ID A0A1G4BQI0_9PEZI Unreviewed; 763 AA.
AC A0A1G4BQI0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Type I phosphodiesterase/nucleotide pyrophosphatase {ECO:0000313|EMBL:OHF03537.1};
GN ORFNames=CORC01_01256 {ECO:0000313|EMBL:OHF03537.1};
OS Colletotrichum orchidophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=1209926 {ECO:0000313|EMBL:OHF03537.1, ECO:0000313|Proteomes:UP000176998};
RN [1] {ECO:0000313|EMBL:OHF03537.1, ECO:0000313|Proteomes:UP000176998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMI 309357 {ECO:0000313|EMBL:OHF03537.1,
RC ECO:0000313|Proteomes:UP000176998};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) 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:OHF03537.1}.
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DR EMBL; MJBS01000006; OHF03537.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4BQI0; -.
DR STRING; 1209926.A0A1G4BQI0; -.
DR OrthoDB; 1366859at2759; -.
DR Proteomes; UP000176998; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0006506; P:GPI anchor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd16018; Enpp; 1.
DR Gene3D; 3.30.1360.180; -; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR002591; Phosphodiest/P_Trfase.
DR PANTHER; PTHR10151:SF120; BIS(5'-ADENOSYL)-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR10151; ECTONUCLEOTIDE PYROPHOSPHATASE/PHOSPHODIESTERASE; 1.
DR Pfam; PF01663; Phosphodiest; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 4: Predicted;
KW GPI-anchor biosynthesis {ECO:0000256|ARBA:ARBA00022502};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000176998};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 201..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..720
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 763 AA; 85811 MW; 5F47AC8168B475BA CRC64;
MSIRRPSAKS RAGRDNASLL APDTYDDDAS SLHSRSDQDS DSDDDQLQLR ARNSRELRAA
DSLVFMEEEE IETLVEETRK KKELQRRGSG LAVTNPLKLF GRGPDGQRPG SKDGSSENLL
NEKDRRQQRR TRRKQKKDRL LEKATYGEDG ELMYEMEEGA MKEGSSTGDS SERDDSDELD
RQRLKMVTNA KSDKRRSWRR WLVIHSMIAV GFAILVLVAW KLSLGRKSAH KAEFVSNGTA
LFAPTTIIIS LDGFRADFLQ RGITPRLNAF IKEGVSPKYM LPAFPSVTFP NHYTLATGLH
PESHGIVGNT FWDPDMQAEF YYTDPVRSLD AKWWSGEPFW VTAERQGIRS AIHMWPGSEA
HILGVEPTFL DKFNGKEVLD NKVSRILEFL DKPGMEDKTA KVEDMRPQLI AAYVPNVDAD
GHRYGPNSTE IRVSIESADA MMDQLFLALE QRNLTHIVNV IVVSDHGMAT TDTTRLLQLE
DLVDTSKIEH TDGWPLYGLR PKNPDDLQGL YDVLVEKSKT NPNFEVYLRD VNMPERYHFS
KNRRIAPLWI VPKTGWAIVT RDEMDVEKAL KDGTVYNPRG LHGYDHEHPL MRAIFIARGP
AFPHPPNSQI DNFQNINVYN ILCDSVGLIP EPNNGTLRLP LTTLGTHKSE DTPPEPEDPV
PPYNTTQVPA SPSAPPAEQP TNTDKAIQVD PVPQPTATAP ASNDDEKGDD DEESDEADED
AIEKGKEAMI GVWDWLKDKF GKVWDKIKGS KGDKESGDKE GSE
//
