PTH_RHIL3
ID PTH_RHIL3 Reviewed; 243 AA.
AC Q1MDL5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=RL3474;
OS Rhizobium leguminosarum bv. viciae (strain 3841).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=216596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3841;
RX PubMed=16640791; DOI=10.1186/gb-2006-7-4-r34;
RA Young J.P.W., Crossman L.C., Johnston A.W.B., Thomson N.R., Ghazoui Z.F.,
RA Hull K.H., Wexler M., Curson A.R.J., Todd J.D., Poole P.S., Mauchline T.H.,
RA East A.K., Quail M.A., Churcher C., Arrowsmith C., Cherevach I.,
RA Chillingworth T., Clarke K., Cronin A., Davis P., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Sanders M., Simmonds M., Whitehead S., Parkhill J.;
RT "The genome of Rhizobium leguminosarum has recognizable core and accessory
RT components.";
RL Genome Biol. 7:R34.1-R34.20(2006).
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_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:0000255|HAMAP-Rule:MF_00083};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC Rule:MF_00083}.
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DR EMBL; AM236080; CAK08962.1; -; Genomic_DNA.
DR RefSeq; WP_011652951.1; NC_008380.1.
DR AlphaFoldDB; Q1MDL5; -.
DR SMR; Q1MDL5; -.
DR STRING; 216596.RL3474; -.
DR EnsemblBacteria; CAK08962; CAK08962; RL3474.
DR KEGG; rle:RL3474; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_1_1_5; -.
DR OMA; HVLSKFH; -.
DR OrthoDB; 1676462at2; -.
DR Proteomes; UP000006575; 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; -; 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 PANTHER; PTHR17224; PTHR17224; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; SSF53178; 1.
DR TIGRFAMs; TIGR00447; pth; 1.
DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..243
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000264088"
FT REGION 190..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 243 AA; 26590 MW; 8C63E976F8E33E59 CRC64;
MLIIAGLGNP GGKYAGNRHN IGFMAVDAIH RRHGFSPWSK KFRAEIAEGE VGGEKVLLMK
PQTFMNLSGE SVGEAMRFYK LQPADLVAIY DELDLPQGKA RLKTGGGHNG HNGIKSLDAH
CGREYRRLRL GIGHPGIKDM VQNHVLGDFA KADKAWLEPL LDTLADNADM LVRNEDSQLM
NKIALALGGK AEEEKPAKEM KDAGKKPASQ SHIHQARNHN QPKLPATGPM ADMLKKMFGK
KGD
