ID YCH1_YEAST Reviewed; 148 AA.
AC P42937; D6VUY5;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=CDC25-like phosphatase YCH1;
DE EC=3.1.3.-;
DE AltName: Full=CDC25 homolog 1;
GN Name=YCH1; OrderedLocusNames=YGR203W; ORFNames=G7731;
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=8904340;
RX DOI=10.1002/(sici)1097-0061(19960315)12:3<273::aid-yea898>3.0.co;2-1;
RA Guerreiro P., Barreiros T., Soares H., Cyrne L., Maia e Silva A.,
RA Rodrigues-Pousada C.;
RT "Sequencing of a 17.6 kb segment on the right arm of yeast chromosome VII
RT reveals 12 ORFs, including CCT, ADE3 and TR-I genes, homologues of the
RT yeast PMT and EF1G genes, of the human and bacterial electron-transferring
RT flavoproteins (beta-chain) and of the Escherichia coli phosphoserine
RT phosphohydrolase, and five new ORFs.";
RL Yeast 12:273-280(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 DOMAIN.
RX PubMed=9733650; DOI=10.1006/jmbi.1998.1998;
RA Hofmann K., Bucher P., Kajava A.V.;
RT "A model of Cdc25 phosphatase catalytic domain and Cdk-interaction surface
RT based on the presence of a rhodanese homology domain.";
RL J. Mol. Biol. 282:195-208(1998).
RN [6]
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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10818363; DOI=10.1107/s0907444900005278;
RA Moon J., Kim Y.S., Lee J.Y., Cho S.J., Song H.K., Cho J.H., Kim B.M.,
RA Kim K.K., Suh S.W.;
RT "Crystallization and preliminary X-ray diffraction analysis of
RT Saccharomyces cerevisiae Ygr203p, a homologue of Acr2 arsenate reductase.";
RL Acta Crystallogr. D 56:778-780(2000).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=19382206; DOI=10.1002/prot.22420;
RA Yeo H.K., Lee J.Y.;
RT "Crystal structure of Saccharomyces cerevisiae Ygr203w, a homolog of
RT single-domain rhodanese and Cdc25 phosphatase catalytic domain.";
RL Proteins 76:520-524(2009).
CC -!- FUNCTION: Protein phosphatase. {ECO:0000269|PubMed:19382206}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.5 mM for p-nitrophenylphosphate (PNPP)
CC {ECO:0000269|PubMed:19382206};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:19382206};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2310 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MPI phosphatase family. {ECO:0000305}.
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DR EMBL; Z49133; CAA88996.1; -; Genomic_DNA.
DR EMBL; Z72988; CAA97230.1; -; Genomic_DNA.
DR EMBL; AY558510; AAS56836.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08296.1; -; Genomic_DNA.
DR PIR; S53926; S53926.
DR RefSeq; NP_011719.1; NM_001181332.1.
DR PDB; 3F4A; X-ray; 1.80 A; A/B=1-148.
DR PDB; 3FS5; X-ray; 1.90 A; A=1-148.
DR PDBsum; 3F4A; -.
DR PDBsum; 3FS5; -.
DR AlphaFoldDB; P42937; -.
DR SMR; P42937; -.
DR BioGRID; 33456; 182.
DR DIP; DIP-885N; -.
DR IntAct; P42937; 9.
DR MINT; P42937; -.
DR STRING; 4932.YGR203W; -.
DR iPTMnet; P42937; -.
DR MaxQB; P42937; -.
DR PaxDb; 4932-YGR203W; -.
DR PeptideAtlas; P42937; -.
DR DNASU; 853117; -.
DR EnsemblFungi; YGR203W_mRNA; YGR203W; YGR203W.
DR GeneID; 853117; -.
DR KEGG; sce:YGR203W; -.
DR AGR; SGD:S000003435; -.
DR SGD; S000003435; YCH1.
DR VEuPathDB; FungiDB:YGR203W; -.
DR eggNOG; KOG3772; Eukaryota.
DR GeneTree; ENSGT00940000176483; -.
DR HOGENOM; CLU_107716_1_0_1; -.
DR InParanoid; P42937; -.
DR OMA; PVCRCTN; -.
DR OrthoDB; 21092at2759; -.
DR BioCyc; YEAST:G3O-30887-MONOMER; -.
DR BioGRID-ORCS; 853117; 0 hits in 10 CRISPR screens.
DR EvolutionaryTrace; P42937; -.
DR PRO; PR:P42937; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P42937; Protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016791; F:phosphatase activity; IDA:SGD.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0004792; F:thiosulfate sulfurtransferase activity; IDA:SGD.
DR GO; GO:0016311; P:dephosphorylation; IDA:SGD.
DR CDD; cd01531; Acr2p; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR PANTHER; PTHR10828:SF38; ARSENICAL-RESISTANCE PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR10828; M-PHASE INDUCER PHOSPHATASE DUAL SPECIFICITY PHOSPHATASE CDC25; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Hydrolase; Nucleus;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..148
FT /note="CDC25-like phosphatase YCH1"
FT /id="PRO_0000202844"
FT DOMAIN 29..137
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:3FS5"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3F4A"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3F4A"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:3F4A"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:3F4A"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:3FS5"
FT HELIX 56..61
FT /evidence="ECO:0007829|PDB:3F4A"
FT HELIX 63..78
FT /evidence="ECO:0007829|PDB:3F4A"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3F4A"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3F4A"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:3F4A"
FT HELIX 96..106
FT /evidence="ECO:0007829|PDB:3F4A"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:3F4A"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3F4A"
FT HELIX 124..132
FT /evidence="ECO:0007829|PDB:3F4A"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3F4A"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3F4A"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:3F4A"
SQ SEQUENCE 148 AA; 17249 MW; 41527DB282CBFF11 CRC64;
MDSYSITNVK YLDPTELHRW MQEGHTTTLR EPFQVVDVRG SDYMGGHIKD GWHYAYSRLK
QDPEYLRELK HRLLEKQADG RGALNVIFHC MLSQQRGPSA AMLLLRSLDT AELSRCRLWV
LRGGFSRWQS VYGDDESVTA GYLPDLWR
//
