I3TCD9 (I3TCD9_THEC1) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 7.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: DNA ligase RuleBase RU000617 HAMAP-Rule MF_00407 EC=6.5.1.1 RuleBase RU000617 HAMAP-Rule MF_00407 Alternative name(s): Polydeoxyribonucleotide synthase [ATP] HAMAP-Rule MF_00407 | ||||
| Gene names |
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| Organism | Thermogladius cellulolyticus (strain 1633) [Complete proteome] [HAMAP] EMBL AFK50427.1 | ||||
| Taxonomic identifier | 1184251 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Thermogladius › ![]() |
Protein attributes
| Sequence length | 600 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). RuleBase RU000617 HAMAP-Rule MF_00407 |
| Cofactor | Divalent metal cations By similarity. HAMAP-Rule MF_00407 |
| Sequence similarities | Belongs to the ATP-dependent DNA ligase family. RuleBase RU004196 HAMAP-Rule MF_00407 |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 259 | 1 | N6-AMP-lysine intermediate By similarity HAMAP-Rule MF_00407 | ||||||
| Binding site | 257 | 1 | ATP By similarity HAMAP-Rule MF_00407 | ||||||
| Binding site | 264 | 1 | ATP By similarity HAMAP-Rule MF_00407 | ||||||
| Binding site | 279 | 1 | ATP By similarity HAMAP-Rule MF_00407 | ||||||
| Binding site | 309 | 1 | ATP By similarity HAMAP-Rule MF_00407 | ||||||
| Binding site | 349 | 1 | ATP By similarity HAMAP-Rule MF_00407 | ||||||
| Binding site | 426 | 1 | ATP By similarity HAMAP-Rule MF_00407 | ||||||
| Binding site | 432 | 1 | ATP By similarity HAMAP-Rule MF_00407 | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the hyperthermophilic cellulolytic Crenarchaeon 'Thermogladius cellulolyticus' 1633." Mardanov A.V., Kochetkova T.V., Beletsky A.V., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G. J. Bacteriol. 194:4446-4447(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1633 EMBL AFK50427.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP003531 Genomic DNA. Translation: AFK50427.1. |
| RefSeq | YP_006362565.1. NC_017954.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AFK50427; AFK50427; TCELL_0002. |
| GeneID | 13012922. |
| KEGG | thg:TCELL_0002. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| KO | K10747. |
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 | I3TCD9_THEC1 | ||||||||
| Accession | Primary (citable) accession number: I3TCD9 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
