(data stored in ACNUC7421 zone)

SWISSPROT: PTH_THEFY

ID   PTH_THEFY               Reviewed;         213 AA.
AC   Q47SW2;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 92.
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=Tfu_0417;
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX;
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
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:
CC       Reaction=H2O + N-acyl-L-alpha-aminoacyl-tRNA = an N-acyl-L-amino
CC         acid + H(+) + tRNA; Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC         Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC         EC=3.1.1.29; Evidence={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}.
DR   EMBL; CP000088; AAZ54455.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0417; -.
DR   EnsemblBacteria; AAZ54455; AAZ54455; Tfu_0417.
DR   KEGG; tfu:Tfu_0417; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004796; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   BioCyc; TFUS269800:G1G4Q-423-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
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   InterPro; IPR036416; Pept_tRNA_hydro_sf.
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;
DR   PRODOM; Q47SW2.
DR   SWISS-2DPAGE; Q47SW2.
KW   Complete proteome; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN         1    213       Peptidyl-tRNA hydrolase.
FT                                /FTId=PRO_0000264131.
SQ   SEQUENCE   213 AA;  22760 MW;  4A4271535746B499 CRC64;
     MRGLLARLWG GRASVSREPD ARPGESGAVV SGERWLVVGL GNPGPKYAGN RHNVGFMVVD
     ELAAQRGERW RLHKAHAQVV ETRVGDAPVV LAKPASYMNL SGGPVAKLSA FYKVPVDRII
     VVHDELDIPF ARLKLKRGGG SAGHNGLRSI TASLGSPDYV RVRVGIGRPP GRMDAASFVL
     QDFSTAERKE LDVHVARAAD AVETVVTSGL EKA
//

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