ID A0A371DCA9_9APHY Unreviewed; 612 AA.
AC A0A371DCA9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 18-JUN-2025, entry version 21.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=OH76DRAFT_1403078 {ECO:0000313|EMBL:RDX50185.1};
OS Lentinus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Lentinus.
OX NCBI_TaxID=2498619 {ECO:0000313|EMBL:RDX50185.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX50185.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX50185.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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DR EMBL; KZ857401; RDX50185.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DCA9; -.
DR STRING; 139420.A0A371DCA9; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000256964; 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; 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:UP000256964};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 503..552
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 69584 MW; D8AC918BF58ED042 CRC64;
MATAAAFPRD PLATRPQSHN AGMSISPCRT TLRRASAAIK RPHSPEPMAD RDDTSSKRVK
TTIVARVAQE SPTLSVVSRV EAKKERDRKR ELEFKAKYSR AFPGFVFYFD LDTGNPEIEA
TRANLVDRVK YMKAEVHDFF SKDVTHFITL HDVDEKENKE KEAKGSALGS PIRLRGRNTM
GESLLQKART FDIKFWSVAK LHTVLDRCDT PRVTSAIGAL STRAQRPSRD RNLARLLETE
RLHGTTERDP SQRRHDYIYF SKDSYFVLVE DIRGELATIT ATEYPIQRTK DGKEKGSWPV
LHLHPLARGP FLEYDDKEER RRQKTDKAEQ DRQAERARRK ARLQHERKQH AQLVRRRSVQ
QPDLRRCASM NNLQRRATFP ATALNGYVDL DEGFGEDIES ANASGYLASA AYMAASGNSV
SITSTTGTTS AAGGLLRTLQ LPPHLKEKMQ QQVTMQRRAS ALPPPAERNK ENVMGPPTTI
PDRAKFLRKS KSTNTLKLPK RDEQSKPGYC ECCRVKFENF KDHIVGRKHR KFAMDDNNFK
HLDAVLSRVK RRTVEEVEEA NERFLAEALA VPSSTADVDE HMLPHPEDED IADDVHWDEW
VDAAKCESEI EA
//
