ID A0A0E3ST90_METMT Unreviewed; 115 AA.
AC A0A0E3ST90;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=MCMEM_1724 {ECO:0000313|EMBL:AKB85777.1};
OS Methanococcoides methylutens MM1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=1434104 {ECO:0000313|EMBL:AKB85777.1, ECO:0000313|Proteomes:UP000033048};
RN [1] {ECO:0000313|EMBL:AKB85777.1, ECO:0000313|Proteomes:UP000033048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM1 {ECO:0000313|EMBL:AKB85777.1,
RC ECO:0000313|Proteomes:UP000033048};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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}.
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DR EMBL; CP009518; AKB85777.1; -; Genomic_DNA.
DR RefSeq; WP_048205830.1; NZ_CP009518.1.
DR AlphaFoldDB; A0A0E3ST90; -.
DR STRING; 1434104.MCMEM_1724; -.
DR GeneID; 24894290; -.
DR KEGG; mmet:MCMEM_1724; -.
DR PATRIC; fig|1434104.5.peg.1871; -.
DR HOGENOM; CLU_073661_2_2_2; -.
DR OrthoDB; 6075at2157; -.
DR Proteomes; UP000033048; 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:UP000033048}.
SQ SEQUENCE 115 AA; 12436 MW; 386599DE7A342542 CRC64;
MADYKQCIVI RDDLKLSKGK LAVQVAHAAV SAAEWAKSSD LEKWKEGGQK KVVLRAEKLQ
DLFQLKEKAR REGLPTALIT DAGLTEVPPG TVTVLGIGPA KVEDIDKVTG SLKLL
//
