P0CL75 (DNLI_PYRAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 19.
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 | Pyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 272844 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › ![]() |
Protein attributes
| Sequence length | 559 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 |
| Subunit structure | Monomer 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 – 559 | 559 | DNA ligase HAMAP-Rule MF_00407 | PRO_0000407282 | |||||
Sites | |||||||||
| Active site | 249 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Binding site | 247 | 1 | ATP By similarity | ||||||
| Binding site | 254 | 1 | ATP By similarity | ||||||
| Binding site | 269 | 1 | ATP By similarity | ||||||
| Binding site | 299 | 1 | ATP By similarity | ||||||
| Binding site | 339 | 1 | ATP By similarity | ||||||
| Binding site | 414 | 1 | ATP By similarity | ||||||
| Binding site | 420 | 1 | ATP By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay. |
| [2] | "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638." Gao J., Wang J. Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: GE5 / Orsay. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ248284 Genomic DNA. Translation: CAB49465.1. HE613800 Genomic DNA. Translation: CCE69932.1. |
| PIR | B75173. |
| RefSeq | NP_126234.1. NC_000868.1. |
3D structure databases | |
| ProteinModelPortal | P0CL75. |
| SMR | P0CL75. Positions 1-559. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB49465; CAB49465; PAB2002. |
| GeneID | 1495445. |
| KEGG | pab:PAB2002. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000036008. |
| KO | K10747. |
| OMA | ARVQVHK. |
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. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DNLI_PYRAB | ||||||||
| Accession | Primary (citable) accession number: P0CL75 Secondary accession number(s): G8ZGQ3, Q9HH10, Q9V185 | ||||||||
| 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
