Reviewed, UniProtKB/Swiss-Prot Q97JS8 (DNLJ1_CLOAB)

Names and origin

Protein names

Recommended name:
    DNA ligase 1
    EC=6.5.1.2
Alternative name(s):
    Polydeoxyribonucleotide synthase [NAD+] 1

Gene names

Name:	ligA1
Ordered Locus Names:	CA_C1195

Organism

Clostridium acetobutylicum [Complete proteome] [HAMAP]

Taxonomic identifier

1488 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	663 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	NAD+ + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + nicotinamide nucleotide + (deoxyribonucleotide)(n+m). HAMAP MF_01588
Cofactor	Magnesium or manganese By similarity.
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 – 663	663	DNA ligase 1 HAMAP MF_01588		PRO_0000313192
Regions
	Domain	583 – 663	81	BRCT
	Nucleotide binding	28 – 32	5	NAD By similarity
	Nucleotide binding	76 – 77	2	NAD By similarity
Sites
	Active site	118	1	N6-AMP-lysine intermediate By similarity
	Metal binding	403	1	Zinc By similarity
	Metal binding	406	1	Zinc By similarity
	Metal binding	419	1	Zinc By similarity
	Metal binding	425	1	Zinc By similarity
	Binding site	139	1	NAD By similarity
	Binding site	173	1	NAD By similarity
	Binding site	310	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q97JS8-1 [UniParc]. Last modified October 1, 2001. Version 1. Checksum: BB72425E32CC6959	FASTA	663	75,209
	10 20 30 40 50 60 MKLIEDLIEK LNKYSYSYYV LDNPIVADKE YDIMYDELKR LEEETEYINP NSPTQRVGDI 70 80 90 100 110 120 ILDKFEKTHH KNKLWSLDKA QKKDEVKAFV NKCVKFVEQY NLTHSEKLPS PQFVVTQKLD 130 140 150 160 170 180 GLTINCSYNE SRLIKSATRG TGEIGEDITE QSKTILNLPN AINYSGEIDV HGEALMTKNA 190 200 210 220 230 240 LEQYNSNLKV NETPLKNLRN GAAGALRNLN IKETARRKLV AQFYDLSYTD KKLKKYSEIL 250 260 270 280 290 300 LFLKSQGFNI TEYNICNNFD EINQAIDNIG EVRSSLQYDI DGVVIRLNDI ETSRLMGYTI 310 320 330 340 350 360 KCPKYAIAYK FKAKETTTKL IDVEWNVGRS GRINPTAILE PVELAGVIVK RATLNNMDDI 370 380 390 400 410 420 KRKKIKKGAR VFLRRSNDVI PEIMGVTEET EGETKEIEAP TICPYCGSEI VKEGVHLFCE 430 440 450 460 470 480 NTLSCKPQMV KSIVHFASRK AMNIEGFSEK TAEQLFEKLN IKSISDLYRI TKEELMSLDK 490 500 510 520 530 540 FKDKKASNLI NAIEKSKECD LDSFVYSLGI PNVGKKTATD LCKQFKSFEN IKKASYFELI 550 560 570 580 590 600 LVQDIGSIVA KSIVDFFKQE KIEKSLNELF KLGVKPSYEE SEVSESVFND KTVVATGSLQ 610 620 630 640 650 660 NYSRTEIKEK LESLGAKVAG SVSKKTDYVI AGENAGSKYD KAVALGVKIL TEEKFEELIE SVK

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
EMBLGenBankDDBJ	AE001437 Genomic DNA. Translation: AAK79167.1.
PIR	D97047.
RefSeq	NP_347827.1.
3D structure databases
HSSP	HSSP built from PDB template 1L7B based on UniProtKB P26996.
ModBase	Search...
Genome annotation databases
GeneID	1117378.
GenomeReviews	Gene locus CA_C1195 in contig AE001437_GR.
KEGG	cac:CAC1195.
NMPDR	fig|272562.1.peg.1356.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q97JS8.
OMA	GERITAN.
Enzyme and pathway databases
BioCyc	CACE272562:CAC1195-MON.
BRENDA	6.5.1.2. 2866.
Family and domain databases
HAMAP	MF_01588. [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. 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.
ProDom	PD003944. DNAligase. 1 hit. [Graphical view] [Entries sharing at least one domain]
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

DNLJ1_CLOAB

Accession

Primary (citable) accession number: Q97JS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 1, 2001
Last modified:	November 3, 2009
This is version 54 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)