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Reviewed, UniProtKB/Swiss-Prot P21888 (SYC_ECOLI)

Last modified June 16, 2009. Version 90. 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:
    Cysteinyl-tRNA synthetase
    EC=6.1.1.16
Alternative name(s):
    Cysteine--tRNA ligase
      Short name=CysRS
Gene names
Name: cysS
Ordered Locus Names: b0526, JW0515
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length461 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-cysteinyl-tRNA(Cys). HAMAP MF_00041

Cofactor

Binds 1 zinc ion per subunit. HAMAP MF_00041

Subunit structure

Monomer. HAMAP MF_00041

Subcellular location

Cytoplasm. HAMAP MF_00041

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family.

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Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processcysteinyl-tRNA aminoacylation

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

cysteine-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 461461Cysteinyl-tRNA synthetase HAMAP MF_00041
PRO_0000159394

Regions

Motif30 – 4011"HIGH" region HAMAP MF_00041
Motif266 – 2705"KMSKS" region HAMAP MF_00041

Sites

Metal binding281Zinc HAMAP MF_00041
Metal binding2091Zinc HAMAP MF_00041
Metal binding2341Zinc HAMAP MF_00041
Metal binding2381Zinc HAMAP MF_00041
Binding site2691ATP By similarity

Experimental info

Sequence conflict3161L → V in CAA39691. Ref.1

Secondary structure

1 .............................................................................. 461
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P21888-1 [UniParc].

Last modified May 1, 1992. Version 2.
Checksum: 2FA77FDBB7C5BA99

FASTA46152,202
        10         20         30         40         50         60 
MLKIFNTLTR QKEEFKPIHA GEVGMYVCGI TVYDLCHIGH GRTFVAFDVV ARYLRFLGYK 

        70         80         90        100        110        120 
LKYVRNITDI DDKIIKRANE NGESFVAMVD RMIAEMHKDF DALNILRPDM EPRATHHIAE 

       130        140        150        160        170        180 
IIELTEQLIA KGHAYVADNG DVMFDVPTDP TYGVLSRQDL DQLQAGARVD VVDDKRNPMD 

       190        200        210        220        230        240 
FVLWKMSKEG EPSWPSPWGA GRPGWHIECS AMNCKQLGNH FDIHGGGSDL MFPHHENEIA 

       250        260        270        280        290        300 
QSTCAHDGQY VNYWMHSGMV MVDREKMSKS LGNFFTVRDV LKYYDAETVR YFLMSGHYRS 

       310        320        330        340        350        360 
QLNYSEENLK QARAALERLY TALRGTDKTV APAGGEAFEA RFIEAMDDDF NTPEAYSVLF 

       370        380        390        400        410        420 
DMAREVNRLK AEDMAAANAM ASHLRKLSAV LGLLEQEPEA FLQSGAQADD SEVAEIEALI 

       430        440        450        460 
QQRLDARKAK DWAAADAARD RLNEMGIVLE DGPQGTTWRR K

« Hide

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References

« Hide 'large scale' references
[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: 2014166] [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: 1992490] [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: 1864365] [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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 10216301] [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: 12032090] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

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.
PIRYYEC. A37868.
RefSeqAP_001173.1.
NP_415059.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1LI5X-ray2.30A/B1-461[»]
1LI7X-ray2.60A/B1-461[»]
1U0BX-ray2.30B1-461[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:9386N.

Genome annotation databases

GeneID946969.
GenomeReviewsGene locus JW0515 in contig AP009048_GR.
Gene locus b0526 in contig U00096_GR.
KEGGecj:JW0515.
eco:b0526.

Organism-specific databases

EchoBASEEB0193.
EcoGeneEG10196. cysS.
CMRSearch...

Phylogenomic databases

HOGENOMP21888.
OMAP21888. VLWKAAK.

Enzyme and pathway databases

BioCycEcoCyc:CYSS-MON.
MetaCyc:CYSS-MON.

Family and domain databases

HAMAPMF_00041.
[Tree]
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR015804. Cys-tRNA-synt_Ia_C.
IPR015273. Cys-tRNA-synt_Ia_DALR.
IPR015803. Cys-tRNA-synt_Ia_N.
IPR002308. Cys-tRNA-synth_1a.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF09190. DALR_2. 1 hit.
PF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
TIGRFAMsTIGR00435. cysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameSYC_ECOLI
AccessionPrimary (citable) accession number: P21888
Secondary accession number(s): Q2MBQ3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1992
Last modified: June 16, 2009
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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