PTH_CERS4
ID PTH_CERS4 Reviewed; 225 AA.
AC Q3IZN0;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=RHOS4_24360;
GN ORFNames=RSP_0824;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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: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; CP000143; ABA80004.1; -; Genomic_DNA.
DR RefSeq; WP_011338521.1; NZ_CP030271.1.
DR RefSeq; YP_353905.1; NC_007493.2.
DR AlphaFoldDB; Q3IZN0; -.
DR SMR; Q3IZN0; -.
DR STRING; 272943.RSP_0824; -.
DR EnsemblBacteria; ABA80004; ABA80004; RSP_0824.
DR KEGG; rsp:RSP_0824; -.
DR PATRIC; fig|272943.9.peg.2787; -.
DR eggNOG; COG0193; Bacteria.
DR OMA; HVLSKFH; -.
DR PhylomeDB; Q3IZN0; -.
DR Proteomes; UP000002703; Chromosome 1.
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; Reference proteome.
FT CHAIN 1..225
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000264089"
FT REGION 184..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 225 AA; 24185 MW; E440B099AAF9FF7D CRC64;
MKLFVGLGNP GARYAGNRHN IGYMAVEAIA ADHGFGPWRA RFQGLTSEGR LGSEQVLLLK
PETFMNLSGQ SVGEAMRFYK LTPADVIVFH DELDLAPGKL RLKQGGGHAG HNGLRSIHAH
VGEAYGRVRL GIGHPGHKDA VAPYVLSDFA KADQDWLADL LRGISDGAEA LARGDGAKFQ
NAVALRMQPP KPEKPKPAAK APEAQAPEAA PDERSALQKL ADRFR
