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Database: UniProt
Entry: A0A2I2GNB1_9EURO
LinkDB: A0A2I2GNB1_9EURO
Original site: A0A2I2GNB1_9EURO 
ID   A0A2I2GNB1_9EURO        Unreviewed;      1124 AA.
AC   A0A2I2GNB1;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=DENN-domain-containing protein {ECO:0000313|EMBL:PLB54364.1};
GN   ORFNames=P170DRAFT_442472 {ECO:0000313|EMBL:PLB54364.1};
OS   Aspergillus steynii IBT 23096.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1392250 {ECO:0000313|EMBL:PLB54364.1, ECO:0000313|Proteomes:UP000234275};
RN   [1] {ECO:0000313|EMBL:PLB54364.1, ECO:0000313|Proteomes:UP000234275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 23096 {ECO:0000313|EMBL:PLB54364.1,
RC   ECO:0000313|Proteomes:UP000234275};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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:PLB54364.1}.
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DR   EMBL; MSFO01000001; PLB54364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2GNB1; -.
DR   VEuPathDB; FungiDB:P170DRAFT_442472; -.
DR   OrthoDB; 1331806at2759; -.
DR   Proteomes; UP000234275; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.11500; -; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001194; cDENN_dom.
DR   InterPro; IPR005112; dDENN_dom.
DR   InterPro; IPR043153; DENN_C.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   InterPro; IPR005113; uDENN_dom.
DR   PANTHER; PTHR12296:SF21; DENN DOMAIN-CONTAINING PROTEIN 3; 1.
DR   PANTHER; PTHR12296; DENN DOMAIN-CONTAINING PROTEIN 4; 1.
DR   Pfam; PF03455; dDENN; 1.
DR   Pfam; PF02141; DENN; 1.
DR   Pfam; PF03456; uDENN; 1.
DR   SMART; SM00801; dDENN; 1.
DR   SMART; SM00799; DENN; 1.
DR   SMART; SM00800; uDENN; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   PROSITE; PS50211; DENN; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000234275};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          237..1011
FT                   /note="UDENN"
FT                   /evidence="ECO:0000259|PROSITE:PS50211"
FT   DOMAIN          878..925
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   REGION          64..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          730..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..759
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..775
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1124 AA;  124678 MW;  109F0BF72E9E91AB CRC64;
     MPFSSSSSSS TPEVSTTPLA DYFWIAGVDG TEILDTFQRL GDEYRANNAT SPGPAVTDTI
     EEDADAEEAH DPRLDGLSRP NSMAGGRNSF QRFSMRSGDP DANENGSSSN RSSMTIKGAQ
     SPRGSSFLED FDFDKALLKF ASERDSFLSD LSHTAGAITP QSQARPRSRL RTQKIISEES
     PSQPSSLLRS GIGSVRRHMA FRDMNSMKRQ PSVARQASIR TSRRLSNYNS VIPVPQPLEI
     SPSMHPLKRR FEPVLLDRYP TRNMSDELKQ RGNFPDYVPM FAFPNDINIV SSDQRPRSTW
     HGFAMTTDNG SRLHAICVII WIPLNQRAAE ELEKRCEEWR KDNMTDEERE LAASLGERLA
     SERAKLSRLL AQLPTVPSGS ESREQLEDEI SAVEEKIGLM TDLLRPVRHG AASKIEGLTD
     GDTGFWIPRA YGILGREENM TSFWKEWLKA VIVPMTDGSI QRVPPSSPRM GIWQPLERYV
     MNLCTEAFSP NTSKTQVELA VRELRLFARK EASNELPGAR NTDIYALFRT LSLSNIVILL
     EYALTESRII FLSSHTSMLY LATKALVDLL FPIPWSGVLI PVLPARLVQA IEAPCPYIVG
     IERRYEKVEL PSDDFVLVDL DADLIESTIQ PTPLPRHQRR KLLSLLQLAA PHHGRFGVPT
     GPPAYAIETF PFDAFSSENS SIFNSRAQST QLAKYVSLNS SAFGQSSVPP SSYQPLVFNA
     YLHARYEQVP SRGYSSKGSD RPGTGSTSKT GSPPSPRDIS PTSGHFPPPP PTPNSRNDSG
     LALQASLREK RSGHFDAASR RSSSFGMEMR QGVPRRPSAP FLGHAPNLSV TTLNTDYNSG
     STYAPSVYAQ STVAASTIVP QASNQPIHNS EGTCWVEGHC LRLQPCDEKA VCAICDERAE
     EGMYRCTACK TLVHNRCALQ ICLVCPAAFH PEQVRAAFVR LFASLFYTYK KYLQPASGDK
     KKAGLTYSFN MDAFMKSLPG EHAEYISILQ QTQGFNEFIS EREHVNPKSR DPRMALFDEI
     VLSKRNRGRS SIFSSRSMTD FLSDTSNHLW RTASATSFGP GSRGQQNLSG DYTRVVTRAP
     AKLDTSLMKE PRMIHGAPRV SKTANNARRK PLPKLMNGLA ISPP
//
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