PP4C_ASHGO
ID PP4C_ASHGO Reviewed; 310 AA.
AC Q74ZR2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Serine/threonine-protein phosphatase 4 catalytic subunit;
DE Short=PP4C;
DE EC=3.1.3.16;
GN Name=PPH3; OrderedLocusNames=AGR136W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
CC -!- FUNCTION: Involved in the dephosphorylation and activation of the
CC transcription factor GLN3 in response to nutrient availability. Forms
CC the histone H2A phosphatase complex in association with the regulatory
CC subunits PSY2 and PSY4, which dephosphorylates H2AS128ph (gamma-H2A)
CC that has been displaced from sites of DNA lesions in the double-
CC stranded DNA break repair process. Dephosphorylation is necessary for
CC efficient recovery from the DNA damage checkpoint (By similarity).
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016820; AAS54626.2; -; Genomic_DNA.
DR RefSeq; NP_986802.2; NM_211864.2.
DR AlphaFoldDB; Q74ZR2; -.
DR SMR; Q74ZR2; -.
DR STRING; 33169.AAS54626; -.
DR EnsemblFungi; AAS54626; AAS54626; AGOS_AGR136W.
DR GeneID; 4623104; -.
DR KEGG; ago:AGOS_AGR136W; -.
DR eggNOG; KOG0372; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; Q74ZR2; -.
DR OMA; HGQFWDM; -.
DR Proteomes; UP000000591; Chromosome VII.
DR GO; GO:0000794; C:condensed nuclear chromosome; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IEA:EnsemblFungi.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
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 GO; GO:0006470; P:protein dephosphorylation; IEA:EnsemblFungi.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 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..310
FT /note="Serine/threonine-protein phosphatase 4 catalytic
FT subunit"
FT /id="PRO_0000223649"
FT ACT_SITE 114
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 55
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 310
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 35699 MW; 1B54B7CC11AF3975 CRC64;
MAGMQLDEII EYLRYSKHIP EETIYELCLK CQELLVNESN VTHVDTPVTI CGDIHGQLHD
LLTLFEKSEG IEKNRFIFLG DFVDRGFYSL ESFLLLLCYK LRYPDRITLI RGNHETRQIT
KVYGFYDEVI RKYGNSNVWR YCCEVFDYLS LGAIINGQIF CVHGGLSPDV MTVDEIRSID
RKQEVPHEGA MCDLLWSDPD EVDTWSLSPR GAGFLFGKNE VDQFLHRNDI SLIARAHQLV
MEGYKEMFDG GLVTVWSAPN YCYRCGNVAA VLRIDDDLSR NYTIFEAVPA QDNRGNAIIP
TKKPQMDYFL
