfamily 1/2, ATP-binding domain

Children

IPR011492 DEAD box, Flavivirus
IPR011545 DNA/RNA helicase, DEAD/DEAH box type, N-terminal

Found in

IPR000330 SNF2-related
IPR003450 Herpesvirus, replication origin-binding protein
IPR004473 Restriction endonuclease, type I, EcoRI, R subunit
IPR004483 DNA helicase, putative
IPR004589 DNA helicase, ATP-dependent, RecQ type
IPR004807 Excinuclease ABC, B subunit
IPR006293 DNA helicase, ATP-dependent, RecQ type, bacterial
IPR006310 DnaQ exonuclease/DinG helicase
IPR006474 Helicase Cas3, CRISPR-associated, core
IPR006935 Restriction endonuclease, type I, R subunit/Type III, Res subunit
IPR010222 RNA helicase, ATP-dependent DEAH box, HrpA type
IPR010225 RNA helicase, ATP-dependent DEAH box, HrpB type
IPR017548 CRISPR-associated DEAD/DEAH-box helicase Csf4
IPR017575 CRISPR-associated helicase, Cyano-type
IPR018329 DNA helicase, ATP-dependent, RecQ type, N-terminal

Contains

IPR000629 RNA helicase, ATP-dependent, DEAD-box, conserved site
IPR002464 DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site
IPR014013 Helicase, superfamily 1/2, ATP-binding domain, DinG/Rad3-type

InterPro annotation

Entry Details in BioMart

Abstract

This entry is found in 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.

Structural links Help

PDB - click here

SCOP: b.47.1.3 , c.37.1.14 , c.37.1.16 , c.37.1.19 , c.37.1.23

CATH: 2.40.10.10 , 2.40.10.120 , 3.40.50.300

Database links Help

Enzyme: EC:3

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR014001

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

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
IPR018329	DNA helicase, ATP-dependent, RecQ type, N-terminal
IPR004589	DNA helicase, ATP-dependent, RecQ type
IPR014021	Helicase, superfamily 1/2, ATP-binding domain
IPR012337	Polynucleotidyl transferase, ribonuclease H fold
IPR013084	Zinc finger, CCHC retroviral-type
IPR002121	Helicase/RNase D C-terminal, HRDC domain
IPR001650	DNA/RNA helicase, C-terminal
IPR001878	Zinc finger, CCHC-type
IPR002562	3'-5' exonuclease
IPR000629	RNA helicase, ATP-dependent, DEAD-box, conserved site
IPR011545	DNA/RNA helicase, DEAD/DEAH box type, N-terminal
IPR014014	RNA helicase, DEAD-box type, Q motif
IPR014001	DEAD-like helicase, N-terminal
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	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
	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
	Aleshin AE, Shiryaev SA, Strongin AY, Liddington RC. Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci. 16 2007 795-806 [PubMed: 17400917] http://dx.doi.org/10.1110/ps.072753207
	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
	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

InterPro 23.1