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Database: UniProt
Entry: A0AA39T3A7_ARMTA
LinkDB: A0AA39T3A7_ARMTA
Original site: A0AA39T3A7_ARMTA 
ID   A0AA39T3A7_ARMTA        Unreviewed;       572 AA.
AC   A0AA39T3A7;
DT   24-JAN-2024, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2024, sequence version 1.
DT   28-JAN-2026, entry version 9.
DE   SubName: Full=Dfp1/Him1, central region-domain-containing protein {ECO:0000313|EMBL:KAK0461411.1};
GN   ORFNames=EV420DRAFT_197366 {ECO:0000313|EMBL:KAK0461411.1};
OS   Armillaria tabescens (Ringless honey mushroom) (Agaricus tabescens).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae; Desarmillaria.
OX   NCBI_TaxID=1929756 {ECO:0000313|EMBL:KAK0461411.1, ECO:0000313|Proteomes:UP001175211};
RN   [1] {ECO:0000313|EMBL:KAK0461411.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCBAS 213 {ECO:0000313|EMBL:KAK0461411.1};
RG   Lawrence Berkeley National Laboratory;
RA   Ahrendt S., Sahu N., Indic B., Wong-Bajracharya J., Merenyi Z., Ke H.-M.,
RA   Monk M., Kocsube S., Drula E., Lipzen A., Balint B., Henrissat B.,
RA   Andreopoulos B., Martin F.M., Harder C.B., Rigling D., Ford K.L.,
RA   Foster G.D., Pangilinan J., Papanicolaou A., Barry K., LaButti K.,
RA   Viragh M., Koriabine M., Yan M., Riley R., Champramary S., Plett K.L.,
RA   Tsai I.J., Slot J., Sipos G., Plett J., Nagy L.G., Grigoriev I.V.;
RL   Submitted (JUN-2023) 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:KAK0461411.1}.
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DR   EMBL; JAUEPS010000011; KAK0461411.1; -; Genomic_DNA.
DR   RefSeq; XP_060333308.1; XM_060481177.1.
DR   AlphaFoldDB; A0AA39T3A7; -.
DR   GeneID; 85364725; -.
DR   Proteomes; UP001175211; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP001175211};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          495..544
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..572
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          318..356
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        35..47
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..78
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..163
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..430
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        548..557
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..572
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  64427 MW;  18C47768AD047E11 CRC64;
     MSTTVGSRPP LVNRATSRSL GQKWARTASG IKRPRSPEID ATVEFKRQRA AGPDTSAPKY
     KDKERRHTER AQKDKEFKDK YSRAFPTFTF HFDLSHLEPD TGLRKSLEAR IVQLGGVIED
     FFSKDVTHLI TNQKGDGDDD ADKENNPKSS ISKTNSTIKS PSKSRTRVVG DDGAMYGLIT
     KAVEWKMKTW STAKLDSVLS RCLEVPMLTG SNPSRATNAA QPMNAVQPYR SLARLLQSER
     VHGSTERDPT QKRHDFTYFS RGSYWVLVED MQQELATIAA HEYEVSKGRD SSIKGSWPVA
     HCHPHARGPF IPFDDRERRR WERNKKEEME QKDEQAREQK KKLLRLEAMK RKARAQVHSK
     GPGDLRRSAS MNNLHRRGIL DEQEVGEALG DDNIDSANAS GYLGSGAYVA ASGNSVSITS
     TTGTTSTTDY SHSRPLPPSL RAQIGNEVTT SRRLASIAKD GDGKSTMGPP TYIPTRSGLR
     KSRSTNSLRL PKREEGSKPG YCESCRVKFD DFKVHVKTKK HDRYANNAAN FSSLDFVLSR
     IRRRTRAEIE ADQQREEQAE EEEEYPCDDD DE
//
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