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Database: UniProt
Entry: A0A8H5MA21_9AGAR
LinkDB: A0A8H5MA21_9AGAR
Original site: A0A8H5MA21_9AGAR 
ID   A0A8H5MA21_9AGAR        Unreviewed;       606 AA.
AC   A0A8H5MA21;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   28-JAN-2026, entry version 15.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=D9615_002435 {ECO:0000313|EMBL:KAF5386259.1};
OS   Tricholomella constricta.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomatineae; Lyophyllaceae;
OC   Tricholomella.
OX   NCBI_TaxID=117010 {ECO:0000313|EMBL:KAF5386259.1, ECO:0000313|Proteomes:UP000565441};
RN   [1] {ECO:0000313|EMBL:KAF5386259.1, ECO:0000313|Proteomes:UP000565441}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 661.87 {ECO:0000313|EMBL:KAF5386259.1,
RC   ECO:0000313|Proteomes:UP000565441};
RX   PubMed=32382073; DOI=10.1038/s41396-020-0667-6;
RA   Floudas D., Bentzer J., Ahren D., Johansson T., Persson P., Tunlid A.;
RT   "Uncovering the hidden diversity of litter-decomposition mechanisms in
RT   mushroom-forming fungi.";
RL   ISME J. 14:2046-2059(2020).
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:KAF5386259.1}.
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DR   EMBL; JAACJP010000003; KAF5386259.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A8H5MA21; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000565441; 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; 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:UP000565441};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          88..138
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          492..541
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          559..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   606 AA;  67938 MW;  29A5E46B32F0A350 CRC64;
     MATLNRPPLT NRSHQFPSTV SPIKSQRTAS GSKRPRSPEP SADPSAFHPT SKRVKAAMDP
     SPAPKARDRL RERKHVEREQ QKAEFKEKYT RAFPSFTFYF DELNLGSVAL DTYEEMIEEL
     GGKIVKFLDR AVTHFISNRP DATLVVSADK ENHPKPGVGL KSPIKLKGRV IENSDHNNSV
     ASSTTLIYKV WNTTKLESVL TRLLDPPTAS TSTAPSTVKK QVPSLARLLK SEQIHGTTER
     DPTQKRYDYK YFARGSKFVL IEDLRHELAT IAAHEYPVPK TREGALAKPP WPVLYCHPQA
     RGPFIAFDEK EKRRWEKVQR AEGEQKAERK EYSNKIRQAE FMKRKAEANM HAKRSGDLRR
     SVSMNNLHRA ARNDECFLDL DGDGDNLDSA VASGFLASGA AGYMAASGNS VSITSTIGTT
     STAGYTSRAF QLPSSVSART KYVTTSRRLT STAADKENKA PLMGPPAVIP ERQPLLRKSR
     STNTLKLPKR EEGSKPGYCE SCRIKFDDFK AHIVGRKHQR FATNDANFLQ LDCVLARVQR
     RTKADVLDAR LKREETRRYH CRGGRHGSGS SSDNPESPLL MGRTFQYGVH EDFDMQGDSD
     RISDCD
//
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