ID   PP4R3_ASHGO             Reviewed;         838 AA.
AC   Q75E32;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 2.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3;
DE            Short=PP4R3;
GN   Name=PSY2; OrderedLocusNames=ABL162C;
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, AND SEQUENCE REVISION TO 633 AND C-TERMINUS.
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: Core regulatory subunit of the histone H2A phosphatase
CC       complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been
CC       displaced from sites of DNA lesions in the double-stranded DNA break
CC       repair process. Dephosphorylation is necessary for efficient recovery
CC       from the DNA damage checkpoint (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Regulatory subunit 3 (R3) of the histone H2A phosphatase
CC       complex (HTP-C) consisting of PPH3, PSY2 and PSY4. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR   EMBL; AE016815; AAS50609.2; -; Genomic_DNA.
DR   RefSeq; NP_982785.2; NM_208138.2.
DR   AlphaFoldDB; Q75E32; -.
DR   SMR; Q75E32; -.
DR   STRING; 33169.AAS50609; -.
DR   EnsemblFungi; AAS50609; AAS50609; AGOS_ABL162C.
DR   GeneID; 4618865; -.
DR   KEGG; ago:AGOS_ABL162C; -.
DR   eggNOG; KOG2175; Eukaryota.
DR   HOGENOM; CLU_004909_4_0_1; -.
DR   InParanoid; Q75E32; -.
DR   OMA; YHRYMIS; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0000794; C:condensed nuclear chromosome; IEA:EnsemblFungi.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0030289; C:protein phosphatase 4 complex; IBA:GO_Central.
DR   GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; 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; IBA:GO_Central.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR006887; DUF625.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   Pfam; PF04802; SMK-1; 1.
PE   3: Inferred from homology;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..838
FT                   /note="Serine/threonine-protein phosphatase 4 regulatory
FT                   subunit 3"
FT                   /id="PRO_0000223655"
FT   REGION          452..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   838 AA;  94911 MW;  448DF95651C21087 CRC64;
     MAKESLRIGV ASTEPKRVKV YILEDNEWRD TGTGFCTGQC EQDKPHAYLL VRDEEQPERV
     LLKSKLEGNI EYQRQEETLI VWKDLQGQDI ALSFEESTGC NALCEFICLV QKTFENNISL
     VSVRSNDDGM GSVHEIITGP VHLPSNDPQQ NEETLMESLR ILNENTSFEF LKNETVDFIL
     NTNYLHTLIN HFHIAEEKLL HKDLLLLSHI IKTLFLYNER EVLEQLIDDK HYMGVVGILE
     YDTDFPDCKA SHRKCLQGVR PKFQEVIPLN DENMRQTINK TFRLQFLKDV VLIRFLDDHA
     FNLITDVMLT YQTTIIRCLQ EGSFIDDLVN LYTNNADTSD SDLIERKRQG IRLLDECVQI
     SCNLDPPDRS IFYKVLVKKG LFNVLDFAFN VETNSDIRIL ATDMIISIIE YDILLINSVR
     NEVDDSPFAA TNEDSNINTG LIDEGGADSA DNNCNGNSAV KAGESNGAES PIAPPGSRSP
     SRHTSDISLL LILSKILLTD QSPGLKEQAF QALITLLDPE DFMGEEYEDQ SNLESLMKFY
     ANSKLREKPS TPPQFQLLEY FTKFYEQVAP VLFQSFISGE VEGMDDQLLL RLVKLVDLLI
     HEHDIMLSRG FILENGILLT IGKLMEPSHI IQLRLAAVRC IKGIVAVNDE FYHNYLISKN
     LFDPICQLLQ ENLYFDNMAN SCVLDLFKVI SARFGQDQEY AEVSTKNFLV LNQYLVERFG
     PLLEKVDYVP YTSSMIQMSR VGRDAINKQQ DNNGERNTTT GGEADNEEFD VMGAMDSSLA
     SESDGENNEN NEESPYGGAQ NSKRSFSDIE DNTIGVEKGN PEPGLPIKKL AEEISESS