ID   PTH_ALCBS               Reviewed;         195 AA.
AC   Q0VS84;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 20.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=ABO_0516;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs which drop off the ribosome during protein synthesis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
CC       substituted amino acid + tRNA.
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the PTH family.
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DR   EMBL; AM286690; CAL15964.1; -; Genomic_DNA.
DR   RefSeq; YP_692236.1; -.
DR   GeneID; 4211233; -.
DR   GenomeReviews; AM286690_GR; ABO_0516.
DR   KEGG; abo:ABO_0516; -.
DR   NMPDR; fig|393595.12.peg.512; -.
DR   HOGENOM; Q0VS84; -.
DR   OMA; Q0VS84; IKFKTGG.
DR   BioCyc; ABOR393595:ABO_0516-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:HAMAP.
DR   GO; GO:0006412; P:translation; IEA:HAMAP.
DR   HAMAP; MF_00083; -; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   Gene3D; G3DSA:3.40.50.1470; Pept_tRNA_hydro; 1.
DR   PANTHER; PTHR17224; Pept_tRNA_hydro; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   ProDom; PD005324; PeptRNAhydrolase; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase.
FT   CHAIN         1    195       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_0000264000.
SQ   SEQUENCE   195 AA;  21465 MW;  EC91E4A06E8944EB CRC64;
     MADPVRLIVG LGNPGREYED TRHNAGVWYV DALARRQGVF LTEDKKYFGL TATFSFEGET
     IRLLVPTTFM NRSGQATAAL ANFFKIPVTQ ILVAHDELDL PPGCARFKQG GGHGGHNGLR
     DIISRHGNSR DFYRLRLGIG HPGSADRVTP HVLSKPSKAD RDLIDRAIDE AVHNTADMLR
     GDLNSAMNRL NGFKA
//