ID A0A9W8A960_9FUNG Unreviewed; 527 AA.
AC A0A9W8A960;
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:KAJ1926243.1};
GN Name=DBF4_2 {ECO:0000313|EMBL:KAJ1926243.1};
GN ORFNames=IWQ60_003966 {ECO:0000313|EMBL:KAJ1926243.1};
OS Tieghemiomyces parasiticus.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Dimargaritomycetes; Dimargaritales; Dimargaritaceae; Tieghemiomyces.
OX NCBI_TaxID=78921 {ECO:0000313|EMBL:KAJ1926243.1, ECO:0000313|Proteomes:UP001150569};
RN [1] {ECO:0000313|EMBL:KAJ1926243.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=RSA 861 {ECO:0000313|EMBL:KAJ1926243.1};
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:KAJ1926243.1}.
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DR EMBL; JANBPT010000180; KAJ1926243.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9W8A960; -.
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..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..328
FT /note="Low complexity"
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; 57515 MW; 1D61DB9A3D048573 CRC64;
MDAQSTAYVA AHRGLQPQPL HHAYPSQPQL LPRLSAIAPV PLLSTNNAAV RWPVTYAGDT
LPTPAALYYS TSHPTEQPTG ADWSLEAYRQ AFPSYTFCFE DIAFPTVSAI SQQIQYLGGT
IEPYFSARVT HVVVSDHRSL VSAAPSLVAL AQLWNRHVWP LSYLTDRLLR YLPAPPTYHP
RPAPPGMLSH PSQLLYPLRP LQPMPPAGTD RPDARYLKQY YLLVEDTTQE HRPIALREYS
PPKEGAEPAW PDMHDVPAGR CPYIRYKDLP RQTDLLRTPP TADSPVLRSI RHMGRGRSNS
AGSTSHCSHL LPPASSTYTL TPGHTTPTAQ DSRRRPVEDT WDTLFPITKR QRVTAAPSPL
AEFILPALQD PKALPLYATP RATSRAASPH GSTATPNSGF LPTPPAVLTP PTLPGSYFTV
LSGSSTATVS PFKHPPLPLQ AATPTAVANP VATAVPSPVL NPPIVSASKS TARPAAKSGY
CENCRLKYDH LGDHIASDLH RKYARNARHF NDLDSLLAGC ARPRVST
//
