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Protein

D-aminoacyl-tRNA deacylase

Gene

dtd

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 3 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.UniRule annotation

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei80 – 801NucleophileUniRule annotation

GO - Molecular functioni

  1. hydrolase activity, acting on ester bonds Source: UniProtKB-HAMAP

GO - Biological processi

  1. D-amino acid catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
D-aminoacyl-tRNA deacylaseUniRule annotation (EC:3.1.1.96UniRule annotation)
Alternative name(s):
D-tyrosyl-tRNA(Tyr) deacylase
Gene namesi
Name:dtdUniRule annotation
Ordered Locus Names:HI_0670
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
ProteomesiUP000000579: Chromosome

Subcellular locationi

Cytoplasm CuratedUniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 144144D-aminoacyl-tRNA deacylasePRO_0000164546Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

STRINGi71421.HI0670.

Structurei

Secondary structure

1
144
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1514Combined sources
Beta strandi18 – 3215Combined sources
Helixi39 – 5113Combined sources
Beta strandi62 – 643Combined sources
Turni66 – 705Combined sources
Beta strandi72 – 776Combined sources
Helixi79 – 824Combined sources
Helixi99 – 11416Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi129 – 14315Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J7GX-ray1.64A1-144[»]
ProteinModelPortaliP44814.
SMRiP44814. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP44814.

Family & Domainsi

Sequence similaritiesi

Belongs to the DTD family.CuratedUniRule annotation

Phylogenomic databases

eggNOGiCOG1490.
KOiK07560.
OMAiENDGPFT.
OrthoDBiEOG6C2WM2.
PhylomeDBiP44814.

Family and domain databases

Gene3Di3.50.80.10. 1 hit.
HAMAPiMF_00518. Deacylase_Dtd.
InterProiIPR023509. DTD-like_dom.
IPR003732. DTyrtRNA_deacyls.
[Graphical view]
PANTHERiPTHR10472. PTHR10472. 1 hit.
PfamiPF02580. Tyr_Deacylase. 1 hit.
[Graphical view]
SUPFAMiSSF69500. SSF69500. 1 hit.
TIGRFAMsiTIGR00256. TIGR00256. 1 hit.

Sequencei

Sequence statusi: Complete.

P44814-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIALIQRVSQ AKVDVKGETI GKIGKGLLVL LGVEKEDNRE KADKLAEKVL
60 70 80 90 100
NYRIFSDEND KMNLNVQQAQ GELLIVSQFT LAADTQKGLR PSFSKGASPA
110 120 130 140
LANELYEYFI QKCAEKLPVS TGQFAADMQV SLTNDGPVTF WLNV
Length:144
Mass (Da):15,862
Last modified:November 1, 1995 - v1
Checksum:iD8F84702EF5A3CBB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22330.1.
PIRiE64156.
RefSeqiNP_438830.1. NC_000907.1.
WP_005694618.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22330; AAC22330; HI_0670.
GeneIDi949713.
KEGGihin:HI0670.
PATRICi20189957. VBIHaeInf48452_0700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22330.1.
PIRiE64156.
RefSeqiNP_438830.1. NC_000907.1.
WP_005694618.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J7GX-ray1.64A1-144[»]
ProteinModelPortaliP44814.
SMRiP44814. Positions 1-144.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI0670.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22330; AAC22330; HI_0670.
GeneIDi949713.
KEGGihin:HI0670.
PATRICi20189957. VBIHaeInf48452_0700.

Phylogenomic databases

eggNOGiCOG1490.
KOiK07560.
OMAiENDGPFT.
OrthoDBiEOG6C2WM2.
PhylomeDBiP44814.

Miscellaneous databases

EvolutionaryTraceiP44814.

Family and domain databases

Gene3Di3.50.80.10. 1 hit.
HAMAPiMF_00518. Deacylase_Dtd.
InterProiIPR023509. DTD-like_dom.
IPR003732. DTyrtRNA_deacyls.
[Graphical view]
PANTHERiPTHR10472. PTHR10472. 1 hit.
PfamiPF02580. Tyr_Deacylase. 1 hit.
[Graphical view]
SUPFAMiSSF69500. SSF69500. 1 hit.
TIGRFAMsiTIGR00256. TIGR00256. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. "A catalytic mechanism for D-Tyr-tRNATyr deacylase based on the crystal structure of Hemophilus influenzae HI0670."
    Lim K., Tempczyk A., Bonander N., Toedt J., Howard A., Eisenstein E., Herzberg O.
    J. Biol. Chem. 278:13496-13502(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS).

Entry informationi

Entry nameiDTD_HAEIN
AccessioniPrimary (citable) accession number: P44814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 98 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, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  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

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 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.