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A4J0Q6 (PTH_DESRM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Peptidyl-tRNA hydrolase

Short name=PTH
EC=3.1.1.29
Gene names
Name:pth
Ordered Locus Names:Dred_0109
OrganismDesulfotomaculum reducens (strain MI-1) [Complete proteome] [HAMAP]
Taxonomic identifier349161 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfotomaculum

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis By similarity. HAMAP MF_00083

Catalytic activity

N-substituted aminoacyl-tRNA + H2O = N-substituted amino acid + tRNA. HAMAP MF_00083

Subunit structure

Monomer By similarity. HAMAP MF_00083

Subcellular location

Cytoplasm By similarity HAMAP MF_00083.

Sequence similarities

Belongs to the PTH family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminoacyl-tRNA hydrolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206Peptidyl-tRNA hydrolase HAMAP MF_00083
PRO_1000071226

Sequences

Sequence LengthMass (Da)Tools
A4J0Q6 [UniParc].

Last modified May 1, 2007. Version 1.
Checksum: F3CE079C989BFC1F

FASTA20622,811
        10         20         30         40         50         60 
MKLIVGLGNP GTEYAKTRHN IGFMVIDRLA DESRVSTEKN QHKAQICQIT IGSEKVILAK 

        70         80         90        100        110        120 
PQTYMNLSGQ SVVALMNWYK LSPDELFVIT DDMDLPPGVL RIRKNGSAGG QRGLKNIIEL 

       130        140        150        160        170        180 
LGTQQFPRMR VGIGRPEHGA VDHVLGKISE AEAELINPAI QTAVEAVKVW VLEGTQAAMN 

       190        200 
KFNQKNKKKK EKEQPEAATD QLLENK 

« Hide

References

[1]"Complete sequence of Desulfotomaculum reducens MI-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000612 Genomic DNA. Translation: ABO48659.1.
RefSeqYP_001111484.1. NC_009253.1.

3D structure databases

ProteinModelPortalA4J0Q6.
ModBaseSearch...

Protein-protein interaction databases

STRINGA4J0Q6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4956652.
GenomeReviewsGene locus Dred_0109 in contig CP000612_GR.
KEGGdrm:Dred_0109.
PATRIC21725984. VBIDesRed82656_0115.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0193.
HOGENOMHBG610927.
OMAIKFKTGG.
PhylomeDBA4J0Q6.
ProtClustDBCLSK2536965.

Enzyme and pathway databases

BioCycDRED349161:DRED_0109-MONOMER.

Family and domain databases

HAMAPMF_00083. Pept_tRNA_hydro_bact.
[Tree]
InterProIPR001328. Pept_tRNA_hydro.
IPR018171. Pept_tRNA_hydro_CS.
[Graphical view]
Gene3DG3DSA:3.40.50.1470. Pept_tRNA_hydro. 1 hit.
KOK01056.
PANTHERPTHR17224. Pept_tRNA_hydro. 1 hit.
PfamPF01195. Pept_tRNA_hydro. 1 hit.
[Graphical view]
SUPFAMSSF53178. Pept_tRNA_hydro. 1 hit.
TIGRFAMsTIGR00447. Pth. 1 hit.
PROSITEPS01195. PEPT_TRNA_HYDROL_1. 1 hit.
PS01196. PEPT_TRNA_HYDROL_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePTH_DESRM
AccessionPrimary (citable) accession number: A4J0Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 2007
Last modified: January 25, 2012
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families