ID A0A165FFT5_9BASI Unreviewed; 633 AA.
AC A0A165FFT5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 32.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=CALCODRAFT_497180 {ECO:0000313|EMBL:KZT56684.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT56684.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT56684.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT56684.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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DR EMBL; KV423974; KZT56684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165FFT5; -.
DR FunCoup; A0A165FFT5; 83.
DR STRING; 1353952.A0A165FFT5; -.
DR InParanoid; A0A165FFT5; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000076842; 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; IPR001357; BRCT_dom.
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; PF00533; BRCT; 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:UP000076842};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 521..570
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 60..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 207..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..89
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..224
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 70329 MW; A00EFA4846F7E35F CRC64;
MAAVAVTPRP PSLLPRPVWT HDPHLSASLT AAAHLMTPSH LPRALEHAAD VFTTSAPARM
AARVKRTRED MRSDAAQPPA PKRPCPSPSK RPIKKQLSKT DKEKIERREK REKFEAQERD
FREKYSAAFP KWTFHFDSLD TATSSELTQR VMQLGARVDT FFSKKVSHVI SARPIPPDVK
ASRGALGKEG TPFATAMKRE GDKENVAPRL SQQQRMSQTQ SSQQWKSAGR PALAPLVRKD
GNLLFEDSAL IKNDLLTKAL HFGMKVWSVE KLTSVLDRIQ LPASPDLQTP NLSHLLADER
LHGTRERDPT ALRPDYTYFQ RGSYFVLVED MSGEHCPIMS KQYDRPNKGD RPPWPCLYAD
KNASGPFSPG YEESTSEEKP IANISRDVST ASAVAAAPAA ALMKAKRPAD LRKVLSMNNV
KRAAAARGTP DASQAVQAPH DRNAYIAASG NSVSVTSAIA TSARSGTGAV LPGTLAHTAN
KQLQERLRQQ VLTNRLAAAN MGPGLRKSKS TNTLKLPMRE ETKKPGYCEN CRIKFADFSQ
HVKSKKHRAF ATTQENFLQL DEVLERLRRP LASEKLDIDE LIAKEDDDEY DADSNMQDEE
LEISDSFDRE AEQFAIEEQI AMRWRALSAA TVI
//
