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Protein

Cysteine--tRNA ligase

Gene

cysS

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Zinc
Metal bindingi209 – 2091Zinc
Metal bindingi234 – 2341Zinc
Metal bindingi238 – 2381Zinc
Binding sitei269 – 2691ATPBy similarity

GO - Molecular functioni

  • aminoacyl-tRNA ligase activity Source: EcoliWiki
  • ATP binding Source: EcoliWiki
  • cysteine-tRNA ligase activity Source: EcoliWiki
  • ligase activity Source: EcoliWiki
  • metal ion binding Source: EcoliWiki
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • cysteinyl-tRNA aminoacylation Source: EcoliWiki
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

BioCyciEcoCyc:CYSS-MONOMER.
ECOL316407:JW0515-MONOMER.
MetaCyc:CYSS-MONOMER.
BRENDAi6.1.1.16. 2026.
SABIO-RKP21888.

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
Name:cysS
Ordered Locus Names:b0526, JW0515
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10196. cysS.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 461461Cysteine--tRNA ligasePRO_0000159394Add
BLAST

Proteomic databases

EPDiP21888.
PaxDbiP21888.
PRIDEiP21888.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi4262015. 12 interactions.
IntActiP21888. 3 interactions.
MINTiMINT-1240309.
STRINGi511145.b0526.

Structurei

Secondary structure

1
461
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Turni7 – 93Combined sources
Beta strandi10 – 145Combined sources
Beta strandi22 – 276Combined sources
Beta strandi31 – 344Combined sources
Helixi38 – 5720Combined sources
Beta strandi60 – 656Combined sources
Helixi72 – 809Combined sources
Helixi85 – 10218Combined sources
Helixi114 – 1163Combined sources
Helixi118 – 13013Combined sources
Beta strandi133 – 1364Combined sources
Beta strandi142 – 1443Combined sources
Helixi146 – 1483Combined sources
Turni150 – 1578Combined sources
Helixi160 – 1656Combined sources
Beta strandi181 – 1866Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi200 – 2034Combined sources
Helixi207 – 21711Combined sources
Beta strandi219 – 2257Combined sources
Helixi228 – 2303Combined sources
Turni231 – 2333Combined sources
Helixi234 – 24512Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi260 – 2623Combined sources
Helixi269 – 2713Combined sources
Helixi277 – 2815Combined sources
Helixi286 – 2949Combined sources
Beta strandi302 – 3043Combined sources
Helixi306 – 32318Combined sources
Helixi336 – 34712Combined sources
Helixi352 – 37221Combined sources
Helixi374 – 38815Combined sources
Turni389 – 3924Combined sources
Helixi398 – 4014Combined sources
Beta strandi406 – 4083Combined sources
Helixi413 – 4164Combined sources
Helixi419 – 42810Combined sources
Helixi432 – 44413Combined sources
Beta strandi447 – 4515Combined sources
Beta strandi456 – 4605Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LI5X-ray2.30A/B1-461[»]
1LI7X-ray2.60A/B1-461[»]
1U0BX-ray2.30B1-461[»]
ProteinModelPortaliP21888.
SMRiP21888. Positions 1-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21888.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 4011"HIGH" regionAdd
BLAST
Motifi266 – 2705"KMSKS" region

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245250.
InParanoidiP21888.
KOiK01883.
OMAiHENEACQ.
OrthoDBiEOG6RVFXC.
PhylomeDBiP21888.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00041. Cys_tRNA_synth.
InterProiIPR015803. Cys-tRNA-ligase.
IPR015273. Cys-tRNA-synt_Ia_DALR.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
IPR009080. tRNAsynth_Ia_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF09190. DALR_2. 1 hit.
PF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SMARTiSM00840. DALR_2. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
TIGRFAMsiTIGR00435. cysS. 1 hit.

Sequencei

Sequence statusi: Complete.

