ID A0A179UEZ6_BLAGS Unreviewed; 1098 AA.
AC A0A179UEZ6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JAN-2026, entry version 35.
DE SubName: Full=Regulatory subunit for Cdc7p protein kinase {ECO:0000313|EMBL:OAT05839.1};
GN ORFNames=BDBG_16495 {ECO:0000313|EMBL:OAT05839.1};
OS Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=559298 {ECO:0000313|EMBL:OAT05839.1, ECO:0000313|Proteomes:UP000002038};
RN [1] {ECO:0000313|Proteomes:UP000002038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLH14081 {ECO:0000313|Proteomes:UP000002038};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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DR EMBL; GG657450; OAT05839.1; -; Genomic_DNA.
DR RefSeq; XP_002627495.2; XM_002627449.2.
DR AlphaFoldDB; A0A179UEZ6; -.
DR STRING; 559298.A0A179UEZ6; -.
DR GeneID; 8506987; -.
DR KEGG; bgh:BDBG_16495; -.
DR VEuPathDB; FungiDB:BDBG_16495; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000002038; Unassembled WGS sequence.
DR GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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; cd00067; GAL4; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 2.
DR Gene3D; 4.10.240.10; Zn(2)-C6 fungal-type DNA-binding domain; 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; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR InterPro; IPR006572; Znf_DBF.
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 Pfam; PF00172; Zn_clus; 1.
DR SMART; SM00066; GAL4; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS51265; ZF_DBF4; 1.
DR PROSITE; PS00463; ZN2_CY6_FUNGAL_1; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00600};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002038};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00600};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00600}.
FT DOMAIN 613..644
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT DOMAIN 675..705
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 388..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1098 AA; 122977 MW; 769D8B90577B45C8 CRC64;
MSSRRVPLVN IPNGTNSPHR GAITSGKRNL PGNYQTEMLF MQPPPKKQML EKNEGDLNNK
SPRKLAVTST EGKVFTRKNT NSQPTAFERK LVAAREKDRA HNSRGTRYDR TGGETLDSIR
QWQKHYRKAF PQFVFYFESI PEDVRNKCSR QIMALGATEE KFFSKVVTHV VTARPIPRGM
DSPNHTEIST NAPLGQQNAD GSVQTVDPSL LEKNYESSHV SQGVGRPRKI SDKRPGQEGD
TRRDNKDVLY RARQMNMKIW ALEKLQRVIS TMNDGENIAH HGHYTRSNGT VSGAGRGRAE
TDLSQVLRNE RLHGPTDRDS ILASKEIIPF KGPFIYIHDY EEKTRPVMVR EYPKVARRQD
GAWPQFRSAA LGKCPFIDEP LTKKELEKRK ATANQTKDKW PATKEKSTAT TEIKTMQPPE
RSVEKRALQD AQEGVNQTIT REAPVPAPKR VETLLMLPAK PASPRTKGFE TFPDAKASLA
TYLAREPAAS GVQPSNITSA IRSQMVSSTA AAPGAKAGTS KEVHGLKRKV LEKGHSTLSA
NGSGIPSSHR MTDISGALKA SRAPVTRAAK SKATGNLDQI DEDGTTQSEG EKVQKPQQAS
RKSNTARSRQ KKRDPKPGYC ENCRDKFEDF EEPNNTNHCR PFVEFGPTEL GKESSLVRHT
KKCVDGRPPV VRQKACRECS AAKTRCDLKR PTCSRCTLRN TICMYPTYPA GPEIGVESHG
FPQKDSQKST SPLQGHVRFG PDPLCGGFNP EVELPTPESE TLDFHSILPP DLGVLENELS
AVFDGYTDVD SLNYNYALVR NIPDSSSGEG VQIAPSTPPP AYALGLTRHT MQTLFRIAQT
WPRMMAKGTQ LPPIIHPKQV SDGIIPEPLT NCFALVKMWH GQPHGGASIV QQTVRREMQT
IANSFQTLDE TELVAALQAL TIYTLMLLFP SNDQQTIPLL EDKLVRQLRS IIQHVVSTGV
VLQEEIERTR PFWECWIAVT CKRRAALSLY TIYWGYSVYH CIPAFDCSEL HHMPAPAPKY
LWQATTNEQW ESLYNRWLAH WDGPYYRHGE IFEINTGIRM DPRAELWFEE VDEFGMIFAA
AINALEREPE LTVMETAA
//
