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Q68XV4 (SYC_RICTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 50. 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:RT0051
OrganismRickettsia typhi (strain ATCC VR-144 / Wilmington) [Complete proteome] [HAMAP]
Taxonomic identifier257363 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiatyphus group

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP MF_00041

Subunit structure

Monomer By similarity. HAMAP MF_00041

Subcellular location

Cytoplasm HAMAP 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: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

cysteine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457Cysteine--tRNA ligase HAMAP MF_00041
PRO_0000159470

Regions

Motif31 – 4111"HIGH" region HAMAP MF_00041
Motif272 – 2765"KMSKS" region HAMAP MF_00041

Sites

Metal binding291Zinc By similarity
Metal binding2141Zinc By similarity
Metal binding2391Zinc By similarity
Metal binding2431Zinc By similarity
Binding site2751ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q68XV4 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: 22BBA46DE77D5384

FASTA45753,143
        10         20         30         40         50         60 
MQLHLYNTLT RTKEVFNPQD HANVKMYVCG PTVYDNPHIG NSRSVVVYDL LYRIIIKIFG 

        70         80         90        100        110        120 
KKAVKYVRNI TDIDDKIIDR AESLGININD LTNKVTREFH INMAYLGCML PSIEPKATEH 

       130        140        150        160        170        180 
IDVMIEIIER LIAQDHAYIT DNHVYFDVLS APNYTELSNR NLEEMFEGVR IENSKTKKNP 

       190        200        210        220        230        240 
QDFVLWKPAK QNEPKNVNFS SPWGLGRPGW HIECSAMSYK YLGENFDIHG GGADLIFPHH 

       250        260        270        280        290        300 
TNEIAQSRCA FPSSTYAKYW IHNGFLTVNG EKMSKSLGNF ITVRDLMDKQ IQGEVVRLFL 

       310        320        330        340        350        360 
LSSHYRRPLD YNDKAIDDAK KTLDYWYRAI KEINVQKVDL PSDFMQSLFD DMNTPLAIKI 

       370        380        390        400        410        420 
INDYAKGVFI SKTEAERKFN ASAIITCANF IGLMRKTQYE WFNNDIDKLY INELINKRLK 

       430        440        450 
AKKQKNWLLA DKIRNQLLEK KIILEDKSDC TTIWRKE 

« Hide

References

[1]"Complete genome sequence of Rickettsia typhi and comparison with sequences of other Rickettsiae."
McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E., McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E., Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A. expand/collapse author list , Hong C., Yu X.-J., Walker D.H., Weinstock G.M.
J. Bacteriol. 186:5842-5855(2004) [PubMed: 15317790] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC VR-144 / Wilmington.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017197 Genomic DNA. Translation: AAU03538.1.
RefSeqYP_067020.1. NC_006142.1.

3D structure databases

ProteinModelPortalQ68XV4.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2958761.
GenomeReviewsGene locus RT0051 in contig AE017197_GR.
KEGGrty:RT0051.
PATRIC17909254. VBIRicTyp34752_0049.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG327651.
OMADFDALNM.
ProtClustDBPRK00260.

Enzyme and pathway databases

BioCycRTYP257363:RT0051-MONOMER.

Family and domain databases

HAMAPMF_00041. Cys_tRNA_synth.
[Tree]
InterProIPR015803. Cys-tRNA-synt.
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]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01883.
PANTHERPTHR10890. Cys_tRNA-synt_1a. 1 hit.
PfamPF01406. 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_RICTY
AccessionPrimary (citable) accession number: Q68XV4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 50 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

Rickettsia typhi

Rickettsia typhi (strain Wilmington): entries and gene names

SIMILARITY comments

Index of protein domains and families