ID   A0A0D2DNR0_9EURO        Unreviewed;       995 AA.
AC   A0A0D2DNR0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Ankyrin repeat protein nuc-2 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PV06_05178 {ECO:0000313|EMBL:KIW44145.1};
OS   Exophiala oligosperma.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW44145.1, ECO:0000313|Proteomes:UP000053342};
RN   [1] {ECO:0000313|EMBL:KIW44145.1, ECO:0000313|Proteomes:UP000053342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW44145.1,
RC   ECO:0000313|Proteomes:UP000053342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL   Submitted (JAN-2015) 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; KN847335; KIW44145.1; -; Genomic_DNA.
DR   RefSeq; XP_016264361.1; XM_016406155.1.
DR   AlphaFoldDB; A0A0D2DNR0; -.
DR   STRING; 215243.A0A0D2DNR0; -.
DR   GeneID; 27357252; -.
DR   VEuPathDB; FungiDB:PV06_05178; -.
DR   HOGENOM; CLU_002842_1_0_1; -.
DR   OrthoDB; 4907at2759; -.
DR   Proteomes; UP000053342; 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; cd14483; SPX_PHO81_NUC-2_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; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1.
DR   PANTHER; PTHR24189; MYOTROPHIN; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF03105; SPX; 2.
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:UP000053342};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          1..161
FT                   /note="SPX"
FT                   /evidence="ECO:0000259|PROSITE:PS51382"
FT   REPEAT          321..345
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          420..453
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          455..487
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          704..992
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
SQ   SEQUENCE   995 AA;  111328 MW;  2DD601780433637E CRC64;
     MKFGKQIQRQ QLDLPEYAAS FLNYKALKKL IKQLSATPTI EAQGGSATED IQAALRANKE
     VFFFRLEREI EKVNVFYLQK EAEFSLRLKT LLAKKRVIQA RIAANSRLSA SFATLVEGFQ
     QFDNDLNKLQ QFVEVNETAI SKILKKWDKT SKSRTKEIYL QRAVEIQPCF NRDVLRDLAD
     KATTARLDLE AWAEGENIQY EVSKPQDRMI GQRVGTEESD VDLQILQASA AGNVAALREW
     ISRLSAAPDA SERFTRIFLA TISEAPDESL HTFLDSGLVD IHAEDDINER NCLHEAAIYG
     KDSVLDYGLA HGVDLTRVDV YGRVPLHYAC LRGRLAMVER LLAAGPSTID LKDHDNFTPL
     IHSIVRHRVE CVRLLLASNV RIDPQSEADH IPLNLACQHE SIEVATMLLE RNARLLPDAE
     GLFPQHLVAR SSHKADLLLL LRQHGADLNQ RDKLYQWTPL FHAASEGRVE CLRALLESGA
     DPEALDEKGL TAMYYATWEG HLQCMDLLWE RTSYRRAERK ISRLGAVVPP HNQMNAMEIT
     PEEPSATEGD GIPDLSLPPP IIPLRRYGHN FLDTKTFIAI SFDSRARAIQ FFNEARYPAA
     RLTISSKTSD LIPRNLMLPI QEDSRSIYFQ VDNLSTFAVD FEIFPTFGSK VIAKSVALPD
     VFRANESSSG TCCLPLFDPR LRAVGQIQFH FQVIKPYRGT PLEITQFATY WKATSALDDH
     SGLVTGSSLS GDYLRLTVQL TRDGIPVVYP SYFVPYDKLQ VPLFQFEFDI LAGLGLAGSL
     AHIDDESDFD RTDILAWQRR LSGPIFLLRD VLSSIPPHIN LNLHILYPSS SEDLNHGVCS
     TIDINTFIDA LLTEVFNHAR ALRNASPDLS HSIVFSSFNP NVCTALNWKQ PNFPVLLCNS
     LGSLRGHGTS IKESARLAQM NNFMGLTCSA QLLRMVPALI ETIKHAGLVL VSNATEEEST
     QTTGAAQSGL FVMPEGVDGM LKPNGVLRFN ESIDM
//