P21888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLKIFNTLTR QKEEFKPIHA GEVGMYVCGI TVYDLCHIGH GRTFVAFDVV
60 70 80 90 100
ARYLRFLGYK LKYVRNITDI DDKIIKRANE NGESFVAMVD RMIAEMHKDF
110 120 130 140 150
DALNILRPDM EPRATHHIAE IIELTEQLIA KGHAYVADNG DVMFDVPTDP
160 170 180 190 200
TYGVLSRQDL DQLQAGARVD VVDDKRNPMD FVLWKMSKEG EPSWPSPWGA
210 220 230 240 250
GRPGWHIECS AMNCKQLGNH FDIHGGGSDL MFPHHENEIA QSTCAHDGQY
260 270 280 290 300
VNYWMHSGMV MVDREKMSKS LGNFFTVRDV LKYYDAETVR YFLMSGHYRS
310 320 330 340 350
QLNYSEENLK QARAALERLY TALRGTDKTV APAGGEAFEA RFIEAMDDDF
360 370 380 390 400
NTPEAYSVLF DMAREVNRLK AEDMAAANAM ASHLRKLSAV LGLLEQEPEA
410 420 430 440 450
FLQSGAQADD SEVAEIEALI QQRLDARKAK DWAAADAARD RLNEMGIVLE
460
DGPQGTTWRR K
Length:461
Mass (Da):52,202
Last modified:May 1, 1992 - v2
Checksum:i2FA77FDBB7C5BA99
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti316 – 3161L → V in CAA39691 (PubMed:2014166).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56234 Genomic DNA. Translation: CAA39691.1.
M59381 Genomic DNA. Translation: AAA23658.1.
X59293 Genomic DNA. Translation: CAA41983.1.
U82664 Genomic DNA. Translation: AAB40279.1.
U00096 Genomic DNA. Translation: AAC73628.1.
AP009048 Genomic DNA. Translation: BAE76303.1.
PIRiA37868. YYEC.
RefSeqiNP_415059.1. NC_000913.3.
WP_000912385.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73628; AAC73628; b0526.
BAE76303; BAE76303; BAE76303.
GeneIDi946969.
KEGGiecj:JW0515.
eco:b0526.
PATRICi32116212. VBIEscCol129921_0547.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56234 Genomic DNA. Translation: CAA39691.1.
M59381 Genomic DNA. Translation: AAA23658.1.
X59293 Genomic DNA. Translation: CAA41983.1.
U82664 Genomic DNA. Translation: AAB40279.1.
U00096 Genomic DNA. Translation: AAC73628.1.
AP009048 Genomic DNA. Translation: BAE76303.1.
PIRiA37868. YYEC.
RefSeqiNP_415059.1. NC_000913.3.
WP_000912385.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LI5X-ray2.30A/B1-461[»]
1LI7X-ray2.60A/B1-461[»]
1U0BX-ray2.30B1-461[»]
ProteinModelPortaliP21888.
SMRiP21888. Positions 1-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262015. 12 interactions.
IntActiP21888. 3 interactions.
MINTiMINT-1240309.
STRINGi511145.b0526.

Proteomic databases

EPDiP21888.
PaxDbiP21888.
PRIDEiP21888.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73628; AAC73628; b0526.
BAE76303; BAE76303; BAE76303.
GeneIDi946969.
KEGGiecj:JW0515.
eco:b0526.
PATRICi32116212. VBIEscCol129921_0547.

Organism-specific databases

EchoBASEiEB0193.
EcoGeneiEG10196. cysS.

Phylogenomic databases

eggNOGiENOG4105C8N. Bacteria.
COG0215. LUCA.
HOGENOMiHOG000245250.
InParanoidiP21888.
KOiK01883.
OMAiHENEACQ.
OrthoDBiEOG6RVFXC.
PhylomeDBiP21888.

Enzyme and pathway databases

BioCyciEcoCyc:CYSS-MONOMER.
ECOL316407:JW0515-MONOMER.
MetaCyc:CYSS-MONOMER.
BRENDAi6.1.1.16. 2026.
SABIO-RKP21888.

Miscellaneous databases

EvolutionaryTraceiP21888.
PROiP21888.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00041. Cys_tRNA_synth.
InterProiIPR015803. Cys-tRNA-ligase.
IPR015273. Cys-tRNA-synt_Ia_DALR.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR032678. tRNA-synt_1_cat_dom.
IPR009080. tRNAsynth_Ia_anticodon-bd.
[Graphical view]
PANTHERiPTHR10890. PTHR10890. 1 hit.
PfamiPF09190. DALR_2. 1 hit.
PF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSiPR00983. TRNASYNTHCYS.
SMARTiSM00840. DALR_2. 1 hit.
[Graphical view]
SUPFAMiSSF47323. SSF47323. 1 hit.
TIGRFAMsiTIGR00435. cysS. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cysteinyl-tRNA synthetase: determination of the last E. coli aminoacyl-tRNA synthetase primary structure."
    Eriani G., Dirheimer G., Gangloff J.
    Nucleic Acids Res. 19:265-269(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
    Strain: K12.
  2. "Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase."
    Hou Y.M., Shiba K., Mottes C., Schimmel P.
    Proc. Natl. Acad. Sci. U.S.A. 88:976-980(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cysteinyl-tRNA synthetase is a direct descendant of the first aminoacyl-tRNA synthetase."
    Avalos J., Corrochano L.M., Brenner S.
    FEBS Lett. 286:176-180(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: K12.
  4. "Sequence of minutes 4-25 of Escherichia coli."
    Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  7. "Crystallization and preliminary diffraction analysis of Escherichia coli cysteinyl-tRNA synthetase."
    Newberry K.J., Kohn J., Hou Y.-M., Perona J.J.
    Acta Crystallogr. D 55:1046-1047(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  8. "Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase."
    Newberry K.J., Hou Y.-M., Perona J.J.
    EMBO J. 21:2778-2787(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).

Entry informationi

Entry nameiSYC_ECOLI
AccessioniPrimary (citable) accession number: P21888
Secondary accession number(s): Q2MBQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1992
Last modified: July 6, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.