P26636 (SYSC_CRIGR) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 63.
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: Serine--tRNA ligase, cytoplasmic EC=6.1.1.11 Alternative name(s): Seryl-tRNA synthetase Short name=SerRS Seryl-tRNA(Ser/Sec) synthetase | ||
| Gene names |
| ||
| Organism | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) | ||
| Taxonomic identifier | 10029 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Cricetulus |
Protein attributes
| Sequence length | 199 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at transcript level |
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). ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec). |
| Pathway | |
| 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 |
| PTM | Acetylation |
| Gene Ontology (GO) | |
| Biological process | seryl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW serine-tRNA ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›199 | ›199 | Serine--tRNA ligase, cytoplasmic | PRO_0000122190 | |||||
Regions | |||||||||
| Nucleotide binding | 85 – 88 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 12 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 19 | 1 | Serine By similarity | ||||||
| Binding site | 123 | 1 | Serine By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 17 | 1 | N6-acetyllysine By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 199 | 1 | |||||||
Sequences
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References
| [1] | "A seryl-tRNA synthetase gene is coamplified with the adenylate deaminase 2 gene in coformycin resistant Chinese hamster fibroblasts." Lunel C., Buttin G., de Saint Vincent B.R. Nucleic Acids Res. 20:2597-2597(1992) [PubMed: 1598219] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M88136 mRNA. Translation: AAA37019.1. |
| PIR | S35441. |
3D structure databases | |
| ProteinModelPortal | P26636. |
| SMR | P26636. Positions 2-164. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR002317. Ser-tRNA-synth_IIa. [Graphical view] |
| PANTHER | PTHR11778. tRNA-synt_ser. 1 hit. |
| Pfam | PF00587. tRNA-synt_2b. 1 hit. [Graphical view] |
| PRINTS | PR00981. TRNASYNTHSER. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYSC_CRIGR | ||||||||
| Accession | Primary (citable) accession number: P26636 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
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 |

Clusters with