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Protein

Cysteine--tRNA ligase

Gene

YNL247W

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys).

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi63 – 631ZincBy similarity
Metal bindingi369 – 3691ZincBy similarity
Metal bindingi394 – 3941ZincBy similarity
Metal bindingi398 – 3981ZincBy similarity
Binding sitei430 – 4301ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cysteine-tRNA ligase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cysteinyl-tRNA aminoacylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-33244-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine--tRNA ligase (EC:6.1.1.16)
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name:
CysRS
Gene namesi
Ordered Locus Names:YNL247W
ORF Names:N0885
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL247W.
SGDiS000005191. YNL247W.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767Cysteine--tRNA ligasePRO_0000159553Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei326 – 3261PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53852.
PeptideAtlasiP53852.

PTM databases

iPTMnetiP53852.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGD2P388792EBI-29230,EBI-6379
TYS1P364212EBI-29230,EBI-18843

Protein-protein interaction databases

BioGridi35592. 17 interactions.
IntActiP53852. 4 interactions.
MINTiMINT-2491982.

Structurei

3D structure databases

ProteinModelPortaliP53852.
SMRiP53852. Positions 35-172, 210-578.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi65 – 7511"HIGH" regionAdd
BLAST
Motifi427 – 4315"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000006347.
HOGENOMiHOG000245252.
InParanoidiP53852.
KOiK01883.
OMAiLMESIAC.
OrthoDBiEOG75B8DZ.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
HAMAPiMF_00041. Cys_tRNA_synth.
InterProiIPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 2 hits.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SUPFAMiSSF47323. SSF47323. 1 hit.
TIGRFAMsiTIGR00435. cysS. 1 hit.

Sequencei

Sequence statusi: Complete.

P53852-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIFIKALRR YTIMSTPKIV QPKWKVPTPQ AKETVLKLYN SLTRSKVEFI
60 70 80 90 100
PQSGNRGVTW YSCGPTVYDA SHMGHARNYV SIDINRRIIQ DYFGYDVQFV
110 120 130 140 150
QNVTDIDDKI ILRARQNYLF DNFVKENDTK FNATVVDKVK TALFQYINKN
160 170 180 190 200
FTIQGSEIKT IEEFETWLSN ADTETLKLEN PKFPMHVTAV QNAIESITKG
210 220 230 240 250
DSMDAEVAFE KVKDVTVPLL DKELGSTISN PEIFRQLPAY WEQKFNDDML
260 270 280 290 300
SLNVLPPTVT TRVSEYVPEI IDFVQKIIDN GYAYATSDGS VYFDTLKFDK
310 320 330 340 350
SPNHDYAKCQ PWNKGQLDLI NDGEGSLSNF ADNGKKSNND FALWKASKAG
360 370 380 390 400
EPEWESPWGK GRPGWHIECS VMASDILGSN IDIHSGGIDL AFPHHDNELA
410 420 430 440 450
QSEARFDNQQ WINYFLHTGH LHIEGQKMSK SLKNFITIQE ALKKFSPRQL
460 470 480 490 500
RLAFASVQWN NQLDFKESLI HEVKSFENSM NNFFKTIRAL KNDAASAGHI
510 520 530 540 550
SKKFSPLEKE LLADFVESES KVHSAFCDNL STPVALKTLS ELVTKSNTYI
560 570 580 590 600
TTAGAALKIE PLIAICSYIT KILRIIGFPS RPDNLGWAAQ AGSNDGSLGS
610 620 630 640 650
LEDTVMPYVK CLSTFRDDVR SLAIKKAEPK EFLQLTDKIR NEDLLNLNVA
660 670 680 690 700
LDDRNGQSAL IKFLTNDEKL EIVKLNEEKH ANELAKKQKK LEQQKLREQK
710 720 730 740 750
ENERKQKAQI KPQDMFKDVT LYSAWDEQGL PTKDKDGNDI TKSMTKKLKK
760
QWEQQKKLHE EYFGEDK
Length:767
Mass (Da):87,530
Last modified:October 1, 1996 - v1
Checksum:i495D526781B4BE2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96722 Genomic DNA. Translation: CAA65497.1.
Z71523 Genomic DNA. Translation: CAA96154.1.
BK006947 Genomic DNA. Translation: DAA10312.1.
PIRiS63220.
RefSeqiNP_014152.1. NM_001183085.1.

Genome annotation databases

EnsemblFungiiYNL247W; YNL247W; YNL247W.
GeneIDi855474.
KEGGisce:YNL247W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X96722 Genomic DNA. Translation: CAA65497.1.
Z71523 Genomic DNA. Translation: CAA96154.1.
BK006947 Genomic DNA. Translation: DAA10312.1.
PIRiS63220.
RefSeqiNP_014152.1. NM_001183085.1.

3D structure databases

ProteinModelPortaliP53852.
SMRiP53852. Positions 35-172, 210-578.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35592. 17 interactions.
IntActiP53852. 4 interactions.
MINTiMINT-2491982.

PTM databases

iPTMnetiP53852.

Proteomic databases

MaxQBiP53852.
PeptideAtlasiP53852.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL247W; YNL247W; YNL247W.
GeneIDi855474.
KEGGisce:YNL247W.

Organism-specific databases

EuPathDBiFungiDB:YNL247W.
SGDiS000005191. YNL247W.

Phylogenomic databases

GeneTreeiENSGT00390000006347.
HOGENOMiHOG000245252.
InParanoidiP53852.
KOiK01883.
OMAiLMESIAC.
OrthoDBiEOG75B8DZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-33244-MONOMER.

Miscellaneous databases

PROiP53852.

Family and domain databases

Gene3Di3.40.50.620. 2 hits.
HAMAPiMF_00041. Cys_tRNA_synth.
InterProiIPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 2 hits.
PfamiPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SUPFAMiSSF47323. SSF47323. 1 hit.
TIGRFAMsiTIGR00435. cysS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence analysis of the 33 kb long region between ORC5 and SUI1 from the left arm of chromosome XIV from Saccharomyces cerevisiae."
    Sen-Gupta M., Gueldener U., Beinhauer J.D., Fiedler T.A., Hegemann J.H.
    Yeast 13:849-860(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Cysteinyl-tRNA synthetase from Saccharomyces cerevisiae. Purification, characterization and assignment to the genomic sequence YNL247w."
    Motorin Y., Le Caer J.-P., Waller J.-P.
    Biochimie 79:731-740(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 137-164; 247-269 AND 407-416, FUNCTION, SUBUNIT.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYC_YEAST
AccessioniPrimary (citable) accession number: P53852
Secondary accession number(s): D6W0U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 23000 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.