(data stored in ACNUC7421 zone)

SWISSPROT: PTH_ALCBS

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   11-DEC-2019, entry version 80.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=ABO_0516;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS   SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA   Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA   Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA   McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA   Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA   Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT   Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acyl-L-alpha-aminoacyl-tRNA = an N-acyl-L-amino acid +
CC         H(+) + tRNA; Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59874,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:138191; EC=3.1.1.29;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00083};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
DR   EMBL; AM286690; CAL15964.1; -; Genomic_DNA.
DR   RefSeq; WP_011587802.1; NC_008260.1.
DR   SMR; Q0VS84; -.
DR   STRING; 393595.ABO_0516; -.
DR   EnsemblBacteria; CAL15964; CAL15964; ABO_0516.
DR   KEGG; abo:ABO_0516; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004796; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   OrthoDB; 1676462at2; -.
DR   BioCyc; ABOR393595:ABO_RS02680-MONOMER; -.
DR   Proteomes; UP000008871; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
DR   Gene3D; 3.40.50.1470; -; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 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;
DR   PRODOM; Q0VS84.
DR   SWISS-2DPAGE; Q0VS84.
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..195
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="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
//

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