ID   MGDP1_YEAST             Reviewed;         178 AA.
AC   P40081; D3DM40;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 148.
DE   RecName: Full=Putative magnesium-dependent phosphatase YER134C;
DE            EC=3.1.3.48;
GN   OrderedLocusNames=YER134C;
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=9169868;
RA   Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA   Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA   Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA   Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA   Botstein D., Davis R.W.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL   Nature 387:78-81(1997).
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   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   [4]
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   [5]
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).
CC   -!- FUNCTION: Magnesium-dependent phosphatase which may act as a tyrosine
CC       phosphatase. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 6190 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; U18916; AAC03232.1; -; Genomic_DNA.
DR   EMBL; AY558562; AAS56888.1; -; Genomic_DNA.
DR   EMBL; BK006939; DAA07794.1; -; Genomic_DNA.
DR   PIR; S50637; S50637.
DR   RefSeq; NP_011060.1; NM_001179024.1.
DR   AlphaFoldDB; P40081; -.
DR   SMR; P40081; -.
DR   BioGRID; 36880; 110.
DR   IntAct; P40081; 21.
DR   STRING; 4932.YER134C; -.
DR   iPTMnet; P40081; -.
DR   MaxQB; P40081; -.
DR   PaxDb; 4932-YER134C; -.
DR   PeptideAtlas; P40081; -.
DR   EnsemblFungi; YER134C_mRNA; YER134C; YER134C.
DR   GeneID; 856873; -.
DR   KEGG; sce:YER134C; -.
DR   AGR; SGD:S000000936; -.
DR   SGD; S000000936; YER134C.
DR   VEuPathDB; FungiDB:YER134C; -.
DR   eggNOG; KOG4549; Eukaryota.
DR   GeneTree; ENSGT00940000165797; -.
DR   HOGENOM; CLU_071162_0_1_1; -.
DR   InParanoid; P40081; -.
DR   OMA; GVWAWRK; -.
DR   OrthoDB; 1327738at2759; -.
DR   BioCyc; YEAST:G3O-30296-MONOMER; -.
DR   BioGRID-ORCS; 856873; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P40081; -.
DR   Proteomes; UP000002311; Chromosome V.
DR   RNAct; P40081; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0003993; F:acid phosphatase activity; IDA:SGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030946; F:protein tyrosine phosphatase activity, metal-dependent; IDA:SGD.
DR   CDD; cd07501; HAD_MDP-1_like; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR010033; HAD_SF_ppase_IIIC.
DR   InterPro; IPR035679; MDP-1_euk.
DR   InterPro; IPR010036; MDP_1_eu_arc.
DR   NCBIfam; TIGR01681; HAD-SF-IIIC; 1.
DR   NCBIfam; TIGR01685; MDP-1; 1.
DR   PANTHER; PTHR17901:SF14; MAGNESIUM-DEPENDENT PHOSPHATASE 1; 1.
DR   PANTHER; PTHR17901; MAGNESIUM-DEPENDENT PHOSPHATASE 1 MDP1; 1.
DR   Pfam; PF12689; Acid_PPase; 1.
DR   SFLD; SFLDG01131; C1.5.2:_MDP_Like; 1.
DR   SFLD; SFLDG01129; C1.5:_HAD__Beta-PGM__Phosphata; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Magnesium; Metal-binding; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..178
FT                   /note="Putative magnesium-dependent phosphatase YER134C"
FT                   /id="PRO_0000202650"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        13
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         11
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         12
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         74
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   178 AA;  20441 MW;  F3F765AC0076CBFC CRC64;
     MTGYPDVAAF DLDYTIWPCY CDTHLHGPFK PVKSSNGEVL TIICRDGYEL TIYKDIPRIL
     GDLKDNGVKL MTASRTWAPE IAQEILKIFK VKYAGVVTPL ANLFDEFQWG ERSKIGHLRD
     GLKDLYNTSD LKSKKICLFD DESRNKEVEK YGVKFVYVRD PENGPSWKLY QDYLSGKV
//