ID A0AAF0F8X7_9BASI Unreviewed; 932 AA.
AC A0AAF0F8X7;
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:WFD44838.1};
GN Name=DBF4 {ECO:0000313|EMBL:WFD44838.1};
GN ORFNames=MPSI1_003509 {ECO:0000313|EMBL:WFD44838.1};
OS Malassezia psittaci.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Malasseziomycetes; Malasseziales; Malasseziaceae; Malassezia.
OX NCBI_TaxID=1821823 {ECO:0000313|EMBL:WFD44838.1, ECO:0000313|Proteomes:UP001214628};
RN [1] {ECO:0000313|EMBL:WFD44838.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 14136 {ECO:0000313|EMBL:WFD44838.1};
RA Coelho M.A.;
RT "Mating type loci evolution in Malassezia.";
RL Submitted (FEB-2023) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP118380; WFD44838.1; -; Genomic_DNA.
DR AlphaFoldDB; A0AAF0F8X7; -.
DR Proteomes; UP001214628; Chromosome 6.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP001214628};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 482..531
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..644
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..774
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 932 AA; 103071 MW; 6BF053C254E2508A CRC64;
MSRSPCGSAR QPFQVKNVQR DPDPGGYVVG TPPRKRQVPA DDVHMRNLPE YASGKRSRMS
RARDLAREVE SPAATTLRID HSTRMSREER YQREFQKAQS QRQWKEAFIK AFPKLVFYLD
HVDSAHKTQF TRQITQLGGH VDAFFSRSVT HVVTTRPIPI PSEKENKEPS KRSRREPTEH
VTARANTSRL TSAAHANMPV HSDRNPLDDT TPSLPATDLL CKAQRFGMKI WRQDKLQNIL
SLLLAADLIV DQQPQDLSEM LHQEKFLGTS ERDPAAQRND YHYFGKHCYY VLVTDATNEH
RPILIQEYDR HAHEAQHKPP PWPVLYGDVE GRGLFTYIRP KDRQRLAIQD PDLKPAHSLS
LRRVASLNMT GSQLYQVPNS SHTPGTPNLM ASDNSIALAS TVASTTSTSL HSQGTLSHAA
AVPGKRLAEL TRRMHAPLDL QKEASRGAMV RRMLDLQQTE DHHPKLRRAH SMTSARDPFK
PREKKPGHCE NCRCKFEDFD EHTRSRRHRK FAMDENNFVA LDELLQRVQR EPIEHGSWDD
YAPMYQQDQS VPTSVLNEDI DLPTDWVQDT DIEPVAEFVA GSDIDGEPLN RLQDCKAHIL
PDLLDTTSTP VCNVDGTLCT PTTMTNQDDP ISGLTARSSG GQHQSQRDKC RDDAQPNSTE
YEVSTNLDTK SNPIVCTPLG DLDRDQDLST KDVRLSHFRT DVETVERANP TESQMECTDS
IATSTATGTA TGAAASIAAI TAANAPTGAA SVTRPITASA TASATSSVGA SEAAPTRAPV
NAPTTALDAA PDAATSIGSG NVSSARENLA TDTAPDIAAE LVKDAATNIP RTIETGTLPV
TTTCPAQAIS LDTAMHDSRN IPFMIISQST NMNEREASQD PGHDTGYRKT ENEHEICAKS
DQLVSNCEQS NDTELLESRL IDIAEHQHGS SI
//
