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Database: UniProt
Entry: A0A9P9L8D9_FUSSL
LinkDB: A0A9P9L8D9_FUSSL
Original site: A0A9P9L8D9_FUSSL 
ID   A0A9P9L8D9_FUSSL        Unreviewed;       614 AA.
AC   A0A9P9L8D9;
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=Dfp1/Him1, central region-domain-containing protein {ECO:0000313|EMBL:KAH7275862.1};
GN   ORFNames=B0J15DRAFT_383138 {ECO:0000313|EMBL:KAH7275862.1};
OS   Fusarium solani (Filamentous fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=169388 {ECO:0000313|EMBL:KAH7275862.1, ECO:0000313|Proteomes:UP000736672};
RN   [1] {ECO:0000313|EMBL:KAH7275862.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FSSC 5 MPI-SDFR-AT-0091 {ECO:0000313|EMBL:KAH7275862.1};
RA   Mesny F., Miyauchi S., Thiergart T., Pickel B., Atanasova L., Karlsson M.,
RA   Huettel B., Barry K.W., Haridas S., Chen C., Bauer D., Andreopoulos W.,
RA   Pangilinan J., LaButti K., Riley R., Lipzen A., Clum A., Drula E.,
RA   Henrissat B., Kohler A., Grigoriev I.V., Martin F.M., Hacquard S.;
RT   "Genetic determinants of endophytism in the Arabidopsis root mycobiome.";
RL   Nat. Commun. 0:0-0(2021).
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:KAH7275862.1}.
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DR   EMBL; JAGTJS010000001; KAH7275862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9P9L8D9; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000736672; 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   Reference proteome {ECO:0000313|Proteomes:UP000736672};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          552..601
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          156..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          201..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..557
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        159..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..525
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        536..555
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   614 AA;  69628 MW;  9C29E9957E907D91 CRC64;
     MSSRRGPLTN NPNVANSPLR GASALAGYAK SRRSHATVQR EEAYGQPPPM KKQVLEYGVQ
     RSARSPTRAS RTVLVQRGVS RPPVKERASR AVSSRDIDTE KEAWKKHHRA KFPKMVFYFE
     SIPDDIRARL TKRVTYLGAR QEPFFSIAVT HVVTTRSIPP ERTEAEPDHG HDDHEPEEQP
     QTINPSLLDR NTEARRKLLF EFRNAPSRSQ HLDDPTKRTK GARNNDVLYK AREMGKKIWS
     LDKFQNMLSV LLEGETGSSY SSRSTSTRGH YSNSREPNLL QLLHHERLNG PSDRDPTAVH
     RELCYFKGPH IYIWDMDEKH KPIMVREYPK VANKADGEWP QFRSVGNGRC PFVEDHDVPD
     KDHRRQQEKA RAVKREESVP ILRPPQIPVP KPVTGKRTLT EMEDAQNRAR AVTPTELFNP
     KAIMSKPADI RQNAFTGRAG TGRLFAGEPV ASGVQPSNIT SAIRSQMVSS TSGVNGAKAG
     TSKEVHGLQR KVLQKAAPAS HDVSSRRLAE VSMDVASSRS TTMGRHTSRP ADVQEEEQKT
     ERKTQQSLKS KRDLKPGYCE NCQDKFRDFD EHILSRKHRK FAENDDNWIE LDSLLSQLKR
     MPKFSPGSDE EEGW
//
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