ID C0NS56_AJECG Unreviewed; 676 AA.
AC C0NS56;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 28-JAN-2026, entry version 55.
DE SubName: Full=G1/S regulator {ECO:0000313|EMBL:EEH05722.1};
GN ORFNames=HCBG_05986 {ECO:0000313|EMBL:EEH05722.1};
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH05722.1, ECO:0000313|Proteomes:UP000001631};
RN [1] {ECO:0000313|EMBL:EEH05722.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=G186AR {ECO:0000313|EMBL:EEH05722.1};
RG The Broad Institute Genome Sequencing Platform;
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GG663370; EEH05722.1; -; Genomic_DNA.
DR RefSeq; XP_045286203.1; XM_045433035.1.
DR AlphaFoldDB; C0NS56; -.
DR FunCoup; C0NS56; 134.
DR STRING; 447093.C0NS56; -.
DR GeneID; 69039002; -.
DR VEuPathDB; FungiDB:I7I50_06267; -.
DR HOGENOM; CLU_017715_0_0_1; -.
DR InParanoid; C0NS56; -.
DR Proteomes; UP000001631; 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 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; IPR036420; BRCT_dom_sf.
DR InterPro; IPR055116; DBF4_BRCT.
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; PF22437; DBF4_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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001631};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 615..664
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 230..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..592
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 676 AA; 75190 MW; 031FBF9224C17295 CRC64;
MSNRRTPLVN VPNGTNSPHR GTITSVKRTL PGNCQTDVCY MQPPPKKQML EKNGVDLNNK
SPRKLAVASR EGKVFTRKNT NSQPSAFERK LVAARDRDRA NNSRGAKYDR AGGETLDSIR
QWQKHYRKAF PQFVFYFESI PEDVRNKCSR QIMALGATEE KFFSKVVTHV VTARPIPPAI
DSPNHTEPSA GEAPLNQQNA DGSIQTVDPS LLEKNFETTH LNHGVGRPRK TPDKRVGQEG
DPKRDNKDIL YRARQMNMKI WALEKLQRVI STMNDGESTS THGHYTRSNG TVSGAGRGRA
ETDLSQVLRN ERLNGPVDRD TILASKEIIP FKGPFIYVHD YEEKTRPVMV REYPKVARGQ
DGAWPQFRSA ALGKCPFIDE PPAKKESEKR KGAASQTRDE KPAAKEKSTT TTEMKMMQPP
ERSVEKRALQ DVQGGVSQTI TRQEPTPAPK RIETLLMLPA KPASPRSKGF EAFPGAKAAL
ATYLAREPAA SGVQPSNITS AIRSQIVSST AAAPGAKAGT SKEVHGLKRK VLEKGNSTLS
TNGNGIPSSH RMADIAGALK ASRAPVTRAA KSKATGNVNQ IDEDGTTQSE DEMVQKLHDP
GRKNTSTVRS RQKKRDPKPG YCENCRDKFE DFEEHIMTRK HRKFALTSSN WVELDALLHS
LERPRKRYLP PDEDNW
//
