ID   A0A4S2MQV9_9PEZI        Unreviewed;       625 AA.
AC   A0A4S2MQV9;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   18-JUN-2025, entry version 19.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=EX30DRAFT_365086 {ECO:0000313|EMBL:TGZ79535.1};
OS   Ascodesmis nigricans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC   Pezizales; Ascodesmidaceae; Ascodesmis.
OX   NCBI_TaxID=341454 {ECO:0000313|EMBL:TGZ79535.1, ECO:0000313|Proteomes:UP000298138};
RN   [1] {ECO:0000313|EMBL:TGZ79535.1, ECO:0000313|Proteomes:UP000298138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 389.68 {ECO:0000313|EMBL:TGZ79535.1,
RC   ECO:0000313|Proteomes:UP000298138};
RG   DOE Joint Genome Institute;
RA   Lutkenhaus R., Traeger S., Breuer J., Kuo A., Lipzen A., Pangilinan J.,
RA   Dilworth D., Sandor L., Poggeler S., Barry K., Grigoriev I.V.,
RA   Nowrousian M.;
RT   "Comparative genomics and transcriptomics to analyze fruiting body
RT   development in filamentous ascomycetes.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; ML220130; TGZ79535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4S2MQV9; -.
DR   FunCoup; A0A4S2MQV9; 132.
DR   STRING; 341454.A0A4S2MQV9; -.
DR   InParanoid; A0A4S2MQV9; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000298138; 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; 6.10.250.3410; DBF zinc finger; 1.
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; PF08630; Dfp1_Him1_M; 1.
DR   Pfam; PF07535; zf-DBF; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000298138};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          563..612
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..100
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          372..403
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        17..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..54
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  71360 MW;  E6050048E51F5606 CRC64;
     MAQVSIPPSP AAMSRRTPLS NIPNAINSTF GVTGTGAKRS RSQSTLTRDT SYGQPPSKKA
     IIEAPPVKRS NVENAVTTTP RRVPVPKAEY KRPTKARSKP AEVETTITDI TQWKVQYGGM
     FPKYKFYIEH YHPYVVKKAM EYIMKSGGVC TNVFEEATHL LTARHPLARS TKLPRTGPAS
     SLWPGFCQAT MEKYIRAGKD HYTRAQNRFM KIWNLDKLER VCGALQDHPN GKLDIAADVQ
     RLYPIDRIER KAHELLDALD GQLRIRPTQR PGVEPRKLQR PQKEPITDLT NILRYEKLHG
     PTDRDPRAPV KEMYYFKGYY LYVHDAQEHH RPVLVKEFPK VSKRENGTWP QFRSSGRFRC
     PFVEDTPSMR ERDREREKYE QYEQEMEQVR KEENARLAAE ERRIRLRASG VELNPSRSAQ
     DVRRAPNAEP VITQQAKKSV RRQENSIAFT SINPPKNSRL THEPVASGVQ PSNITSAIRS
     QVVSSHRDIP GQRAGISKEI YGLQRKVAGN ALISHTTSLR KSQAVPERNQ VEPRPSKQAL
     SARATEVSRT SSRKVVEKTP VEKVPKPGYC ENCRDKYDDF DTHILGRKHR KFATDASNWE
     ELDELLSQLH RPLKSGGYCH PLQSK
//