ID S3C0S7_OPHP1 Unreviewed; 1258 AA.
AC S3C0S7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Glycerophosphodiester phosphodiesterase gde1 {ECO:0000313|EMBL:EPE05291.1};
GN ORFNames=F503_03896 {ECO:0000313|EMBL:EPE05291.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE05291.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE05291.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE05291.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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DR EMBL; KE148157; EPE05291.1; -; Genomic_DNA.
DR AlphaFoldDB; S3C0S7; -.
DR STRING; 1262450.S3C0S7; -.
DR VEuPathDB; FungiDB:F503_03896; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1162; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_005444_1_0_1; -.
DR OMA; TYGVENN; -.
DR OrthoDB; 1005457at2759; -.
DR Proteomes; UP000016923; 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; PF00023; Ank; 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; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
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:UP000016923};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..144
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 496..528
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 567..599
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 873..1236
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 236..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 953..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1258 AA; 137880 MW; BB1EDC1D5E55C7F0 CRC64;
MKFGRNLPRN QVPEWASSYI NYKGLKKLVK AASDKAERGG TADLAEFFFA LDRNLEDVNS
FYNKKFADIA RRLRLLQDRY GTSPDVASNL DQDEVEELMG ALLELRSQLR NLQWFGEINR
RGFVKITKKL DKKVPNTTTQ HRYIATKVDP CPFARDTTIT RVMAEVNRWL LALGDANQHD
DARSERSVRS LGRASIKAML QLPSALLDRL DQAIRSDDVK SLEECLCEGQ IDLNEHQLEE
PAATDAPAME RSTSSASSSS TPPLLASTAS SQSLLLNLLQ RATSVRSKKA VHFLLNHVQS
IDEPDDINQR NCIHRLVIHI GRSRSAPQGV STGNIAQPET TAAVKPFPHM NHFTTQYLKP
ASSPMPEALS SISETQPLTA EDTRVQMLIY LLDNLTKGQR HSLSTRDSFG RTPLHYAAQF
GFVIVCQTII SRMQAWGQFN VENGIDAPEW QDKEGYAPLH LSVISGHPLT TEALLRSEDW
QGVSESKGAT RRRIAKSSAV LAIATKHDHS GIVQMLVDAG VDVNWQDDTG ETALHIAARF
GYDKCAKILI AGSDTQKADL ELAEKSFAWT PLHISAVDGH LSVATLLVEA GADVDKADSS
GWTAREHAAL RGHLDIGRLL MNHSRLPEKA AEVPLPADEG AIDTPPNESA ASLAPGHQFG
TSPKPEGHQS LGDRRSKGAS RLASAHHDSS PPPQPVRTYG HRYLTDETLV LVSLGSMDMR
KNVEAVQLDQ VPLTEAHQTQ LDTALSIVVS ATGATGEASV IDLPVQENIS TEPIVFTTKD
VSGVTLNFNI VPTYSGNSKN KIGRAFALLP SVRPTIGLKR MNLQGDVCVP IISPELEIIG
TVNFNFLVVT PFSHPNMSVK SDQTYWRKVS STPMVIGHRG LGKNMASNRS LQLGENTVPS
FIAAANLGAN YVEFDVQLTK DHIPVIYHDF LVSETGIDAP VHTLTLEQFL HINDGGRSTN
AGGRRSDSPR NGEKALVNGS VIADSPAAAK NSVHFDADAL SNGNGQRKNG YRIPRRAMSM
SLEDTTGPHG NLNERMKHTR DFKEKGFKAN SRGNFIQAPF ATLEDLFQQV PSGVGFNIEM
KYPMLHESED HGMDTYAVEL NSFCDTVLSK VYDLAHGRDV IFSSFNPDIC LCLSFKQPNF
PIMFLTDAGG EAVGDIRASS LQEAIRFARR WNLLGIVSLS EPFIISPRLV RVVKQSGLVC
VSYGAQNNQP ELVEKQVKEG IDAVIVDSVL AIRKGLTKDE GKPAVPADAA EERKSRPE
//
