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P00953 (SYW_GEOSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
OrganismGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifier1422 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Protein attributes

Sequence length328 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp). HAMAP-Rule MF_00140_B

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00140_B.

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 term3D-structure
Direct protein sequencing
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 – 328328Tryptophan--tRNA ligase HAMAP-Rule MF_00140_B
PRO_0000136601

Regions

Motif10 – 189"HIGH" region HAMAP-Rule MF_00140_B
Motif192 – 1965"KMSKS" region HAMAP-Rule MF_00140_B

Sites

Binding site1951ATP By similarity

Secondary structure

.................................................... 328
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00953 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: B8C4C6028F0913B0

FASTA32837,193
        10         20         30         40         50         60 
MKTIFSGIQP SGVITIGNYI GALRQFVELQ HEYNCYFCIV DQHAITVWQD PHELRQNIRR 

        70         80         90        100        110        120 
LAAKYLAVGI DPTQATLFIQ SEVPAHAQAA WMLQCIVYIG ELERMTQFKE KSAGKEAVSA 

       130        140        150        160        170        180 
GLLTYPPLMA ADILLYNTDI VPVGEDQKQH IELTRDLAER FNKRYGELFT IPEARIPKVG 

       190        200        210        220        230        240 
ARIMSLVDPT KKMSKSDPNP KAYITLLDDA KTIEKKIKSA VTDSEGTIRY DKEAKPGISN 

       250        260        270        280        290        300 
LLNIYSTLSG QSIEELERQY EGKGYGVFKA DLAQVVIETL RPIQERYHHW MESEELDRVL 

       310        320 
DEGAEKANRV ASEMVRKMEQ AMGLGRRR 

« Hide

References

[1]"Cloning and complete nucleotide sequence of the Bacillus stearothermophilus tryptophanyl tRNA synthetase gene."
Barstow D.A., Sharman A.F., Atkinson T., Minton N.P.
Gene 46:37-45(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The amino acid sequence of tryptophanyl tRNA synthetase from Bacillus stearothermophilus."
Winter G.P., Hartley B.S.
FEBS Lett. 80:340-342(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-327.
[3]"Tryptophanyl-tRNA synthetase crystal structure reveals an unexpected homology to tyrosyl-tRNA synthetase."
Doublie S., Bricogne G., Gilmore C., Carter C.W. Jr.
Structure 3:17-31(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
[4]"2.9-A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site."
Ilyin V.A., Temple B., Hu M., Li G.-P., Yin Y., Vachette P., Carter C.W. Jr.
Protein Sci. 9:218-231(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14742 Genomic DNA. Translation: AAA22873.1.
PIRYWBSF. A26055.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D2RX-ray2.90A/B/C/D/E/F1-326[»]
1I6KX-ray1.72A1-328[»]
1I6LX-ray1.72A1-328[»]
1I6MX-ray1.72A1-328[»]
1M83X-ray2.20A1-328[»]
1MAUX-ray2.15A1-328[»]
1MAWX-ray3.00A/B/C/D/E/F1-328[»]
1MB2X-ray2.70A/B/C/D/E/F1-328[»]
2OV4X-ray2.50A1-328[»]
3FHJX-ray2.65A/B/C/D/E/F1-328[»]
3FI0X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R1-326[»]
ProteinModelPortalP00953.
SMRP00953. Positions 1-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48697N.

Chemistry

DrugBankDB00150. L-Tryptophan.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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...

Other

EvolutionaryTraceP00953.

Entry information

Entry nameSYW_GEOSE
AccessionPrimary (citable) accession number: P00953
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: February 19, 2014
This is version 99 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries