ID A0A9Q8ZHP5_CURCL Unreviewed; 660 AA.
AC A0A9Q8ZHP5;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=yc1106_08953 {ECO:0000313|EMBL:USP81679.1};
OS Curvularia clavata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX NCBI_TaxID=95742 {ECO:0000313|EMBL:USP81679.1, ECO:0000313|Proteomes:UP001056012};
RN [1] {ECO:0000313|EMBL:USP81679.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Yc1106 {ECO:0000313|EMBL:USP81679.1};
RA Cao Y.;
RT "Curvularia clavata genome.";
RL Submitted (DEC-2021) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP089280; USP81679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q8ZHP5; -.
DR VEuPathDB; FungiDB:yc1106_08953; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP001056012; Chromosome 7.
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 CDD; cd00027; BRCT; 1.
DR FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
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:UP001056012};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 536..585
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..349
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..522
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 73996 MW; EBE1EFFE65356765 CRC64;
MSSRRVPLAN LQNATNSPMR APAIGGKRQR SHASEQRDVT YGQPPPKKQI IEVDDAEARR
HGLVRRSGAQ PTALTRKLEA AREVKAPSKQ AAQRAAQDLE TIRQWQRHYR KLFPQFAFYF
DSVSDPQKDK LMSRARILGS REVKFFSREV THVITTRPIP VDIDNSSSAH KGTVNPAQLE
NKKSVFDAAL EKSDRGDILY KAKSLGMKIW SVDKVQRMID TMFNKETGED VSIHPTRQTT
ASQQKGRPAD LQRLLQNEKM DRDYVMASQD MIPLRGYYVY VHDMDEVTRP VMIREYQKVE
KEKGKWPQFR ASGNGKCPFV EDPHFGRRQQ EEQEARRRQA AAAPRTRAAS ALEEKNALVE
NNVARRPSAP AAITKEDTDN AKPLDPPKSL PLKRCSTADG SPPLFGSAQA SIRAMPRCIA
GEPVASGLHQ SNMTSAIRSQ MISSTAAAPR AGNSKEVNQL KRKVLEKNSM PSANTNSGHS
SVTNDVRTAL AQEHTQPMRA AKRKAQETMG RMHDDGDEER QARKAAALRR RKTVEKELKP
GYCENCREKF NDFDEHVVSR KHRKFAANDD NWVELDQLLA QLDRRLHPTY IMSESPTERI
PEEDEVTEAP LSMAASVVLS DLPKDASKAL ETAGNLNVQK GKVQLVPGPT CLDIHCCPVL
//