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C6A032 (SYW_THESM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 30. 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:TSIB_1964
OrganismThermococcus sibiricus (strain MM 739 / DSM 12597) [Complete proteome] [HAMAP]
Taxonomic identifier604354 [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_1000203257

Regions

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

Sequences

Sequence LengthMass (Da)Tools
C6A032 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 5EE79B3DAC942C65

FASTA38444,610
        10         20         30         40         50         60 
MPEFEVTPWE VTGVVDYNKL IEEFGTTPLT DDLLKKTEEL TKKELPMYFK RKFFFSHRDY 

        70         80         90        100        110        120 
DLVLKDYEAG KGFFLYTGRG PSGPMHIGHI IPFFATKWLQ ENFGVNLYVQ ITDDEKFLFK 

       130        140        150        160        170        180 
PQLTFEGTKR WAYENILDII AVGFDPDKTF IFQDSEFTKI YEMAIPIAKK VTYSMAKAVF 

       190        200        210        220        230        240 
GFNEQSKIGM IFFPAIQAAP TFFEEKRSLI PAAIDQDPYW RIQRDFAESL GYYKTAALHS 

       250        260        270        280        290        300 
KFVPGLMGLG GKMSASKPET AIYLTDDPEE AGKKIWKYAL TGGRATAKEQ RELGGEPDKC 

       310        320        330        340        350        360 
VVFKWLEIFF EPDEKKLLER YIACKNGEIL CGQCKRYLIE KVQNFLKEHQ EKREKAKKEI 

       370        380 
EKFKYTGDLA REQWDKAIPE PLRK 

« Hide

References

[1]"Metabolic versatility and indigenous origin of the archaeon Thermococcus sibiricus, isolated from a siberian oil reservoir, as revealed by genome analysis."
Mardanov A.V., Ravin N.V., Svetlitchnyi V.A., Beletsky A.V., Miroshnichenko M.L., Bonch-Osmolovskaya E.A., Skryabin K.G.
Appl. Environ. Microbiol. 75:4580-4588(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MM 739 / DSM 12597.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001463 Genomic DNA. Translation: ACS91013.1.
RefSeqYP_002995362.1. NC_012883.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING604354.TSIB_1964.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS91013; ACS91013; TSIB_1964.
GeneID8096977.
KEGGtsi:TSIB_1964.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000224742.
KOK01867.
OMAKPETAIY.
ProtClustDBPRK12285.

Enzyme and pathway databases

BioCycTSIB604354:GHMS-2010-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_THESM
AccessionPrimary (citable) accession number: C6A032
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 30 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