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Q2YN22 (SYC_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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
Ordered Locus Names:BAB1_0697
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length506 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. HAMAP-Rule MF_00041

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00041

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00041.

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: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

cysteine-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 506506Cysteine--tRNA ligase HAMAP-Rule MF_00041
PRO_0000240894

Regions

Motif36 – 4611"HIGH" region HAMAP-Rule MF_00041
Motif302 – 3065"KMSKS" region HAMAP-Rule MF_00041

Sites

Metal binding341Zinc By similarity
Metal binding2301Zinc By similarity
Metal binding2691Zinc By similarity
Metal binding2731Zinc By similarity
Binding site3051ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YN22 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 5B1DB5A1554DA639

FASTA50656,284
        10         20         30         40         50         60 
MPDTTPQLRL YNTLTRTKEA FAPIDAKNVR MYVCGPTVYD FAHIGNARPV IVFDVLFRLL 

        70         80         90        100        110        120 
RHVYGAQHVT YARNITDVDD KINARAARDY PDLPFNEAIR KVTESTNAQF QADVTALGNL 

       130        140        150        160        170        180 
QPTVQPRATE HMDEMRAMID RLVQRGVAYV AQDHVLFSPS AMNARKGPRY GALARRSLDE 

       190        200        210        220        230        240 
MLAGARVDVA SYKRDEMDFV LWKPSKKGEP GWPSPAGIET LGRPGWHIEC SAMSMAKLLE 

       250        260        270        280        290        300 
PFGGGLKCDD PERNQFDIHG GGIDLVFPHH ENEIAQSCCA LGTERMANIW MHNGFLQVEG 

       310        320        330        340        350        360 
QKMSKSLGNF ITIRDVLNDG LPQLGEWGDN TVRDHWAGLA ARLSMLQTHY REPINWTAQR 

       370        380        390        400        410        420 
LAESADELHR WYGLLRDEGF GAPEKLSHAS AVAAALCDDL NSWAAITALR QAFKVRDVAA 

       430        440        450        460        470        480 
LGEGMALMGL LDPYFVTASD VPIFARADVD ASAIAARIAE RLNFINAKNW AEADRIRDEL 

       490        500 
LQEGVQLKDS KDPATGERIT TWDVVG 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ10653.1.
RefSeqYP_414139.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YN22.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_0697.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ10653; CAJ10653; BAB1_0697.
GeneID3787412.
KEGGbmf:BAB1_0697.
PATRIC17844286. VBIBruMel86222_0726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHOG000245250.
KOK01883.
OMAFGTERMA.
OrthoDBEOG6RVFXC.

Enzyme and pathway databases

BioCycBABO359391:GKDV-706-MONOMER.
BMEL359391:GJOQ-706-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00041. Cys_tRNA_synth.
InterProIPR015803. Cys-tRNA-ligase.
IPR024909. Cys-tRNA/MSH_ligase.
IPR014729. Rossmann-like_a/b/a_fold.
IPR009080. tRNAsynth_1a_anticodon-bd.
[Graphical view]
PANTHERPTHR10890. PTHR10890. 1 hit.
PfamPF01406. tRNA-synt_1e. 1 hit.
[Graphical view]
PRINTSPR00983. TRNASYNTHCYS.
SUPFAMSSF47323. SSF47323. 1 hit.
TIGRFAMsTIGR00435. cysS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYC_BRUA2
AccessionPrimary (citable) accession number: Q2YN22
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries