ID A0A0D2XPN8_FUSOF Unreviewed; 629 AA.
AC A0A0D2XPN8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 28-JAN-2026, entry version 43.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EnsemblFungi:FOXG_05926P0, ECO:0000313|Proteomes:UP000002489};
RN [1] {ECO:0000313|Proteomes:UP000002489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|Proteomes:UP000002489};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
RN [2] {ECO:0000313|EnsemblFungi:FOXG_05926P0}
RP IDENTIFICATION.
RC STRAIN=4287 / CBS 123668 / FGSC 9935 / NRRL 34936
RC {ECO:0000313|EnsemblFungi:FOXG_05926P0};
RG EnsemblFungi;
RL Submitted (AUG-2025) to UniProtKB.
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DR AlphaFoldDB; A0A0D2XPN8; -.
DR STRING; 426428.A0A0D2XPN8; -.
DR EnsemblFungi; FOXG_05926T0; FOXG_05926P0; FOXG_05926.
DR Proteomes; UP000002489; 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 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; 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 567..616
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 168..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..402
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 528..538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 71101 MW; 6216DD9C744FDC41 CRC64;
MSSRRGPLTN NPNVANSPLR GASALAGYAK QKRSYATVQR EETYGQPPPL KKQVLDNGVQ
RPVRSPTRST RTQVLVQRGA TRPSTKERTS RAAPTNVSRE ADTEKEAWKK HHRAKFPKMV
FYFESIPDDV RARLTKRVNY LGARQEPFFS IDVTHVVTTR TIPPERQEAH QDHNQGHHGE
HNESEEQPQT INPSLLNRNT EARRKLLSEF RNAPSRSQQL DDPLKRTRGS KNNDVLYKAR
EMGKKIWTLD KFQNMLAVLL EAETSHSTYG SRSTATRGNY GASREPNLLQ LLHNERLNGP
SDRDPSAVHR ELCYFKGPHI YVWDMDEKNK PIMVREYPKV ANKADGEWPQ FRSVGNGRCP
FVEDHDVPEK DHRRQREQEK ARLAKREEAA PVLKPPQVPM PKPVTGKRTI AEMEDGQSRA
RAATPTDIFN PARAAMSKAV DARPQNAFTS RAAAGRLFAG EPVASGVQPS NITSAIRSQM
VSSTSGINGA KAGTSKEVHG LQRKVLQKAA PASFDVSSRR LAEVSMDVAS SRSTTMGRHT
SRPAEVQEED AQKTERRTQS QPLKSKRDLK PGYCENCQDK FRDFDEHILS RKHRKFAEND
ENWTELDSLL SQIKRMPKYA SGSDEEEVW
//
