A3DP49 (DNLI_STAMF) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 54.
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 | Staphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 399550 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Staphylothermus › ![]() |
Protein attributes
| Sequence length | 597 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. |
| Sequence similarities | Belongs to the ATP-dependent DNA ligase family. |
| Sequence caution | The sequence ABN70409.1 differs from that shown. Reason: Erroneous initiation. |
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 – 597 | 597 | DNA ligase HAMAP-Rule MF_00407 | PRO_0000365264 | |||||
Sites | |||||||||
| Active site | 264 | 1 | N6-AMP-lysine intermediate By similarity | ||||||
| Binding site | 262 | 1 | ATP By similarity | ||||||
| Binding site | 269 | 1 | ATP By similarity | ||||||
| Binding site | 284 | 1 | ATP By similarity | ||||||
| Binding site | 314 | 1 | ATP By similarity | ||||||
| Binding site | 354 | 1 | ATP By similarity | ||||||
| Binding site | 431 | 1 | ATP By similarity | ||||||
| Binding site | 437 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Staphylothermus marinus reveals differences in sulfur metabolism among heterotrophic Crenarchaeota." Anderson I.J., Dharmarajan L., Rodriguez J., Hooper S., Porat I., Ulrich L.E., Elkins J.G., Mavromatis K., Sun H., Land M., Lapidus A., Lucas S., Barry K., Huber H., Zhulin I.B., Whitman W.B., Mukhopadhyay B., Woese C., Bristow J., Kyrpides N. BMC Genomics 10:145-145(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1. |
| [2] | "Complete genome sequence of Staphylothermus marinus Stetter and Fiala 1986 type strain F1." Anderson I.J., Sun H., Lapidus A., Copeland A., Glavina Del Rio T., Tice H., Dalin E., Lucas S., Barry K., Land M., Richardson P., Huber H., Kyrpides N.C. Stand. Genomic Sci. 1:183-188(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 43588 / DSM 3639 / F1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000575 Genomic DNA. Translation: ABN70409.1. Different initiation. |
| RefSeq | YP_001041317.1. NC_009033.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 399550.Smar_1318. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ABN70409; ABN70409; Smar_1318. |
| GeneID | 4906593. |
| KEGG | smr:Smar_1318. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1793. |
| HOGENOM | HOG000036008. |
| KO | K10747. |
| ProtClustDB | PRK01109. |
Enzyme and pathway databases | |
| BioCyc | SMAR399550:GHK2-1363-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. 1 hit. PS50160. DNA_LIGASE_A3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DNLI_STAMF | ||||||||
| Accession | Primary (citable) accession number: A3DP49 | ||||||||
| 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
