ID B6JWP5_SCHJY Unreviewed; 349 AA.
AC B6JWP5;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 2.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN Name=pph3 {ECO:0000313|JaponicusDB:SJAG_00823};
GN ORFNames=SJAG_00823 {ECO:0000313|EMBL:EEB05796.2};
OS Schizosaccharomyces japonicus (strain yFS275 / FY16936) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=402676 {ECO:0000313|EMBL:EEB05796.2, ECO:0000313|Proteomes:UP000001744};
RN [1] {ECO:0000313|EMBL:EEB05796.2, ECO:0000313|Proteomes:UP000001744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=yFS275 / FY16936 {ECO:0000313|Proteomes:UP000001744};
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
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 Evidence={ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|RuleBase:RU004273}.
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DR EMBL; KE651166; EEB05796.2; -; Genomic_DNA.
DR RefSeq; XP_002172089.2; XM_002172053.2.
DR AlphaFoldDB; B6JWP5; -.
DR STRING; 402676.B6JWP5; -.
DR EnsemblFungi; EEB05796; EEB05796; SJAG_00823.
DR GeneID; 7048897; -.
DR JaponicusDB; SJAG_00823; pph3.
DR VEuPathDB; FungiDB:SJAG_00823; -.
DR eggNOG; KOG0372; Eukaryota.
DR HOGENOM; CLU_004962_8_1_1; -.
DR OMA; NDINMIC; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000001744; Unassembled WGS sequence.
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: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 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 Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Reference proteome {ECO:0000313|Proteomes:UP000001744}.
FT DOMAIN 111..116
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 258..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 38740 MW; BAD8E357AF668D01 CRC64;
MSGGLDLDWQ LEQLQKCRSV PESNVIELCQ LAREILIEES NLQWVNSPVT VCGDIHGQLH
DLLELFRVSG PCPNTNYLFL GDYVDRGFYS VETFLLLLTL KCKYPSRITL IRGNHESRQI
TQVYGFYDEC NRKYGSANVW RYCCEIFDYM ALGAIIDGKV LCVHGGLSPS ITSLDQIGLL
DRKQEVPHEG AMCDLLWSDP DDIGGWGLSP RGAGYLFGAN IAEAFNHANG LSFVARAHQL
VMEGYKLHFS SAEKQVPSYQ DAEEELDTDS HSISEDNTPS PGDIVTIANK DLGSVVTVWS
APNYCYRCGN VASVMQISDG DTQTFKIFGA APQERTGIPA KQPIADYFL
//
