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Database: UniProt
Entry: A0AAD6IKI8_PENCN
LinkDB: A0AAD6IKI8_PENCN
Original site: A0AAD6IKI8_PENCN 
ID   A0AAD6IKI8_PENCN        Unreviewed;       651 AA.
AC   A0AAD6IKI8;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=N7460_002811 {ECO:0000313|EMBL:KAJ6052277.1};
OS   Penicillium canescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5083 {ECO:0000313|EMBL:KAJ6052277.1, ECO:0000313|Proteomes:UP001219568};
RN   [1] {ECO:0000313|EMBL:KAJ6052277.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 15450 {ECO:0000313|EMBL:KAJ6052277.1};
RX   PubMed=36726175;
RA   Petersen C., Sorensen T., Nielsen M.R., Sondergaard T.E., Sorensen J.L.,
RA   Fitzpatrick D.A., Frisvad J.C., Nielsen K.L.;
RT   "Comparative genomic study of the Penicillium genus elucidates a diverse
RT   pangenome and 15 lateral gene transfer events.";
RL   IMA Fungus 14:0-0(2023).
RN   [2] {ECO:0000313|EMBL:KAJ6052277.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 15450 {ECO:0000313|EMBL:KAJ6052277.1};
RA   Petersen C.;
RL   Submitted (JAN-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:KAJ6052277.1}.
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DR   EMBL; JAQJZL010000002; KAJ6052277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD6IKI8; -.
DR   Proteomes; UP001219568; 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   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:UP001219568};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          593..642
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          280..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        190..206
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..409
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..438
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..461
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   651 AA;  73246 MW;  4219246C8111303B CRC64;
     MATVFVPPSP RTSLTMATRR PLANVPNATN SPHRSGPVPA KRSRSTQMEI PYGQPPPKKQ
     VMEAIENDGR SPSRSRSATA QNTDSKLFAR RSNNATPSAF EKKLVAAREK ERQPLVKTIK
     TEKASADTMD TIRQWQRHYR KAFPQFVFYF DSIPEDVRRK FSRQVIALGA REEKFFSRLV
     THVVTSRAIP PESTSPTEAE TTADATNGDG NVQTVNPSML ERNGDTHLHV SLKTDTRRDQ
     GTMDVLQRAR QMGMKIWALE KLQRMITTIN DSDIGAQADT ASRSKTAGGN AANGKGENDL
     SRVLRQELLN GPSDRDPLSS MEMLMFKGPF VYIHDMNEKT KPVMVREYSR VARRQDGSWP
     QFRSAPLGKC PFIDEPPSRK EYDRHRLRQL QKEKKAALHN TDGNREAKPK ATAPAHRVQD
     TKLVTEVTKS KPSEHEQRIP PAIQTESQKP SFDENNERKS SESFIPPHFP RTGPFYTGRE
     PAASGVQPSN MTSAIRSQMI SSTAAAPGAK AGLSKEVHGL KRKVLEKGTG AIGAGSMAAP
     QRREGSVPVQ CKNMNPPGRS NLRHEDDGNQ SEVAGSKRQR EDKEQQRKSE RRRDPKPGYC
     ENCRDKFDDF EEHTLTRKHR RFAANSTNWA ELDALLFEIQ RPLKDKYEYD E
//
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