A6CQT3 (A6CQT3_9BACI) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 39.
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: Serine--tRNA ligase HAMAP-Rule MF_00176 EC=6.1.1.11 HAMAP-Rule MF_00176 Alternative name(s): Seryl-tRNA synthetase HAMAP-Rule MF_00176 Seryl-tRNA(Ser/Sec) synthetase HAMAP-Rule MF_00176 | ||||
| Gene names |
| ||||
| Organism | Bacillus sp. SG-1 EMBL EDL63797.1 | ||||
| Taxonomic identifier | 161544 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus![]() |
Protein attributes
| Sequence length | 426 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) By similarity. HAMAP-Rule MF_00176 |
| Catalytic activity | ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP-Rule MF_00176 ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP-Rule MF_00176 |
| Pathway | Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP-Rule MF_00176 |
| Subunit structure | Homodimer. The tRNA molecule binds across the dimer By similarity. HAMAP-Rule MF_00176 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00176. |
| Domain | Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. HAMAP-Rule MF_00176 |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily. HAMAP-Rule MF_00176 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis HAMAP-Rule MF_00176 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00176 |
| Ligand | ATP-binding HAMAP-Rule MF_00176 Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase HAMAP-Rule MF_00176 EMBL EDL63797.1 Ligase |
| Gene Ontology (GO) | |
| Biological_process | selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP selenocysteinyl-tRNA(Sec) biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway seryl-tRNA aminoacylationInferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP serine-tRNA ligase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 262 – 264 | 3 | ATP By similarity HAMAP-Rule MF_00176 | ||||||
| Nucleotide binding | 349 – 352 | 4 | ATP By similarity HAMAP-Rule MF_00176 | ||||||
| Region | 231 – 233 | 3 | Serine binding By similarity HAMAP-Rule MF_00176 | ||||||
Sites | |||||||||
| Binding site | 285 | 1 | Serine By similarity HAMAP-Rule MF_00176 | ||||||
| Binding site | 385 | 1 | Serine By similarity HAMAP-Rule MF_00176 | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: SG-1 EMBL EDL63797.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ABCF01000039 Genomic DNA. Translation: EDL63797.1. |
3D structure databases | |
| ProteinModelPortal | A6CQT3. |
| SMR | A6CQT3. Positions 1-426. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EDL63797; EDL63797; BSG1_10723. |
| PATRIC | 25232543. VBIBacSp59792_2887. |
Enzyme and pathway databases | |
| UniPathway | UPA00906; UER00895. |
Family and domain databases | |
| Gene3D | 1.10.287.40. 1 hit. |
| HAMAP | MF_00176. Ser_tRNA_synth_type1. |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-ligase_type_1. IPR015866. Ser-tRNA-synth_1_N. IPR010978. tRNA-bd_arm. [Graphical view] |
| PANTHER | PTHR11778. PTHR11778. 1 hit. |
| Pfam | PF02403. Seryl_tRNA_N. 1 hit. PF00587. tRNA-synt_2b. 1 hit. [Graphical view] |
| PIRSF | PIRSF001529. Ser-tRNA-synth_IIa. 1 hit. |
| PRINTS | PR00981. TRNASYNTHSER. |
| SUPFAM | SSF46589. tRNA_binding_arm. 1 hit. |
| TIGRFAMs | TIGR00414. serS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | A6CQT3_9BACI | ||||||||
| Accession | Primary (citable) accession number: A6CQT3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
