ID A0A109QZ85_9MICO Unreviewed; 195 AA.
AC A0A109QZ85;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00083};
DE Short=PTH {ECO:0000256|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00083};
GN Name=pth {ECO:0000256|HAMAP-Rule:MF_00083};
GN ORFNames=AWU67_09770 {ECO:0000313|EMBL:AMB60465.1};
OS Microterricola viridarii.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microterricola.
OX NCBI_TaxID=412690 {ECO:0000313|EMBL:AMB60465.1, ECO:0000313|Proteomes:UP000058305};
RN [1] {ECO:0000313|EMBL:AMB60465.1, ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|EMBL:AMB60465.1,
RC ECO:0000313|Proteomes:UP000058305};
RX PubMed=26854947; DOI=10.1016/j.jbiotec.2016.02.011;
RA Himanshu, Swarnkar M.K., Singh D., Kumar R.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing bacterial strain ERGS5:02
RT isolated from Sikkim Himalaya.";
RL J. Biotechnol. 222:17-18(2016).
RN [2] {ECO:0000313|Proteomes:UP000058305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ERGS5:02 {ECO:0000313|Proteomes:UP000058305};
RA Kumar R., Singh D., Swarnkar M.K.;
RT "First complete genome sequence of a species in the genus Microterricola,
RT an extremophilic cold active enzyme producing strain ERGS5:02 isolated from
RT Sikkim Himalaya.";
RL Submitted (JAN-2016) 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|HAMAP-Rule:MF_00083}.
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|HAMAP-Rule:MF_00083};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000256|ARBA:ARBA00038063,
CC ECO:0000256|HAMAP-Rule:MF_00083}.
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DR EMBL; CP014145; AMB60465.1; -; Genomic_DNA.
DR RefSeq; WP_067232536.1; NZ_CP014145.1.
DR AlphaFoldDB; A0A109QZ85; -.
DR KEGG; mvd:AWU67_09770; -.
DR OrthoDB; 9800507at2; -.
DR Proteomes; UP000058305; 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; cd00462; PTH; 1.
DR Gene3D; 3.40.50.1470; Peptidyl-tRNA hydrolase; 1.
DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR InterPro; IPR001328; Pept_tRNA_hydro.
DR InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR NCBIfam; TIGR00447; pth; 1.
DR PANTHER; PTHR17224; PEPTIDYL-TRNA HYDROLASE; 1.
DR PANTHER; PTHR17224:SF1; PEPTIDYL-TRNA HYDROLASE-RELATED; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; Peptidyl-tRNA hydrolase-like; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00083};
KW Reference proteome {ECO:0000313|Proteomes:UP000058305}.
SQ SEQUENCE 195 AA; 20555 MW; 0FCB2DEBE7415D9C CRC64;
MPGNTWLVVG LGNPGPGYAN HRHNVGQMVV DELAARIGAT FKKHKTPAQV AEGFLRPGGP
KLVLAKSNSY MNTSGGPVSA LLKFYSLPLE RLIVVHDELD IPFDTVKLKS GGGHGGHNGL
RDIAKAADSP DYVRVRVGVG RPPGRQDPAD FVLQGFSSTE RAVLPNLLSD AADAVELVIT
DGLLAAQQKV HAPSA
//
