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P84066 (DTD_LEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 8, 2011. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable D-tyrosyl-tRNA(Tyr) deacylase

EC=3.1.-.-
OrganismLeishmania major
Taxonomic identifier5664 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmania

Protein attributes

Sequence length181 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes D-tyrosyl-tRNA(Tyr) into D-tyrosine and free tRNA(Tyr). Could be a defense mechanism against a harmful effect of D-tyrosine By similarity. UniProtKB P32147

Subunit structure

Homodimer. Ref.1

Subcellular location

Cytoplasm By similarity UniProtKB P32147.

Sequence similarities

Belongs to the DTD family. Highly divergent.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical term3D-structure
Gene Ontology (GO)
   Biological processD-amino acid catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhydrolase activity, acting on ester bonds

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 181181Probable D-tyrosyl-tRNA(Tyr) deacylase
PRO_0000164628

Secondary structure

............................. 181
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P84066 [UniParc].

Last modified February 15, 2005. Version 2.
Checksum: 406E11C5B03123A1

FASTA18120,114
        10         20         30         40         50         60 
MLQAMDQGHL LVNNVDKYVR AGRGVMVYIA FLSDRDSAPI TDEALRHAVG VLLHTKIFTH 

        70         80         90        100        110        120 
FSPEKMINQP QSLEECPEMD ILIVPQASLG GKVKGRSVQF HQLVAKDVGA ALYDRFCHFV 

       130        140        150        160        170        180 
RVARGVDESR VDANGAPRSE GDAPKAEGWI KYNSRVISGT FGNRQGLRFE SEGPFTHMFD 


I 

« Hide

References

[1]"Structural analysis of a probable eukaryotic D-amino acid tRNA deacylase."
Robein M.A., Hol W.G.J.
Submitted (JUN-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS), SUBUNIT.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TC5X-ray1.93A/B/C/D1-181[»]
ProteinModelPortalP84066.
SMRP84066. Positions 1-181.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR023509. DTD-like_dom.
IPR003732. DTyrtRNA_deacyls.
[Graphical view]
Gene3DG3DSA:3.50.80.10. DTyrtRNA_deacyls. 1 hit.
PANTHERPTHR10472. DTyrtRNA_deacyls. 1 hit.
PfamPF02580. Tyr_Deacylase. 1 hit.
[Graphical view]
SUPFAMSSF69500. DTyrtRNA_deacyls. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDTD_LEIMA
AccessionPrimary (citable) accession number: P84066
Entry history
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: March 8, 2011
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families