ID A0A364MT19_9PLEO Unreviewed; 559 AA.
AC A0A364MT19;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=PP2C-domain-containing protein {ECO:0000313|EMBL:RAR02674.1};
DE EC=3.1.3.16 {ECO:0000313|EMBL:RAR02674.1};
DE EC=3.1.3.41 {ECO:0000313|EMBL:RAR02674.1};
GN ORFNames=DDE83_008490 {ECO:0000313|EMBL:RAR02674.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR02674.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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:RAR02674.1}.
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DR EMBL; QGDH01000206; RAR02674.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A364MT19; -.
DR STRING; 183478.A0A364MT19; -.
DR OrthoDB; 11028at2759; -.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR PANTHER; PTHR13832:SF876; PROTEIN PHOSPHATASE 1G; 1.
DR PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR Pfam; PF00481; PP2C; 2.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619}.
FT DOMAIN 141..478
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 559 AA; 59620 MW; FC91F1FCB61183C0 CRC64;
MFGNAKDDEV SAIDTPAGND APKSTAAPTT DHGAAAGGTA MASNGSPSLD RKTSDSSVPA
ERKRRSSGVS RARDMFSSAK QSLHIGGSSP TSTSSTTMPE KPTTQTPMQK LGKSDAALSV
PQGSLNNSAG ESAPGPRSTF RVGVTEDKNK KCRRTMEDTH AYLYNFLSTP APSYGLEKAR
ALSDASSVQS DALSSQSVVE SDNGYFAIFD GHAGTFAADW CGKKLHLILE ETIRKNPNTP
IPELLDQTFT SVDQQLEKLP LKNSGCTAVI AVLRWEDRVP NAQSSTGSVL FAPAAVSAIK
HAGEGGEAKD GADATTTEPA AEQQVEARLR TEASRQRVLY TANVGDARIV LCRNGRALRL
SYDHKGSDEN EGRRVASAGG LILNNRVNGV LAVTRALGDA YMKDLVTGHP YTTETVIQAD
QDEFLILACD GLWDVCSDQE AVDLVRQVHD PQEASKKLVD YALARFSTDN LSCMVVRFDN
KALRQRKNEA ATPLDQDQAA MKGGITEADL LVAQARKSIG EPETSVEHAA QEIIMEEAEA
EPGPELNLEA AKAARKNEV
//
