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Q06752 (SYC_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Cysteine--tRNA ligase

EC=6.1.1.16
Alternative name(s):
Cysteinyl-tRNA synthetase
Short name=CysRS
Gene names
Name:cysS
Synonyms:spnA
Ordered Locus Names:BSU00940
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length466 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00041.

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 466466Cysteine--tRNA ligase HAMAP-Rule MF_00041
PRO_0000159352

Regions

Motif31 – 4111"HIGH" region HAMAP-Rule MF_00041
Motif266 – 2705"KMSKS" region HAMAP-Rule MF_00041

Sites

Metal binding291Zinc By similarity
Metal binding2091Zinc By similarity
Metal binding2341Zinc By similarity
Metal binding2381Zinc By similarity
Binding site2691ATP By similarity

Amino acid modifications

Modified residue2701Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q06752 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 742D225C2E377CC3

FASTA46653,908
        10         20         30         40         50         60 
MTITLYNTLT RQKETFVPLE EGKVKMYVCG PTVYNYIHIG NARPAIVYDT VRNYLEYKGY 

        70         80         90        100        110        120 
DVQYVSNFTD VDDKLIKAAN ELGEDVPTIS ERFIKAYFED VGALGCRKAD LHPRVMENMD 

       130        140        150        160        170        180 
AIIEFVDQLV KKGYAYESEG DVYFKTRAFE GYGKLSQQSI DELRSGARIR VGEKKEDALD 

       190        200        210        220        230        240 
FALWKAAKEG EISWDSPWGK GRPGWHIECS AMVKKYLGDQ IDIHAGGQDL TFPHHENEIA 

       250        260        270        280        290        300 
QSEALTGKTF AKYWLHNGYI NIDNEKMSKS LGNFVLVHDI IKQHDPQLLR FFMLSVHYRH 

       310        320        330        340        350        360 
PINYSEELLE NTKSAFSRLK TAYSNLQHRL NSSTNLTEDD DQWLEKVEEH RKAFEEEMDD 

       370        380        390        400        410        420 
DFNTANAISV LFDLAKHANY YLQKDHTADH VITAFIEMFD RIVSVLGFSL GEQELLDQEI 

       430        440        450        460 
EDLIEKRNEA RRNRDFALSD QIRDQLKSMN IILEDTAQGT RWKRGE 

« Hide

References

« Hide 'large scale' references
[1]"Clustering and co-transcription of the Bacillus subtilis genes encoding the aminoacyl-tRNA synthetases specific for glutamate and for cysteine and the first enzyme for cysteine biosynthesis."
Gagnon Y., Breton R., Putzer H., Pelchat M., Grunberg-Manago M., Lapointe J.
J. Biol. Chem. 269:7473-7482(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"A mutant cysteinyl-tRNA synthetase affecting timing of chromosomal replication initiation in B. subtilis and conferring resistance to a protein kinase C inhibitor."
Seror S.J., Casaregola S., Vannier F., Zouari N., Dahl M., Boye E.
EMBO J. 13:2472-2480(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270, MASS SPECTROMETRY.
Strain: 168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L14580 Genomic DNA. Translation: AAA21798.1.
D26185 Genomic DNA. Translation: BAA05328.1.
X73989 Genomic DNA. Translation: CAA52167.1.
AL009126 Genomic DNA. Translation: CAB11870.1.
PIRC53402.
RefSeqNP_387975.1. NC_000964.3.

3D structure databases

ProteinModelPortalQ06752.
SMRQ06752. Positions 3-464.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU00940.

PTM databases

PhosSiteP0802198.

Proteomic databases

PaxDbQ06752.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB11870; CAB11870; BSU00940.
GeneID936859.
KEGGbsu:BSU00940.
PATRIC18971697. VBIBacSub10457_0097.

Organism-specific databases

GenoListBSU00940. [Micado]

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHOG000245250.
KOK01883.
OMADFDALNM.
ProtClustDBPRK00260.

Enzyme and pathway databases

BioCycBSUB:BSU00940-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00041. Cys_tRNA_synth.
InterProIPR015803. Cys-tRNA-ligase.
IPR015273. Cys-tRNA-synt_Ia_DALR.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR10890. PTHR10890. 1 hit.
PfamPF09190. DALR_2. 1 hit.
PF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SMARTSM00840. DALR_2. 1 hit.
[Graphical view]
SUPFAMSSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00435. cysS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYC_BACSU
AccessionPrimary (citable) accession number: Q06752
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families