PTH_HALMA
ID PTH_HALMA Reviewed; 112 AA.
AC Q5V1D3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00628};
DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00628};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00628};
GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00628}; OrderedLocusNames=rrnAC1774;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(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_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:0000255|HAMAP-Rule:MF_00628};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00628}.
CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000255|HAMAP-
CC Rule:MF_00628}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAV46669.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY596297; AAV46669.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_004591375.1; NZ_CP039138.1.
DR AlphaFoldDB; Q5V1D3; -.
DR SMR; Q5V1D3; -.
DR STRING; 272569.rrnAC1774; -.
DR EnsemblBacteria; AAV46669; AAV46669; rrnAC1774.
DR GeneID; 40152722; -.
DR KEGG; hma:rrnAC1774; -.
DR PATRIC; fig|272569.17.peg.2449; -.
DR eggNOG; arCOG04228; Archaea.
DR HOGENOM; CLU_073661_2_2_2; -.
DR Proteomes; UP000001169; Chromosome I.
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; -; 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 PANTHER; PTHR12649; PTHR12649; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; SSF102462; 1.
DR TIGRFAMs; TIGR00283; arch_pth2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..112
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000120289"
SQ SEQUENCE 112 AA; 11713 MW; 20997FFD81D58A63 CRC64;
MKQAIVARAD IGMGEGKLAA QVAHASLSAY EDAGPKPRKA WKGAGQKKVV LKATSESELF
ELADVAEREG LPHAVVRDAG HTQLDPGTVT ALAVGPAEDE LVDRVTGDLP LF
