ID A0A420JBC2_9PEZI Unreviewed; 679 AA.
AC A0A420JBC2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
DE SubName: Full=Putative g1 s regulator {ECO:0000313|EMBL:RKF84103.1};
GN ORFNames=GcM3_001018 {ECO:0000313|EMBL:RKF84103.1};
OS Golovinomyces cichoracearum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Golovinomyces.
OX NCBI_TaxID=62708 {ECO:0000313|EMBL:RKF84103.1, ECO:0000313|Proteomes:UP000283383};
RN [1] {ECO:0000313|EMBL:RKF84103.1, ECO:0000313|Proteomes:UP000283383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMSG3 {ECO:0000313|EMBL:RKF84103.1};
RX PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA Deng X., Wei C.I., Xiao S.;
RT "Comparative genome analyses reveal sequence features reflecting distinct
RT modes of host-adaptation between dicot and monocot powdery mildew.";
RL BMC Genomics 19:705-705(2018).
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:RKF84103.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MCBQ01000165; RKF84103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A420JBC2; -.
DR STRING; 62708.A0A420JBC2; -.
DR Proteomes; UP000283383; 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; 2.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000283383};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 619..668
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 399..426
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 93..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..241
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 76577 MW; 92B4AAD26A325057 CRC64;
MAAISLSPLP SSVPGMSGRR VPLSNNPNAV NSPFKAASAT TASKTKRSHA NVQREEIYAQ
PPPAKKQMLE SHQLLKTPPR HQSTQSAAPG FQSRRDTGSQ QVTHERKVSK IREKTQKAAT
KVEWHLTDDH ESIRQWQKHY RRIFPSFVFY FENVSLEAQA KYTNAVMSLG AREDKFFSNT
VTHVITTRTI PPQIQSKSTV STVDSSIPQP QTIPPQMCRS SINLPHESTN SSESTTKSKP
TLEASTCKKI IASCSNGDSK RSQGRCTDFL HKARELGMKI WSLEKLERII NVIFDTDAGY
HKNQAVGSRF NINSTACRLG RETDLQQLLR NERIYGPSDR DLTVASKELY IFKGPYIYIH
DIEQKQKPIM VREYPKVYNK EDGDWPQFRS VANGKCPFID EVDYSKREAE KEMEKIRIRR
QLDKERAYSL AKVTPTSTIQ PKPMVNKRAL DEQFDDANNE GTVKKQKCSM AKSMKSLSSN
LDSKASVGDN AFVSRASIGR LHDGEPIASG VQPAITSAIR STMSSTAAQP GFKAGTSKEV
HGMQRKVLEK KTIFSSSHDS HSTRPIGEIK TSALAQKQTF DKSTTLEQKI DCSHVQDASE
KTEITRKVKS IQQSTTTQQE PKPGYCENCQ DKFEDFNEHV ISRKHRKFAE KVENWKLLDE
LLAQLSRPLR ENIDRKDNS
//