ID A0A4T0IDR9_WALIC Unreviewed; 821 AA.
AC A0A4T0IDR9;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 08-OCT-2025, entry version 21.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
DE Flags: Fragment;
GN ORFNames=E3P86_04012 {ECO:0000313|EMBL:TIB27768.1};
OS Wallemia ichthyophaga.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=245174 {ECO:0000313|EMBL:TIB27768.1, ECO:0000313|Proteomes:UP000310689};
RN [1] {ECO:0000313|EMBL:TIB27768.1, ECO:0000313|Proteomes:UP000310689}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-6200 {ECO:0000313|EMBL:TIB27768.1,
RC ECO:0000313|Proteomes:UP000310689};
RA Gostincar C.;
RT "Sequencing 23 genomes of Wallemia ichthyophaga.";
RL Submitted (MAR-2019) 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:TIB27768.1}.
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DR EMBL; SPOI01000404; TIB27768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0IDR9; -.
DR Proteomes; UP000310689; 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 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 719..768
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..684
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..434
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..471
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..518
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..784
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 821
FT /evidence="ECO:0000313|EMBL:TIB27768.1"
SQ SEQUENCE 821 AA; 92344 MW; 84F2D67B3F02AC35 CRC64;
MDDQFKRPIN AKKRVLEPTA SNNREHEPER ERTKRVKVDR QGDQDYIRKW TRAFRNIVLY
FDKPPENGIK GDIVQMAVKL GASVDDFFSN KVTHVITSRE IPKAATDSTS STKENKPKVL
SRQATPTYGD EAVTGSAAYT VVDPLNHTQH SIVDTQPKNP FLGPIQQADD LLLRAQEFKI
KVWSYPKIYN ILRHLLANDT GGNPLSHSQT QAHAHVHSHS HSHATAREQS LKAMLKREKL
QGTTERDRSV RQIDQYYFPR NVRYVLVEDA SETHRPVLIQ EYAVPRANEE AAWPILFACR
DERNPFTKYY QNEAPFDGRV YASKGWGMQE HVNYVVEAQL ARLCKQGVIT MVGSEQHGEQ
EMEMEQDMEV DQHHHQAQLQ MQMQLQEDVD KNQNLIQSHS HSRQKDKAED AYAAASGNSV
TITSTNATSQ AQAARVPGQR DKRVLQLDKR TTEHRPKTAQ ANAQARANAN ARSREADANA
IANETAVAST STSTSASASA SANTTLSTPT TTNTTTRTTP RRVSDHSHAP AHTSFAQLLQ
HRRSSRGKAV VEDSSKPTNA AQALLRAREH NKFEESVAAL KNRGAHDGVD DNFDSANYSA
NESVISSAPT PPPKDILATK EARAAFKEVL PRRKVPTTKP PKEHTQSGKT TQTAQTNDLI
APKTQYTQQK ETAQSKEENK QVDKQVDAQV SQETVDMYNH MEKLQAKQKH KEKLSKRQEN
FKPGYCEICR VKFEDFDRHI NTSTHQKKAT DPKIWSSLDS LLTQTARPPA KDLPPIPVSP
PSPPKKVNML KRLEKNEDDV AHEELEEMIL NPHVPVNVES T
//
