ID A2BKV8_HYPBU Unreviewed; 125 AA.
AC A2BKV8;
DT 20-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 20-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00628};
DE Short=PTH {ECO:0000256|HAMAP-Rule:MF_00628};
DE EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00628};
GN Name=pth {ECO:0000256|HAMAP-Rule:MF_00628};
GN OrderedLocusNames=Hbut_0765 {ECO:0000313|EMBL:ABM80619.1};
OS Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Hyperthermus.
OX NCBI_TaxID=415426 {ECO:0000313|EMBL:ABM80619.1, ECO:0000313|Proteomes:UP000002593};
RN [1] {ECO:0000313|EMBL:ABM80619.1, ECO:0000313|Proteomes:UP000002593}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5456 / JCM 9403 / PLM1-5
RC {ECO:0000313|Proteomes:UP000002593};
RX PubMed=17350933;
RA Brugger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA She Q., Garrett R.A., Klenk H.P.;
RT "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL Archaea 2:127-135(2007).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis.
CC {ECO:0000256|ARBA:ARBA00003043, ECO:0000256|HAMAP-Rule:MF_00628}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC amino acid + H(+); 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|ARBA:ARBA00033690,
CC ECO:0000256|HAMAP-Rule:MF_00628};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00628}.
CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000256|ARBA:ARBA00038050,
CC ECO:0000256|HAMAP-Rule:MF_00628}.
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DR EMBL; CP000493; ABM80619.1; -; Genomic_DNA.
DR RefSeq; WP_011821937.1; NC_008818.1.
DR AlphaFoldDB; A2BKV8; -.
DR STRING; 415426.Hbut_0765; -.
DR EnsemblBacteria; ABM80619; ABM80619; Hbut_0765.
DR GeneID; 4782569; -.
DR KEGG; hbu:Hbut_0765; -.
DR eggNOG; arCOG04228; Archaea.
DR HOGENOM; CLU_073661_2_2_2; -.
DR OrthoDB; 6075at2157; -.
DR Proteomes; UP000002593; 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; cd02430; PTH2; 1.
DR Gene3D; 3.40.1490.10; Bit1; 1.
DR HAMAP; MF_00628; Pept_tRNA_hydro_arch; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR034759; Pept_tRNA_hydro_arch.
DR InterPro; IPR002833; PTH2.
DR NCBIfam; TIGR00283; arch_pth2; 1.
DR PANTHER; PTHR12649; PEPTIDYL-TRNA HYDROLASE 2; 1.
DR PANTHER; PTHR12649:SF11; PEPTIDYL-TRNA HYDROLASE 2, MITOCHONDRIAL; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; Peptidyl-tRNA hydrolase II; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00628};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00628};
KW Reference proteome {ECO:0000313|Proteomes:UP000002593}.
SQ SEQUENCE 125 AA; 13744 MW; 2D79FC3B8477FCB4 CRC64;
MVDGTEYKQV IVVRADLKMS RGKLAAQAAH AAVEAVLEIL DSGHPEWRRW LEEWRRQGQK
KVVVKVDSEA ELLRVYQEAL RLGLPTSLIA DAGRTELPPG TRTAVAVGPA PSPIVDRVTG
KLKLL
//
