ID S8FNK8_FOMSC Unreviewed; 615 AA.
AC S8FNK8;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 18-JUN-2025, entry version 57.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=FOMPIDRAFT_1016810 {ECO:0000313|EMBL:EPS99884.1};
OS Fomitopsis schrenkii (Brown rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Fomitopsis.
OX NCBI_TaxID=2126942 {ECO:0000313|EMBL:EPS99884.1, ECO:0000313|Proteomes:UP000015241};
RN [1] {ECO:0000313|EMBL:EPS99884.1, ECO:0000313|Proteomes:UP000015241}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FP-58527 {ECO:0000313|Proteomes:UP000015241};
RX PubMed=22745431; DOI=10.1126/science.1221748;
RA Floudas D., Binder M., Riley R., Barry K., Blanchette R.A., Henrissat B.,
RA Martinez A.T., Otillar R., Spatafora J.W., Yadav J.S., Aerts A., Benoit I.,
RA Boyd A., Carlson A., Copeland A., Coutinho P.M., de Vries R.P.,
RA Ferreira P., Findley K., Foster B., Gaskell J., Glotzer D., Gorecki P.,
RA Heitman J., Hesse C., Hori C., Igarashi K., Jurgens J.A., Kallen N.,
RA Kersten P., Kohler A., Kuees U., Kumar T.K.A., Kuo A., LaButti K.,
RA Larrondo L.F., Lindquist E., Ling A., Lombard V., Lucas S., Lundell T.,
RA Martin R., McLaughlin D.J., Morgenstern I., Morin E., Murat C., Nagy L.G.,
RA Nolan M., Ohm R.A., Patyshakuliyeva A., Rokas A., Ruiz-Duenas F.J.,
RA Sabat G., Salamov A., Samejima M., Schmutz J., Slot J.C., St John F.,
RA Stenlid J., Sun H., Sun S., Syed K., Tsang A., Wiebenga A., Young D.,
RA Pisabarro A., Eastwood D.C., Martin F., Cullen D., Grigoriev I.V.,
RA Hibbett D.S.;
RT "The Paleozoic origin of enzymatic lignin decomposition reconstructed from
RT 31 fungal genomes.";
RL Science 336:1715-1719(2012).
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; KE504153; EPS99884.1; -; Genomic_DNA.
DR AlphaFoldDB; S8FNK8; -.
DR FunCoup; S8FNK8; 89.
DR STRING; 743788.S8FNK8; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_1_0_1; -.
DR InParanoid; S8FNK8; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000015241; 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; 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:UP000015241};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 509..558
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 565..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..588
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 615 AA; 69570 MW; A7D7901E43BF4741 CRC64;
MATITRNPLS MRPHSQHHAI ALSPYQGTAV PRRASGSGKR ARSPEPTKDE GPSQSVKRLK
AVAAPLPPAL TTREDPREEA RRDKERKRAE REEEFRVKYT RAFPSWTFHF DLDTMSPDVA
TLKDNLERRV RHMGARVEDF FSRDITHLIT LDAEGSEKEN STKPSTSATT NLLLSPIKLK
GRATGDAPTT ASERIAKKAL AFGIKVWSPV KLESVLDRCH APAAYNARPP ARGPAAASRP
LTRLLEEERT YGTTTERDPT QKRHGFTYFS KGTYFVLVED MRQELATIAA GEYPIRRGRD
GQERPTWPVL YCHPLARGPF MPYDEREERR RERADRIDRE REQERARRKA RLREEERRRQ
AQAQAQAKQH DLRRSVSMHN LHRRASLGDV GFALDGFVDL DADFGDGDTQ SANASGYLAS
GAYMAASGNS VGVTSTTGTT SAAGNTLRNL QLPPGLRGRV QQQVVTSRRV VSGAEGKEKM
GPPLNIPEKQ HILRKSRSTN TLRLPKREEG VKPGYCESCR VKFEDFKHHI NGRRHRKFAV
DDSNFTALDA ILSRVRRRTR DEAEEERHRW AARCADAEDD EDEDEDEEPR MLPTTIVGSD
DDVRWGEWVE DGEEL
//