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Database: UniProt
Entry: A0A9W9VSA1_9EURO
LinkDB: A0A9W9VSA1_9EURO
Original site: A0A9W9VSA1_9EURO 
ID   A0A9W9VSA1_9EURO        Unreviewed;       634 AA.
AC   A0A9W9VSA1;
DT   08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2023, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=N7509_010781 {ECO:0000313|EMBL:KAJ5388240.1};
OS   Penicillium cosmopolitanum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=1131564 {ECO:0000313|EMBL:KAJ5388240.1, ECO:0000313|Proteomes:UP001147747};
RN   [1] {ECO:0000313|EMBL:KAJ5388240.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 29677 {ECO:0000313|EMBL:KAJ5388240.1};
RA   Petersen C.;
RL   Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ5388240.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 29677 {ECO:0000313|EMBL:KAJ5388240.1};
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).
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:KAJ5388240.1}.
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DR   EMBL; JAPZBU010000009; KAJ5388240.1; -; Genomic_DNA.
DR   RefSeq; XP_056486038.1; XM_056635418.1.
DR   AlphaFoldDB; A0A9W9VSA1; -.
DR   GeneID; 81374398; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP001147747; 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:UP001147747};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          578..627
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          191..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..290
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          342..455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..95
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..208
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        366..386
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        400..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..448
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   634 AA;  71952 MW;  785B1753231BFD85 CRC64;
     MAAVFVPPSP QTSLNMSTRR PLANVPNATN SPHRTGLLPA KRARSTQIEI PYGQPPPKKQ
     VMDVAEQETR SPSRSRSTLQ QSTESRLFAR RSNNANPSAF EKKLVAARDR ERQPVVKGTK
     GERPSADTLD NIRQWQRHYR KAFPQFVFYF DSIPEDVRQK FSRQVVALGA REEKFFSRLV
     THVVTSRPIP AEAVTSPTEE STATPEASGD AHVQTVNPSL LDKSAGRRDQ GSMDVLQRAR
     QMGMKIWALE KLQRMITTIN DNELAGQHDA VSRSKAAGGH ASHGKGDNDL SRVLRQEMLN
     GPSDRDPLAS MEMLVFKGPF IYIHDMNEKT KPVMVREYSR VAKRQDGSWP QFRSAPLGKC
     PFIDEPPSRK EYDRHRMRQA QKEKKATRQN VEEPQPQPAP TNETPVDTKT STEASKPQTS
     IEEHFKPSTQ VEIPAKPSFE ESHERKSSES FIPPHFPRTG PFYTGREPAA SGVQPSNVTS
     AIRSQMISST AAAPGAKAGL SKEIHGLKRK VLEKGDWWYH HWINGRASTS QQWISNKSAV
     PEKTGQEEDG NQSEGVGNKR RRDERRDNQQ KKPEQRRRDP KPGYCENCRD KFDDFEEHTL
     TRKHRRFAQN TSNWAELDAL LFEIQRPLKD EYQF
//
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