ID A0A0J0XQ95_9TREE Unreviewed; 597 AA.
AC A0A0J0XQ95;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 18-JUN-2025, entry version 37.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=CC85DRAFT_244511 {ECO:0000313|EMBL:KLT43247.1};
OS Cutaneotrichosporon oleaginosum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Cutaneotrichosporon.
OX NCBI_TaxID=879819 {ECO:0000313|EMBL:KLT43247.1, ECO:0000313|Proteomes:UP000053611};
RN [1] {ECO:0000313|EMBL:KLT43247.1, ECO:0000313|Proteomes:UP000053611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBC0246 {ECO:0000313|EMBL:KLT43247.1,
RC ECO:0000313|Proteomes:UP000053611};
RG DOE Joint Genome Institute;
RA Kourist R., Kracht O., Bracharz F., Lipzen A., Nolan M., Ohm R.,
RA Grigoriev I., Sun S., Heitman J., Bruck T., Nowrousian M.;
RT "Genomics and transcriptomics of the oil-accumulating basidiomycete yeast
RT T. oleaginosus allow insights into substrate utilization and the diverse
RT evolutionary trajectories of mating systems in fungi.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ087197; KLT43247.1; -; Genomic_DNA.
DR RefSeq; XP_018279738.1; XM_018420321.1.
DR AlphaFoldDB; A0A0J0XQ95; -.
DR STRING; 879819.A0A0J0XQ95; -.
DR GeneID; 28980924; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000053611; 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 PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053611};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 398..447
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 68..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..526
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..562
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 67108 MW; 3BA07526C588D978 CRC64;
MKGLEKEQEA WVAKWQQAFP NLTFHFELGT EEGLGRKMRP RVLKLGARVD QFFSRRITHL
IVKSEQSPQK PRVAAMKRGQ SDNPFLQASP TDLRSKAEEY GIKVWTVKKL LEMIDRLDPV
NVVQRESLSH MLADEKLHGT RERDESAPRP DHYYFRPGSK YVLIEDATGK HRTIMVKEYS
AKEQDWPVLH DQFLRLTTSC ALPRSIKSVD HLHRDLRARA MALYVNHEPY NGEEPPTRSL
KRSASDRQFT VPALPEPDQL PYCKASGNSV VLTSNIASTS TNPQHPTPGG VLAQPQNGGR
RGAMQVSKRV EVLKRNLPAA RGGAVKRSDA AARQSLLGRR KSAADLPPSF SSKQFLSQAE
VVKMLQGIRK PTNLPKPTFE ERLANRELVD AGQKRKEQDT ASGYCENCRI RYTDLSVHMA
SRKHRRFALN EANFAELDKM LHCLQRPPNP MICVPSRVCR PCTERHTQAD ECSRCMDDTE
LSEDGSSESD FSIRDGMIHW YPSPWVGLSK QVGDDATAEC ESEGEEDSHS AATCTQHEHS
SQGWVEEEDV EMTEGEGEDG GEDDVRGPTT SSQLVREEDD ESTVSEFNGE GAEVVGH
//