ID A0A317WES8_9EURO Unreviewed; 1199 AA.
AC A0A317WES8;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=GDPD-domain-containing protein {ECO:0000313|EMBL:PWY84903.1};
GN ORFNames=BO70DRAFT_313210 {ECO:0000313|EMBL:PWY84903.1};
OS Aspergillus heteromorphus CBS 117.55.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448321 {ECO:0000313|EMBL:PWY84903.1, ECO:0000313|Proteomes:UP000247233};
RN [1] {ECO:0000313|EMBL:PWY84903.1, ECO:0000313|Proteomes:UP000247233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117.55 {ECO:0000313|EMBL:PWY84903.1,
RC ECO:0000313|Proteomes:UP000247233};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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:PWY84903.1}.
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DR EMBL; MSFL01000009; PWY84903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317WES8; -.
DR STRING; 1448321.A0A317WES8; -.
DR VEuPathDB; FungiDB:BO70DRAFT_313210; -.
DR OrthoDB; 1005457at2759; -.
DR Proteomes; UP000247233; 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; 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; 3.
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; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51704; GP_PDE; 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:UP000247233};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..144
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 371..394
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 458..490
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 491..523
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 529..561
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 813..1140
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 599..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1142..1165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1199 AA; 132028 MW; 9003E3AED865D83E CRC64;
MKFGRNLPRN MVPEWSASYI RYKALKKLIK AAAENVKAGQ EADLAGFFYS LDRNLEDVDY
FYNKKYADFA RRLKLLEDRY GHSLDRGHRL DSEEVEDLLA ALLELRGQLR KLQWYGEVNR
RGFNKITKKL DKKVGVQAQQ KYLETKVEPA PFASNTRVTD ALKKINDRLS VLGEQKVNDD
ASSTHSSLSL KKGPARPNLN LPASMLQTVD DALRKDDTHV LLELLETLKA AADDYGKDVY
PKVLSNLLQR SIYYRSKACV SALLGRMETL EEEDDINKRN CIHRLVIAIG RAQSTSDSEQ
SASMVLDFPL ETSNYITPAA LPTLQPPRSV VMEADLPSHL DRSDPSVSLL QHVLDQLKRE
HRSALLAKDI SGRTPLHYAA QYGFKVVCEV IIEHLQAWDM FEVTEGIDSP RWQDNDGWAP
LHLSVVGGHP LTTRVLLDSE NWHGANKDKA KIRKQVSRSS AVLALATKAN FVDIVQLLVE
AGVDINYQDE QGETALHVAA RFGHDKCAKI LLDGNDEQKA DTELAENTYS WTPLFIACVD
GALGVAELLI EAGANVERLD SSGWTAKEHA ALRGHLDIAR CLAKVTPEPE IAEAEPVIPV
PTPLAEPPSP PLSSLAERRS NVNPGASSTL RNSEPIKTFG HRYLTDESMI LVSLGTMDMR
SHVEAVNLDR IPMENAHSTQ LDTALSLVVS ASGAHGEPEV IDLPVQENIS TEPIVFHAAD
ATKVRLLFDL IPTYAGSKDK VVGRGVALLS SIKPTVGSHR INLKGDSTVP IVAANTLEVI
GSVTFNFLII TPFQHPNMTV TGAQTYWRSM ASTMVIGHRG LGKNMASRNS LQLGENTIQS
FIAAANLGAS YVEFDVQLTK DHVPVIYHDF LVSETGIDAP VHTLTLEQFL QLGDKGPIRR
PGSPSQADIF GDKFNSSSFR QRSMSVGGSE YDPSEMNEKI KHTRDFKKKG FKGNSRGNHI
QAPFATLEEL FHKLPSSVGF NIELKYPMLH ESEEEEMDTY AVELNSFVDT ILAKVYDMGQ
GRNMIFSSFN PDICLLLSFK QPSIPVLFLS DSGASPVGDI RASSLQEAIR FASRWNLLGV
VSQAEALVLC PRLVRVVKES GLVCVSYGAI NNEPNNVKLQ VSEGIDAVIV DSVLAIRKGL
TEHQGKGDTP GVSPQPSPLA QPASGALKDS ISIPVLSHTE QKDDHLHVKP EAIFASHLE
//
