ID C1G8L0_PARBD Unreviewed; 676 AA.
AC C1G8L0;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 08-OCT-2025, entry version 62.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=PADG_03596 {ECO:0000313|EMBL:EEH47512.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH47512.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH47512.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH47512.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H., Longo L.V.,
RA Ma L.J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275960; EEH47512.2; -; Genomic_DNA.
DR RefSeq; XP_010759108.1; XM_010760806.1.
DR AlphaFoldDB; C1G8L0; -.
DR FunCoup; C1G8L0; 130.
DR STRING; 502780.C1G8L0; -.
DR GeneID; 22582879; -.
DR KEGG; pbn:PADG_03596; -.
DR VEuPathDB; FungiDB:PADG_03596; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_0_0_1; -.
DR InParanoid; C1G8L0; -.
DR OMA; GMKIWAI; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000001628; 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; 2.
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:UP000001628};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 615..664
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 75667 MW; 341EF04CB6986621 CRC64;
MSTLRVPLIN VPNGTNSPHR GALASMKRTR SIHGQGENSY THPPLKKQMV EKDEYELTSR
FPQKATVVST EGKVFTRKNT NSQPTAFEKK LVAVRDKDRN NTLRGAKYDR TGGETVDTIR
QWQKHYRKVF PQFVFYFESI PEDVRNKCSR HIMALGATEE KFFSKIVTHV VTARPIPPEI
DTPNSTELST GQVPPVSQFN ADGPIQTVDP SLLDKNTENT QNNQGIGRSK KASDKRAGQL
DGDGKRDNKD VLYRARQMNM KIWALEKLQR VISTMNDGNA TSSHSHYTRS NGTVSGTGRG
RAETDLSQVL RNERLHGPAD RDSILASKEV IPFKGPFIYV HDFEEKTRPV MVREYPKVAK
RQDGAWPQFR SAALGKCPFI DEPLSKKELE KRKAVAHQAK EKEPAPTTKS KETVEVKAMR
PPERSVEKQA VQGAEGRATQ HQTREGPMPA PKRVESLLML PKKPASPRGK GLETFPGTKT
SLATYLGREP AASGVQPSNI TSAIRSQMIS STAAAPGAKA GTSKEVHELK RKVLEKGNNP
LSMNVMTSSH RMTDISGALK ASRAPVTRGA KTKAHGNLDH IDEDGMTQSE EEKAQKALQA
GKKSSNTEQP KQKKRDPKPG YCENCRDKFD DFEEHVMTRK HRKFALTLSN WTELDELLRS
LKRSRKRLLP DDEDKW
//
