ID A0A5M9JAG9_MONFR Unreviewed; 643 AA.
AC A0A5M9JAG9;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=EYC84_009432 {ECO:0000313|EMBL:KAA8565580.1};
OS Monilinia fructicola (Brown rot fungus) (Ciboria fructicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Monilinia.
OX NCBI_TaxID=38448 {ECO:0000313|EMBL:KAA8565580.1, ECO:0000313|Proteomes:UP000322873};
RN [1] {ECO:0000313|EMBL:KAA8565580.1, ECO:0000313|Proteomes:UP000322873}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mfrc123 {ECO:0000313|EMBL:KAA8565580.1,
RC ECO:0000313|Proteomes:UP000322873};
RA De Miccolis Angelini R.M., Landi L., Abate D., Pollastro S., Romanazzi G.,
RA Faretra F.;
RT "Genome Sequence of the Brown Rot Fungal Pathogen Monilinia fructicola.";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAA8565580.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; VICG01000013; KAA8565580.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5M9JAG9; -.
DR VEuPathDB; FungiDB:MFRU_006g01600; -.
DR Proteomes; UP000322873; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000322873};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 592..641
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 21..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 549..588
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 23..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 72979 MW; 01AF8FE477F662E3 CRC64;
MSTRRQPLST ISNVANSPYR AVASTTTKQK RSYANIQRED AYGQPPPAKK QMLDAHHQTL
RTPPRQSASQ ASVEGRVFTR KSNSQQSNFE RKCVAVRDRG SQQQITKADK VPEENLESIR
QWQKHYRKSF PKFVFYFESI PEEVRLKYTK QVLALGARDE KFFSNEVTHV VTTRSIPPES
LFNSSTTAEL HSQHGTINPS LLDRSSEATE SRDPRSKFTF EAPVPRRLAG HDGDARRQQA
RTSDVLYKAR ELGMKIWALE KLQRMMTTMF DTDTGYQTAH GHNTRSHSVQ GNTASRVREA
DLSQLLRNER INGPSDRDLS VTTKEMTIFR GPYIYIHDID EKQKPIMVRE YSKVAHKEEG
DWPQFRSVAN GKCPFVEEPE YSRRELEKEK ELIRIQRQKE KEREREKAAV PRTRSAAAVE
AAKMHPPKAM SKRALSQLED GANRSATVST KQANPFDTDR IVLVSVDYIG GEPVASGVQP
SNITSAIRSQ MISSTAAQPG LKAGTSKEVH GLQRKVLEKT NGGPASHGAH RLTDITATVR
DDTNTRPAKR EAQKKLGVIE EDVVSAEKEE ASRKVEAARR TKAVQQRKLE KRDPKPGYCE
NCADKFEDFD EHVLSRKHRR FAEKAENWRE LDALLSQLVR PLV
//
