Reviewed,
UniProtKB/Swiss-Prot Q73FJ3 (SYS_BACC1)
Last modified
November 3, 2009.
Version 39.
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 EC=6.1.1.11 Alternative name(s): Seryl-tRNA(Ser/Sec) synthetase Serine--tRNA ligase Short name=SerRS | ||||
| Gene names |
| ||||
| Organism | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 222523 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 424 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 – 424 | 424 | Seryl-tRNA synthetase HAMAP MF_00176 | PRO_0000121998 | |||||
Regions | |||||||||
| Nucleotide binding | 262 – 264 | 3 | ATP By similarity | ||||||
| Nucleotide binding | 349 – 352 | 4 | ATP By similarity | ||||||
| Region | 231 – 233 | 3 | Serine binding By similarity | ||||||
Sites | |||||||||
| Binding site | 285 | 1 | Serine By similarity | ||||||
| Binding site | 385 | 1 | Serine By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AE017194 Genomic DNA. Translation: AAS38949.1. | |
| RefSeq | NP_976341.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q73FJ3. |
Genome annotation databases | |
| GeneID | 2751256. |
| GenomeReviews | Gene locus BCE_0013 in contig AE017194_GR. |
| KEGG | bca:BCE_0013. |
| NMPDR | fig|222523.1.peg.13. |
| TIGR | BCE_0013. |
Phylogenomic databases | |
| HOGENOM | Q73FJ3. |
| OMA | LKPYMGG. |
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 | SYS_BACC1 | ||||||||
| Accession | Primary (citable) accession number: Q73FJ3 | ||||||||
| 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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