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Q87L13 (SYW_VIBPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 65. 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:VP2804
OrganismVibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) [Complete proteome] [HAMAP]
Taxonomic identifier223926 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length338 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 – 338338Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136707

Regions

Motif12 – 209"HIGH" region HAMAP-Rule MF_00140
Motif198 – 2025"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site2011ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87L13 [UniParc].

Last modified May 23, 2003. Version 1.
Checksum: 4D7F6D9D20587C96

FASTA33837,648
        10         20         30         40         50         60 
MSKPIVLSGV QPSGELSIGN YLGALRQWQQ MQDDYDCQYC VVDLHAVTVR QDPKALHEAT 

        70         80         90        100        110        120 
LDALAICLAV GVDPKKSTLF VQSHVPEHAQ LGWLLNCYTQ MGELSRMTQF KDKSARYAND 

       130        140        150        160        170        180 
VNVGLFDYPV LMAADILLYG AHQVPVGSDQ KQHLELARDI ATRFNNIYSP ESPIFTVPEP 

       190        200        210        220        230        240 
YIPTVNARVM SLQDATKKMS KSDDNRKNVI TLLEEPKSII KKINKAQTDT ETPPSIRHDV 

       250        260        270        280        290        300 
ENKAGIANLM GLYSAATGMS FEEIEAKYKG VEMYGPFKKD VGEAVVAMLE PIQEEYRRIR 

       310        320        330 
ADRAFMDEVM KQGAEKASAR AAETLKKAYE AVGFVARP 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000031 Genomic DNA. Translation: BAC61067.1.
RefSeqNP_799183.1. NC_004603.1.

3D structure databases

ProteinModelPortalQ87L13.
SMRQ87L13. Positions 5-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING223926.VP2804.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC61067; BAC61067; BAC61067.
GeneID1190354.
KEGGvpa:VP2804.
PATRIC20143808. VBIVibPar50997_2696.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000059940.
KOK01867.
OMAGWGQFKP.
OrthoDBEOG686NJQ.
ProtClustDBPRK00927.

Enzyme and pathway databases

BioCycVPAR223926:GHK4-2898-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00140_B. Trp_tRNA_synth_B.
InterProIPR002305. 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.
ProtoNetSearch...

Entry information

Entry nameSYW_VIBPA
AccessionPrimary (citable) accession number: Q87L13
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: May 23, 2003
Last modified: February 19, 2014
This is version 65 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