ID A0AAF0IQ00_9BASI Unreviewed; 696 AA.
AC A0AAF0IQ00;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE SubName: Full=Cdc7p-Dbf4p kinase complex regulatory subunit {ECO:0000313|EMBL:WFC95520.1};
GN Name=DBF4 {ECO:0000313|EMBL:WFC95520.1};
GN ORFNames=MBRA1_002168 {ECO:0000313|EMBL:WFC95520.1};
OS Malassezia brasiliensis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1821822 {ECO:0000313|EMBL:WFC95520.1, ECO:0000313|Proteomes:UP001216638};
RN [1] {ECO:0000313|EMBL:WFC95520.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 14135 {ECO:0000313|EMBL:WFC95520.1};
RA Coelho M.A.;
RT "Mating type loci evolution in Malassezia.";
RL Submitted (MAR-2023) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP119952; WFC95520.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAF0IQ00; -.
DR Proteomes; UP001216638; Chromosome 2.
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:UP001216638};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 473..522
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..188
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 696 AA; 75430 MW; F0DF0410F64355EF CRC64;
MSRMPRPYTR QPLRVKNGGA ELEHVPSVLG TPPRKREVPA DDVHVRNIPE YASGKRSRIR
SARDVATPYA SPAATTLRID HAARMSREER YQREHQKAAS QRQWKEAFVK AFPKLVFYLD
HVDSAQKAQF THQITQLGGT VEAFFSRSVT HVVTTRPIPV AREKENTEPR RPRPRAPASS
HAVPPAVAGG PVHSDKNPLD DTTPALPPSD LLCKAQQFGM KIWRQDKLQH ILSLLLAEDT
GVEDTRQNLS EMLHQEKLHG TTERDPQAMR TDYHYFGKHS YYVLVTDATN EHRPIVVGEF
DKTAHEAQLK PPPWPVLYGD VEGRGLFVYV KPKDRQRLAA QDTEGARPTP LSLRRAASLN
LAGALPHAPA SSHATGTPSL MASDNSIALA STVASTTSAS LHSQSTQLGS SAIADKRLAE
LTRRMHTPVD LKRGAGSGAV VRRMLSLAPN EAEAPGLRRA HSLSSARAPR KPREKRPGHC
ENCRCRFEDF DEHTRSRRHR KFAMDESNFV ALDELLQRVQ REPVDQGMWD AYTCHDALSD
DAPSAADTDA YVAHAPSDYV AGSDVDGEPM DTDALGVGAG MATDSSIEVV GERRADVTVP
PAPPTTLRAD LDAIVAEVEQ AAVVGNAQAT LVSHAAEAQV EPAAPAAGPQ GAPAALLPAA
LVTEAPVARV AGPAGEPVAG PTEEPVADPV DTHATV
//
