(data stored in SCRATCH3701 zone)

SWISSPROT: PTH_RICTY

ID   PTH_RICTY               Reviewed;         185 AA.
AC   Q68WD4;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 83.
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}; OrderedLocusNames=RT0593;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       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 acid +
CC         H(+) + tRNA; Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59874,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:138191; EC=3.1.1.29;
CC         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; AE017197; AAU04058.1; -; Genomic_DNA.
DR   RefSeq; WP_011191039.1; NC_006142.1.
DR   SMR; Q68WD4; -.
DR   STRING; 257363.RT0593; -.
DR   EnsemblBacteria; AAU04058; AAU04058; RT0593.
DR   KEGG; rty:RT0593; -.
DR   eggNOG; ENOG4108ZPD; Bacteria.
DR   eggNOG; COG0193; LUCA.
DR   HOGENOM; HOG000004797; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   OrthoDB; 1676462at2; -.
DR   BioCyc; RTYP257363:G1G0L-599-MONOMER; -.
DR   Proteomes; UP000000604; 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; Q68WD4.
DR   SWISS-2DPAGE; Q68WD4.
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..185
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000187806"
SQ   SEQUENCE   185 AA;  21000 MW;  E883C0F496FCE7E9 CRC64;
     MILVIGLGNP GIVYQYTRHN IGFIAIERIA NKYHLSFSTK QKFNCKIAEA IIDRQKICFI
     KPTTYMNLSG KSVILVKTYY NINYEKVFVI HDDIDLEIGR IKFKTGGSNG GHNGLKSIDS
     IIGSHYNRIR IGIGRPQNNH DVADYVLSNF SESEYKTVMQ SIDNVANNFG LILEHKLAEF
     KNKIV
//

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