ID A0A9W8DWN3_9FUNG Unreviewed; 527 AA.
AC A0A9W8DWN3;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
DE SubName: Full=Cdc7p-Dbf4p kinase complex regulatory subunit {ECO:0000313|EMBL:KAJ1927101.1};
GN Name=DBF4_1 {ECO:0000313|EMBL:KAJ1927101.1};
GN ORFNames=IWQ60_003221 {ECO:0000313|EMBL:KAJ1927101.1};
OS Tieghemiomyces parasiticus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Dimargaritomycetes; Dimargaritales; Dimargaritaceae; Tieghemiomyces.
OX NCBI_TaxID=78921 {ECO:0000313|EMBL:KAJ1927101.1, ECO:0000313|Proteomes:UP001150569};
RN [1] {ECO:0000313|EMBL:KAJ1927101.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RSA 861 {ECO:0000313|EMBL:KAJ1927101.1};
RA Reynolds N.K., Stajich J.E., Barry K., Grigoriev I.V., Crous P.,
RA Smith M.E.;
RT "Phylogenomic reconstructions and comparative analyses of Kickxellomycotina
RT fungi.";
RL Submitted (JUL-2022) to the EMBL/GenBank/DDBJ databases.
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:KAJ1927101.1}.
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DR EMBL; JANBPT010000134; KAJ1927101.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W8DWN3; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP001150569; 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; 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; 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:UP001150569};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 474..523
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 295..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 57494 MW; 00B9C571C2E0803B CRC64;
MDAQSTAYVA AHRGLQPQPL HHAYPSQPQL LPRLSAIAPV PLLSTNSAAV RWPVTYAGDT
LPTPAALYYA TSHPTEQPTG ADWSLEAYRQ AFPSYTFCFE DVAFPTVSAI SQQIQYLGGT
IEPYFSARVT HVVVPDHRSL VSTAPSLVAL AQLWNRHVWP LSYLTDRLLR YLPAPPTYHP
RPAPPGMLSH PSQLLYPLRP LQPMPPAGTD RPDARYLKQY YLLVEDTTQE HRPIALREYS
PPKEGAEPAW PDMHDVPAGR CPYIRYKDLP RQTDMLRTPP TADSPVLRSI RHMGRGRSNS
AGSTSHCPHL PPPASSTYAL TPGHTTPTAQ DSRRRPVEDT WDTLFPITKR QRLTAAPSPL
AEFILPALQD PKALPLYATP RATSRAASPH GSTATPNSGF LPTPPAVLTP PTLPGSYFTV
LSGSSTATVS PFKHPPLPLQ AATPTAVTNP VAAAVPSPVL NPPIVSASKS TARPAAKSGY
CENCRLKYDH LGDHIASDLH RKYARNARHF NDLDSLLAGC ARPRVST
//
