ID X0CHB7_FUSOX Unreviewed; 1175 AA.
AC X0CHB7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 13-SEP-2023, entry version 41.
DE RecName: Full=Glycerophosphodiester phosphodiesterase GDE1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOQG_05005 {ECO:0000313|EMBL:EXK93805.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK93805.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK93805.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK93805.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH658368; EXK93805.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CHB7; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_005444_1_0_1; -.
DR Proteomes; UP000030663; 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; 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; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 1.
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:UP000030663};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..144
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 453..485
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 486..518
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 524..556
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 802..1135
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 289..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1175 AA; 130229 MW; B190FFFB2490E2A0 CRC64;
MKFGRNLPRN QVPEWAGSYI NYKGLKKLVK AAAEKARNGE KVDPAEFFFA LDRNLEDVDF
FYNKKYAEFC RRLNLLQNRY GRTVDVVATL DQDEVEEVMG ALLELRSQFR NLQWFGEINH
KGFVKITKKL DKKVPDLVTQ GPYIDTKVKV KPFAKQANTT RLLDEINKWM SVLSEAQTFD
DTMSEHSTRS LGRASAKGML SLPQAQLDAL DQAVRNDDVP ALEAGLKTSN VIEEGAQPLM
LGLLQRSISS RSKTCLAFLL SNLKSLDEPD DINARNCIHR LVIHIGRTKS VPEGEQDSKS
RPVPAGSQFS NKHLEPGLAT SKAPKSLNQK ESLLLTKDDE AVQLFIFLLE QLRPEQRVAL
KSRDSFGRMP LHYAAQFGIV VVCQIIMSKM QQWDQFHVKD GIDTPEWQDN DGYAPLHLSV
VGGHPLTTQA LLQGENWEGS SPYKAEIRKS ISKSGAVLAI ATKSNYSVIV QLLIDAGVDI
NWRDKTDETA LHVAARFGHE ECARIILKGT ADQKADLEAT ESTYSWTPLH VAAVDGKYNV
AELLVEAGAD ITRLDSSGWT AREHAALRGH MDIARLLETN DVEIESPPTR PVDTLQPTPS
DMSSIGERRS NGNGINNGSR APDAAIKSFG HRYLTNESLV LVSLGSMDMR KNIEPVSLDR
VPLTEAHNTQ LDTALSIVVS ATGASGEPTI IDLPVHDSIA TEPVVFTTTD AGKVKLLFDI
VPTYSGNDKH KVGRAVALLS SVRQTLGSSR MNLQGDVCVP IMSSSFDVIG TVNFNFLVIT
PFHHPNMEIT SRQTYWKKLE STMVIGHRGL GKNLTSNRSL QLGENTLPSF IAAANLGAQY
VEFDVQLTKD HVPVIYHDFL VSETGIDAPV HTLTLEQFLH INPDKNRDSK QQSRKKPAPT
GEPGDFRARS NSLTPKRSQS MGFAGSGPDE LDERMKHTKD FKDKGFKGNT RGNFIQAPFA
TLEELFRELP QETGFNIEMK YPMLHESEEH EMDTYAVELN SFCDTVLSKV YDLAGERHII
FSSFNPDICL CLSYKQPSIP ILFLTDAGCC EVCDIRASSL QEAIRFARRW NLLGIVAAAE
PFVNSPRLIK IVKENGIVCF SYGTLNNDPE MVRRQVKQGI DAVIVDSVLA IRKGLTSGET
PTEPVNGENG TNGTLKPDHE LKEKLDELTI NGGGP
//
