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Database: UniProt
Entry: T0LK39_COLGC
LinkDB: T0LK39_COLGC
Original site: T0LK39_COLGC 
ID   T0LK39_COLGC            Unreviewed;       640 AA.
AC   T0LK39;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   28-JAN-2026, entry version 42.
DE   SubName: Full=Dfp1/Him1 {ECO:0000313|EMBL:EQB51976.1};
GN   ORFNames=CGLO_08428 {ECO:0000313|EMBL:EQB51976.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB51976.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB51976.1}.
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DR   EMBL; AMYD01001697; EQB51976.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0LK39; -.
DR   STRING; 1237896.T0LK39; -.
DR   eggNOG; KOG4139; Eukaryota.
DR   HOGENOM; CLU_017715_0_0_1; -.
DR   OMA; GMKIWAI; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000015530; 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   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          572..621
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          160..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          350..438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          481..576
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..28
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..200
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..388
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..537
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  72523 MW;  EB34269FC1E8E28F CRC64;
     MSTRRTPLSS NPNVANSPLR SASALALAKQ RRSHANIQRE ELYGQPPPLK KQVVENTASR
     HQRSPSKIAK PSQLPQRVAR PVTKERSTHH HDDANVDKIR QWQAEYRGRF PKMVFYFDSV
     AEDQRAKLSR HAMSLGARDE RFFSSSITHV VTARPVPAQE EVHAPAHQDP EPEEQPQTIN
     PSLLDRAPDA RRRLLFDHPS RRTHTQPQDD GVRRARPTRS NDVLHKARDM GKKIWSVEKF
     QRMLQFLLEP DPHVVAQIGH KGESRSLSTK RTADEPGLMQ LLQKERLNGP SDAVTSREMI
     NFKGPYIYVY DIDEKQKPIM VREYPKVNNK YDGEWPQFRT VTDGRCPFVE EPEQAERPSR
     KPQPQQKELK EPKGDKERVT KPVDEERASL QPPEVPAPKT AIGKRTLAEM QDGQNKDKAP
     VKPVEMFNPP KVVASNPIDF RPQNAFTSRA GTARFFAGEP VASGLQPSNV TSAIRSQMIS
     STSGVNGAKA GTSKEVHGLQ RKVLQRGAPA PHDPSSRRLT EMSLDVTSTR STSVSRTTSR
     RMELIEEDAE KQTAKLVRTS SKTQAPPAKS KRDLKPGYCE NCQDKFKDFD EHILTRKHRK
     FAENTDNWLE LDELLGQLGR MPKGYGDYKH RAEEVSIDDS
//
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