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Protein

Tryptophan--tRNA ligase 2

Gene

trpS2

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the formation of 5'adenyl-Trp and tRNA(Trp) but with 5-fold less activity than TrpRS. Increases the solubility of the nitric oxide synthase oxygenase (nos), as well as its affinity for substrate L-arginine and its nitric-oxide synthase activity. The complex between trpS2 and nos catalyzes the regioselective nitration of tryptophan at the 4-position.1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei218ATPBy similarity1

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

BRENDAi6.1.1.2. 1856.

Names & Taxonomyi

Protein namesi
Recommended name:
Tryptophan--tRNA ligase 2 (EC:6.1.1.2)
Alternative name(s):
Tryptophanyl-tRNA synthetase 2
Short name:
TrpRS 2
Tryptophanyl-tRNA synthetase II
Short name:
TrpRS II
Gene namesi
Name:trpS2
Synonyms:trpSII
Ordered Locus Names:DR_1093
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Chemistry databases

DrugBankiDB02959. Oxitriptan.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001367171 – 351Tryptophan--tRNA ligase 2Add BLAST351

Expressioni

Inductioni

The level of expression increases 2.2-fold, 5 hours after exposure to radiation, and returns to near a base line 5 hours later.

Interactioni

Subunit structurei

Homodimer. Forms a complex with nos; one homodimer of trpS2 binds one homodimer of nos.

Protein-protein interaction databases

STRINGi243230.DR_1093.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi23 – 29Combined sources7
Helixi37 – 42Combined sources6
Helixi44 – 50Combined sources7
Beta strandi52 – 60Combined sources9
Helixi62 – 69Combined sources8
Helixi73 – 89Combined sources17
Turni94 – 96Combined sources3
Beta strandi97 – 101Combined sources5
Helixi102 – 104Combined sources3
Helixi107 – 116Combined sources10
Helixi121 – 125Combined sources5
Helixi128 – 137Combined sources10
Helixi145 – 161Combined sources17
Beta strandi164 – 168Combined sources5
Helixi170 – 172Combined sources3
Helixi173 – 189Combined sources17
Beta strandi198 – 201Combined sources4
Beta strandi212 – 214Combined sources3
Turni218 – 221Combined sources4
Helixi230 – 238Combined sources9
Helixi261 – 267Combined sources7
Helixi271 – 283Combined sources13
Helixi288 – 314Combined sources27
Helixi317 – 345Combined sources29

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YI8X-ray2.10A/B/C1-351[»]
1YIAX-ray3.70A/B/C1-351[»]
1YIDX-ray2.40A/B/C1-351[»]
2A4MX-ray2.30A/B/C21-351[»]
ProteinModelPortaliQ9RVD6.
SMRiQ9RVD6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9RVD6.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi31 – 39"HIGH" region9
Motifi215 – 219"KMSKS" region5

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105C31. Bacteria.
COG0180. LUCA.
HOGENOMiHOG000059941.
InParanoidiQ9RVD6.
KOiK01867.
OMAiAMTDNAH.
OrthoDBiPOG091H00I9.

Family and domain databases

CDDicd00806. TrpRS_core. 1 hit.
Gene3Di3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
[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.

Q9RVD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFVDLEVPT MTTPTPAATP ARPRVLTGDR PTGALHLGHL AGSLQNRVRL
60 70 80 90 100
QDEAELFVLL ADVQALTDHF DRPEQVRENV LAVALDYLAA GLDPQKTTCV
110 120 130 140 150
VQSAVPELAE LTVYFLNLVT VSHLRQNPTV KAEIAQKGYG ERVPAGFFVY
160 170 180 190 200
PVSQAADIAA FGATLVPVGD DQLPMLEQTR EIVRRFNALY APVLAEPQAQ
210 220 230 240 250
LSRVPRLPGL DGQAKMSKSL GNAIALGDSA DEVARKVMGM YTDPGHLRAS
260 270 280 290 300
DPGRVEGNPV FTFLDAFDPD PARVQALKDQ YRAGGLGDVK VKKHLIDVLN
310 320 330 340 350
GVLAPIRTRR AEYERDPDAV LRFVTEGTAR GREVAAQTLG QVRRAMRLFG

H
Length:351
Mass (Da):38,180
Last modified:May 1, 2000 - v1
Checksum:i7CBE69160F6CB9C5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10665.1.
PIRiE75438.
RefSeqiNP_294817.2. NC_001263.1.

Genome annotation databases

EnsemblBacteriaiAAF10665; AAF10665; DR_1093.
GeneIDi1797478.
KEGGidra:DR_1093.
PATRICi21629774. VBIDeiRad64572_1289.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000513 Genomic DNA. Translation: AAF10665.1.
PIRiE75438.
RefSeqiNP_294817.2. NC_001263.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YI8X-ray2.10A/B/C1-351[»]
1YIAX-ray3.70A/B/C1-351[»]
1YIDX-ray2.40A/B/C1-351[»]
2A4MX-ray2.30A/B/C21-351[»]
ProteinModelPortaliQ9RVD6.
SMRiQ9RVD6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_1093.

Chemistry databases

DrugBankiDB02959. Oxitriptan.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF10665; AAF10665; DR_1093.
GeneIDi1797478.
KEGGidra:DR_1093.
PATRICi21629774. VBIDeiRad64572_1289.

Phylogenomic databases

eggNOGiENOG4105C31. Bacteria.
COG0180. LUCA.
HOGENOMiHOG000059941.
InParanoidiQ9RVD6.
KOiK01867.
OMAiAMTDNAH.
OrthoDBiPOG091H00I9.

Enzyme and pathway databases

BRENDAi6.1.1.2. 1856.

Miscellaneous databases

EvolutionaryTraceiQ9RVD6.
PROiQ9RVD6.

Family and domain databases

CDDicd00806. TrpRS_core. 1 hit.
Gene3Di3.40.50.620. 1 hit.
InterProiIPR001412. aa-tRNA-synth_I_CS.
IPR002305. aa-tRNA-synth_Ic.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002306. Trp-tRNA-ligase.
[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...

Entry informationi

Entry nameiSYW2_DEIRA
AccessioniPrimary (citable) accession number: Q9RVD6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: May 1, 2000
Last modified: November 30, 2016
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein may not be involved in protein biosynthesis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference 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.