Reviewed,
UniProtKB/Swiss-Prot Q82KS8 (SYS2_STRAW)
Last modified
November 3, 2009.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Seryl-tRNA synthetase 2 EC=6.1.1.11 Alternative name(s): Seryl-tRNA(Ser/Sec) synthetase 2 Serine--tRNA ligase 2 Short name=SerRS 2 | ||||
| Gene names |
| ||||
| Organism | Streptomyces avermitilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 33903 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces |
Protein attributes
| Sequence length | 427 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | ATP + L-serine + tRNA(Ser) = AMP + diphosphate + L-seryl-tRNA(Ser). HAMAP MF_00176 ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). HAMAP MF_00176 |
| Pathway | Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1. HAMAP MF_00176 |
| Subunit structure | Homodimer. The tRNA molecule binds across the dimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Domain | Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding By similarity. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | selenocysteine biosynthetic process Inferred from electronic annotation. Source: HAMAP 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 | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 427 | 427 | Seryl-tRNA synthetase 2 HAMAP MF_00176 | PRO_0000122130 | |||||
Regions | |||||||||
| Nucleotide binding | 261 – 263 | 3 | ATP By similarity | ||||||
| Nucleotide binding | 348 – 351 | 4 | ATP By similarity | ||||||
| Region | 230 – 232 | 3 | Serine binding By similarity | ||||||
Sites | |||||||||
| Binding site | 284 | 1 | Serine By similarity | ||||||
| Binding site | 383 | 1 | Serine By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites." Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M. Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed: 11572948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165. |
| [2] | "Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis." Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S. Nat. Biotechnol. 21:526-531(2003) [PubMed: 12692562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165. |
Cross-references
Sequence databases | |
|---|---|
| BA000030 Genomic DNA. Translation: BAC70005.1. | |
| RefSeq | NP_823470.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1210391. |
| GenomeReviews | Gene locus SAV_2294 in contig BA000030_GR. |
| KEGG | sma:SAV_2294. |
| NMPDR | fig|227882.1.peg.2296. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q82KS8. |
| OMA | EHFEIGE. |
Enzyme and pathway databases | |
| BioCyc | SAVE227882:SAV2294-MON. |
| BRENDA | 6.1.1.11. 140873. |
Family and domain databases | |
| HAMAP | MF_00176. [Tree] |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-reg. IPR006195. aa-tRNA-synth_II_cons-reg. IPR002317. Ser-tRNA-synth_IIa. IPR018156. Ser-tRNA-synth_IIa_C. IPR015866. Ser-tRNA-synth_IIa_N. [Graphical view] |
| Gene3D | G3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit. |
| PANTHER | PTHR11778. tRNA-synt_ser. 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. |
| TIGRFAMs | TIGR00414. serS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYS2_STRAW | ||||||||
| Accession | Primary (citable) accession number: Q82KS8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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