A5UKX2 (DNLI_METS3) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 39.
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: DNA ligase EC=6.5.1.1 Alternative name(s): Polydeoxyribonucleotide synthase [ATP] | ||||
| Gene names |
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| Organism | Methanobrevibacter smithii (strain PS / ATCC 35061 / DSM 861) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 420247 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanobrevibacter |
Protein attributes
| Sequence length | 551 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 MF_00407 |
| Catalytic activity | ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). HAMAP MF_00407 |
| Cofactor | Divalent metal cations By similarity. HAMAP 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: UniProtKB-KW DNA replicationInferred from electronic annotation. Source: UniProtKB-KW 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: UniProtKB-KW DNA bindingInferred from electronic annotation. Source: InterPro DNA ligase (ATP) activityInferred from electronic annotation. Source: EC 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 – 551 | 551 | DNA ligase HAMAP MF_00407 | PRO_1000049872 | |||||
Sites | |||||||||
| Active site | 248 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Binding site | 246 | 1 | ATP By similarity | ||||||
| Binding site | 253 | 1 | ATP By similarity | ||||||
| Binding site | 268 | 1 | ATP By similarity | ||||||
| Binding site | 298 | 1 | ATP By similarity | ||||||
| Binding site | 337 | 1 | ATP By similarity | ||||||
| Binding site | 414 | 1 | ATP By similarity | ||||||
| Binding site | 420 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "Genomic and metabolic adaptations of Methanobrevibacter smithii to the human gut." Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B., Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007) [PubMed: 17563350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PS / ATCC 35061 / DSM 861. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000678 Genomic DNA. Translation: ABQ86850.1. |
| RefSeq | YP_001273218.1. NC_009515.1. |
3D structure databases | |
| ProteinModelPortal | A5UKX2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5UKX2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5216232. |
| GenomeReviews | Gene locus Msm_0645 in contig CP000678_GR. |
| KEGG | msi:Msm_0645. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | arNOG04596. |
| HOGENOM | HBG570821. |
| OMA | GRPRPFQ. |
| ProtClustDB | CLSK798208. |
Family and domain databases | |
| HAMAP | MF_00407. DNA_ligase. [Tree] |
| 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. IPR016027. NA-bd_OB-fold-like. [Graphical view] |
| Gene3D | G3DSA:1.10.3260.10. DNA_ligase_ATP-dep_N. 1 hit. G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| KO | K10747. |
| 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. False negative. PS00333. DNA_LIGASE_A2. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DNLI_METS3 | ||||||||
| Accession | Primary (citable) accession number: A5UKX2 | ||||||||
| 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 |

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