ID A0A4T0M782_9BASI Unreviewed; 966 AA.
AC A0A4T0M782;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 28-JAN-2026, entry version 20.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=E3Q22_02442 {ECO:0000313|EMBL:TIB78700.1};
OS Wallemia mellicola.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1708541 {ECO:0000313|EMBL:TIB78700.1, ECO:0000313|Proteomes:UP000310685};
RN [1] {ECO:0000313|EMBL:TIB78700.1, ECO:0000313|Proteomes:UP000310685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-6152 {ECO:0000313|EMBL:TIB78700.1,
RC ECO:0000313|Proteomes:UP000310685};
RA Gostincar C.;
RT "Sequencing 25 genomes of Wallemia mellicola.";
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:TIB78700.1}.
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DR EMBL; SPRC01000024; TIB78700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4T0M782; -.
DR Proteomes; UP000310685; 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 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 Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 629..678
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 742..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 944..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..360
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..583
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..699
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..755
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 966 AA; 110813 MW; AB64F297C27240A3 CRC64;
MDDQFKRPTA GKKRSLDVQQ STSKRPKVDK PEKHIEDYMK KWIKAFKNIV LHFDKPEDIA
LKNEIIFMSR ILGARVENFF SRKVTHVITS RQIPKDSSVV KSPPTEKENQ PKLNRQATPT
YGEQTVVKSN YVMFDSNNQR TQSIVDTQPK NPFLDGSQQN DLLLKAQEFK MKVWSFGKIY
NMLDFIFGNS PELKSVYKNL KSDRRARKEQ EVTLKALLTK EKLQGTTERD RSVRTQDFYY
FHRNIKYILV EDTESIYRPI LIQEYAQPRS HEEPSWPILF ACRDERNPFQ KYYQNETPFD
GKCFASRNWG MREHVNYILE AQLSRLVKQG VITMESPVQK DEEEQAEDPP EAGKAEEDDA
YVAASGNSVT ITSNTATSQA ASRHMQHRDK RVSQFDRRIT EHRPKTAHPR ASLEIPPSSS
KYIVQQSLGK ASDASPAAST SRRVLEQSAN TSLEQRRGSK SKPIVENGAT PTNAAQALLR
AREHSIHLPQ ESVVRRKSND KFEEHVNALK NRSGEVSKER RVSGSKDVQE SPPPKEILAT
KEARAAFKEV VPKRDIPKKE NTIIEKAKPE ETAKLTNEFK EPVKPSQPAK ASKEEPETSI
SKETATLYQE MEKLQAKEKH KERLSRRHEN LKPGYCEICR IKFDDFNKHV NSNKHKKQST
DPKIWSSIDL LLRYTARPLA KATEKPPSPA TKPSPPPSPK KLRRYENEEK EEVIVHNNIQ
NTVSNTQEPL LAESTFIQNS QATTAGGAPQ TTQSQESSKR SQEVVKKADC FEIAQDGVQP
PNEDDMQEFD QIEDYYRDGF YSNYDQQQLQ QQEDIELLNS QWDELQSVIN MEHDLPKAIS
HDSITREDVL NFIEGDNIAA REYNNTVQAY EDGDGYVEED QLEEMAPSMP AKETSPETAE
VQRSFDVFEG QPIYETQNKP RLNHNGGSID WLNTLTEVFK QHLSEPNDQP HSHHQSSSHS
LIEHLA
//
