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B6YUH1 (SYW_THEON) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 33. 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:TON_1666
OrganismThermococcus onnurineus (strain NA1) [Complete proteome] [HAMAP]
Taxonomic identifier523850 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length384 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

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 – 384384Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_1000096114

Regions

Motif81 – 899"HIGH" region HAMAP-Rule MF_00140
Motif252 – 2565"KMSKS" region HAMAP-Rule MF_00140

Sequences

Sequence LengthMass (Da)Tools
B6YUH1 [UniParc].

Last modified January 20, 2009. Version 1.
Checksum: F51516595CC2B64C

FASTA38444,884
        10         20         30         40         50         60 
MDEFKVTPWD VEGLVDYNKL IEEFGTSPLT DELLEKTAQL TKSELPLYFR RRFFFSHRDY 

        70         80         90        100        110        120 
DKVLQDYESG KGFFLYTGRG PSGPMHIGHI IPFFATKWLQ EKFGVNLYIQ ITDDEKFLFK 

       130        140        150        160        170        180 
DKLTFEDTKY WAYQNILDII AVGFDPDRTF IFQDSEFTKI YEMAIPIAKK INFSMAKAVF 

       190        200        210        220        230        240 
GFTEQSKIGM IFYPAIQAAP TFFEKKRCLI PAAIDQDPYW RLQRDFAESL GYYKTAAIHS 

       250        260        270        280        290        300 
KFVPGLMGLE GKMSASKPET AIYLTDDPEE VGRKIWKYAL TGGRATAKEQ REKGGEPEKC 

       310        320        330        340        350        360 
VVFKWLEIFF EEDDKKLMER YHACKNGELL CGQCKRYLIK KVQEFLKEHQ KKRKEAEKKV 

       370        380 
EKFKYTGELA REQWDKAVPE ALKG 

« Hide

References

[1]"The complete genome sequence of Thermococcus onnurineus NA1 reveals a mixed heterotrophic and carboxydotrophic metabolism."
Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H., Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J., Colwell R.R., Kim S.-J., Lee J.-H.
J. Bacteriol. 190:7491-7499(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000855 Genomic DNA. Translation: ACJ17156.1.
RefSeqYP_002308053.1. NC_011529.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING523850.TON_1666.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ17156; ACJ17156; TON_1666.
GeneID7017335.
KEGGton:TON_1666.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000224742.
KOK01867.
OMAKTFIFNN.

Enzyme and pathway databases

BioCycTONN523850:GC7X-1716-MONOMER.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00140_A. Trp_tRNA_synth_A.
InterProIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
IPR020653. Tryptophan-tRNA-ligase_arc.
[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_THEON
AccessionPrimary (citable) accession number: B6YUH1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 20, 2009
Last modified: May 14, 2014
This is version 33 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