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Database: UniProt
Entry: A0A8H7F845_AGABI
LinkDB: A0A8H7F845_AGABI
Original site: A0A8H7F845_AGABI 
ID   A0A8H7F845_AGABI        Unreviewed;       545 AA.
AC   A0A8H7F845;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 16.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=Agabi119p4_1848 {ECO:0000313|EMBL:KAF7782472.1};
OS   Agaricus bisporus var. burnettii.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Agaricus.
OX   NCBI_TaxID=192524 {ECO:0000313|EMBL:KAF7782472.1, ECO:0000313|Proteomes:UP000629468};
RN   [1] {ECO:0000313|EMBL:KAF7782472.1, ECO:0000313|Proteomes:UP000629468}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H119_p4 {ECO:0000313|EMBL:KAF7782472.1,
RC   ECO:0000313|Proteomes:UP000629468};
RX   PubMed=32887908;
RA   Sonnenberg A.S.M., Sedaghat-Telgerd N., Lavrijssen B., Ohm R.A.,
RA   Hendrickx P.M., Scholtmeijer K., Baars J.J.P., van Peer A.;
RT   "Telomere-to-telomere assembled and centromere annotated genomes of the two
RT   main subspecies of the button mushroom Agaricus bisporus reveal especially
RT   polymorphic chromosome ends.";
RL   Sci. Rep. 10:0-0(0).
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:KAF7782472.1}.
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DR   EMBL; JABXXO010000003; KAF7782472.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8H7F845; -.
DR   Proteomes; UP000629468; 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; 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; PS50172; BRCT; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          61..112
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          461..510
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          108..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..145
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   545 AA;  62923 MW;  CE71406BDA4CB4EB CRC64;
     MNRRPLAPRQ LLLQQPPLPQ KRPRSPDPAA LPLKKHRRDR DPLRDNHRLE REQQRLEFKE
     KYCRAFPGWI FYLDSDTIDR PHQLESFRSR IQQLGARIDP FFSRETTHLI SNRPNPPGSV
     DPSEKENAPK TRILSRIKSP LKNRSRQPED ADATELIANA LKFKIKIWDT AKLDSVLSRC
     LEEPSTIIPT QTSSTKQRNP HTLSKLLQSE RLHGSSERDP TQKRHDFHYF GRGSHFVLIE
     DMYGELATIA AHEYPAPKKA DDDKTPWPTL YCHPQARGPF VRFDEREKRR WERLQQAEKK
     EKEERRLRRE TLLKKLPLDN EMHMRPLARK AGDLRRSVSL NNMANIDPFA YHDGDGDVIE
     SANASGYLAS GLMGYTAASG NSVNITSTTG TTSTSNFASR ALQIPCNLTS RMRMEVVMRK
     QPQEKLAQTN PMGPPADVPQ RSMVLKKSKS TNTLKLPKRE EGSKPGYCES CRQKFDDFKE
     HIRGRKHRKF AADDSNFLSL DYIIHRVQRR TLKETQALHQ GRMDICSQIS NQDFDSDFDP
     IPVED
//
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