Reviewed, UniProtKB/Swiss-Prot A6VR16 (DNLJ_ACTSZ)

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:	Asuc_2067

Organism

Actinobacillus succinogenes (strain ATCC 55618 / 130Z) [Complete proteome] [HAMAP]

Taxonomic identifier

339671 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Actinobacillus

Protein attributes

Sequence length	672 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 – 672	672	DNA ligase HAMAP MF_01588		PRO_0000340323
Regions
	Domain	592 – 672	81	BRCT
	Nucleotide binding	32 – 36	5	NAD By similarity
	Nucleotide binding	81 – 82	2	NAD By similarity
Sites
	Active site	116	1	N6-AMP-lysine intermediate By similarity
	Metal binding	409	1	Zinc By similarity
	Metal binding	412	1	Zinc By similarity
	Metal binding	427	1	Zinc By similarity
	Metal binding	433	1	Zinc By similarity
	Binding site	114	1	NAD By similarity
	Binding site	137	1	NAD By similarity
	Binding site	174	1	NAD By similarity
	Binding site	291	1	NAD By similarity
	Binding site	315	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A6VR16-1 [UniParc]. Last modified August 21, 2007. Version 1. Checksum: 03C6470823FEE503	FASTA	672	74,733
	10 20 30 40 50 60 MTDIQNQINQ LRNTLRHHEY QYHVLDNPEI PDSEYDRLFH RLKALEQQHP ELISADSPTQ 70 80 90 100 110 120 RVGAKPLAGF AQITHELPML SLDNVFSDEE FYAFVKRIQE RLITLPDNLE FCCEPKLDGL 130 140 150 160 170 180 AVSILYENGR LVQAATRGDG TTGEDITLNI RTIRNIPLQL LTDNPPVRLE VRGEVFMPQE 190 200 210 220 230 240 GFDRLNEAAL ARGEKTFANP RNAAAGSLRQ LDPKITSQRP LVWNAYSIGI AEGADLPPTH 250 260 270 280 290 300 YERLQWLKSI GIPVNGEIRL CRGAENVLKF YRTIQEKRPE LGYDIDGTVL KVNEIALQER 310 320 330 340 350 360 LGFISKAPRW AIAYKFPAQE EMTVLNDVEF QVGRTGAITP VAKLQPVFVA GVTVSNATLH 370 380 390 400 410 420 NGDEIARLDI AIGDTVIVRR AGDVIPQIIG VVHDRRPPNA EPIIFPTLCP VCHSAIVRIE 430 440 450 460 470 480 GEAVARCTGG LFCDAQRKES LKHFVSRRAM DIDGVGAKLI EQLVDRELIR TPADLFKLDL 490 500 510 520 530 540 ITLMRLERMG EKSAQKALDS LEKAKKTTLA RFIFALGIRE VGEATALNLA NFFKNLTALQ 550 560 570 580 590 600 TADLEQLQAV SDVGEVVANR IYVFWREQHN IDVVNDLIAQ GVHWDDVEEK QVNENPFKEK 610 620 630 640 650 660 TVVLTGTLSQ MGRNEAKALL QQMGAKVAGS VSAKTHIVIA GDSAGSKLSK AQDLGVAVMS 670 EAEFLEIVNS FS

References

[1]

"Complete sequence of Actinobacillus succinogenes 130Z." Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Vieille C., Richardson P. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000746 Genomic DNA. Translation: ABR75413.1.
RefSeq	YP_001345348.1.
3D structure databases
SMR	A6VR16. Positions 1-584, 592-670.
ModBase	Search...
Protein-protein interaction databases
STRING	A6VR16.
Genome annotation databases
GeneID	5347710.
GenomeReviews	Gene locus Asuc_2067 in contig CP000746_GR.
KEGG	asu:Asuc_2067.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0272.
HOGENOM	HBG620317.
OMA	IKHFASR.
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. 4 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_ACTSZ

Accession

Primary (citable) accession number: A6VR16

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	August 21, 2007
Last modified:	February 9, 2010
This is version 23 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)