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InterPro: IPR012310 ATP dependent DNA ligase, central

Protein matches Help

UniProtKB

Matches:

1755 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

IPR012310 DNA_ligase_A_M

Secondary

IPR000977

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01068	DNA_ligase_A_M	1735
PROSITE profile	PS50160	DNA_LIGASE_A3	1483
Signatures in BioMart

InterPro Relationships Help

Children

IPR001072 Y414

Found in

IPR000977 ATP-dependent DNA ligase
IPR014143 DNA ligase D
IPR014146 DNA polymerase LigD, ligase domain
IPR016306 DNA ligase, bacteriophage

Contains

IPR016059 ATP-dependent DNA ligase, conserved site

GO Term annotation Help

Process

GO:0006260 DNA replication
GO:0006281 DNA repair
GO:0006310 DNA recombination

Function

GO:0003910 DNA ligase (ATP) activity
GO:0005524 ATP binding

InterPro annotation

Entry Details in BioMart

Abstract

This domain belongs to a more diverse superfamily, including catalytic domain of the mRNA capping enzyme (IPR001339) and NAD-dependent DNA ligase (IPR001679) [1].

Structural links Help

PDB - click here

SCOP: b.40.4.6 , d.142.2.1

CATH: 1.10.3260.10 , 2.40.50.140 , 3.30.1490.70 , 3.30.470.30

Database links Help

Enzyme: EC:6.5.1.1

PROSITE doc: PDOC00295

PANDIT: PF01068

Blocks: IPB012310

Pfam Clan: CL0078.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR012310

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P04819 DNA ligase 1

P18858 DNA ligase 1

P37913 DNA ligase 1

Q27474 DNA ligase 1

Q9W1H4 DNA ligase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR012340	Nucleic acid-binding, OB-fold
IPR000977	ATP-dependent DNA ligase
IPR012309	ATP dependent DNA ligase, C-terminal
IPR012308	DNA ligase, N-terminal
IPR012310	ATP dependent DNA ligase, central
IPR016027	Nucleic acid-binding, OB-fold-like
IPR016059	ATP-dependent DNA ligase, conserved site
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Open in usermanual
1.	Subramanya HS, Doherty AJ, Ashford SR, Wigley DB. Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. Cell 85 607-15 1996 [PubMed: 8653795] http://dx.doi.org/10.1016/S0092-8674(00)81260-X

Additional Reading Open in usermanual
	Kletzin A. Molecular characterisation of a DNA ligase gene of the extremely thermophilic archaeon Desulfurolobus ambivalens shows close phylogenetic relationship to eukaryotic ligases. Nucleic Acids Res. 20 1992 5389-96 [PubMed: 1437556] http://dx.doi.org/10.1093/nar/20.20.5389
	Tomkinson AE, Levin DS. Mammalian DNA ligases. Bioessays 19 1997 893-901 [PubMed: 9363683] http://dx.doi.org/10.1002/bies.950191009
	Odell M, Sriskanda V, Shuman S, Nikolov DB. Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining. Mol. Cell 6 2000 1183-93 [PubMed: 11106756] http://dx.doi.org/10.1016/S1097-2765(00)00115-5
	Pascal JM, O'Brien PJ, Tomkinson AE, Ellenberger T. Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature 432 2004 473-8 [PubMed: 15565146] http://dx.doi.org/10.1038/nature03082
	Odell M, Malinina L, Sriskanda V, Teplova M, Shuman S. Analysis of the DNA joining repertoire of Chlorella virus DNA ligase and a new crystal structure of the ligase-adenylate intermediate. Nucleic Acids Res. 31 2003 5090-100 [PubMed: 12930960] http://dx.doi.org/10.1093/nar/gkg665
	Lindahl T, Barnes DE. Mammalian DNA ligases. Annu. Rev. Biochem. 61 1992 251-81 [PubMed: 1497311] http://dx.doi.org/10.1146/annurev.bi.61.070192.001343
	Nair PA, Nandakumar J, Smith P, Odell M, Lima CD, Shuman S. Structural basis for nick recognition by a minimal pluripotent DNA ligase. Nat. Struct. Mol. Biol. 14 2007 770-8 [PubMed: 17618295] http://dx.doi.org/10.1038/nsmb1266
	Tomkinson AE, Totty NF, Ginsburg M, Lindahl T. Location of the active site for enzyme-adenylate formation in DNA ligases. Proc. Natl. Acad. Sci. U.S.A. 88 1991 400-4 [PubMed: 1988940] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1988940
	Aravind L, Koonin EV. Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287 1999 1023-40 [PubMed: 10222208] http://dx.doi.org/10.1006/jmbi.1999.2653

InterPro 23.1