Reviewed,
UniProtKB/Swiss-Prot Q8G830 (DNLJ_BIFLO)
Last modified
February 9, 2010.
Version 50.
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 |
| ||||
| Organism | Bifidobacterium longum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216816 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Bifidobacteriales › Bifidobacteriaceae › Bifidobacterium |
Protein attributes
| Sequence length | 920 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 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 – 920 | 920 | DNA ligase HAMAP MF_01588 | PRO_0000313140 | |||||
Regions | |||||||||
| Domain | 839 – 920 | 82 | BRCT | ||||||
| Nucleotide binding | 90 – 94 | 5 | NAD By similarity | ||||||
| Nucleotide binding | 139 – 140 | 2 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 175 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Metal binding | 481 | 1 | Zinc By similarity | ||||||
| Metal binding | 484 | 1 | Zinc By similarity | ||||||
| Metal binding | 500 | 1 | Zinc By similarity | ||||||
| Metal binding | 506 | 1 | Zinc By similarity | ||||||
| Binding site | 173 | 1 | NAD By similarity | ||||||
| Binding site | 196 | 1 | NAD By similarity | ||||||
| Binding site | 235 | 1 | NAD By similarity | ||||||
| Binding site | 360 | 1 | NAD By similarity | ||||||
| Binding site | 384 | 1 | NAD By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bifidobacterium longum reflects its adaptation to the human gastrointestinal tract." Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G., Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F. Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002) [PubMed: 12381787] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCC 2705. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014295 Genomic DNA. Translation: AAN23919.1. |
| RefSeq | NP_695283.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ZAU based on UniProtKB P63973. |
| SMR | Q8G830. Positions 67-388, 77-831, 841-918. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1023212. |
| GenomeReviews | Gene locus BL0052 in contig AE014295_GR. |
| KEGG | blo:BL0052. |
| NMPDR | fig|206672.1.peg.52. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG620317. |
| OMA | IKHFASR. |
Enzyme and pathway databases | |
| BioCyc | BLON206672:BL0052-MONOMER. |
| BRENDA | 6.5.1.2. 39917. |
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] |
| 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_BIFLO | ||||||||
| Accession | Primary (citable) accession number: Q8G830 | ||||||||
| 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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