ID M0FX77_9EURY Unreviewed; 112 AA.
AC M0FX77;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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 ORFNames=C459_10784 {ECO:0000313|EMBL:ELZ63194.1};
OS Haloferax sp. ATCC BAA-645.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=1227463 {ECO:0000313|EMBL:ELZ63194.1, ECO:0000313|Proteomes:UP000011673};
RN [1] {ECO:0000313|EMBL:ELZ63194.1, ECO:0000313|Proteomes:UP000011673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-645 {ECO:0000313|EMBL:ELZ63194.1,
RC ECO:0000313|Proteomes:UP000011673};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELZ63194.1}.
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DR EMBL; AOLE01000022; ELZ63194.1; -; Genomic_DNA.
DR RefSeq; WP_008577443.1; NZ_AOLE01000022.1.
DR AlphaFoldDB; M0FX77; -.
DR PATRIC; fig|1227463.4.peg.2172; -.
DR Proteomes; UP000011673; Unassembled WGS sequence.
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}.
SQ SEQUENCE 112 AA; 11927 MW; AC277B9C03B51A32 CRC64;
MKQAIVARAD LGMGRGKLAA QVAHASLSAY EDTDSQTRKR WKGEGQKKVV LKANGESELF
TLADKAERAG IPHAIIRDAG HTQLDPGTVT ALAVGPAEDD DIDRVTGDLS LY
//
