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Database: UniProt
Entry: A0A090XU77_PAEMA
LinkDB: A0A090XU77_PAEMA
Original site: A0A090XU77_PAEMA 
ID   A0A090XU77_PAEMA        Unreviewed;       186 AA.
AC   A0A090XU77;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
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   ECO:0000313|EMBL:KFM89824.1};
GN   ORFNames=DJ90_6278 {ECO:0000313|EMBL:KFM89824.1}, GNQ08_29265
GN   {ECO:0000313|EMBL:MUG26437.1};
OS   Paenibacillus macerans (Bacillus macerans).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=44252 {ECO:0000313|EMBL:KFM89824.1, ECO:0000313|Proteomes:UP000029278};
RN   [1] {ECO:0000313|EMBL:KFM89824.1, ECO:0000313|Proteomes:UP000029278}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8244 {ECO:0000313|EMBL:KFM89824.1,
RC   ECO:0000313|Proteomes:UP000029278};
RA   Bishop-Lilly K.A., Broomall S.M., Chain P.S., Chertkov O., Coyne S.R.,
RA   Daligault H.E., Davenport K.W., Erkkila T., Frey K.G., Gibbons H.S., Gu W.,
RA   Jaissle J., Johnson S.L., Koroleva G.I., Ladner J.T., Lo C.-C.,
RA   Minogue T.D., Munk C., Palacios G.F., Redden C.L., Rosenzweig C.N.,
RA   Scholz M.B., Teshima H., Xu Y.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MUG26437.1, ECO:0000313|Proteomes:UP000442469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3CT49 {ECO:0000313|EMBL:MUG26437.1,
RC   ECO:0000313|Proteomes:UP000442469};
RA   Olajide A.M., Chen S., Lapointe G.;
RT   "Draft genome sequences of five Paenibacillus species of dairy origin.";
RL   Submitted (NOV-2019) 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         ECO:0000256|RuleBase:RU000673};
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, ECO:0000256|RuleBase:RU004320}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KFM89824.1}.
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DR   EMBL; JMQA01000059; KFM89824.1; -; Genomic_DNA.
DR   EMBL; WNZZ01000043; MUG26437.1; -; Genomic_DNA.
DR   RefSeq; WP_036618128.1; NZ_WNZZ01000043.1.
DR   AlphaFoldDB; A0A090XU77; -.
DR   STRING; 44252.DJ90_6278; -.
DR   GeneID; 77010398; -.
DR   PATRIC; fig|44252.3.peg.6390; -.
DR   HOGENOM; CLU_062456_4_1_9; -.
DR   OrthoDB; 9800507at2; -.
DR   Proteomes; UP000029278; Unassembled WGS sequence.
DR   Proteomes; UP000442469; Unassembled WGS sequence.
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; PS01195; PEPT_TRNA_HYDROL_1; 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:UP000029278}.
SQ   SEQUENCE   186 AA;  20804 MW;  591FE85507648AB1 CRC64;
     MKWIVGLGNP GKQYEKTRHN IGFMAVDELA RRHGIEIKQS KCKALIGEGV LPGGKVVLIK
     PMTFMNLSGE AVRAYMDYYK ASLEDMIVVY DDLDTEIGRN RLRYQGSSGG HNGIKSIIQH
     TGTQVFNRIR MGISRPEPGY AVVDYVLSGF AKKDQPLLQQ SIEAACDALE YSLDHTFEQT
     MAKFNV
//
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