A1KN60 (DNLI_MYCBP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 56.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Probable DNA ligase EC=6.5.1.1 Alternative name(s): Polydeoxyribonucleotide synthase [ATP] | ||||
| Gene names |
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| Organism | Mycobacterium bovis (strain BCG / Pasteur 1173P2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 410289 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex › ![]() |
Protein attributes
| Sequence length | 507 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair By similarity. HAMAP-Rule MF_00407 |
| Catalytic activity | ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). HAMAP-Rule MF_00407 |
| Cofactor | Divalent metal cations By similarity. HAMAP-Rule MF_00407 |
| Sequence similarities | Belongs to the ATP-dependent DNA ligase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Cell cycle Cell division DNA damage DNA recombination DNA repair DNA replication |
| Ligand | ATP-binding Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA ligation involved in DNA repair Inferred from electronic annotation. Source: InterPro DNA recombinationInferred from electronic annotation. Source: HAMAP DNA replicationInferred from electronic annotation. Source: HAMAP cell cycleInferred from electronic annotation. Source: UniProtKB-KW cell divisionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP DNA bindingInferred from electronic annotation. Source: InterPro DNA ligase (ATP) activityInferred from electronic annotation. Source: HAMAP metal 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 – 507 | 507 | Probable DNA ligase HAMAP-Rule MF_00407 | PRO_0000365223 | |||||
Sites | |||||||||
| Active site | 211 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Binding site | 209 | 1 | ATP By similarity | ||||||
| Binding site | 216 | 1 | ATP By similarity | ||||||
| Binding site | 231 | 1 | ATP By similarity | ||||||
| Binding site | 260 | 1 | ATP By similarity | ||||||
| Binding site | 300 | 1 | ATP By similarity | ||||||
| Binding site | 372 | 1 | ATP By similarity | ||||||
| Binding site | 378 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Genome plasticity of BCG and impact on vaccine efficacy." Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T. Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BCG / Pasteur 1173P2. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM408590 Genomic DNA. Translation: CAL73076.1. |
| RefSeq | YP_979171.1. NC_008769.1. |
3D structure databases | |
| ProteinModelPortal | A1KN60. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 410289.BCG_3087. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAL73076; CAL73076; BCG_3087. |
| GeneID | 4699121. |
| KEGG | mbb:BCG_3087. |
| PATRIC | 18017256. VBIMycBov80988_3372. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1793. |
| HOGENOM | HOG000036008. |
| KO | K01971. |
| OMA | ARVQVHK. |
| ProtClustDB | PRK03180. |
Enzyme and pathway databases | |
| BioCyc | MBOV410289:GJW7-3128-MONOMER. |
Family and domain databases | |
| Gene3D | 1.10.3260.10. 1 hit. 2.40.50.140. 1 hit. |
| HAMAP | MF_00407. DNA_ligase. |
| InterPro | IPR022865. DNA_ligae_ATP-dep_bac/arc. IPR000977. DNA_ligase_ATP-dep. IPR012309. DNA_ligase_ATP-dep_C. IPR012310. DNA_ligase_ATP-dep_cent. IPR016059. DNA_ligase_ATP-dep_CS. IPR012308. DNA_ligase_ATP-dep_N. IPR012340. NA-bd_OB-fold. [Graphical view] |
| Pfam | PF04679. DNA_ligase_A_C. 1 hit. PF01068. DNA_ligase_A_M. 1 hit. PF04675. DNA_ligase_A_N. 1 hit. [Graphical view] |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. SSF117018. SSF117018. 1 hit. |
| TIGRFAMs | TIGR00574. dnl1. 1 hit. |
| PROSITE | PS00697. DNA_LIGASE_A1. 1 hit. PS00333. DNA_LIGASE_A2. False negative. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DNLI_MYCBP | ||||||||
| Accession | Primary (citable) accession number: A1KN60 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
