P13642 (SYSC_RABIT) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
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): 62 kDa RNA-binding protein Seryl-tRNA synthetase Short name=SerRS Seryl-tRNA(Ser/Sec) synthetase | ||||
| Gene names |
| ||||
| Organism | Oryctolagus cuniculus (Rabbit) [Complete proteome] | ||||
| Taxonomic identifier | 9986 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Protein attributes
| Sequence length | 39 AA. |
| Sequence status | Fragment. |
| Protein existence | Evidence at protein 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. |
| Caution | Was originally (Ref.1) thought to function in mRNA expression. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | translation Inferred from electronic annotation. Source: UniProtKB-KW |
| 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)
Sequences
References
| [1] | "Purification and properties of a protein component of messenger ribonucleoprotein particles that shares a common epitope with eucaryotic elongation factor Tu." Slobin L.I., Greenberg J.R. Eur. J. Biochem. 173:305-310(1988) [PubMed: 2452088] [Abstract] Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | S00490. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P13642. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Phylogenomic databases | |
| eggNOG | maNOG08939. |
| GeneTree | ENSGT00550000074862. |
| OrthoDB | EOG4320Z0. |
Family and domain databases | |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. Partial match. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | SYSC_RABIT | ||||||||
| Accession | Primary (citable) accession number: P13642 | ||||||||
| Entry history |
| ||||||||
| 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