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Q5HW79 (SYW_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 56. 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:
Tryptophan--tRNA ligase

EC=6.1.1.2
Alternative name(s):
Tryptophanyl-tRNA synthetase
Short name=TrpRS
Gene names
Name:trpS
Ordered Locus Names:CJE0437
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). HAMAP-Rule MF_00140

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00140

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00140.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtryptophanyl-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

tryptophan-tRNA ligase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136614

Regions

Motif9 – 179"HIGH" region HAMAP-Rule MF_00140
Motif189 – 1935"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site1921ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HW79 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: CB620B2B67AA6666

FASTA31936,084
        10         20         30         40         50         60 
MRVLTGLQPS GDLHIGNYFG AIKQMVDAQE KSQMFMFIAN YHAMTSSQDG EKLKQNSLKA 

        70         80         90        100        110        120 
AAAFLSLGID PQKSVFWLQS DVKEVMELYW ILSQFTPMGL LERAHSYKDK VAKGLSASHG 

       130        140        150        160        170        180 
LFSYPVLMAA DILLFDTRIV PVGKDQIQHV EIARDIALKV NNEWGEIFTL PEARVNEEVA 

       190        200        210        220        230        240 
VVVGTDGAKM SKSYQNTIDI FSSEKTLKKQ ISSIVTDSTA LEDPKDHENC NIFKIAKLFL 

       250        260        270        280        290        300 
DESGQKELQI RYEKGGEGYG HFKIYLNELV NAYFKEAREK YNELLEKPSH LKEILDFGAT 

       310 
KARKIAQEKM QKIYEKIGL 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35026.1.
RefSeqYP_178456.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HW79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE0437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW35026; AAW35026; CJE0437.
GeneID3231199.
KEGGcjr:CJE0437.
PATRIC20042574. VBICamJej134361_0436.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000059939.
KOK01867.
OMAKHRISAG.
OrthoDBEOG686NJQ.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-442-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00140_B. Trp_tRNA_synth_B.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
IPR024109. Trp-tRNA-ligase_bac-type.
[Graphical view]
PANTHERPTHR10055. PTHR10055. 1 hit.
PfamPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSPR01039. TRNASYNTHTRP.
TIGRFAMsTIGR00233. trpS. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYW_CAMJR
AccessionPrimary (citable) accession number: Q5HW79
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 56 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

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries