ID A0A2G5HQA1_CERBT Unreviewed; 535 AA.
AC A0A2G5HQA1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE SubName: Full=Putative phosphatase PSR2 {ECO:0000313|EMBL:PIA94714.1};
GN ORFNames=CB0940_08847 {ECO:0000313|EMBL:PIA94714.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIA94714.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIA94714.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIA94714.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:PIA94714.1}.
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DR EMBL; LKMD01000104; PIA94714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5HQA1; -.
DR OrthoDB; 5473812at2759; -.
DR Proteomes; UP000230605; Chromosome 6.
DR GO; GO:0016791; F:phosphatase activity; IEA:InterPro.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR011948; Dullard_phosphatase.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02251; HIF-SF_euk; 1.
DR PANTHER; PTHR12210; DULLARD PROTEIN PHOSPHATASE; 1.
DR PANTHER; PTHR12210:SF171; PHOSPHATASE HERZOG; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
FT DOMAIN 361..519
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT REGION 1..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 535 AA; 57121 MW; 8FF0D562B07F73BC CRC64;
MSQPGTQPVP GGVGQGPAEV SQTAQNVDAT KAGENGAGAS VPASSSLEPN QQNVSAADRS
ESIGPRSKRS FGRRKRDPST GSRRRGRRGE PANEKSTRSA PGASASRTNL GDENKPKKKS
GLFAILCCSA SDKSPGGDGQ DAAEPAKPVT KPLQGRTQQQ PQAVTQAGSS NANTSADESK
EVIDEKAAQQ HPQANGSKGE PRTSTSGSAL DEKTAAIQST FPRNSIDAAA SGSASPAVVP
PIVTGGAASL APGPSVQVQA PTPTVPQQED EPIFDRTAEQ QQRDEDIEMK DSNVLTEKEA
QKEIEEMQHA HQEETSTAQP TTGLPPPPGP PPGTNEKSNE TSMVSTPEGT SKWLLPPTRP
EHKGRKCLVL DLDETLVHSS FKILHQADFT IPVEIEGQYH NVYVIKRPGV DAFLKRVGEI
YEVVVFTASV SKYGDPLLDQ LDIHNVVHHR LFRESCYNHQ GNYVKDLSQV GRDLKETIII
DNSPTSYIFH PQHAVPISSW FSDAHDNELL DLIPVLEDLA GDQVADVSLV LDVAL
//
