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Database: UniProt
Entry: B9ME46
LinkDB: B9ME46
Original site: B9ME46 
ID   PTH_ACIET               Reviewed;         211 AA.
AC   B9ME46;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   29-OCT-2014, entry version 41.
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};
GN   OrderedLocusNames=Dtpsy_0822;
OS   Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=535289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TPSY;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Coates J.D.;
RT   "Complete sequence of Diaphorobacter sp. TPSY.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001392; ACM32300.1; -; Genomic_DNA.
DR   RefSeq; YP_002552300.1; NC_011992.1.
DR   STRING; 535289.Dtpsy_0822; -.
DR   EnsemblBacteria; ACM32300; ACM32300; Dtpsy_0822.
DR   GeneID; 7383516; -.
DR   KEGG; dia:Dtpsy_0822; -.
DR   PATRIC; 21778674; VBIDiaSp55748_0849.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004796; -.
DR   KO; K01056; -.
DR   OMA; FCTIRIK; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   BioCyc; AEBR535289:GHOO-826-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.
FT   CHAIN         1    211       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_1000118388.
SQ   SEQUENCE   211 AA;  22978 MW;  0D0E354CE20B4BCA CRC64;
     MIKLFVGLGN PGPEYEATRH NAGFWWIDAL ARELKVTLVP ERSYHGLVAR ASVAGHSVWL
     LQPQTFMNLS GKSVAALARF FKIPPEEILV AHDELDIPPG QAKLKRGGSH AGHNGLRDIH
     AQLGTSDYWR LRIGIGHPGV KAEVVNWVLK KPAPDQRTLI EDSILHSLKA YPALLAGDMD
     KATLLVHTTK PPRPKATRPA QAQAAPQAGA D
//
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