PTH_YEAST
ID PTH_YEAST Reviewed; 190 AA.
AC P38876; D3DLD7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000303|PubMed:12799450};
DE Short=PTH {ECO:0000303|PubMed:12799450};
DE EC=3.1.1.29 {ECO:0000269|PubMed:12799450};
GN Name=PTH1; OrderedLocusNames=YHR189W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP SIMILARITY TO PTH.
RX PubMed=8563640; DOI=10.1002/pro.5560041121;
RA Ouzounis C., Bork P., Casari G., Sander C.;
RT "New protein functions in yeast chromosome VIII.";
RL Protein Sci. 4:2424-2428(1995).
RN [4]
RP FUNCTION.
RX PubMed=12475929; DOI=10.1073/pnas.222659199;
RA Rosas-Sandoval G., Ambrogelly A., Rinehart J., Wei D., Cruz-Vera L.R.,
RA Graham D.E., Stetter K.O., Guarneros G., Soell D.;
RT "Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase
RT are nonessential in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16707-16712(2002).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=12799450; DOI=10.1093/nar/gkg428;
RA Fromant M., Ferri-Fioni M.-L., Plateau P., Blanquet S.;
RT "Peptidyl-tRNA hydrolase from Sulfolobus solfataricus.";
RL Nucleic Acids Res. 31:3227-3235(2003).
CC -!- FUNCTION: Peptidyl-tRNA hydrolase involved in the recycling of tRNA-Lys
CC from diacetyl-lysyl-tRNA-Lys and is important for mitochondrial
CC function. {ECO:0000269|PubMed:12799450}.
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:0000269|PubMed:12799450};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000305}.
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DR EMBL; U00030; AAB68361.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06881.1; -; Genomic_DNA.
DR PIR; S46683; S46683.
DR RefSeq; NP_012059.3; NM_001179320.3.
DR AlphaFoldDB; P38876; -.
DR SMR; P38876; -.
DR BioGRID; 36623; 388.
DR DIP; DIP-5239N; -.
DR IntAct; P38876; 2.
DR STRING; 4932.YHR189W; -.
DR PaxDb; P38876; -.
DR PRIDE; P38876; -.
DR TopDownProteomics; P38876; -.
DR EnsemblFungi; YHR189W_mRNA; YHR189W; YHR189W.
DR GeneID; 856596; -.
DR KEGG; sce:YHR189W; -.
DR SGD; S000001232; PTH1.
DR VEuPathDB; FungiDB:YHR189W; -.
DR eggNOG; KOG2255; Eukaryota.
DR GeneTree; ENSGT00390000004247; -.
DR HOGENOM; CLU_062456_2_1_1; -.
DR InParanoid; P38876; -.
DR OMA; SQWLGTR; -.
DR BioCyc; YEAST:G3O-31218-MON; -.
DR PRO; PR:P38876; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38876; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:SGD.
DR GO; GO:0032543; P:mitochondrial translation; IMP:SGD.
DR CDD; cd00462; PTH; 1.
DR Gene3D; 3.40.50.1470; -; 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 1: Evidence at protein level;
KW Hydrolase; Mitochondrion; Reference proteome.
FT CHAIN 1..190
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187867"
SQ SEQUENCE 190 AA; 21036 MW; A5979D8AB0FC88F9 CRC64;
MSGKWRLVLT GIGNPEPQYA GTRHNVGLYM LELLRKRLGL QGRTYSPVPN TGGKVHYIED
EHCTILRSDG QYMNLSGEQV CKVWARYAKY QARHVVIHDE LSVACGKVQL RAPSTSIRGH
NGLRSLLKCS GGRVPFAKLA IGIGREPGSR SRDPASVSRW VLGALTPQEL QTLLTQSEPA
AWRALTQYIS
