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Database: UniProt
Entry: B2RHF2
LinkDB: B2RHF2
Original site: B2RHF2 
ID   PTH_PORG3               Reviewed;         185 AA.
AC   B2RHF2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   01-OCT-2014, entry version 42.
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=PGN_0278;
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / JCM 12257).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=431947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / JCM 12257;
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis
RT   strain ATCC 33277 and genomic comparison with strain W83 revealed
RT   extensive genome rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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; AP009380; BAG32797.1; -; Genomic_DNA.
DR   RefSeq; WP_012457388.1; NC_010729.1.
DR   RefSeq; YP_001928394.1; NC_010729.1.
DR   STRING; 431947.PGN_0278; -.
DR   EnsemblBacteria; BAG32797; BAG32797; PGN_0278.
DR   GeneID; 6328938; -.
DR   KEGG; pgn:PGN_0278; -.
DR   PATRIC; 22973492; VBIPorGin26334_0277.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; AMHRLHS; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   BioCyc; PGIN431947:GC9J-291-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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    185       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_1000092969.
SQ   SEQUENCE   185 AA;  20744 MW;  65F314EBF0BE7A14 CRC64;
     MKYLIVGLGN IGGEYNGTRH NVGFRMVNAL AEDGGVQFVE ARYGAIAHMR VKNAELILLK
     PNTYMNLSGN AVRYWMQQEN IPREQVLVLV DDLALPFGTL RLKPKGSDAG HNGLKNIAEV
     MGSIDYARLR FGLGDEFSKG RQVDFVLGRF TPEEEEKLPE LTKHAVEIIK SFCLAGIQRT
     MNRYN
//
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