ID A0A3D8QWJ1_9HELO Unreviewed; 1147 AA.
AC A0A3D8QWJ1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=GDPD-domain-containing protein {ECO:0000313|EMBL:RDW66060.1};
GN ORFNames=BP6252_09695 {ECO:0000313|EMBL:RDW66060.1};
OS Coleophoma cylindrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Dermateaceae; Coleophoma.
OX NCBI_TaxID=1849047 {ECO:0000313|EMBL:RDW66060.1, ECO:0000313|Proteomes:UP000256645};
RN [1] {ECO:0000313|EMBL:RDW66060.1, ECO:0000313|Proteomes:UP000256645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BP6252 {ECO:0000313|EMBL:RDW66060.1,
RC ECO:0000313|Proteomes:UP000256645};
RX PubMed=30018880; DOI=10.5598/imafungus.2018.09.01.13;
RA Wingfield B.D., Bills G.F., Dong Y., Huang W., Nel W.J.,
RA Swalarsk-Parry B.S., Vaghefi N., Wilken P.M., An Z., de Beer Z.W.,
RA De Vos L., Chen L., Duong T.A., Gao Y., Hammerbacher A., Kikkert J.R.,
RA Li Y., Li H., Li K., Li Q., Liu X., Ma X., Naidoo K., Pethybridge S.J.,
RA Sun J., Steenkamp E.T., van der Nest M.A., van Wyk S., Wingfield M.J.,
RA Xiong C., Yue Q., Zhang X.;
RT "IMA Genome-F 9: Draft genome sequence of Annulohypoxylon stygium,
RT Aspergillus mulundensis, Berkeleyomyces basicola (syn. Thielaviopsis
RT basicola), Ceratocystis smalleyi, two Cercospora beticola strains,
RT Coleophoma cylindrospora, Fusarium fracticaudum, Phialophora cf. hyalina,
RT and Morchella septimelata.";
RL IMA Fungus 9:199-223(2018).
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:RDW66060.1}.
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DR EMBL; PDLM01000011; RDW66060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8QWJ1; -.
DR STRING; 1849047.A0A3D8QWJ1; -.
DR Proteomes; UP000256645; 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; 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; 3.
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:UP000256645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..145
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 525..557
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 802..1126
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 314..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1147 AA; 126510 MW; 355E5521DEA452C4 CRC64;
MKFGRNLPRN QVPEWSSSYI NYKGLKKLIK AAAATAKEGN KDVDLAEFFF SLDRNLEDVD
AFYNKKFADA ARRLKLLQDR YGSSPDALAA LDQEEIEELM GALLELRGQL RKLQWFGEVN
RRGFLKITKK LDKKVAVTAG TQQRYLASKV DPKPFATNVA LSQAMNAIND RLSILGENNV
PDDVRSVHST HSMKRVSSRS ILHLPPGLQE TVDQAVRTDD EPILKETLKE ANLEPQEPAM
QKLFVNLLQR SITSKAKKCI AYLLGEIKSL DETDDINQRN CLHRLVISIG RAKTIQAEGL
DPKSVLTAEP NSQHYITPAA SPPPGPRPSK NQESLLSLDD EHVKLLEYVL NRLEPHQRVA
LKSRDSYGRF PLHYAAQFGF VVVCQLVMKY MQDWGQFNVE HGIDAEEWQD NEGMAPLHLS
VIGGHPLTTQ ALLDGENWQG VNDEKLAMRR DISKSSAVLA LATKSNFTPI VKLLVDAGVN
INWQDEMGET ALHVAARFGH EECAKILIDG TPDQKANLQL AEKTFAWTAL HVACVDGHLN
IVELLIAGGA ELNKRDASGW TGREHAALRG HMAIAERLAE AAPDLESSES EGSVTSESSP
TESSAMSSVE ALHSQIAVPK ATEPVKSFGH RYLTNETMVL VSLGSMDMRK DAPAVKLDRI
PLAEAHSTQL DTALSVIVSA TGAQGEPTIV DLPVQDNIST EPIVFTTHDA SKVKILFDIV
PTYSGRQENK VARGVAVLSL IKPTIGLKRM NLQGDISVPI VAASTLEVIG LVNFNFLIIT
PFSHPNMGIT AKQTYWKELS SPMVIGHRGL GKNQTANKSL QLGENTIQSF IAAANLGANY
VEFDVQLTKD HVPVIYHDFL VSETGIDAPV HTLTLEQFLH VNDTIRASRP PSPPHTETET
KVRGTDRQRS LSMGHVHPEL DMAERMKHTR DFKAKGYKGN SRGNFIQAPF TTLEEMFKKL
PENVGFNVEM KYPMLYETEQ EEMDTYAVEL NSFVDTVLTT VYDLGKKRNI IFSSFNPDIC
LLLSFKQPSI PILFLTDAGT SPVGDIRASS LQEAIRFASR WNLLGVVSAA EPLVNSPRLV
KVVKDSGLVC VSYGTLNNDP VRVQQQVKQG IDAVIVDSVL AIRKGLTNSE GKSKAGSMPP
WTGPVDI
//
