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Protein

Tryptophan--tRNA ligase

Gene

trpS

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1925-MONOMER.
BRENDAi6.1.1.2. 5244.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan--tRNA ligaseUniRule annotation (EC:6.1.1.2UniRule annotation)
Alternative name(s):
Tryptophanyl-tRNA synthetaseUniRule annotation
Short name:
TrpRSUniRule annotation
Gene namesi
Name:trpSUniRule annotation
Ordered Locus Names:PH1921
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 386386Tryptophan--tRNA ligasePRO_0000136730Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi70601.PH1921.

Structurei

Secondary structure

1
386
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 143Combined sources
Helixi18 – 247Combined sources
Helixi32 – 4110Combined sources
Helixi48 – 514Combined sources
Beta strandi54 – 607Combined sources
Helixi61 – 699Combined sources
Beta strandi75 – 806Combined sources
Helixi88 – 10417Combined sources
Beta strandi107 – 1126Combined sources
Helixi114 – 1207Combined sources
Helixi126 – 14116Combined sources
Beta strandi149 – 1546Combined sources
Turni155 – 1573Combined sources
Helixi160 – 17112Combined sources
Helixi174 – 1818Combined sources
Helixi189 – 19911Combined sources
Helixi200 – 2034Combined sources
Beta strandi204 – 2074Combined sources
Beta strandi209 – 2146Combined sources
Helixi215 – 2173Combined sources
Helixi218 – 22710Combined sources
Helixi229 – 2313Combined sources
Beta strandi237 – 2415Combined sources
Beta strandi250 – 2523Combined sources
Helixi259 – 2613Combined sources
Helixi269 – 2779Combined sources
Helixi302 – 3098Combined sources
Helixi315 – 32612Combined sources
Helixi332 – 35726Combined sources
Helixi361 – 3655Combined sources
Helixi369 – 3757Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JXEX-ray3.00A/B1-386[»]
ProteinModelPortaliO59584.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59584.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi82 – 909"HIGH" region
Motifi253 – 2575"KMSKS" region

Sequence similaritiesi

Belongs to the class-I aminoacyl-tRNA synthetase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG01887. Archaea.
COG0180. LUCA.
HOGENOMiHOG000224742.
KOiK01867.
OMAiFFFSHRD.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00140_A. Trp_tRNA_synth_A.
InterProiIPR001412. 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]
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.

O59584-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVEEFKVTPW EVEGVVDYDK LIKHFGTSPL TEDLLEKTAE LTKSELPIFF
60 70 80 90 100
RRKFFFSHRD YDLILKDYEE GRGFFLYTGR GPSGPMHIGH IIPFFATKWL
110 120 130 140 150
QEKFGVNLYI QITDDEKFLF KENLTFDDTK RWAYDNILDI IAVGFDPDKT
160 170 180 190 200
FIFQNSEFTK IYEMAIPIAK KINFSMAKAV FGFTEQSKIG MIFFPAIQIA
210 220 230 240 250
PTFFERKRCL IPAAIDQDPY WRLQRDFAES LGYYKTAALH SKFVPSLTSL
260 270 280 290 300
SGKMSASKPE TAIYLTDSPE DVEKKVWKFT LTGGRPTLKE QREKGGEPEK
310 320 330 340 350
CVVFKWLEIF FEEDDKKLKE RYYACKNGEL TCGECKRYLI SKIQEFLKEH
360 370 380
QRRRKKAEKL VEKFKYTGKL AQEMWNEAIP EPLKRS
Length:386
Mass (Da):45,305
Last modified:April 16, 2002 - v2
Checksum:i9E3C392F4028B2DD
GO

Sequence cautioni

The sequence BAA31046.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA31046.1. Different initiation.
PIRiG71206.
RefSeqiWP_010885986.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA31046; BAA31046; BAA31046.
GeneIDi1442768.
KEGGipho:PH1921.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA31046.1. Different initiation.
PIRiG71206.
RefSeqiWP_010885986.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JXEX-ray3.00A/B1-386[»]
ProteinModelPortaliO59584.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1921.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA31046; BAA31046; BAA31046.
GeneIDi1442768.
KEGGipho:PH1921.

Phylogenomic databases

eggNOGiarCOG01887. Archaea.
COG0180. LUCA.
HOGENOMiHOG000224742.
KOiK01867.
OMAiFFFSHRD.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1925-MONOMER.
BRENDAi6.1.1.2. 5244.

Miscellaneous databases

EvolutionaryTraceiO59584.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00140_A. Trp_tRNA_synth_A.
InterProiIPR001412. 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]
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]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Entry informationi

Entry nameiSYW_PYRHO
AccessioniPrimary (citable) accession number: O59584
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: April 16, 2002
Last modified: November 11, 2015
This is version 90 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.