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Q6P799 (SYSC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:Sars1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR 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
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
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

Initiator methionine11Removed By similarity
Chain2 – 512511Serine--tRNA ligase, cytoplasmic
PRO_0000270765

Regions

Nucleotide binding302 – 3043ATP By similarity
Nucleotide binding391 – 3944ATP By similarity
Region271 – 2733Serine binding By similarity

Sites

Binding site3181ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site3251Serine By similarity
Binding site4291Serine By similarity

Amino acid modifications

Modified residue2411Phosphoserine By similarity
Modified residue3231N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6P799 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 960A30015F1F4A37

FASTA51258,588
        10         20         30         40         50         60 
MVLDLDLFRV DKGGDPALIR ETQEKRFKDP GLVDQLVKAD SEWRRCRFRA DNLNKLKNLC 

        70         80         90        100        110        120 
SKTIGEKMKK KEPVGEDESI PEDVLNFDDL TADTLAALKV SQIKKVRLLV DEAIQKCDGE 

       130        140        150        160        170        180 
RVKLEAERFE NLREIGNLLH PSVPISNDED ADNKVERIWG DCTVRKKYSH VDLVVMVDGF 

       190        200        210        220        230        240 
EGEKGAVVAG SRGYFLKGVL VFLEQALIQY ALRTLGSRGY TPIYTPFFMR KEVMQEVAQL 

       250        260        270        280        290        300 
SQFDEELYKV IGKGSEKSDD SSYDEKYLIA TSEQPIAALH RDEWLRPEDL PIKYAGFSTC 

       310        320        330        340        350        360 
FRQEVGSHGR DTRGIFRVHQ FEKIEQFVYS SPHDNKSWEM FDEMITTAEE FYQSLGIPYH 

       370        380        390        400        410        420 
IVNIVSGSLN HAASKKLDLE AWFPGSGAFR ELVSCSNCTD YQARRLRIRY GQTKKMMDKV 

       430        440        450        460        470        480 
EFVHMLNATM CATTRTICAI LENYQTEKGI VVPEKLREFM PPGLQELIPF VKPAPIDQEP 

       490        500        510 
SKKQKKQHEG SKKKAKEVTL ENQLQNMEVT EA

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[2]Lubec G., Afjehi-Sadat L.
Submitted (NOV-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 134-157, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Spinal cord.
[3]Heneberg P., Draber P.
Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 173-349.
Strain: Wistar.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		BC061765 mRNA. Translation: AAH61765.1.
AY145052 mRNA. Translation: AAN52758.1.
IPIIPI00391119.
RefSeqNP_001007607.1. NM_001007606.1.
UniGeneRn.73067.

3D structure databases

HSSPHSSP built from PDB template 1WLE based on UniProtKB Q9N0F3.
ProteinModelPortalQ6P799.
ModBaseSearch...

Protein-protein interaction databases

IntActQ6P799. 1 interaction.
STRINGQ6P799.

Proteomic databases

PRIDEQ6P799.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000033015; ENSRNOP00000038448; ENSRNOG00000020255.
GeneID266975.
KEGGrno:266975.
UCSCNM_001007606. rat.

Organism-specific databases

CTD6301.
RGD628813. Sars.

Phylogenomic databases

eggNOGroNOG06243.
GeneTreeENSGT00550000074862.
HOVERGENHBG023172.
PhylomeDBQ6P799.

Gene expression databases

ArrayExpressQ6P799.
GenevestigatorQ6P799.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-synth_IIa.
IPR015866. Ser-tRNA-synth_IIa_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
KOK01875.
PANTHERPTHR11778. tRNA-synt_ser. 1 hit.
PfamPF02403. Seryl_tRNA_N. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]
PIRSFPIRSF001529. Ser-tRNA-synth_IIa. 1 hit.
PRINTSPR00981. TRNASYNTHSER.
SUPFAMSSF46589. tRNA_binding_arm. 1 hit.
TIGRFAMsTIGR00414. SerS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio624745.

Entry information

Entry nameSYSC_RAT
AccessionPrimary (citable) accession number: Q6P799
Secondary accession number(s): Q8CIQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 23, 2007
Last modified: January 25, 2012
This is version 69 of the entry and version 3 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents