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P13642 (SYSC_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
Name:SARS
Synonyms:SERS
OrganismOryctolagus cuniculus (Rabbit) [Complete proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length39 AA.
Sequence statusFragment.
Protein existenceEvidence 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

Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.

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 processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processtranslation

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›39›39Serine--tRNA ligase, cytoplasmic
PRO_0000122193

Experimental info

Non-terminal residue391

Sequences

Sequence LengthMass (Da)Tools
P13642 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 1D23FBEBDDC82DF5

FASTA394,411
        10         20         30 
VLDLDLFRVD KGGDPALIRE TQEKRFKDPG LVDQLVKAD 

« Hide

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

PIRS00490.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGP13642.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGmaNOG08939.
GeneTreeENSGT00550000074862.
OrthoDBEOG4320Z0.

Family and domain databases

PROSITEPS50862. AA_TRNA_LIGASE_II. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYSC_RABIT
AccessionPrimary (citable) accession number: P13642
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: January 25, 2012
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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