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P07284 (SYSC_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
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:SES1
Synonyms:SERS
Ordered Locus Names:YDR023W
ORF Names:YD9813.01
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processselenocysteinyl-tRNA(Sec) biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

seryl-tRNA aminoacylation

Inferred from direct assay Ref.1. Source: SGD

   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 direct assay Ref.1. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Serine--tRNA ligase, cytoplasmic
PRO_0000122199

Regions

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

Sites

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

Experimental info

Sequence conflict2241L → P in CAA28572. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P07284 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 451-462.
Strain: ATCC 204508 / S288c.
[6]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
BK006938 Genomic DNA. Translation: DAA11869.1.
PIRYSBYC. S50930.
RefSeqNP_010306.1. NM_001180331.1.

3D structure databases

ProteinModelPortalP07284.
SMRP07284. Positions 1-451.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32074. 46 interactions.
DIPDIP-5181N.
IntActP07284. 3 interactions.
MINTMINT-513156.
STRING4932.YDR023W.

Proteomic databases

MaxQBP07284.
PaxDbP07284.
PeptideAtlasP07284.
PRIDEP07284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR023W; YDR023W; YDR023W.
GeneID851587.
KEGGsce:YDR023W.

Organism-specific databases

CYGDYDR023w.
SGDS000002430. SES1.

Phylogenomic databases

eggNOGCOG0172.
GeneTreeENSGT00750000117703.
HOGENOMHOG000035937.
KOK01875.
OMAINTRINQ.
OrthoDBEOG7PVWZM.

Enzyme and pathway databases

BioCycYEAST:G3O-29640-MONOMER.
UniPathwayUPA00906; UER00895.

Gene expression databases

GenevestigatorP07284.

Family and domain databases

Gene3D1.10.287.40. 1 hit.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR002317. Ser-tRNA-ligase_type_1.
IPR015866. Ser-tRNA-synth_1_N.
IPR010978. tRNA-bd_arm.
[Graphical view]
PANTHERPTHR11778. PTHR11778. 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. SSF46589. 1 hit.
TIGRFAMsTIGR00414. serS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969063.
PROP07284.

Entry information

Entry nameSYSC_YEAST
AccessionPrimary (citable) accession number: P07284
Secondary accession number(s): D6VS09
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries