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InterPro: IPR004150 NAD-dependent DNA ligase, OB-fold

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UniProtKB

Matches:

1873 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

IPR004150 DNA_ligase_OB

Secondary

IPR001679

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF03120	DNA_ligase_OB	1873
Signatures in BioMart

InterPro Relationships Help

Parent

IPR012340 Nucleic acid-binding, OB-fold

Found in

IPR001679 NAD-dependent DNA ligase
IPR013840 NAD-dependent DNA ligase, N-terminal
IPR020923 DNA ligase B

Contains

IPR018239 NAD-dependent DNA ligase, active site

GO Term annotation Help

Process

GO:0006260 DNA replication
GO:0006281 DNA repair

Function

GO:0003911 DNA ligase (NAD+) activity

InterPro annotation

Entry Details in BioMart

Abstract

DNA ligases catalyse the crucial step of joining the breaks in duplex DNA during DNA replication, repair and recombination, utilizing either ATP or NAD(+) as a cofactor [1]. This family is a small domain found after the adenylation domain DNA_ligase_N in NAD+-dependent ligases (IPR001679). OB-fold domains generally are involved in nucleic acid binding.

Structural links Help

PDB - click here

SCOP: b.40.4.6 , d.142.2.2

CATH: 2.40.50.140 , 3.30.1490.70

Database links Help

Enzyme: EC:6.5.1.2

PANDIT: PF03120

Blocks: IPB004150

Pfam Clan: CL0021.14

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR004150

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2C5E6 DNA ligase

B9LU22 DNA ligase

O87703 DNA ligase

P72588 DNA ligase

Q197A8 Putative DNA ligase 052L

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001679	NAD-dependent DNA ligase
IPR003583	Helix-hairpin-helix DNA-binding motif, class 1
IPR004149	Zinc-finger, NAD-dependent DNA ligase C4-type
IPR010994	RuvA domain 2-like
IPR013839	NAD-dependent DNA ligase, adenylation
IPR004150	NAD-dependent DNA ligase, OB-fold
IPR016027	Nucleic acid-binding, OB-fold-like
IPR012340	Nucleic acid-binding, OB-fold
IPR018239	NAD-dependent DNA ligase, active site
IPR001357	BRCT
IPR013840	NAD-dependent DNA ligase, N-terminal
IPR000445	Helix-hairpin-helix motif
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Open in usermanual
1.	Lee JY, Chang C, Song HK, Moon J, Yang JK, Kim HK, Kwon ST, Suh SW. Crystal structure of NAD(+)-dependent DNA ligase: modular architecture and functional implications. EMBO J. 19 1119-29 2000 [PubMed: 10698952] http://dx.doi.org/10.1093/emboj/19.5.1119

Additional Reading Open in usermanual
	Gajiwala KS, Pinko C. Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal. Structure 12 2004 1449-59 [PubMed: 15296738] http://dx.doi.org/10.1016/j.str.2004.05.017
	Singleton MR, Hakansson K, Timson DJ, Wigley DB. Structure of the adenylation domain of an NAD+-dependent DNA ligase. Structure 7 1999 35-42 [PubMed: 10368271] http://dx.doi.org/10.1016/S0969-2126(99)80007-0

InterPro 23.1