ID A0A139IC24_9PEZI Unreviewed; 1191 AA.
AC A0A139IC24;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=GP-PDE domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AC579_818 {ECO:0000313|EMBL:KXT12250.1};
OS Pseudocercospora musae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=113226 {ECO:0000313|EMBL:KXT12250.1, ECO:0000313|Proteomes:UP000073492};
RN [1] {ECO:0000313|EMBL:KXT12250.1, ECO:0000313|Proteomes:UP000073492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 116634 {ECO:0000313|EMBL:KXT12250.1,
RC ECO:0000313|Proteomes:UP000073492};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-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:KXT12250.1}.
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DR EMBL; LFZO01000159; KXT12250.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139IC24; -.
DR STRING; 113226.A0A139IC24; -.
DR Proteomes; UP000073492; Unassembled WGS sequence.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd14484; SPX_GDE1_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR InterPro; IPR004331; SPX_dom.
DR PANTHER; PTHR22958:SF1; GLYCEROPHOSPHOCHOLINE PHOSPHODIESTERASE GPCPD1; 1.
DR PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF03009; GDPD; 2.
DR Pfam; PF03105; SPX; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS51704; GP_PDE; 1.
DR PROSITE; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS51382; SPX; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000073492};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..146
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 454..486
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 487..509
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 526..558
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 806..1131
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 589..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1191 AA; 133183 MW; 2E9373DBF960FBB7 CRC64;
MKFGQNLPRN QVPEWASSYI DYKALKKLIK AATKNADEHG GEEPDLAEFF YTLDRQLEDV
DTFYNRKYAE FSRRLRLLYD RYGMASKLKD GMEKEDMEDL MGTLLELRGQ YRKLQWYGEV
NRRGFVKITK KLDKKIESSS TQSRYLATKV DPKPFATNNK LTLDMRGINE WLSSLGEIKV
LDDSSSVHSG SSGSIHRMGS RAALRIPSSA LEAMENAVRE DDTAKLFELV STHLPNANNG
MQKGLLLDLL QRAISFQKLD CIAAIIDKVP SIDPDDDMNK RNCLHRLIIA TGRARASHVS
GGYQEISKTT GYINAAEPPV RAPGAFKVEE RDPNQDPFKD DHIEKLLAFI LEHLRKELQP
AVLTKDVYGR MPLHYAAQYG LVFATDMLMK HMQQWNLFDV SGGIDATEWQ DDEGYAPLHL
AVIGGHYRTS KALLLVDDWH NFKDARLTNK HAEKSGLSLE LATKSNYHKI VKLLVDVGVD
VNFRDENGET ALHIAARFGY EDCARALLDA KEGEQRINVG IGEKAYNWTP LFIACVNGHM
NIVKLLIAAG AQINRLDSSL WTPQEHAALR GHMDIAKYLA QFTPPPSIHP SPELQAQLSG
SPPKSSSLED RRSNGVQREE VQRMRIPEPV KSFGHRYLSD ESMVLVSLGT LDENKDLKPI
SLEDIAITDA HATQLDTALS LVVTAQGATG EPNVIDLPIQ EEISTTPITF MCKDPSKVKL
LFDLVPTYSG STDKRIARAV ALLSSIKTGV GNKRTTLQTD LSVPLLAGPN FDVIGTINFN
FLIITPFKHP NLSISEEKTY WTKSSTRVIG HRGLGKNMST KTSLQLGENT IQSFITAANL
GASYVEFDVQ MTKDHVPVIY HDFTVSETGA DVPVHTLTLE QFLALSDTPK PSRPNSPPTT
NGRSERAIHD RRVQRSYSVG APFEDTKRDR LKHTRDFKIK GFKGNTRGDV IQSQFTTLEQ
MFDSLPEDVG FNIEMKYPML FELVEEEMDT YAIELNLFVD TVLKMVYDRR KKRNIVFSSF
HPDICLMLTF KQPSIPVLFL TDAGVSPVGD IRASSLQEAV RFASRWNLLG IVSAAEPFVL
CPRLINVVQS SELICVSYGT LNNDPHNSNL QAQAGIDAVI VDSVARIRKG LTEAEAPKSI
TNGEQEETEN EAEVKRTHHT TEGVSMLTQE LKDGLQLAAR VQNIQHSQDS Q
//
