ID A0A2P5IE25_9PEZI Unreviewed; 372 AA.
AC A0A2P5IE25;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Protein phosphatase {ECO:0000256|RuleBase:RU366020};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366020};
GN ORFNames=DHEL01_v200843 {ECO:0000313|EMBL:POS80756.1};
OS Diaporthe helianthi.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=158607 {ECO:0000313|EMBL:POS80756.1, ECO:0000313|Proteomes:UP000094444};
RN [1] {ECO:0000313|EMBL:POS80756.1, ECO:0000313|Proteomes:UP000094444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7/96 {ECO:0000313|EMBL:POS80756.1,
RC ECO:0000313|Proteomes:UP000094444};
RA Baroncelli R.;
RT "Polyketide synthases of a Diaporthe helianthi virulent isolate.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU366020};
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:RU366020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU366020};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU366020}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:POS80756.1}.
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DR EMBL; MAVT02000034; POS80756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P5IE25; -.
DR STRING; 158607.A0A2P5IE25; -.
DR InParanoid; A0A2P5IE25; -.
DR OrthoDB; 240602at2759; -.
DR Proteomes; UP000094444; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR039123; PPTC7.
DR PANTHER; PTHR12320; PROTEIN PHOSPHATASE 2C; 1.
DR PANTHER; PTHR12320:SF1; PROTEIN PHOSPHATASE PTC7 HOMOLOG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366020};
KW Magnesium {ECO:0000256|RuleBase:RU366020};
KW Manganese {ECO:0000256|RuleBase:RU366020};
KW Metal-binding {ECO:0000256|RuleBase:RU366020};
KW Protein phosphatase {ECO:0000256|RuleBase:RU366020};
KW Reference proteome {ECO:0000313|Proteomes:UP000094444}.
FT DOMAIN 55..358
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
SQ SEQUENCE 372 AA; 39448 MW; 1778A9DC44C4680F CRC64;
MPPKYRKLST TPVLGSQPPP KQFTYDVAAS YIAKDRPYDP STHVFHFNPY NRVQPPRKHT
KRTRPDSGQD AFFVTRLNGT GGVALGVADG VGGWMDSGVD PADFSHGFCD YMAEAAYSHN
SNGDGKPRAL SARSLMQTGY EAICADPAVT AGGSTAIVGL LDPSGILEVA NLGDSGYIHL
RLNAVHGSSE PQTHAFNTPF QLSIIPPWVL RRMSAFGGSQ LADMPSDAEV SRHSLRHGDV
LVFATDGVWD NLFNQDILRI VSAAMEGSGA WVHSDAGGIR VRPDLSAYTS GPSGGDGDGT
KAVSLQSLIA TSITGAAKAA SANTKLDGPF AKEVKKYFPM ETWRGGKVDD ICVVAVVVSE
TTPDDGPVKA KL
//
