ID A0A9P3PJS1_LYOSH Unreviewed; 619 AA.
AC A0A9P3PJS1;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Zinc finger in DBF-like proteins {ECO:0000313|EMBL:GLB37228.1};
GN Name=DBF4 {ECO:0000313|EMBL:GLB37228.1};
GN ORFNames=LshimejAT787_0402790 {ECO:0000313|EMBL:GLB37228.1};
OS Lyophyllum shimeji (Hon-shimeji) (Tricholoma shimeji).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae; Lyophyllum.
OX NCBI_TaxID=47721 {ECO:0000313|EMBL:GLB37228.1, ECO:0000313|Proteomes:UP001063166};
RN [1] {ECO:0000313|EMBL:GLB37228.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AT787 {ECO:0000313|EMBL:GLB37228.1};
RA Kobayashi Y., Shibata T., Hirakawa H., Shigenobu S., Nishiyama T.,
RA Yamada A., Hasebe M., Kawaguchi M.;
RT "The genome of Lyophyllum shimeji provides insight into the initial
RT evolution of ectomycorrhizal fungal genome.";
RL Submitted (JUL-2022) 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:GLB37228.1}.
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DR EMBL; BRPK01000004; GLB37228.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P3PJS1; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP001063166; 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; IPR001357; BRCT_dom.
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; PF00533; 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:UP001063166};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 496..545
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 68891 MW; 8DA73118C196DDAF CRC64;
MATLNRRPLA TRSLQASSTL SPLKSHRTVS ASKRPRSPEP PVDPSTSQPT TKRVKALDPS
PASKARDQLR ERKHLEREQQ KAEFKEKYTR AFPAFTFYFD ELNIGSVALD AYEERIEQLG
AKIVKFLDKT VTHFISNRPD AAVAVPVDKE NALKPGNTLQ SPIKLKGRTA EETECGNAVA
PSTTLSYKIW NTAKLESVLS RLLDSPVGST SIGPAAARKQ VPSLARLLKS EQIHGTTERD
PTQRRHDFKY FNRGSKFVLV EDLRQEIATI IAYEYAAPKT RDGVTARPPW PVLHCHPQAR
GPFIAFDEKE KRRWEKLQKA EGEQKAERKE YSSRIRQAEL VKRKAQANLR ARRAGDLRRC
VSMNNLHRTA TFPDPPDDEN LLGADGDGEN LDSAIASGFL ASGTAGYMAA SGNSVGITST
TGTTSTTGYT TRALQLPSTL SGRMKHVVTS RKFPSAAADK ENKAPLMGPP ASIPERQPLL
RKSRSTNTLK LPKREEGCKP GYCESCRTKF DDFRAHVAGR KHQRFATNDA NFLQLDCVLA
RVHRRTKSEV LEARMKSEER RKNYCSNAHE GRGSPVDEPE FSSLVHHAIE YDAYEDIDML
GGSDRTSSTV ALSTSHTYH
//