ID J4H1V0_9APHY Unreviewed; 565 AA.
AC J4H1V0;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 18-JUN-2025, entry version 48.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=FIBRA_02439 {ECO:0000313|EMBL:CCM00409.1};
OS Fibroporia radiculosa.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fibroporiaceae; Fibroporia.
OX NCBI_TaxID=599839 {ECO:0000313|EMBL:CCM00409.1, ECO:0000313|Proteomes:UP000006352};
RN [1] {ECO:0000313|EMBL:CCM00409.1, ECO:0000313|Proteomes:UP000006352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFFH 294 {ECO:0000313|EMBL:CCM00409.1,
RC ECO:0000313|Proteomes:UP000006352};
RX PubMed=22247176; DOI=10.1128/AEM.06745-11;
RA Tang J.D., Perkins A.D., Sonstegard T.S., Schroeder S.G., Burgess S.C.,
RA Diehl S.V.;
RT "Short-read sequencing for genomic analysis of the brown rot fungus
RT Fibroporia radiculosa.";
RL Appl. Environ. Microbiol. 78:2272-2281(2012).
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DR EMBL; HE796981; CCM00409.1; -; Genomic_DNA.
DR RefSeq; XP_012179692.1; XM_012324302.1.
DR AlphaFoldDB; J4H1V0; -.
DR FunCoup; J4H1V0; 78.
DR STRING; 599839.J4H1V0; -.
DR GeneID; 24095320; -.
DR HOGENOM; CLU_017715_1_0_1; -.
DR InParanoid; J4H1V0; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000006352; 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 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:UP000006352};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 469..518
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 64261 MW; C80E8BB39BDF0543 CRC64;
MVRKAAASKR GRSPDPARED TISHDTKRLR SSAESPAPTR DETREEKRER RRVGREQEFK
VKYLNAFPNW IFYFDLDTLN PDVVAMREGL ERRVSHTGAR VEDFFSKDIT HLITLEAEDA
DKENVSRPSQ SANPGGLLGS PIRLRGRTGN DAASASMDNL ARKAHAFGIK VWSAGKLASV
LDRCHVPVAF SATPTSRPIS APKERSLTRL LEDERIHGTT SERDPTQKRH DYKYFSKGVY
FVLVEDMRQE LATIAAVEFP LYKGRDGKER PSWPILYCHP RARGPFIPYD EKEERRCEKM
GKLDRERARD LARRKARLRE EERKRRTQAQ IQAKQQDLRR SVSLNNLHRR TMYPDPGLVD
LDADIGEMDS LNASGYLASG AYMAASGNSV GITSTTGTTS TAGRPSRNIQ LPVGLRGRIQ
QQVVTSRKVA PAGEDKANRM GPPATIPGRQ NILRKSKSTN TLRLPKREEG VKPGYCESCR
VKFEDFSQHI NGRRHRKFAI DDSNFVSLDY VLERVRRRTL SEVEEERRLW YSKIAQSKGQ
KNAEDAAFSP HDDVRWDEWV DGSEM
//