Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

D-aminoacyl-tRNA deacylase

Gene

dtdA

Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

D-aminoacyl-tRNA deacylase with broad substrate specificity. By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl-tRNA entities in vivo. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr) and D-aspartyl-tRNA(Asp).2 Publications

Catalytic activityi

A D-aminoacyl-tRNA + H2O = a D-amino acid + tRNA.UniRule annotation2 Publications

Cofactori

Zn2+UniRule annotation1 PublicationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation1 Publication

Temperature dependencei

Thermostable.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.1.1.96. 5242.

Names & Taxonomyi

Protein namesi
Recommended name:
D-aminoacyl-tRNA deacylaseUniRule annotation (EC:3.1.1.96UniRule annotation2 Publications)
Alternative name(s):
D-tyrosyl-tRNA(Tyr) deacylase
Gene namesi
Name:dtdAUniRule annotation
Synonyms:dtd2
Ordered Locus Names:PYRAB00070
ORF Names:PAB2349
OrganismiPyrococcus abyssi (strain GE5 / Orsay)
Taxonomic identifieri272844 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000810 Componenti: Chromosome
  • UP000009139 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781S → A: Reduces deacylase activity. 1 Publication
Mutagenesisi80 – 801H → A: Reduces deacylase activity. 1 Publication
Mutagenesisi92 – 921H → A: Reduces deacylase activity. 1 Publication
Mutagenesisi137 – 1371E → A: 10-fold decrease of deacylase activity. 1 Publication
Mutagenesisi140 – 1401H → A: Loss of deacylase activity. 1 Publication
Mutagenesisi141 – 1411H → A: No effect. 1 Publication
Mutagenesisi154 – 1541E → A: Reduces deacylase activity. 1 Publication
Mutagenesisi162 – 1621W → A: Increases deacylase activity. 1 Publication
Mutagenesisi197 – 1971H → A: Increases deacylase activity. 1 Publication
Mutagenesisi198 – 1981Y → A: No effect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272D-aminoacyl-tRNA deacylasePRO_0000158969Add
BLAST

Interactioni

Subunit structurei

Monomer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi272844.PAB2349.

Structurei

3D structure databases

ProteinModelPortaliQ9V2R8.
SMRiQ9V2R8. Positions 1-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DtdA deacylase family.UniRule annotationCurated

Phylogenomic databases

eggNOGiarCOG01616. Archaea.
COG1650. LUCA.
HOGENOMiHOG000015484.
KOiK09716.
OMAiLAMPGWH.

Family and domain databases

HAMAPiMF_00562. Deacylase_DtdA.
InterProiIPR018033. Deacylase_DtdA_archaea.
IPR007508. DtdA.
[Graphical view]
PfamiPF04414. tRNA_deacylase. 1 hit.
[Graphical view]
PIRSFiPIRSF016210. UCP016210. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9V2R8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVIMTTKVD KASMNIMQKL IENFGFKETE LKFDGNPVYK KDDMVILTTN
60 70 80 90 100
DEMIYYDYLD REIEKQLSFK PEIIAFASRH SSKQKLPALT THVTGNWGEA
110 120 130 140 150
MYGGKDESFA IAIPSAMKLA LLKMNELNDL GWTVCYEATH HGPSELEVPS
160 170 180 190 200
FFIEIGSSEE EWVNDRAGEI IAETIVYVLD NYENSKFKVA LGIGGGHYAP
210 220 230 240 250
KQTKRALNSD LAFGHILPKY AQPVSRDVIL KAINRFHEKV EAIYVDWKGS
260 270
KGETRQLAKS LAQELGLEFI KD
Length:272
Mass (Da):30,781
Last modified:May 1, 2000 - v1
Checksum:i3B75F554B602D3EB
GO

Sequence cautioni

The sequence CCE69373.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Mass spectrometryi

Molecular mass is 30907 Da from positions 1 - 272. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248283 Genomic DNA. Translation: CAB48930.1.
HE613800 Genomic DNA. Translation: CCE69373.1. Different initiation.
PIRiC75185.
RefSeqiWP_010867130.1. NC_000868.1.

Genome annotation databases

EnsemblBacteriaiCAB48930; CAB48930; PAB2349.
GeneIDi1495689.
KEGGipab:PAB2349.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ248283 Genomic DNA. Translation: CAB48930.1.
HE613800 Genomic DNA. Translation: CCE69373.1. Different initiation.
PIRiC75185.
RefSeqiWP_010867130.1. NC_000868.1.

3D structure databases

ProteinModelPortaliQ9V2R8.
SMRiQ9V2R8. Positions 1-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272844.PAB2349.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB48930; CAB48930; PAB2349.
GeneIDi1495689.
KEGGipab:PAB2349.

Phylogenomic databases

eggNOGiarCOG01616. Archaea.
COG1650. LUCA.
HOGENOMiHOG000015484.
KOiK09716.
OMAiLAMPGWH.

Enzyme and pathway databases

BRENDAi3.1.1.96. 5242.

Family and domain databases

HAMAPiMF_00562. Deacylase_DtdA.
InterProiIPR018033. Deacylase_DtdA_archaea.
IPR007508. DtdA.
[Graphical view]
PfamiPF04414. tRNA_deacylase. 1 hit.
[Graphical view]
PIRSFiPIRSF016210. UCP016210. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GE5 / Orsay.
  2. "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
    Gao J., Wang J.
    Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: GE5 / Orsay.
  3. Cited for: FUNCTION, CATALYTIC ACTIVITY, MASS SPECTROMETRY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF SER-78; HIS-80; HIS-92; GLU-137; HIS-140; HIS-141; GLU-154; TRP-162; HIS-197 AND TYR-198.
  4. "GEK1, a gene product of Arabidopsis thaliana involved in ethanol tolerance, is a D-aminoacyl-tRNA deacylase."
    Wydau S., Ferri-Fioni M.-L., Blanquet S., Plateau P.
    Nucleic Acids Res. 35:930-938(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE SPECIFICITY.

Entry informationi

Entry nameiDTDA_PYRAB
AccessioniPrimary (citable) accession number: Q9V2R8
Secondary accession number(s): G8ZFI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: May 1, 2000
Last modified: December 9, 2015
This is version 87 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

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.