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P57558 (SYC_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. 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:BU487
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length464 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
Reference 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 – 464464Cysteine--tRNA ligase HAMAP-Rule MF_00041
PRO_0000159366

Regions

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

Sites

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

Sequences

Sequence LengthMass (Da)Tools
P57558 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 2EBD5EADA503AAC3

FASTA46454,541
        10         20         30         40         50         60 
MLKIFNTLTS TKEIFTPIKK NRVNLYVCGV TVYDFCHIGH GRTFVVFDMI VRYLRFSGFQ 

        70         80         90        100        110        120 
VKYVRNITDI DDKIISKSTK EKKKINTFTA SMIKEMHKDF DLLGISVPDE EPRVTDYIDN 

       130        140        150        160        170        180 
IIRIITTLIK KKHAYIHKNG DVIFSIDSDP NYGTLSRQSL TSLESGSRIP LNNMKKNPLD 

       190        200        210        220        230        240 
FILWKSSNKE EYSWDSPWGK GRPGWHIECS AITNVFFNNS IDIHGGGSDL LFPHHENERS 

       250        260        270        280        290        300 
QSICFNNKSM INFWMHTGMV ILNNKKMSKS LGNVYFLRNI LKDCDAEVLR YFFLSTHYRH 

       310        320        330        340        350        360 
PIYYCEKNLD QAYTSLKYLY TALYDTNPFF NNEEGLNFEL EFYNAMNDDF NTPAVFSIFF 

       370        380        390        400        410        420 
KIARKINFLK NKDILKTNKF AFRLKYLANN LGFLFQDPKE FLQKKTTLNL LTLKEIQLLI 

       430        440        450        460 
EKRNIARQSK LWQEADNIRK KLMSLDIILE DLPDKTIWRK NKKS 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB13183.1.
RefSeqNP_240297.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57558.
SMRP57558. Positions 1-402.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB13183; BAB13183; BAB13183.
GeneID1109833.
KEGGbuc:BU487.
PATRIC21244516. VBIBucAph127364_0495.

Phylogenomic databases

eggNOGCOG0215.
HOGENOMHOG000245250.
KOK01883.
OMAQIDIHAG.
OrthoDBEOG6RVFXC.
ProtClustDBPRK00260.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-487-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. SSF47323. 1 hit.
TIGRFAMsTIGR00435. cysS. 1 hit.
ProtoNetSearch...

Entry information

Entry nameSYC_BUCAI
AccessionPrimary (citable) accession number: P57558
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: February 19, 2014
This is version 87 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

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries