ID   PTH_ANAPZ               Reviewed;         183 AA.
AC   Q2GII6;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=APH_1301;
OS   Anaplasma phagocytophilum (strain HZ).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S.,
RA   Lewis M., Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N.,
RA   Nelson W.C., Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P.,
RA   Daugherty S.C., Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H.,
RA   Selengut J.D., Sullivan S.A., Zafar N., Zhou L., Benahmed F.,
RA   Forberger H., Halpin R., Mulligan S., Robinson J., White O.,
RA   Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(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; CP000235; ABD44175.1; -; Genomic_DNA.
DR   RefSeq; YP_505815.1; -.
DR   GeneID; 3930906; -.
DR   GenomeReviews; CP000235_GR; APH_1301.
DR   KEGG; aph:APH_1301; -.
DR   NMPDR; fig|212042.5.peg.1249; -.
DR   TIGR; APH_1301; -.
DR   HOGENOM; Q2GII6; -.
DR   OMA; Q2GII6; TEIDINN.
DR   BioCyc; APHA212042:APH_1301-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    183       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_0000264004.
SQ   SEQUENCE   183 AA;  19809 MW;  088993A721CA9400 CRC64;
     MLLLVGLGNP GKRYAETRHN VGFMIIDAVA RGFFFPEFCS KHDALVSIGN IGTHRVMLMK
     PLLYMNRSGT SVLSCTSMHK IAPEHITVFH DDVELQPGTI RVKLGGGSGG HNGLRSIDSA
     IGKAYWRVRF GVGRAELCNL SDYVLSDFEN IAQVTDLVNS VAANLQMLLD GNAAGFVSKV
     TSV
//