(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHK4_GEOS0

ID   A0A0F6BHK4_GEOS0        Unreviewed;       187 AA.
AC   A0A0F6BHK4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 15.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU000673};
DE            Short=PTH {ECO:0000256|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU000673};
GN   Name=pth {ECO:0000256|HAMAP-Rule:MF_00083};
GN   OrderedLocusNames=GY4MC1_0049 {ECO:0000313|EMBL:ADP72905.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72905.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72905.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72905.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00083,
CC         ECO:0000256|RuleBase:RU000673};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000256|HAMAP-
CC       Rule:MF_00083, ECO:0000256|RuleBase:RU004320}.
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DR   EMBL; CP002293; ADP72905.1; -; Genomic_DNA.
DR   EnsemblBacteria; ADP72905; ADP72905; GY4MC1_0049.
DR   KEGG; gmc:GY4MC1_0049; -.
DR   KO; K01056; -.
DR   OMA; RYAHTRH; -.
DR   BioCyc; GSP581103:G1GOQ-60-MONOMER; -.
DR   Proteomes; UP000002034; 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; A0A0F6BHK4.
DR   SWISS-2DPAGE; A0A0F6BHK4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00083,
KW   ECO:0000256|RuleBase:RU000673, ECO:0000313|EMBL:ADP72905.1}.
SQ   SEQUENCE   187 AA;  21008 MW;  491AA538E29B97E4 CRC64;
     MLKLFVGLGN PGKEYEQTRH NVGFMVIDEL AKRWNISFQT AKFNGMIASH IISGEKVILC
     KPLTYMNLSG ECVRPLIDYY RIDINDVVVI YDDLDLPVGK IRLRMKGSAG GHNGIKSLIH
     HLGTQEFKRI RIGIGRPASG EKVIDYVLGR FHEEESGAIM EAILRSADAC EKAVTEPFLQ
     VMNEFNV
//

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