ID A0A1V6R473_9EURO Unreviewed; 1200 AA.
AC A0A1V6R473;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 13-SEP-2023, entry version 22.
DE RecName: Full=GP-PDE domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENSOL_c017G11836 {ECO:0000313|EMBL:OQD96012.1};
OS Penicillium solitum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60172 {ECO:0000313|EMBL:OQD96012.1, ECO:0000313|Proteomes:UP000191612};
RN [1] {ECO:0000313|Proteomes:UP000191612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 29525 {ECO:0000313|Proteomes:UP000191612};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD96012.1}.
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DR EMBL; MDYO01000017; OQD96012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6R473; -.
DR STRING; 60172.A0A1V6R473; -.
DR OrthoDB; 1005457at2759; -.
DR Proteomes; UP000191612; 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; cd08606; GDPD_YPL110cp_fungi; 1.
DR CDD; cd14484; SPX_GDE1_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
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; 1.
DR Pfam; PF13637; Ank_4; 2.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
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; 4.
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:UP000191612};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..144
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 376..404
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 463..495
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 496..528
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 534..566
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 822..1145
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 588..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..935
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1200 AA; 132204 MW; 9EF27D9538B740CA CRC64;
MKFGRNLSQF TVPEWSTSYI KYKALKKLIK SAAEQIKAGQ DPDLAGFFYN LDRNVEDVDY
FYNKKYAEFA RRLKLLEERY GYSMEGRHPL ESEDRHDLRE ALLDLRYHLR RLQWYGEVNR
RGFVKITKKL DKKVGAQAQK RYLETKVDPA PFASNERVFR SQDRINAWMA IITDQSKVDD
KASDDASSTH SSLSLKRGSA RPYLNLPTSI LTAVDDALRK DDTHVLLELL ETLKVTADEA
GETVYPRVLR TLIQRSILHR SRAVLTLLLT RVDTLEEDDD INRRNCLHRV VISIGREQPT
TDSEPAASMV LNFPPETSRY ITPAAPPTLQ PPRPVVKEEH MPQQLARDDS AVTHFQFLLD
SLRPDQRESL MAKDLSGRTP LHYAAQYGFK VVCEVIIEHL IEWGMFDVSD GIDGPLWQDN
DGWAPLHLSV VGGHPKTTRC LLDAEKDNDP SPERSIIRKQ VPKSSAVLAL ATKANFIDIV
QLLVDAGVDI NYQDEQGETA LHVAARFCHG ECAKILLDGT EDQKADTELA ENTYSWTPLF
IACVDGCLSV AKMLISAGAD VDRFDSSGWT AKEHAALRGH LDIARCLAEV SPGPPPTELD
FSSSTPTLPG SESSSPPTQS SLTDRRSNAP GPTSGGSGVR TTEPIKTFGH RYLTDESMIL
VSLGTMDMRK PLETVSLDRI PMENAHATQL DTSLSMVITA SGAHGEPEVI DLPVQDNIST
EPIVFHTTDP SKVRLLFDLV PTYAGSKEKI VGRGVALLSS IKPTVGSHRI NLKGDSTVPI
VAANTLEVIG SVTFNFLVIT PFKHPKMSIA GNQTYWRSMS STMVIGHRGL GKNMAGRNSL
QLGENTVESF IAAANLGASY VEFDVQLTKD HVPVIYHDFL VSETGIDAPV HTMTLDQFLE
LGVGRYRHAL PGSVKAGETS GDGPRQRSMS VGGSEYDPAE LTEKIKHTRD FKKKGFKGNT
RGEHIQAPFA TLEELFTKIP KPVGFNIELK YPMLHESEEE EMDTYAVELN SFVDTMLKTV
YDLGGGRDML FSSFNPDICL LLSFKQPSIP VLFLSDAGAS PVGDIRASSL QEAIRFASRW
NLLGIVTQAE PLVLCPRLVR IVKESGLVCV SYGTLNNDGN NVDSQVAEGI DAVIVDSVLG
ITNGLIQRQG KGDRTPGLSP NPSAVSDQAA DSAKGAVTVP TLERTNQNNL SPDTIPPALL
//
