GenomeNet

Database: UniProt
Entry: C4Z4L5
LinkDB: C4Z4L5
Original site: C4Z4L5 
ID   PTH_EUBE2               Reviewed;         186 AA.
AC   C4Z4L5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   14-MAY-2014, entry version 33.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=EUBELI_01915;
OS   Eubacterium eligens (strain ATCC 27750 / VPI C15-48).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=515620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27750 / VPI C15-48;
RX   PubMed=19321416; DOI=10.1073/pnas.0901529106;
RA   Mahowald M.A., Rey F.E., Seedorf H., Turnbaugh P.J., Fulton R.S.,
RA   Wollam A., Shah N., Wang C., Magrini V., Wilson R.K., Cantarel B.L.,
RA   Coutinho P.M., Henrissat B., Crock L.W., Russell A., Verberkmoes N.C.,
RA   Hettich R.L., Gordon J.I.;
RT   "Characterizing a model human gut microbiota composed of members of
RT   its two dominant bacterial phyla.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:5859-5864(2009).
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001104; ACR72904.1; -; Genomic_DNA.
DR   RefSeq; YP_002931351.1; NC_012778.1.
DR   STRING; 515620.EUBELI_01915; -.
DR   EnsemblBacteria; ACR72904; ACR72904; EUBELI_01915.
DR   GeneID; 7957656; -.
DR   KEGG; eel:EUBELI_01915; -.
DR   PATRIC; 21866904; VBIEubEli113401_1798.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; MGVVEHV; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   BioCyc; EELI515620:GH1N-1914-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    186       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_1000202582.
SQ   SEQUENCE   186 AA;  20441 MW;  E8202B930FE4821A CRC64;
     MYIIAGLGNP GKEYMGTRHN AGFSVIDELA DKYNISVDTA KHKGLIGKGV IAGQKVILVK
     PMTYMNNSGE CIREVMDYYK CDIDDFLVIF DDISLDVGKL RLRAKGSAGG HNGIKSIIAH
     LGSDKFKRIK FGVGDKPKNW DLADWVLGKF PAEEYATLRE ANKKACEAVE CILTDGIESG
     MNKYNG
//
DBGET integrated database retrieval system