Q058C9 (DNLJ_BUCCC) Reviewed, UniProtKB/Swiss-Prot

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:	BCc_039

Organism

Buchnera aphidicola subsp. Cinara cedri (strain Cc) [Complete proteome] [HAMAP]

Taxonomic identifier

372461 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	587 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.

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
Molecular function	DNA ligase (NAD+) activity Inferred from electronic annotation. Source: EC metal 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 – 587	587	DNA ligase HAMAP MF_01588		PRO_0000313157
Regions
	Nucleotide binding	32 – 36	5	NAD By similarity
	Nucleotide binding	84 – 85	2	NAD By similarity
Sites
	Active site	118	1	N6-AMP-lysine intermediate By similarity
	Metal binding	411	1	Zinc By similarity
	Metal binding	414	1	Zinc By similarity
	Metal binding	429	1	Zinc By similarity
	Metal binding	435	1	Zinc By similarity
	Binding site	116	1	NAD By similarity
	Binding site	139	1	NAD By similarity
	Binding site	176	1	NAD By similarity
	Binding site	293	1	NAD By similarity
	Binding site	317	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q058C9 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 521F5E67946A233A	FASTA	587	68,400
	10 20 30 40 50 60 MKDIYNQILK LQLQIKYHNY MYHTLDSPII SDILYDELYN KLLQLEKLYF KKKSLDKKIK 70 80 90 100 110 120 LLDQVGAKKL HIFTEFFHKI PMLSLRSINN ISDFDLFDKK IKEYFKHINV ITYFCDFKFD 130 140 150 160 170 180 GLAVNLFYKN GILISASTRG NGSVGENITK NILMISSIPK KIAGSNIPKK IEIRGEIFMR 190 200 210 220 230 240 KSDFFILNQS CKLSGKKEFS NPRNAAAGSV RQLNPEIVKK RKLNFFVYGF GLFDYNKKID 250 260 270 280 290 300 SHYQRLLQIK KWGFPLYKNY CVCKNKKEVI HFYHYANKIR SQLDFEIDGI VIKLDSIKLQ 310 320 330 340 350 360 NNLGCIEKYP KWAIALKFFS LDKETKIFKI SFKVGRTGII TPVAYFFPIN LFGVSISKAS 370 380 390 400 410 420 LYNIKTIKLL DIRLHDYVTV YRAGDVIPKI RNVLIHKRNK YTQKIIIPTY CPSCCTKLIF 430 440 450 460 470 480 SDDLKTCYCP ASFSCFSQNV KRLIYFSSKN GLNFKGLGKK NIIKLINYGY LYTPIDFFSL 490 500 510 520 530 540 TVKKLKNIFR MGDKLSEKII KNIAFSKRVS LDKFICSLGI FGVGTSIAKR LAYYYRSVEK 550 560 570 580 FFNTNYDTLS KIDHIGYNIS NAIISFLKNK SNRSIILKLI RILNIFI

References

[1]

"A small microbial genome: the end of a long symbiotic relationship?" Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A. Science 314:312-313(2006) [PubMed: 17038625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Cc.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000263 Genomic DNA. Translation: ABJ90520.1.
RefSeq	YP_802613.1. NC_008513.1.
3D structure databases
ProteinModelPortal	Q058C9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q058C9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBUCT00000001514; EBBUCP00000001424; EBBUCG00000001514.
GeneID	4440714.
GenomeReviews	Gene locus BCc_039 in contig CP000263_GR.
KEGG	bcc:BCc_039.
PATRIC	21246015. VBIBucAph7855_0035.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0272.
GeneTree	EBGT00050000007874.
HOGENOM	HBG620317.
OMA	TQKVGAT.
Enzyme and pathway databases
BioCyc	BAPH372461:BCC_039-MONOMER.
Family and domain databases
HAMAP	MF_01588. DNA_ligase_A. [Tree]
InterPro	IPR018239. DNA_ligase_AS. IPR004150. DNA_ligase_OB. IPR001679. DNAligase. IPR013839. DNAligase_adenylation. IPR013840. DNAligase_N. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR010994. RuvA_2-like. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KO	K01972.
Pfam	PF01653. DNA_ligase_aden. 1 hit. PF03120. DNA_ligase_OB. 1 hit. [Graphical view]
PIRSF	PIRSF001604. LigA. 1 hit.
SMART	SM00532. LIGANc. 1 hit. [Graphical view]
SUPFAM	SSF50249. Nucleic_acid_OB. 1 hit. SSF47781. RuvA_2_like. 1 hit.
TIGRFAMs	TIGR00575. Dnlj. 1 hit.
PROSITE	PS50172. BRCT. False negative. PS01055. DNA_LIGASE_N1. 1 hit. PS01056. DNA_LIGASE_N2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DNLJ_BUCCC

Accession

Primary (citable) accession number: Q058C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 14, 2006
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program