ID   A0A9Q9AEX0_9PEZI        Unreviewed;       667 AA.
AC   A0A9Q9AEX0;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   SubName: Full=Zinc finger, DBF-type, regulatory subunit Dfp1/Him1, central region {ECO:0000313|EMBL:USW48184.1};
GN   ORFNames=Slin15195_G015030 {ECO:0000313|EMBL:USW48184.1};
OS   Septoria linicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Septoria.
OX   NCBI_TaxID=215465 {ECO:0000313|EMBL:USW48184.1, ECO:0000313|Proteomes:UP001056384};
RN   [1] {ECO:0000313|EMBL:USW48184.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SE15195 {ECO:0000313|EMBL:USW48184.1};
RA   Lapalu N., Simon A., Demenou B., Paumier D., Guillot M.-P., Gout L.,
RA   Valade R.;
RT   "Complete genome sequences of two strains of the flax pathogen Septoria
RT   linicola.";
RL   Submitted (JUN-2022) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP099418; USW48184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9Q9AEX0; -.
DR   Proteomes; UP001056384; Chromosome 1.
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   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP001056384};
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..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..120
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..438
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   667 AA;  74823 MW;  4EA020B51ADB8CBD CRC64;
     MASRRVALAD VPSAANSPMR NTNLINGKRT RAQAGEQRDA IFGQPPAKKH ILEVPTANDE
     NVDPRRRNGM TIVAVDKLEE PFLKRASHGP PTAFEKKLAS VREKRPTLQQ QVHTQQVSQR
     QESRAQRQHA ENLESIRQWQ KHYRRQFPQF VFYFDSVADD VRHKAARKIH ALGAREDKFF
     SKAVTHVVTT RTIPAEGSST STDNDEQEAA RQRSTQQSVA ALDQRRTTNA LDAHIQRRSQ
     LAFTGAQAGT DARRPQAYNA YSTDILSKAR SLNTKIWALE KLHRVLDTIL DTETADQAAE
     PRGAATRVSS RPAPNADLEQ LLRHEKVKGP ADRDMTVATQ DMVTLRGCYI YIHDMDEKTK
     PVMVRDYLRP QAKEQGKWPQ FRLSAPGRCP FVEDPAHTKK LAQQDREIQE AREDLQRKTR
     AKASSHSIPP LQGTNPYRET TLRRSPRKLT QSNLSATSQA GSFQYQGSTM RQPSGETLPP
     LFNSTQANLR GMPRMVRGEP VASGVQPSNV TSAIRSQAVS SAAISSTTGL SRRVGDSREM
     SMLKRKVLGS NTVPTSYTND MRAAINEDAV PPPRAAKRKA QETLGVLHET EVDADAQASA
     HIVKKKKIVE KEAKPGYCEN CRDKFDDFDD HIASRKHRKF ATSAENWHDL DELLAVLKRP
     HKKKQPL
//