ID A0A9W9EYB9_9EURO Unreviewed; 650 AA.
AC A0A9W9EYB9;
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=N7532_008830 {ECO:0000313|EMBL:KAJ5090146.1};
OS Penicillium argentinense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1131581 {ECO:0000313|EMBL:KAJ5090146.1, ECO:0000313|Proteomes:UP001149074};
RN [1] {ECO:0000313|EMBL:KAJ5090146.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 30761 {ECO:0000313|EMBL:KAJ5090146.1};
RA Petersen C.;
RL Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ5090146.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 30761 {ECO:0000313|EMBL:KAJ5090146.1};
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:KAJ5090146.1}.
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; JAPQKI010000009; KAJ5090146.1; -; Genomic_DNA.
DR RefSeq; XP_056472128.1; XM_056621322.1.
DR AlphaFoldDB; A0A9W9EYB9; -.
DR GeneID; 81360301; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP001149074; 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:UP001149074};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 595..644
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..568
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..582
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 650 AA; 73324 MW; 7510E58969996233 CRC64;
MSTRRPLANV PNATNSPHKA GLLPAKRARS TQMEVPYGQP PPKKQVTDSF EPESRSPSRA
KSTVQQSTES RLFARRSNNA NPSAFEKKLV AARDRERHPV VKGAKGEKPS ADTLDTIRQW
QRHYRKAFPQ FVFYFDSIPE DVRRKFSSQV VALGAREENF FSRTVTHVVT SRPIPAETAT
SPTDESAPTT EANGDANVQT VNPSLLDKNA GRRDQGNMDV LQRARQMGMK IWALEKLQRM
ITTINDNDIS GHHDAASRSK TAGGHTAHGK GDNALSRVLR QELLNGPSDR DPLSSMEMQV
FKGPFIYIHD MNEKTKPVMV REYPRVAKRQ DGAWPQFRSA PLGKCPFIDE PPSRKEMDRQ
RMRQAQKEKK AARQNAEETR SQSKSVSVTA NEKNVDTKLV TELSKPQKPF EEQTNTATHP
EITRKPSFEE AKERKSSESF APPPIPRTGS FYTGREPAAS GVQPSNVTSA IRSQMVSSTA
GVPGAKAGLS KEMHGLKRKV LEKETGGIVT GSMAAPQRPI NGSSLNPSRA QSAESNNSAK
PEKRPREDDG YQSEGDRPKR RREDEKNQHQ HKIPHKVQHK TQHRELPKKP EQRRRDPKPG
YCENCREKFD DFEEHTLTRK HRRFAQNSSN WAELDSLLFE LQRPLKEERI
//
