ID A0A316ZIU3_9BASI Unreviewed; 523 AA.
AC A0A316ZIU3;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
GN ORFNames=FA09DRAFT_117260 {ECO:0000313|EMBL:PWO00873.1};
OS Tilletiopsis washingtonensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Entylomatales; Entylomatales incertae sedis;
OC Tilletiopsis.
OX NCBI_TaxID=58919 {ECO:0000313|EMBL:PWO00873.1, ECO:0000313|Proteomes:UP000245946};
RN [1] {ECO:0000313|EMBL:PWO00873.1, ECO:0000313|Proteomes:UP000245946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4186 {ECO:0000313|EMBL:PWO00873.1,
RC ECO:0000313|Proteomes:UP000245946};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
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 Evidence={ECO:0000256|PIRNR:PIRNR000909};
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|PIRNR:PIRNR000909,
CC ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|PIRNR:PIRNR000909};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR000909}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-Z subfamily.
CC {ECO:0000256|ARBA:ARBA00029458, ECO:0000256|PIRNR:PIRNR000909}.
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DR EMBL; KZ819284; PWO00873.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316ZIU3; -.
DR STRING; 58919.A0A316ZIU3; -.
DR OrthoDB; 19833at2759; -.
DR Proteomes; UP000245946; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR011159; PPPtase_PPZ/Ppq1.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR031675; STPPase_N.
DR PANTHER; PTHR11668; SERINE/THREONINE PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR11668:SF484; SERINE_THREONINE-PROTEIN PHOSPHATASE PP-Z1-RELATED; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF16891; STPPase_N; 1.
DR PIRSF; PIRSF000909; PPPtase_PPZ; 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 {ECO:0000256|PIRNR:PIRNR000909};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR000909, ECO:0000256|RuleBase:RU004273};
KW Manganese {ECO:0000256|PIRNR:PIRNR000909};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000909};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|PIRNR:PIRNR000909};
KW Reference proteome {ECO:0000313|Proteomes:UP000245946}.
FT DOMAIN 313..318
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 523 AA; 55420 MW; 19B1691D807183D8 CRC64;
MFKSFGKMMG GSSKKGKKSG ESSDYGNDDS GSVAASQDSF GRSSKARDSV ASTAAASENG
NGKGRGRSGS AATAADDPAH PQRIEKHGGL SRHESPLPSP SGSQADGLNG NGMPNTPTPG
RSDSGESPAP GGSAAAQAAG AAANAPAGIP TTQTILANPL GASGSVVAPA SAGARGSMAG
SAGAGAGAGA AGEGVRTFDI DDMITRLLEA GYSTSKLPKP ALKNAEITAV CTAAREVFLS
QPTLIELSPP VKIVGDTHGQ YQDLLRLFEM CGFPPQANYL FLGDYVDRGK QSLETILLLL
CYKIKYPENF FLLRGNHECA NVTRVYGFYD ECKRRVNIKI WKTFIDVFNT LPIAAVVASK
IFCVHGGLSP SLSNMDDIRR IERPTDVPDY GLLNDLLWSD PSDTALDWED NERGVSYCFG
KAVIQQFLAQ YDFDLICRAH MVVEDGYEFW NERTLVTIFS APNYCGEFDN FGAVMSVSED
LLCAFELLKP LDGAALKKEM ARSRRKSSSA ATTHQSPPAR GSY
//
