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Q7VPB2 (SYW_HAEDU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 63. 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:HD_0177
OrganismHaemophilus ducreyi (strain 35000HP / ATCC 700724) [Complete proteome] [HAMAP]
Taxonomic identifier233412 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length342 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 – 342342Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136634

Regions

Motif12 – 209"HIGH" region HAMAP-Rule MF_00140
Motif205 – 2095"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site2081ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7VPB2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 16D373FF7AF2F82C

FASTA34238,548
        10         20         30         40         50         60 
MTKSIVFSGV QPSGELTIGN YLGALRNWVT LQDDYDCLFC IVDLHAITVR QDPIALRKST 

        70         80         90        100        110        120 
LDVLALYLAC GIDPNKSTIF IQSQVPEHSQ LAWVLNCYTY FGEMGRMTQF KDKSARYEEN 

       130        140        150        160        170        180 
VNVGLFTYPV LMAADILLYQ ANQVPVGDDQ KQHLEITRDI ANRFNTLYGK KDAEGKLIES 

       190        200        210        220        230        240 
VFTVPECFIA KACARVMSLL EPTKKMSKSD DNRNNVIGLL EDPKAVAKKI KRAMTDSDEP 

       250        260        270        280        290        300 
PVIKYDQKNK AGVSNLLDIL AAITGKSMVE LEAEFEGKMY GHLKTEVADQ VMAMLTGLQE 

       310        320        330        340 
RYQRFRQDEA LLEKIYRDGA EKARMRAKKT LDEVYKLIGF VG 

« Hide

References

[1]"The complete genome sequence of Haemophilus ducreyi."
Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L., Nguyen D., Wang J., Forst C., Hood L.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 35000HP / ATCC 700724.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017143 Genomic DNA. Translation: AAP95170.1.
RefSeqNP_872781.1. NC_002940.2.

3D structure databases

ProteinModelPortalQ7VPB2.
SMRQ7VPB2. Positions 5-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233412.HD0177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP95170; AAP95170; HD_0177.
GeneID1490187.
KEGGhdu:HD0177.
PATRIC20176941. VBIHaeDuc133973_0139.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
KOK01867.
OMAGWGQFKP.
OrthoDBEOG686NJQ.
ProtClustDBPRK00927.

Enzyme and pathway databases

BioCycHDUC233412:GH5F-165-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_HAEDU
AccessionPrimary (citable) accession number: Q7VPB2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 63 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