Reviewed, UniProtKB/Swiss-Prot A9NHW0 (DNLJ_ACHLI)

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:	ACL_1348

Organism

Acholeplasma laidlawii (strain PG-8A) [Complete proteome] [HAMAP]

Taxonomic identifier

441768 [NCBI]

Taxonomic lineage

Bacteria › Tenericutes › Mollicutes › Acholeplasmatales › Acholeplasmataceae › Acholeplasma

Protein attributes

Sequence length	659 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 – 659	659	DNA ligase HAMAP MF_01588		PRO_0000340321
Regions
	Domain	581 – 659	79	BRCT
	Nucleotide binding	31 – 35	5	NAD By similarity
	Nucleotide binding	80 – 81	2	NAD By similarity
Sites
	Active site	111	1	N6-AMP-lysine intermediate By similarity
	Metal binding	398	1	Zinc By similarity
	Metal binding	401	1	Zinc By similarity
	Metal binding	416	1	Zinc By similarity
	Metal binding	421	1	Zinc By similarity
	Binding site	109	1	NAD By similarity
	Binding site	132	1	NAD By similarity
	Binding site	166	1	NAD By similarity
	Binding site	281	1	NAD By similarity
	Binding site	305	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9NHW0-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: F908EA25064E7893	FASTA	659	74,009
	10 20 30 40 50 60 MDIQTRIKEL RKQINEANYL YHTKDQPIIS DFVYDGLMRE LIELETKYPE YDDETSPTKK 70 80 90 100 110 120 IGGVVLDAFK KHTHTVPMMS LSNIFNKEEL KVFYDRIQKV IPNTSFTTEL KIDGLAVTLI 130 140 150 160 170 180 YEKGIFKKAA TRGNGVVGED ITENVKTIKT LPLQLSKPLD IEVRGEIYMS HKTFKEVNLE 190 200 210 220 230 240 RANSNLDLFV NPRNAAAGTV RQLDSKVVAK RRLDLFTYTV VGASNFNSTQ KETLEFLSEL 250 260 270 280 290 300 GFPVNPHYKL VDNLDALSDA IDNYDILRKT LPYDTDGVVI KVNQFEHYET IGYTAKYPKY 310 320 330 340 350 360 AGAYKFEAEK QITKVEDIIF QVGRTGVITP VAVLTPVFIS GSLVSRATLH NEDYILNKDI 370 380 390 400 410 420 RIDDQVLVHK AGEIIPEVIE VVLGSRTNQA PFEMVKHCPA CESNLVRKQG EADYYCANDN 430 440 450 460 470 480 CPGKNVFGLI HFASRAAMDI DTLGEKVVEL LHDQTYLQTI PDIYKLHTFK DQLEELPGFG 490 500 510 520 530 540 KKKVEKLLNA IEASKMQTLD RLIFGLGIKN VGAKVAKTLL NHYPSITLLA DAKYEDLIQI 550 560 570 580 590 600 PDIGPEIADS VTTYFSNESN QHMLEELKNL GLQMTYKIDV VTTHPFNGKT FVVTGTLDDF 610 620 630 640 650 SRTEASDIIE KLGGKVSGSV SKKTDYVLAG KEAGSKLTKA LELGIEVMDE ATFKVKINE

References

[1]

"Acholeplasma laidlawii complete genome." Kovaleva G.Y., Kazanov M.D., Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A., Vereshchagin V.A., Kostrjukova E.S., Selezneva O.V., Vtyurin N.N., Rogov S.I., Alekseev D.G., Ladygina V.G. , Titova G.A., Karpov V.A., Govorun V.M. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000896 Genomic DNA. Translation: ABX81940.1.
RefSeq	YP_001621316.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5804454.
GenomeReviews	Gene locus ACL_1348 in contig CP000896_GR.
KEGG	acl:ACL_1348.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	YKFPAQE.
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. 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_ACHLI

Accession

Primary (citable) accession number: A9NHW0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 10, 2008
Last sequence update:	February 5, 2008
Last modified:	November 3, 2009
This is version 17 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)