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P26636 (SYSC_CRIGR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. 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):
Seryl-tRNA synthetase
Short name=SerRS
Seryl-tRNA(Ser/Sec) synthetase
Gene names
Name:SARS
OrganismCricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Taxonomic identifier10029 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeCricetulus

Protein attributes

Sequence length199 AA.
Sequence statusFragment.
Protein existenceEvidence 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

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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Gene Ontology (GO)
   Biological processseryl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Chain‹1 – ›199›199Serine--tRNA ligase, cytoplasmic
PRO_0000122190

Regions

Nucleotide binding85 – 884ATP By similarity

Sites

Binding site121ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site191Serine By similarity
Binding site1231Serine By similarity

Amino acid modifications

Modified residue171N6-acetyllysine By similarity

Experimental info

Non-terminal residue11
Non-terminal residue1991

Sequences

Sequence LengthMass (Da)Tools
P26636 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 930B45C77613EA19

FASTA19922,813
        10         20         30         40         50         60 
LHGRDTRGIF RVHQFEKIEQ FVYTSPHDNK SWEMFEEMIG TAEEFYQSLG IPYHIVNIVS 

        70         80         90        100        110        120 
GSLNHAASKK LDLEAWFPGS GAFRELVSCS NCTDYQARRL RIRYGQTKKM MDKVEFVHML 

       130        140        150        160        170        180 
NATMCATTRT ICAILENYQT EKGIIVPEKL REFMPPGLQE LIPFVKPAPI DQEPSKKQKK 

       190 
QHEGSKKESK RGHPGEPAA 

« Hide

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.
PIRS35441.

3D structure databases

ProteinModelPortalP26636.
SMRP26636. Positions 2-164.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-synth_IIa.
[Graphical view]
PANTHERPTHR11778. tRNA-synt_ser. 1 hit.
PfamPF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PRINTSPR00981. TRNASYNTHSER.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYSC_CRIGR
AccessionPrimary (citable) accession number: P26636
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 25, 2012
This is version 63 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