ID A0A0P7HUK3_9EURY Unreviewed; 112 AA.
AC A0A0P7HUK3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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 ECO:0000313|EMBL:KPN30376.1};
GN ORFNames=SY89_01105 {ECO:0000313|EMBL:KPN30376.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN30376.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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:KPN30376.1}.
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DR EMBL; LGUC01000001; KPN30376.1; -; Genomic_DNA.
DR RefSeq; WP_054583373.1; NZ_LGUC01000001.1.
DR AlphaFoldDB; A0A0P7HUK3; -.
DR STRING; 699431.SY89_01105; -.
DR PATRIC; fig|699431.3.peg.1132; -.
DR OrthoDB; 6075at2157; -.
DR Proteomes; UP000050535; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535}.
SQ SEQUENCE 112 AA; 11906 MW; 5D29572DDE63D84E CRC64;
MKQAIVARTD LGMGTGKLAA QVAHASLSAY EDADDRTRRA WKGEGQKKVV LKGSGEDQLF
ELADRAEREG LPNAVVRDAG HTQLDPGTAT TVAIGPGEDE IVDRVTGDLS LY
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