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P00953

- SYW_GEOSE

UniProt

P00953 - SYW_GEOSE

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Protein
Tryptophan--tRNA ligase
Gene
trpS
Organism
Geobacillus stearothermophilus (Bacillus stearothermophilus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp).UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei195 – 1951ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. tryptophan-tRNA ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. tryptophanyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan--tRNA ligase (EC:6.1.1.2)
Alternative name(s):
Tryptophanyl-tRNA synthetase
Short name:
TrpRS
Gene namesi
Name:trpS
OrganismiGeobacillus stearothermophilus (Bacillus stearothermophilus)
Taxonomic identifieri1422 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 328328Tryptophan--tRNA ligaseUniRule annotation
PRO_0000136601Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

DIPiDIP-48697N.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86
Helixi16 – 216
Helixi23 – 297
Turni30 – 323
Beta strandi33 – 397
Helixi41 – 444
Helixi51 – 6717
Turni72 – 743
Beta strandi75 – 795
Helixi80 – 823
Helixi85 – 9612
Helixi99 – 1035
Helixi106 – 1127
Helixi120 – 1234
Helixi125 – 13410
Turni135 – 1373
Beta strandi139 – 1424
Helixi145 – 1473
Helixi148 – 16518
Beta strandi173 – 1753
Beta strandi178 – 1825
Helixi200 – 2023
Helixi210 – 21910
Turni232 – 2343
Helixi236 – 24914
Helixi253 – 2597
Turni260 – 2623
Helixi265 – 29127
Helixi295 – 32228

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/F1-326[»]
3FI0X-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R1-326[»]
ProteinModelPortaliP00953.
SMRiP00953. Positions 1-328.

Miscellaneous databases

EvolutionaryTraceiP00953.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi10 – 189"HIGH" regionUniRule annotation
Motifi192 – 1965"KMSKS" regionUniRule annotation

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00140_B. Trp_tRNA_synth_B.
InterProiIPR001412. 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]
PANTHERiPTHR10055. PTHR10055. 1 hit.
PfamiPF00579. tRNA-synt_1b. 1 hit.
[Graphical view]
PRINTSiPR01039. TRNASYNTHTRP.
TIGRFAMsiTIGR00233. trpS. 1 hit.
PROSITEiPS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00953-1 [UniParc]FASTAAdd to Basket

« Hide

MKTIFSGIQP SGVITIGNYI GALRQFVELQ HEYNCYFCIV DQHAITVWQD    50
PHELRQNIRR LAAKYLAVGI DPTQATLFIQ SEVPAHAQAA WMLQCIVYIG 100
ELERMTQFKE KSAGKEAVSA GLLTYPPLMA ADILLYNTDI VPVGEDQKQH 150
IELTRDLAER FNKRYGELFT IPEARIPKVG ARIMSLVDPT KKMSKSDPNP 200
KAYITLLDDA KTIEKKIKSA VTDSEGTIRY DKEAKPGISN LLNIYSTLSG 250
QSIEELERQY EGKGYGVFKA DLAQVVIETL RPIQERYHHW MESEELDRVL 300
DEGAEKANRV ASEMVRKMEQ AMGLGRRR 328
Length:328
Mass (Da):37,193
Last modified:November 1, 1988 - v1
Checksum:iB8C4C6028F0913B0
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14742 Genomic DNA. Translation: AAA22873.1.
PIRiA26055. YWBSF.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M14742 Genomic DNA. Translation: AAA22873.1 .
PIRi A26055. YWBSF.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1D2R X-ray 2.90 A/B/C/D/E/F 1-326 [» ]
1I6K X-ray 1.72 A 1-328 [» ]
1I6L X-ray 1.72 A 1-328 [» ]
1I6M X-ray 1.72 A 1-328 [» ]
1M83 X-ray 2.20 A 1-328 [» ]
1MAU X-ray 2.15 A 1-328 [» ]
1MAW X-ray 3.00 A/B/C/D/E/F 1-328 [» ]
1MB2 X-ray 2.70 A/B/C/D/E/F 1-328 [» ]
2OV4 X-ray 2.50 A 1-328 [» ]
3FHJ X-ray 2.65 A/B/C/D/E/F 1-326 [» ]
3FI0 X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R 1-326 [» ]
ProteinModelPortali P00953.
SMRi P00953. Positions 1-328.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-48697N.

Chemistry

DrugBanki DB00150. L-Tryptophan.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P00953.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00140_B. Trp_tRNA_synth_B.
InterProi IPR001412. 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 ]
PANTHERi PTHR10055. PTHR10055. 1 hit.
Pfami PF00579. tRNA-synt_1b. 1 hit.
[Graphical view ]
PRINTSi PR01039. TRNASYNTHTRP.
TIGRFAMsi TIGR00233. trpS. 1 hit.
PROSITEi PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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).

Entry informationi

Entry nameiSYW_GEOSE
AccessioniPrimary (citable) accession number: P00953
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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