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Database: UniProt
Entry: A0A1J9QUI9_9EURO
LinkDB: A0A1J9QUI9_9EURO
Original site: A0A1J9QUI9_9EURO 
ID   A0A1J9QUI9_9EURO        Unreviewed;       672 AA.
AC   A0A1J9QUI9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   18-JUN-2025, entry version 32.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=AJ78_00503 {ECO:0000313|EMBL:OJD19532.1};
OS   Emergomyces pasteurianus Ep9510.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emergomyces.
OX   NCBI_TaxID=1447872 {ECO:0000313|EMBL:OJD19532.1, ECO:0000313|Proteomes:UP000182235};
RN   [1] {ECO:0000313|EMBL:OJD19532.1, ECO:0000313|Proteomes:UP000182235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 9510 {ECO:0000313|EMBL:OJD19532.1,
RC   ECO:0000313|Proteomes:UP000182235};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C.A., Munoz J.F., Imamovic A., Priest M.E., Young S., Clay O.K.,
RA   McEwen J.G.;
RT   "Emmonsia species relationships and genome sequence.";
RL   Submitted (JUL-2015) 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:OJD19532.1}.
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DR   EMBL; LGRN01000008; OJD19532.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J9QUI9; -.
DR   STRING; 1447872.A0A1J9QUI9; -.
DR   VEuPathDB; FungiDB:AJ78_00503; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000182235; Unassembled WGS sequence.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IEA:TreeGrafter.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IEA:TreeGrafter.
DR   GO; GO:1901987; P:regulation of cell cycle phase transition; IEA:TreeGrafter.
DR   FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 2.
DR   Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR055116; DBF4_BRCT.
DR   InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR   InterPro; IPR051590; Replication_Regulatory_Kinase.
DR   InterPro; IPR006572; Znf_DBF.
DR   InterPro; IPR038545; Znf_DBF_sf.
DR   PANTHER; PTHR15375; ACTIVATOR OF S-PHASE KINASE-RELATED; 1.
DR   PANTHER; PTHR15375:SF26; PROTEIN CHIFFON; 1.
DR   Pfam; PF22437; DBF4_BRCT; 1.
DR   Pfam; PF08630; Dfp1_Him1_M; 1.
DR   Pfam; PF07535; zf-DBF; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182235};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          611..660
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          172..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          372..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          558..618
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..193
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        228..244
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        588..605
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   672 AA;  75470 MW;  8267E5CB1910F5E0 CRC64;
     MSSHRAPLVN VPNGTNSPHR VTITSMKRGR TFQANMYFME PPPKKQMLEK DEVDPTNKSP
     RKVAVAGTEG KVFTRKNTNS QPTAFERKLV AVRDKDRVNN SRGTKYDRTG GEPLDSIRQW
     QKHYRKAFPR FVFYFESIPE DVRNKCSRQI MALGATEEKF FSKVVTHVVT ARPIPPGVDS
     PNSTEPPTGN VPLNQRGADG SVQTVDPSLL EKNFETNHVT QGAGRSKKIA DKRPGQEGDV
     RRDNKDVLYR ARQMNMKIWA LEKLQRVIST MNDGENISHH GHYTRSNGTL SGSGKGRAEA
     DLSHVLRNER LNGPADRDSI LASKEIIPFK GPFIYIHDYE EKTRPVMVRE YPKVARRQDG
     AWPQFRSAPL GKCPFIDEPP SKRELEKRKA ATNQAKDKRP APKAKSTTTA EVKTMQPPER
     SVEKRVLQEV HGGVNQSLPR EEPMPAPKQV EGLLMLPAKP VSPRSKVFAT FPGTKASLAT
     YLAREPAASG VQPSNITSAI RSQMISSTAA APGAKAGTSK EVHELKRKVL EKGNSALSMN
     GNGNPSSHRM TDISGALKAS RAPMTRSAKS KANGNLDQID EDGTTQSEEE KVQKLQQANR
     KDRAQPKQKK RDPKPGYCEN CRDKFEDFEE HVMTRKHRKF ALTLSNWTEL DELLHSLQRT
     RKRYLPQERD NW
//
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