Reviewed, UniProtKB/Swiss-Prot Q2INT9 (DNLJ_ANADE)

Names and origin

Protein names

Recommended name:
    DNA ligase
    EC=6.5.1.2
Alternative name(s):
    Polydeoxyribonucleotide synthase [NAD+]

Gene names

Name:	ligA
Ordered Locus Names:	Adeh_0693

Organism

Anaeromyxobacter dehalogenans (strain 2CP-C) [Complete proteome] [HAMAP]

Taxonomic identifier

290397 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Deltaproteobacteria › Myxococcales › Cystobacterineae › Myxococcaceae › Anaeromyxobacter

Protein attributes

Sequence length	687 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA By similarity. HAMAP MF_01588
Catalytic activity	NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588
Cofactor	Magnesium or manganese By similarity. HAMAP MF_01588
Sequence similarities	Belongs to the NAD-dependent DNA ligase family. LigA subfamily. Contains 1 BRCT domain.

Ontologies

Keywords
Biological process	DNA damage DNA repair DNA replication
Ligand	Magnesium Manganese Metal-binding NAD Zinc
Molecular function	Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW DNA replication Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: InterPro DNA ligase (NAD+) activity Inferred from electronic annotation. Source: HAMAP magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 687	687	DNA ligase HAMAP MF_01588		PRO_0000313111
Regions
	Domain	609 – 687	79	BRCT
	Nucleotide binding	34 – 38	5	NAD By similarity
	Nucleotide binding	83 – 84	2	NAD By similarity
Sites
	Active site	119	1	N6-AMP-lysine intermediate By similarity
	Metal binding	416	1	Zinc By similarity
	Metal binding	419	1	Zinc By similarity
	Metal binding	434	1	Zinc By similarity
	Metal binding	439	1	Zinc By similarity
	Binding site	117	1	NAD By similarity
	Binding site	140	1	NAD By similarity
	Binding site	182	1	NAD By similarity
	Binding site	298	1	NAD By similarity
	Binding site	322	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q2INT9-1 [UniParc]. Last modified March 7, 2006. Version 1. Checksum: E65AAA74C69A1EDF	FASTA	687	76,280
	10 20 30 40 50 60 MKKADAAARA RDLRERIRAA DHAYYVLDQP VLADAEYDRL MHELQAIEAE HPELVTADSP 70 80 90 100 110 120 TQRVSGAPSE RFERVVHREP MLSLGNVQSD DELHEFDARV RRLLGLPEGE AVGYVVEPKL 130 140 150 160 170 180 DGLAVELVYR DGAFTGGSTR GDGVNGEDVT ANLRVVGGLG ANRGVPHALE GTPPPRVEVR 190 200 210 220 230 240 GEVLLFKEHF EAMNRQLVRA GDEPFANPRN AAAGTLRQLD WRVTARRPLS FVAYEALVPG 250 260 270 280 290 300 GDPWRTHWEK LEALAAWGFE TNPENRRCRG LGEVLAYRDR MAERRFELPY DTDGIVVKVD 310 320 330 340 350 360 DLDWRRRLGA ASKFPRWAVA FKYPPQEEAT RIRRIWASVG RTGVLTPVVD FDPVRLSGAM 370 380 390 400 410 420 VARATLHNED EMRRKDILEG DWVLVRRAGE VIPEVVKPLP ERRTGEERPF RFPAECPVCG 430 440 450 460 470 480 ARVVREEGEK VYRCTGAACP AQLVGRICHF AQRRALDIEG LGEKLAAGLV ERGQVKDFAD 490 500 510 520 530 540 LYAVPFEVWQ QLFSRPRKEQ DAGAARELPE KSAQNMVAAL ERSRSTTLRR FLFALGIPQV 550 560 570 580 590 600 GEATAATLAR HFGDLARILD ADEEALKGVR DVGPETASEI RAWTQEPQNR RVVERLLAAG 610 620 630 640 650 660 VRPEPEVVEA RGPFAGKTVV LTGGLSAMSR DDAKAEVERR GGKVSGSVSR KTDLVVAGEE 670 680 AGSKLEKARS LGVRVVGEEE FVRLLKE

References

[1]

"Complete sequence of Anaeromyxobacter dehalogenans 2CP-C." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. , Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S., Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000251 Genomic DNA. Translation: ABC80469.1.
RefSeq	YP_463906.1.
3D structure databases
SMR	Q2INT9. Positions 3-326, 5-604, 598-687.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2INT9.
Genome annotation databases
GeneID	3886813.
GenomeReviews	Gene locus Adeh_0693 in contig CP000251_GR.
KEGG	ade:Adeh_0693.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0272.
HOGENOM	HBG620317.
OMA	IKHFASR.
PhylomeDB	Q2INT9.
Enzyme and pathway databases
BioCyc	ADEH290397:ADEH_0693-MONOMER.
Family and domain databases
HAMAP	MF_01588. DNA_ligase_A. [Tree]
InterPro	IPR001357. BRCT. IPR018239. DNA_ligase_AS. IPR004150. DNA_ligase_OB. IPR001679. DNAligase. IPR013839. DNAligase_adenylation. IPR013840. DNAligase_N. IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR010994. RuvA_2-like. IPR004149. Znf_DNAligase_C4. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF00533. BRCT. 1 hit. PF01653. DNA_ligase_aden. 1 hit. PF03120. DNA_ligase_OB. 1 hit. PF03119. DNA_ligase_ZBD. 1 hit. [Graphical view]
PIRSF	PIRSF001604. LigA. 1 hit.
SMART	SM00292. BRCT. 1 hit. SM00278. HhH1. 3 hits. SM00532. LIGANc. 1 hit. [Graphical view]
TIGRFAMs	TIGR00575. dnlj. 1 hit.
PROSITE	PS50172. BRCT. 1 hit. PS01055. DNA_LIGASE_N1. 1 hit. PS01056. DNA_LIGASE_N2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ_ANADE

Accession

Primary (citable) accession number: Q2INT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	March 7, 2006
Last modified:	February 9, 2010
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)