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Database: UniProt
Entry: P57287
LinkDB: P57287
Original site: P57287 
ID   PTH_BUCAI               Reviewed;         177 AA.
AC   P57287;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   29-OCT-2014, entry version 79.
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=BU190;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
OS   (Acyrthosiphon pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids
RT   Buchnera sp. APS.";
RL   Nature 407:81-86(2000).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-
CC       tRNAs which drop off the ribosome during protein synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N-
CC       substituted amino acid + tRNA. {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}.
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DR   EMBL; BA000003; BAB12907.1; -; Genomic_DNA.
DR   RefSeq; NP_240021.1; NC_002528.1.
DR   RefSeq; WP_010895991.1; NC_002528.1.
DR   ProteinModelPortal; P57287; -.
DR   EnsemblBacteria; BAB12907; BAB12907; BAB12907.
DR   GeneID; 1109633; -.
DR   KEGG; buc:BU190; -.
DR   PATRIC; 21243898; VBIBucAph127364_0201.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004796; -.
DR   KO; K01056; -.
DR   OMA; AMHRLHS; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   BioCyc; BAPH107806:GBZJ-189-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN         1    177       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_0000187707.
SQ   SEQUENCE   177 AA;  20576 MW;  BD18DA8FEF0DFAAF CRC64;
     MIVGLSNPKK EYHSTRHNVG SWYLYSLAES YLRNFKNEKK FFGFTTSLNI ESNYIRLLIP
     NIFMNINGQS VFKMASFYNI NLSEILIVHD DLELQPGISK LKYSYGHNGH NGLRDIVNTF
     NKNINFYRFR IGIGRPINRD QIASFVLSNP TKKEKILIQK SILHAIEKNV LSNILKF
//
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