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Q9UY11 (SYW_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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:PYRAB16970
ORF Names:PAB1111
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length385 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 – 385385Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136727

Regions

Motif82 – 909"HIGH" region HAMAP-Rule MF_00140
Motif253 – 2575"KMSKS" region HAMAP-Rule MF_00140

Sequences

Sequence LengthMass (Da)Tools
Q9UY11 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4C29D01414976B12

FASTA38545,100
        10         20         30         40         50         60 
MVEDFKVTPW EVEGVVDYNK LIEHFGTSPL TEELLEKTAE LTKSELPLFF RRKFFFSHRD 

        70         80         90        100        110        120 
YDKVLQDYEE GRGFFLYTGR GPSGPMHIGH IIPFFATKWL QEKFGVNLYI QITDDEKFLF 

       130        140        150        160        170        180 
KENLTFEDTK HWAYENILDI IAVGFDPDKT FIFQNSEFTK IYEMAIPIAK KINFSMAKAV 

       190        200        210        220        230        240 
FGFTEQSKIG MIFFPAIQIA PTFFEKRRCL IPAAIDQDPY WRLQRDFAES LGYYKTAAIH 

       250        260        270        280        290        300 
SKFVPSLTSL SGKMSASKPE TAIYLTDSPE DVEKKVWKFA LTGGRPTLKE QREKGGEPEK 

       310        320        330        340        350        360 
CVVFKWLEIF FEEDDKKLKE RYYACKNGEL TCGECKRYLI SKIQEFLKEH QKRRKKAEKQ 

       370        380 
IEKFKYTGKL AQEMWDKAIP EPLKG 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248288 Genomic DNA. Translation: CAB50601.1.
HE613800 Genomic DNA. Translation: CCE71167.1.
PIRC75020.
RefSeqNP_127372.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UY11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50601; CAB50601; PAB1111.
GeneID1495996.
KEGGpab:PAB1111.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000224742.
KOK01867.
OMAKPETAIY.
ProtClustDBPRK12285.

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_PYRAB
AccessionPrimary (citable) accession number: Q9UY11
Secondary accession number(s): G8ZK60
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 80 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