ID A0A100IAW5_ASPNG Unreviewed; 1650 AA.
AC A0A100IAW5;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Ankyrin repeat protein nuc-2 {ECO:0000313|EMBL:GAQ37241.1};
GN ORFNames=ABL_02021 {ECO:0000313|EMBL:GAQ37241.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ37241.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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:GAQ37241.1}.
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DR EMBL; BCMY01000003; GAQ37241.1; -; Genomic_DNA.
DR PaxDb; 5061-CADANGAP00003641; -.
DR VEuPathDB; FungiDB:An04g00230; -.
DR VEuPathDB; FungiDB:An04g00250; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1031201; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1177275; -.
DR VEuPathDB; FungiDB:ATCC64974_76580; -.
DR VEuPathDB; FungiDB:ATCC64974_76590; -.
DR VEuPathDB; FungiDB:M747DRAFT_30570; -.
DR VEuPathDB; FungiDB:M747DRAFT_341048; -.
DR OMA; PIGETEN; -.
DR Proteomes; UP000068243; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; PTHR22958:SF23; DEPENDENT KINASE INHIBITOR PHO81, PUTATIVE (AFU_ORTHOLOGUE AFUA_4G06020)-RELATED; 1.
DR PANTHER; PTHR22958; GLYCEROPHOSPHORYL DIESTER PHOSPHODIESTERASE; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF03009; GDPD; 1.
DR Pfam; PF03105; SPX; 1.
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; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 188..210
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 608..781
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT REPEAT 942..966
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1041..1074
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1076..1108
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1330..1639
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
FT REGION 1..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1650 AA; 178059 MW; 53BF8A918988865E CRC64;
MSSGAAAAAA GAAAATSANA AGAATTTPTE TQAETTSQST TEATPTSEAT TSQETSAEPT
TSVSTPSTTS TSSTSESTSS ATTISIPSTS STSTSSTSTT EAPSTTTSAT SHTTATPVVT
EVVTTTPSNG STGVETLTIT STDTTLPTGT AGTVGNGVTA TGSGSAAAAS STGGSGGGSS
GLSAGGTIAV AVVVPVASVA IIILAALYFW RKWKAKKAAE EERRKEVEEY GFNPNNDPSL
PPIMGGGAFE PKDDNTSSGY RGWGTTSAGR KASTNLSSSA GVGLAMSEAG SAPGYHHAAT
PSDGTIQYSE GQGTLGETEP IGVLGAAPAA AANSRNVDIH RGPSNASSAY SAANHSEASE
ESHMSATHPS GGFYDDNPYY NDMQPQYGAY GDGPYGGAPP VIRDVQARRN TRIENPAVFP
RQGNAVPSPI PSLCLLSTCP VTADADAAAT ASVKERRVRR RYQYPEISLP TSEGTWIRSI
VTLTGVLAFR SPSLGFLVDA PPSRLVQSSL VVFSRPPSIP PAELKRGADV LTPYSHSLPF
FFHFPLYHCC CTLSLFLQSC IPGPSAFAST GHQRIKGPVT SLSRLRAELA SEDVSPVCSQ
LMNFELVMKF GKQIQRRQLD LPEYAASFVN YKALKKVGLT LTYLALIKQL SATPTIPAQS
AAGVPQNVPE AQAALRANKE VFFFRLEREI EKVNAFYLQK EAEFSLRLKT LVDKKRVIQS
RAVTSSKAPA NFVALFEGFQ QFDGDLNKLQ QFVEINETAM SKILKKWDKT SKSRMKELYL
HRAVEVQPCF NRDVLRDLSD RATTARLELE AWAEGENIHF DTARPVDRAM AVQAFGTDEE
DLDLQILQSA MAGNLQTLRE WTAKLQSSPD AQARATRTFL AAINEFSDDV LAVLLESGLV
NLLAEDDINE RNCLHEAAIS GREFVFKAGL EAGVDVSRTD VYGRIPLHYA CMHGRVDMVR
DLLAAGPHTV DVMDHDNFTP LIHSIVKDQL ACAEQLLHNN ARIDPASESD HIPLNLACQH
GSLSIVQMLL QRRARLLPDA EGLYPQHMVA RASQSPQLLL LLKQYGADMN QRDKLYQWTP
LFHAASEGCV GCLRTLLELG VDASAVDEKG LSAMYYAAWE GHLECMLLLW SIRTDSRPAR
TPFDIMNGMR QPEASQNIDL QISDATETGD METADGIPDL SLPPPIIPLR RYGHNFLDKK
VFVQILFDTG ASGSICFDQA GRHPAARLTI SSKLSDLIPR TIMLPIQEDS RMISFHVDNL
ESFAVDFEIF PTFGSKVIAK TVALPTVFRA ENSSTGTCTL PLFDPRLRSI GQLQFGFQVI
KPYHGDPLEI THFATYWKAT SAIDPEHNGL VTGSSLSGDH VQLFVQLTKD RVPVLYPHFT
IGHHNIEIPI CHLTYAQFQA MGAERGINHS EMLQFLQTRA VEDLTQAHRL LASSFLSLRD
VFHHLPLSVS INLSILYPSA AEERALNMTS LADVNTFADA ILTEVFDHAR ISRDQNPDYM
RSVVFTSYNP NICIALNWKQ PNYPVLLCND LGQIRDLARD VKSLPDVDSS GRASMSIKES
ARIAQSNNLM GLICRSSLLN VVPALVETIK ELGLVLVADT SDDSEQPDQL DAMQVASPLG
VAEWAYRMPD GVNGVMKANG ILKFNDMIDM
//
