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Q71XG7 (SYW_LISMF) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. 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:LMOf2365_2231
OrganismListeria monocytogenes serotype 4b (strain F2365) [Complete proteome] [HAMAP]
Taxonomic identifier265669 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria

Protein attributes

Sequence length331 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 – 331331Tryptophan--tRNA ligase HAMAP-Rule MF_00140
PRO_0000136643

Regions

Motif11 – 199"HIGH" region HAMAP-Rule MF_00140
Motif193 – 1975"KMSKS" region HAMAP-Rule MF_00140

Sites

Binding site1961ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q71XG7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 1DA8E6A00DEDBBCD

FASTA33136,963
        10         20         30         40         50         60 
MKKVIFSGIQ PSGQLTLGNY IGALKQFGQF QDEYECFYCI VDEHAITVPQ DRLKLREQTR 

        70         80         90        100        110        120 
SLAALYLAVG LDPEKATLFI QSEVAAHAQA AWILQCNVYI GELERMTQFK DKSDGKAGVS 

       130        140        150        160        170        180 
AGLLTYPPLM AADILLYQTD LVPVGEDQKQ HIELTRDLAE RFNKKHADIF TMPEVFIPKQ 

       190        200        210        220        230        240 
GARVMSLQDP TKKMSKSDAN LKNAIFLLDP PATIRKKIKS AVTDSSGIIE YNKEEKPGVS 

       250        260        270        280        290        300 
NLLTIYSVIT GETISTIEEK YVGKGYGDFK TDLAELVVAE LEPIQERYYA YLKSEELDTI 

       310        320        330 
LDAGAEKAAR VANKTLKKME NGVGLGRKRR R 

« Hide

References

[1]"Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne pathogen Listeria monocytogenes reveal new insights into the core genome components of this species."
Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M., Daugherty S.C., Dodson R.J. expand/collapse author list , Durkin A.S., Madupu R., Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O., Luchansky J.B., Fraser C.M.
Nucleic Acids Res. 32:2386-2395(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: F2365.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017262 Genomic DNA. Translation: AAT04998.1.
RefSeqYP_014821.1. NC_002973.6.

3D structure databases

ProteinModelPortalQ71XG7.
SMRQ71XG7. Positions 3-329.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265669.LMOf2365_2231.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT04998; AAT04998; LMOf2365_2231.
GeneID2799514.
KEGGlmf:LMOf2365_2231.
PATRIC20325785. VBILisMon105049_2246.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0180.
HOGENOMHOG000059940.
KOK01867.
OMAIDPKKHI.
OrthoDBEOG686NJQ.

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_LISMF
AccessionPrimary (citable) accession number: Q71XG7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 64 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