ID A0A0U5G0C4_ASPCI Unreviewed; 647 AA.
AC A0A0U5G0C4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 18-JUN-2025, entry version 35.
DE SubName: Full=Putative G1/S regulator {ECO:0000313|EMBL:CEL05094.1};
GN ORFNames=ASPCAL06214 {ECO:0000313|EMBL:CEL05094.1};
OS Aspergillus calidoustus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=454130 {ECO:0000313|EMBL:CEL05094.1, ECO:0000313|Proteomes:UP000054771};
RN [1] {ECO:0000313|Proteomes:UP000054771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF006504 {ECO:0000313|Proteomes:UP000054771};
RX PubMed=26966204; DOI=10.1128/genomea.00102-16;
RA Horn F., Linde J., Mattern D.J., Walther G., Guthke R., Scherlach K.,
RA Martin K., Brakhage A.A., Petzke L., Valiante V.;
RT "Draft genome sequences of fungus Aspergillus calidoustus.";
RL Genome Announc. 4:0-0(2016).
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DR EMBL; CDMC01000005; CEL05094.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5G0C4; -.
DR STRING; 454130.A0A0U5G0C4; -.
DR OMA; GMKIWAI; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000054771; 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; 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 PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054771};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 591..640
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..211
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 647 AA; 72817 MW; 3993ACCBF066CFA1 CRC64;
MAAVFVPPSH ENPLNMSTRR PLANVPNATN SPHRVGLVPA KRPRATTAQI DIAYGQPPPK
KQVVEGNETE NQTTVHTKTS TLRGTDSKLF TRRTNNAQPS AFERRLVDAR DKERQPQSKT
TKQEKPSTEN ISIKQWQRHY RKAFPHFVFY FDCVPIDVRS KCSRQVMALG AREEKFFSRL
VTHVVTSRPI PPEIDRRAPA EPAQDAPQDS PGDVQTVNPA ELEMHLHLAV CPKREPSQDV
LHRAREMGMK IWAVEKLQRM IATINDADIA NSNPTRNATG AQSKSRGKDD LSQVLQNELN
GPSDRSHLSV LKDLVLFKGP FIYVHDMDEK TRPVMVREYP KVAKRQDGIW PQFRSAPLGK
CPFIEDAPTK REVERQRPRQ EKEEKEKKTF IKPTVPLFGK GVEITHQPQQ LPAKKETSPA
EDDEPPAPPV KLEDSPDISQ EVPLSPKKSS ESFVPPPLHR KGPFYHGREP AASGVQPSNI
TSAIRSQMVS STAAAPGAKA GLSKEVHELK RKVLEKSNGG FSAAVAHAYR PLDAPTTANT
EKSYTSRMSK SSRPDKLGHI EEETTQSESN DTKHWTKPRK GAEIRKKERR RDPKPGYCEN
CRDKFDDFDE HVMTRKHRKF AANGANWAEL DSLLLQLARP EKAERTA
//
