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Database: UniProt
Entry: A0A2G8SKD3_9APHY
LinkDB: A0A2G8SKD3_9APHY
Original site: A0A2G8SKD3_9APHY 
ID   A0A2G8SKD3_9APHY        Unreviewed;       654 AA.
AC   A0A2G8SKD3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   18-JUN-2025, entry version 25.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=GSI_03924 {ECO:0000313|EMBL:PIL34213.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL34213.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL34213.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL34213.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(2015).
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:PIL34213.1}.
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DR   EMBL; AYKW01000006; PIL34213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G8SKD3; -.
DR   STRING; 1077348.A0A2G8SKD3; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000230002; 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   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230002};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          544..593
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          336..414
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        362..375
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        376..392
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        492..505
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   654 AA;  73632 MW;  23A9669BA589A875 CRC64;
     MATAAPLPRN PLATRPQQHN TGMSISPCRT TLKKASVALK RPLSPEPADT PTDHSSKRVK
     TTLSAPVIQE SPTPAAAARM EAKKDKERRR EKERVQREEE FKVKYSRAFP SWVFYFDLDS
     GNPETASIRN HLEKRVGFMG ARIDDFFSKD ITHFITLHDV DDKENKEKET SRAGSASAAA
     AATGGGLLAS PIKLRGRALA TNTKMETLVQ KAQSFNMKIW SATKLHNILD RCDAPRVSAS
     GHLPTAAQRA SKEHNLAHLL KTERLHGTTS ERDPSQRRHD FSYFSKESYF VLVEDLKQEL
     ATISVAEYQI QKTRDGKEKG AWPVLHCHPK ARGPFLEYDD REERRRQKQE KAELDRREER
     ARRKARLVQH ERKRRAQEVR MRAQQHQHDL RRTASMTNLQ RRATYPDASL QAPGKGLVDL
     DADFPEESHV EGESVHASGY LASAAYMAAS GNSVRVASTT GTSAAGDLLR SLAVTSALKD
     KLAQQITMNR RASAAASTTT GTAPPTDREN KENVMGPPAM IPDRAKFVRK SKSMSTLKLP
     KREEGSKPGY CECCRQKFEN FREHIITRRH RKFAADDNNF KALDAILSRV RRRTVEEVAE
     EEERWLAEAR GDVDAHADED DEELLQPKLE DASDDDVRWD EWVAMDAVKV EACA
//
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