Reviewed, UniProtKB/Swiss-Prot Q97FQ5 (DNLJ2_CLOAB)

Names and origin

Protein names

Recommended name:
    DNA ligase 2
    EC=6.5.1.2
Alternative name(s):
    Polydeoxyribonucleotide synthase [NAD+] 2

Gene names

Name:	ligA2
Ordered Locus Names:	CA_C2673

Organism

Clostridium acetobutylicum [Complete proteome] [HAMAP]

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	669 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 – 669	669	DNA ligase 2 HAMAP MF_01588		PRO_0000313193
Regions
	Domain	590 – 669	80	BRCT
	Nucleotide binding	35 – 39	5	NAD By similarity
	Nucleotide binding	83 – 84	2	NAD By similarity
Sites
	Active site	125	1	N6-AMP-lysine intermediate By similarity
	Metal binding	410	1	Zinc By similarity
	Metal binding	413	1	Zinc By similarity
	Metal binding	426	1	Zinc By similarity
	Metal binding	432	1	Zinc By similarity
	Binding site	147	1	NAD By similarity
	Binding site	181	1	NAD By similarity
	Binding site	317	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97FQ5-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: A4A4C9CAB72767DF	FASTA	669	75,901
	10 20 30 40 50 60 MNEKESNILR MQELIEELNK YSYSYYVLDN PIVADKEYDK RYDELVELEE KTGITYPYSP 70 80 90 100 110 120 TNRVGDVILK QFQKYTHKSR LWSLDKAQSF EEIIDWHNRN KKAVAEYNSN HEDKLPELKY 130 140 150 160 170 180 VLTKKFDGLT INCTYDESGV MIKAATRGTG VIGEDITSQA KTIKSIPLKI KNGSVVEVHG 190 200 210 220 230 240 EAIMTKTAFN EYNKKAEVPL KNLRNGAAGA LRNLNVRETA RRNLSAFFYD VGYNEGKAFK 250 260 270 280 290 300 SYMEMMNFIK EMGFPVDEYL KECNTIEEIN KEIQYVGDIR SSLDYDIDGV VIVIDDYRTR 310 320 330 340 350 360 EYLGYTVKFP KWAIAYKFEA EEATTKLLDV EWNVGRSGRV SPTAILEPVE LAGVIVKRAT 370 380 390 400 410 420 LNNMDDIGRK KVKIGSRVFV RRSNDVIPEI MGVTEETEGE TNEIEAPTIC PYCGSEIVKE 430 440 450 460 470 480 GVHLFCENTL SCKPQMVKSI VHFASREAMN IEGFSEKTAE QLFEKLNIKS ISDLYRITKE 490 500 510 520 530 540 ELMSLDKFKD KKASNLINAI EKSKKCDLAS FVYSLGIPNV GKKTATDLCK QFKSFENIKK 550 560 570 580 590 600 ASYDELILVQ DIGSIVAESI VEFFKQEKIE KSLNELFELG VTPFYEESEV VENAFTGKTV 610 620 630 640 650 660 VATGTLQNYS RTAIKEKLES LGANVAGSVS KKTDYVIAGE NAGSKYDKAV QLGVKILTEE EFEQLINNM

References

[1]

"Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum." Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V., Smith D.R. J. Bacteriol. 183:4823-4838(2001) [PubMed: 11466286] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE001437 Genomic DNA. Translation: AAK80620.1.
PIR	A97229.
RefSeq	NP_349280.1.
3D structure databases
HSSP	HSSP built from PDB template 1L7B based on UniProtKB P26996.
SMR	Q97FQ5. Positions 8-321, 592-668.
ModBase	Search...
Genome annotation databases
GeneID	1118856.
GenomeReviews	Gene locus CA_C2673 in contig AE001437_GR.
KEGG	cac:CAC2673.
NMPDR	fig|272562.1.peg.2809.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG620317.
OMA	IKHFASR.
Enzyme and pathway databases
BioCyc	CACE272562:CAC2673-MONOMER.
BRENDA	6.5.1.2. 2866.
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. False negative. PS01056. DNA_LIGASE_N2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ2_CLOAB

Accession

Primary (citable) accession number: Q97FQ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 1, 2001
Last modified:	February 9, 2010
This is version 58 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)