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Reviewed, UniProtKB/Swiss-Prot P07284 (SYSC_YEAST)

Last modified November 3, 2009. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Seryl-tRNA synthetase, cytoplasmic
    EC=6.1.1.11
Alternative name(s):
    Seryl-tRNA(Ser/Sec) synthetase
    Serine--tRNA ligase
      Short name=SerRS
Gene names
Name: SES1
Synonyms: SERS
Ordered Locus Names: YDR023W
ORF Names: YD9813.01
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the attachment of serine to tRNA(Ser). Is also probably 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). Ref.1

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 probably binds across the dimer. Ref.1

Subcellular location

Cytoplasm.

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.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processseryl-tRNA aminoacylation Ref.1

Inferred from direct assay. Source: SGD

   Cellular componentcytoplasm

Inferred from direct assay. Source: SGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-tRNA ligase activity Ref.1

Inferred from direct assay. Source: SGD

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Seryl-tRNA synthetase, cytoplasmic
PRO_0000122199

Regions

Nucleotide binding279 – 2813ATP By similarity
Nucleotide binding366 – 3694ATP By similarity
Region246 – 2483Serine binding By similarity

Sites

Binding site2951ATP; via carbonyl oxygen and amide nitrogen By similarity
Binding site3021Serine By similarity
Binding site4041Serine By similarity

Amino acid modifications

Modified residue1191Phosphoserine Ref.5

Experimental info

Sequence conflict2241L → P in CAA28572. Ref.1

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Sequences

Sequence LengthMass (Da)Tools
P07284-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: BBED6EA47E6F547B

FASTA46253,310
        10         20         30         40         50         60 
MLDINQFIED KGGNPELIRQ SQKARNASVE IVDEIISDYK DWVKTRFELD ELNKKFNKLQ 

        70         80         90        100        110        120 
KDIGLKFKNK EDASGLLAEK EKLTQQKKEL TEKEQQEDKD LKKKVFQVGN IVHPSVVVSN 

       130        140        150        160        170        180 
DEENNELVRT WKPEDLEAVG PIASVTGKPA SLSHHEILLR LDGYDPDRGV KICGHRGYFF 

       190        200        210        220        230        240 
RNYGVFLNQA LINYGLQFLA AKGYIPLQAP VMMNKELMSK TAQLSEFDEE LYKVIDGEDE 

       250        260        270        280        290        300 
KYLIATSEQP ISAYHSGEWF EKPQEQLPIH YVGYSSCFRR EAGSHGKDAW GVFRVHAFEK 

       310        320        330        340        350        360 
IEQFVITEPE KSWEEFEKMI SYSEEFYKSL KLPYRIVGIV SGELNNAAAK KYDLEAWFPY 

       370        380        390        400        410        420 
QKEYKELVSC SNCTDYQSRN LEIRCGIKKM GDREKKYVHC LNSTLAATQR ALCCILENYQ 

       430        440        450        460 
TEDGLVVPEV LRKYIPGEPE FLPFVNELPK NSTSSKDKKK KN

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and characterization of the gene coding for cytoplasmic seryl-tRNA synthetase from Saccharomyces cerevisiae."
Weygand-Durasevic I., Johnson-Burke D., Soell D.
Nucleic Acids Res. 15:1887-1904(1987) [PubMed: 3031581] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
[2]"Sequencing and analysis of a 35.4 kb region on the right arm of chromosome IV from Saccharomyces cerevisiae reveal 23 open reading frames."
Eide L.G., Sander C., Prydz H.
Yeast 12:1085-1090(1996) [PubMed: 8896275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"Reduced dosage of genes encoding ribosomal protein S18 suppresses a mitochondrial initiation codon mutation in Saccharomyces cerevisiae."
Folley L.S., Fox T.D.
Genetics 137:369-379(1994) [PubMed: 8070651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 451-462.
Strain: ATCC 204508 / S288c.
[5]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X04884 Genomic DNA. Translation: CAA28572.1.
Z47814 Genomic DNA. Translation: CAA87802.1.
X95966 Genomic DNA. Translation: CAA65216.1.
Z74319 Genomic DNA. Translation: CAA98844.1.
L15408 Genomic DNA. Translation: AAC37412.1.
PIRYSBYC. S50930.
RefSeqNP_010306.1.

3D structure databases

HSSPHSSP built from PDB template 1SER based on UniProtKB P34945.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5181N.
IntActP07284. 10 interactions.
STRINGP07284.

Proteomic databases

PeptideAtlasP07284.
PRIDEP07284.

Genome annotation databases

EnsemblYDR023W; YDR023W; YDR023W; Saccharomyces cerevisiae. [Genome view]
GeneID851587.
GenomeReviewsGene locus YDR023W in contig Z71256_GR.
KEGGsce:YDR023W.
NMPDRfig|4932.3.peg.1049.

Organism-specific databases

CYGDYDR023w.
SGDS000002430. SES1.

Phylogenomic databases

HOGENOMP07284.
OMAMCATTRV.

Enzyme and pathway databases

BRENDA6.1.1.11. 250.

Gene expression databases

ArrayExpressP07284.
GenevestigatorP07284.
GermOnlineYDR023W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR002317. Ser-tRNA-synth_IIa.
IPR018156. Ser-tRNA-synth_IIa_C.
IPR015866. Ser-tRNA-synth_IIa_N.
[Graphical view]
Gene3DG3DSA:1.10.287.40. Ser-tRNA-synth_IIa_N. 1 hit.
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.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio969063.

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Entry information

Entry nameSYSC_YEAST
AccessionPrimary (citable) accession number: P07284
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1996
Last modified: November 3, 2009
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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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

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents