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Database: UniProt
Entry: A0A9W8ZVP6_9AGAR
LinkDB: A0A9W8ZVP6_9AGAR
Original site: A0A9W8ZVP6_9AGAR 
ID   A0A9W8ZVP6_9AGAR        Unreviewed;       569 AA.
AC   A0A9W8ZVP6;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 10.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=J3R30DRAFT_1684342 {ECO:0000313|EMBL:KAJ4468205.1};
OS   Lentinula aciculospora.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Omphalotaceae; Lentinula.
OX   NCBI_TaxID=153920 {ECO:0000313|EMBL:KAJ4468205.1, ECO:0000313|Proteomes:UP001150266};
RN   [1] {ECO:0000313|EMBL:KAJ4468205.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JLM2183 {ECO:0000313|EMBL:KAJ4468205.1};
RG   DOE Joint Genome Institute;
RA   Sierra-Patev S., Min B., Naranjo-Ortiz M., Looney B., Konkel Z., Slot J.C.,
RA   Sakamoto Y., Steenwyk J.L., Rokas A., Carro J., Camarero S., Ferreira P.,
RA   Molpeceres G., Ruiz-Duenas F.J., Serrano A., Henrissat B., Drula E.,
RA   Hughes K.W., Mata J.L., Ishikawa N.K., Vargas-Isla R., Ushijima S.,
RA   Smith C.A., Ahrendt S., Andreopoulos W., He G., Labutti K., Lipzen A.,
RA   Ng V., Riley R., Sandor L., Barry K., Martinez A.T., Xiao Y., Gibbons J.G.,
RA   Terashima K., Grigoriev I.V., Hibbett D.S.;
RT   "A Global Phylogenomic Analysis of the Shiitake Genus Lentinula.";
RL   Submitted (AUG-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:KAJ4468205.1}.
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DR   EMBL; JAOTPV010000037; KAJ4468205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9W8ZVP6; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP001150266; 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; SM00292; BRCT; 1.
DR   SMART; SM00586; ZnF_DBF; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP001150266};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          75..154
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          480..529
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          130..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          194..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        130..140
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..556
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   569 AA;  64390 MW;  4E85797D81C973DC CRC64;
     MATTGRNPLS QRSRSTLVST RVAKTSLGLK RPRSPGPAPE DQPSNGTLKR AKAAAEAPLD
     KHRRREQEEI EWREKYTRAF RGFKFHFSED IQDADYVKHL QRRILQLGAT VEDFFSSSIT
     HLIVKDIEQS KASSDKENRH GTKSPTKRPG FVIEVPQVYR RTVDEAKIKE WGVRKLDSVL
     SRCLQQSLIL PTSGPLPARL NPSTSTYPTD QSRSLNKLLQ SEKIHGTTER DPTQKRHDFA
     YFARGSYFVL VEDIHRELAT IVAHQYTPPK KGSTRTPWPV LHCHPQSRGP FVPFDEKEKK
     RWEKAQKIEK EDKIEAHERE LKEQKLFQER ISREREVRHR GFDLRRSVSM NNLRRRESLE
     AEAANDQYLD MGDPDSACAS GYLASGNGGY VAASGNSVSV TSTTGTTSTT STGHNLGLGP
     KLSAKLKAFA DQQVPTSLKT SRRNSIKGDM GPPAVPEGRV GVGLRRAKST NNLKLPKREE
     GTKPGYCESC RQKFEDFKQH IRSSRHRRFA KEDAHFAELD IVLATVKRKT VAEIRQERDV
     QYCPGDIAED DPFVDDPDTK MPDVDLDDV
//
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