PTH2_YEAST
ID PTH2_YEAST Reviewed; 208 AA.
AC P34222; D6VPU3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Peptidyl-tRNA hydrolase 2 {ECO:0000303|PubMed:12475929};
DE Short=PTH 2 {ECO:0000303|PubMed:12475929};
DE EC=3.1.1.29 {ECO:0000269|PubMed:12799450};
GN Name=PTH2 {ECO:0000303|PubMed:12475929}; OrderedLocusNames=YBL057C;
GN ORFNames=YBL0510, YBL0514;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154187; DOI=10.1002/yea.320091210;
RA Scherens B., el Bakkoury M., Vierendeels F., Dubois E., Messenguy F.;
RT "Sequencing and functional analysis of a 32,560 bp segment on the left arm
RT of yeast chromosome II. Identification of 26 open reading frames, including
RT the KIP1 and SEC17 genes.";
RL Yeast 9:1355-1371(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
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 [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).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-152, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis.
CC {ECO:0000269|PubMed:12475929, 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 -!- INTERACTION:
CC P34222; P48510: DSK2; NbExp=11; IntAct=EBI-2345448, EBI-6174;
CC P34222; P32628: RAD23; NbExp=5; IntAct=EBI-2345448, EBI-14668;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MISCELLANEOUS: Present with 2190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAT92782.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA80790.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA84877.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z23261; CAA80790.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z35818; CAA84877.1; ALT_INIT; Genomic_DNA.
DR EMBL; AY692763; AAT92782.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006936; DAA07063.2; -; Genomic_DNA.
DR PIR; S39831; S39831.
DR RefSeq; NP_009496.2; NM_001178297.2.
DR AlphaFoldDB; P34222; -.
DR SMR; P34222; -.
DR BioGRID; 32642; 75.
DR IntAct; P34222; 3.
DR MINT; P34222; -.
DR STRING; 4932.YBL057C; -.
DR iPTMnet; P34222; -.
DR MaxQB; P34222; -.
DR PaxDb; P34222; -.
DR PRIDE; P34222; -.
DR EnsemblFungi; YBL057C_mRNA; YBL057C; YBL057C.
DR GeneID; 852223; -.
DR KEGG; sce:YBL057C; -.
DR SGD; S000000153; PTH2.
DR VEuPathDB; FungiDB:YBL057C; -.
DR eggNOG; KOG3282; Eukaryota.
DR GeneTree; ENSGT00390000015991; -.
DR HOGENOM; CLU_073661_0_1_1; -.
DR InParanoid; P34222; -.
DR OMA; PNSYDVK; -.
DR BioCyc; YEAST:G3O-28955-MON; -.
DR PRO; PR:P34222; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P34222; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:SGD.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
DR CDD; cd02430; PTH2; 1.
DR Gene3D; 3.40.1490.10; -; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR002833; PTH2.
DR PANTHER; PTHR12649; PTHR12649; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; SSF102462; 1.
DR TIGRFAMs; TIGR00283; arch_pth2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Isopeptide bond; Reference proteome; Ubl conjugation.
FT CHAIN 1..208
FT /note="Peptidyl-tRNA hydrolase 2"
FT /id="PRO_0000120284"
FT REGION 32..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 152
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 208 AA; 22435 MW; A77F3A5BAC578943 CRC64;
MEKMTVSSNY TIALWATFTA ISFAVGYQLG TSNASSTKKS SATLLRSKEM KEGKLHNDTD
EEESESEDES DEDEDIESTS LNDIPGEVRM ALVIRQDLGM TKGKIAAQCC HAALSCFRHI
ATNPARASYN PIMTQRWLNA GQAKITLKCP DKFTMDELYA KAISLGVNAA VIHDAGRTQI
AAGSATVLGL GPAPKAVLDQ ITGDLKLY
