ID   PP4C_CANGA              Reviewed;         309 AA.
AC   Q6FM81;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 117.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE            Short=PP4C;
DE            EC=3.1.3.16;
GN   Name=PPH3; OrderedLocusNames=CAGL0K10208g;
OS   Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 /
OS   NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS
RC   138;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Forms the histone H2A phosphatase complex in association with
CC       the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph
CC       (gamma-H2A) that has been displaced from sites of DNA lesions in the
CC       double-stranded DNA break repair process. Dephosphorylation is
CC       necessary for efficient recovery from the DNA damage checkpoint (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Catalytic subunit of the histone H2A phosphatase complex (HTP-
CC       C) containing PPH3, PSY2 and PSY4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-4 (PP-X)
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR380957; CAG61626.1; -; Genomic_DNA.
DR   RefSeq; XP_448663.1; XM_448663.1.
DR   AlphaFoldDB; Q6FM81; -.
DR   SMR; Q6FM81; -.
DR   STRING; 284593.Q6FM81; -.
DR   EnsemblFungi; CAGL0K10208g-T; CAGL0K10208g-T-p1; CAGL0K10208g.
DR   GeneID; 2890113; -.
DR   KEGG; cgr:CAGL0K10208g; -.
DR   CGD; CAL0134435; CAGL0K10208g.
DR   VEuPathDB; FungiDB:B1J91_K10208g; -.
DR   VEuPathDB; FungiDB:CAGL0K10208g; -.
DR   eggNOG; KOG0372; Eukaryota.
DR   HOGENOM; CLU_004962_8_1_1; -.
DR   InParanoid; Q6FM81; -.
DR   OMA; ANAWRWC; -.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IEA:EnsemblFungi.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR   GO; GO:0030289; C:protein phosphatase 4 complex; IEA:EnsemblFungi.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR   GO; GO:0051598; P:meiotic recombination checkpoint signaling; IEA:EnsemblFungi.
DR   GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IEA:EnsemblFungi.
DR   GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IEA:EnsemblFungi.
DR   GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   CDD; cd07415; MPP_PP2A_PP4_PP6; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR047129; PPA2-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45619; SERINE/THREONINE-PROTEIN PHOSPHATASE PP2A-RELATED; 1.
DR   PANTHER; PTHR45619:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 4 CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Manganese; Metal-binding; Methylation; Nucleus;
KW   Protein phosphatase; Reference proteome.
FT   CHAIN           1..309
FT                   /note="Serine/threonine-protein phosphatase 4 catalytic
FT                   subunit"
FT                   /id="PRO_0000223650"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         309
FT                   /note="Leucine methyl ester"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   309 AA;  35186 MW;  18E0E819D03D0EBD CRC64;
     MLVDLDEILV SLKEGRHIPE ETVYALCMDS QELLMNESNV ARVDTPVTIC GDIHGQLHDL
     LTLFEKSGGV EKTRYVFLGD FVDRGFYSLE SFLLLLVYKL RYPDRITLIR GNHETRQITK
     VYGFYDEVMR KYGNSNVWRY CCEVFDYLSL GAIINDSIFC VHGGLSPDIT TLNEIRAIDR
     KQEVPHEGGM CDLLWSDPDE VDTWSMSPRG AGFLFGKGEV DEFLHVNNVD LIARAHQLVM
     EGYKEMFDGG LVTVWSAPNY CYRCGNVAAV LKIEDNLERK YTIFEAVQAQ NGVGNTIIPT
     KKAQMDYFL
//