Reviewed,
UniProtKB/Swiss-Prot Q6G2R5 (DNLJ_BARHE)
Last modified
November 3, 2009.
Version 39.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: DNA ligase EC=6.5.1.2 Alternative name(s): Polydeoxyribonucleotide synthase [NAD+] | ||||
| Gene names |
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| Organism | Bartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 38323 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella |
Protein attributes
| Sequence length | 716 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 replicationInferred 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+) activityInferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred 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 – 716 | 716 | DNA ligase HAMAP MF_01588 | PRO_0000313135 | |||||
Regions | |||||||||
| Domain | 638 – 716 | 79 | BRCT | ||||||
| Nucleotide binding | 42 – 46 | 5 | NAD By similarity | ||||||
| Nucleotide binding | 91 – 92 | 2 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 127 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Metal binding | 429 | 1 | Zinc By similarity | ||||||
| Metal binding | 432 | 1 | Zinc By similarity | ||||||
| Metal binding | 447 | 1 | Zinc By similarity | ||||||
| Metal binding | 453 | 1 | Zinc By similarity | ||||||
| Binding site | 125 | 1 | NAD By similarity | ||||||
| Binding site | 148 | 1 | NAD By similarity | ||||||
| Binding site | 184 | 1 | NAD By similarity | ||||||
| Binding site | 300 | 1 | NAD By similarity | ||||||
| Binding site | 324 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49882 / Houston 1. |
Cross-references
Sequence databases | |
|---|---|
| BX897699 Genomic DNA. Translation: CAF27899.1. | |
| RefSeq | YP_033886.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2865583. |
| GenomeReviews | Gene locus BH11140 in contig BX897699_GR. |
| KEGG | bhe:BH11140. |
| NMPDR | fig|283166.1.peg.1014. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q6G2R5. |
| OMA | YKFPAQE. |
Enzyme and pathway databases | |
| BioCyc | BHEN283166:BH11140-MON. |
| BRENDA | 6.5.1.2. 277357. |
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. 2 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_BARHE | ||||||||
| Accession | Primary (citable) accession number: Q6G2R5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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