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Database: UniProt
Entry: A8GD97
LinkDB: A8GD97
Original site: A8GD97 
ID   PTH_SERP5               Reviewed;         196 AA.
AC   A8GD97;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   16-APR-2014, entry version 41.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=Spro_1984;
OS   Serratia proteamaculans (strain 568).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Serratia.
OX   NCBI_TaxID=399741;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=568;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL   Submitted (SEP-2007) 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 (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; CP000826; ABV41087.1; -; Genomic_DNA.
DR   RefSeq; YP_001478215.1; NC_009832.1.
DR   ProteinModelPortal; A8GD97; -.
DR   SMR; A8GD97; 3-195.
DR   STRING; 399741.Spro_1984; -.
DR   EnsemblBacteria; ABV41087; ABV41087; Spro_1984.
DR   GeneID; 5603312; -.
DR   KEGG; spe:Spro_1984; -.
DR   PATRIC; 32416685; VBISerPro44537_2020.
DR   eggNOG; COG0193; -.
DR   HOGENOM; HOG000004796; -.
DR   KO; K01056; -.
DR   OMA; IKFKTGG; -.
DR   OrthoDB; EOG6C5RTR; -.
DR   ProtClustDB; PRK05426; -.
DR   BioCyc; SPRO399741:GI55-2041-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    196       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_1000057554.
SQ   SEQUENCE   196 AA;  21480 MW;  E89154DF0737688E CRC64;
     MSSIKLIVGL ANPGAEYAQT RHNAGAWYVD LLAQRHNQQL KEESKFYGYT ARLNLAGNDV
     RLLVPTTFMN LSGKAVLAMA NFYRIEPDEI LVAHDELDIP PGVAKIKLGG GNGGHNGLKD
     IQSKFGNNPN FYRLRIGIGH PGDKNKVVGF VLGKPPASEQ KMIDEAIDEA ARCTEILLTD
     GLEKTVRRLH SFKAQA
//
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