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Database: UniProt
Entry: A0A395S4D4_FUSSP
LinkDB: A0A395S4D4_FUSSP
Original site: A0A395S4D4_FUSSP 
ID   A0A395S4D4_FUSSP        Unreviewed;       629 AA.
AC   A0A395S4D4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   18-JUN-2025, entry version 23.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=FSPOR_6354 {ECO:0000313|EMBL:RGP66972.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP66972.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP66972.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP66972.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP66972.1}.
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DR   EMBL; PXOF01000088; RGP66972.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395S4D4; -.
DR   STRING; 5514.A0A395S4D4; -.
DR   Proteomes; UP000266152; 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; 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:UP000266152};
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          29..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          359..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..74
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        163..185
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..390
FT                   /note="Basic and acidic 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;  71548 MW;  5659F24B96B27E51 CRC64;
     MSSRRGPLTN NPNVANSPLR GVSALAGYAK QKRSYATVQR EETYGQPPPL KKQVLDNGVQ
     RPVRSPSRST RTQVLVQRGT TRPSTKERSS RTAPTNVARD MDNEKEAWKR HHRAKFPKMV
     FYFESIPDEV RARLTKRVAY LGARQEPFFS ISVTHVVTTR SIPPERPEGH QEQEQDHHDE
     HHETEEQPQT INPSLLNRNT EARRKLLSEF RNAPARTQQI DDPTKRTRGT RNSDVLHKAR
     EMGKKIWSLE KFQNMLSVLL EVETSHASHN SRSASTRSHY GNPREANLLQ LLHNERVNGP
     SDRDPTAVHR ELTYFKGPHI YVWDMDEKNK PIMVREYPKV ANKSDGEWPQ FRSVGNGRCP
     FVEDHDVPEK DHRRQREQEK ARQAKREEAA HAIKPPQVPM PKPVTGKRTI AEMEDGQNRI
     RAVTPTDVFN TAKTVIPKQA DVRPQNAFTS RAAAGRLFAG EPVASGVQPS NITSAIRSQM
     ISSTSGVNGA KAGTSKEVHG LQRKVLQKAA PASFDVSSRR LAEVSMDVAS SRSTTMGRHT
     SRPAEVQEEE AQKTERRTQS QPLKSKKDLK PGYCENCQDK FRDFDEHILS RKHRKFAEND
     DNWIELDSLL SQIKRMPKYA PGSDEEEAW
//
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