ID W2S8Q2_9EURO Unreviewed; 1210 AA.
AC W2S8Q2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=GP-PDE domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF1541_09982 {ECO:0000313|EMBL:ETN45106.1};
OS Cyphellophora europaea CBS 101466.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Cyphellophoraceae; Cyphellophora.
OX NCBI_TaxID=1220924 {ECO:0000313|EMBL:ETN45106.1, ECO:0000313|Proteomes:UP000030752};
RN [1] {ECO:0000313|EMBL:ETN45106.1, ECO:0000313|Proteomes:UP000030752}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101466 {ECO:0000313|EMBL:ETN45106.1,
RC ECO:0000313|Proteomes:UP000030752};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phialophora europaea CBS 101466.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KB822713; ETN45106.1; -; Genomic_DNA.
DR RefSeq; XP_008712876.1; XM_008714654.1.
DR AlphaFoldDB; W2S8Q2; -.
DR STRING; 1220924.W2S8Q2; -.
DR GeneID; 19977321; -.
DR VEuPathDB; FungiDB:HMPREF1541_09982; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG1162; Eukaryota.
DR eggNOG; KOG2421; Eukaryota.
DR HOGENOM; CLU_005444_1_0_1; -.
DR InParanoid; W2S8Q2; -.
DR OrthoDB; 1005457at2759; -.
DR Proteomes; UP000030752; 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; 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; 7.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
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:UP000030752};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..145
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 461..493
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 494..515
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 532..564
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 809..1143
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 183..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1210 AA; 133702 MW; 76C2818BFD782087 CRC64;
MKFGRNLPRN QVPEWDSNYI NYKGLKKLIK NASDGTQQDG GEPDLAGFFH SLDRNLEDVD
YFYNKKFHDF SRRLKLLDDR YGFALHAAKD FDADEIQDLL AALLELRGQM RKLQWYGEVN
RRGFIKITKK LDKKIAGAHA QKKYLELKVD PAPFATNAQL LQSLARVNDW ISVLTEVSAS
TKSDDNTSIA SGSLKRTTSR PSLEISPEQI TALETYLRTD NAEKLEIFIV DAQKSLSKSC
EPAFQAFLKT LLHKSISVRG RECTAVLLRN IVFLDEPDDL NRRNCIHRLI ISICKAHTAA
EKEAAGSDAL DLEDESQDFI VPAAAPSKPF KRAVPNEDKH FKTLTREDDP SLFLVFLLDS
LQPTQRSGLM ARDNAGRTPL HHAAEFGVRA LCEIIVEHLQ LWKMFDVRQG IDGPNWHDEE
GWAPLHLSVI GGHPRTTQYL LDSENWQKAG KPATVRRSSP KSSAVLALAT KSNYIEVVRI
LVKAGVDINY QDEQGETALH VAARFGHADC ARLLLAGSDA QVVNTEMAEL TYSWTPLFIA
CVDGHFPIVE LLLDANADVD RVDSSGWTAK EHAALRGHVD IAARLDELTS TSEQDSLATS
TSTSPPISTS LNDRNSNGLG AAMPATKVTE SVKTFGHRYL TDKSMILVSL GSMDARRNVR
PVNLDRIPLA NAHSTQLDTA LSIVVSAKGA DGEPEVFDLP VQDNVSTEPI VFLSSETDKV
KIYFDLVPTY SGSRDRVVGR GVALLSSLKT HLGSSKMPLK GDLTVPIVAQ ADMEVIGTVT
FNYLIINPFK HPNMALSENK TYWKSMASTM VIGHRGLGKN FAAGRRSLQL GENTIQSFIA
AANLGASYVE FDVQLTKDHV PVIYHDFLVS ETGIDAPVHT LTLEQFLHVN DMRTPRHSRP
ASPITFDNGT KANTPYTDYR KGSRLRSMSM GGPSESVEMD ERMKHTRDFK KKGFKGNSRG
NHIQAPFTTL EEMFRKLPKE TGFNIEMKYP MLFESVDEDM DTYAVELNSF VDTVLKMVYD
LGKGRNIIFS SFHPDICLLL SFKQPNIPVL FLTDAGSCEV GDIRASSLQE AIRFASRWNL
LGVVSAAAPL VYAPRLVRVV KESGLVCVSY GVFNNDPEKV ALQVKQGIDA VIVDSVLAIR
RGLTGDGKPL ANGSSPKPSR LPQSLTGSTH SLEIPDTSEP LNMSLDDHIG NGEKSEVLVK
NDKNSGVNGA
//