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Q1G8Z0 (SYC_LACDA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Ordered Locus Names:Ldb1680
OrganismLactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081) [Complete proteome] [HAMAP]
Taxonomic identifier390333 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Metal-binding
Nucleotide-binding
Zinc
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
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: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Cysteine--tRNA ligase HAMAP-Rule MF_00041
PRO_0000332838

Regions

Motif29 – 3911"HIGH" region HAMAP-Rule MF_00041
Motif271 – 2755"KMSKS" region HAMAP-Rule MF_00041

Sites

Metal binding271Zinc By similarity
Metal binding2121Zinc By similarity
Metal binding2371Zinc By similarity
Metal binding2411Zinc By similarity
Binding site2741ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1G8Z0 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 5EC6439AEE65F809

FASTA47453,673
        10         20         30         40         50         60 
MKLFNTLTRQ KEEFKPLVPG QVSMYVCGPT VYNYIHIGNA RSAIAFDTIR RYFEYKGYKV 

        70         80         90        100        110        120 
NYVSNFTDVD DKMINEAGAE GTTVPELAER YIQAFLEDTR ALNIEEATLH PRATHEIPAI 

       130        140        150        160        170        180 
IDFIQTLIDK GYAYEADGDV YYRTKKFADY GHLSDQNIDQ LEEGASQHVN DEEQGRKEDP 

       190        200        210        220        230        240 
IDFALWKGQK AADEIAWDSP WGKGRPGWHI ECSVMSTKYL GDTLDIHGGG QDLEFPHHEN 

       250        260        270        280        290        300 
EIAQSEAKTG KKFVNYWLHN GFVTVGKDEE KMSKSLHNCV TVHDILKNVD PQVLRFFMAS 

       310        320        330        340        350        360 
VQYRSQINYS EENLEQAANI LGRFKNTLEG INYRLADATE GLPDPDLAKL VTETTAKFEA 

       370        380        390        400        410        420 
AMDDDFNVQN ALTAIYEALP AVNSNANAEK ADKESLRLFA KKLAAWLSVF GLDVDKLLAK 

       430        440        450        460        470 
EAGDDDAVIE ELVAQRTEAR KNKDWAKSDE LRDQLKEMGV VLKDTPQGTR WSRE 

« Hide

References

[1]"The complete genome sequence of Lactobacillus bulgaricus reveals extensive and ongoing reductive evolution."
van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P., Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R., Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P. expand/collapse author list , Weissenbach J., Ehrlich S.D., Maguin E.
Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 11842 / DSM 20081.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954253 Genomic DNA. Translation: CAI98469.1.
RefSeqYP_619450.1. NC_008054.1.

3D structure databases

ProteinModelPortalQ1G8Z0.
ModBaseSearch...

Protein-protein interaction databases

STRING390333.Ldb1680.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI98469; CAI98469; Ldb1680.
GeneID4084553.
KEGGldb:Ldb1680.
PATRIC22218804. VBILacDel123523_1508.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHOG000245250.
KOK01883.
OMADFDALNM.
ProtClustDBPRK00260.

Enzyme and pathway databases

BioCycLDEL390333:GIXG-1659-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_LACDA
AccessionPrimary (citable) accession number: Q1G8Z0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 27, 2006
Last modified: May 1, 2013
This is version 57 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

SIMILARITY comments

Index of protein domains and families