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Database: UniProt
Entry: A0A9W9TGD1_PENCI
LinkDB: A0A9W9TGD1_PENCI
Original site: A0A9W9TGD1_PENCI 
ID   A0A9W9TGD1_PENCI        Unreviewed;       631 AA.
AC   A0A9W9TGD1;
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=N7469_010276 {ECO:0000313|EMBL:KAJ5221389.1};
OS   Penicillium citrinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5077 {ECO:0000313|EMBL:KAJ5221389.1, ECO:0000313|Proteomes:UP001147733};
RN   [1] {ECO:0000313|EMBL:KAJ5221389.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 23319 {ECO:0000313|EMBL:KAJ5221389.1};
RA   Petersen C.;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAJ5221389.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IBT 23319 {ECO:0000313|EMBL:KAJ5221389.1};
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:KAJ5221389.1}.
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DR   EMBL; JAPQKT010000009; KAJ5221389.1; -; Genomic_DNA.
DR   RefSeq; XP_056496312.1; XM_056649181.1.
DR   AlphaFoldDB; A0A9W9TGD1; -.
DR   GeneID; 81388348; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP001147733; 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:UP001147733};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          575..624
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          175..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          248..274
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..462
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..586
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..71
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..377
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        423..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..498
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        516..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        561..586
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   631 AA;  70858 MW;  A043942FEDDFFAAB CRC64;
     MSTRRPLANV PNATNSPHRA GLLPGKRARS TQMEIPYGQP PPKKQVMDSV EHESRSPSRS
     RSTLQQSTES RLFARRSNNA NPSAFEKKLV AARDRERQPT VKATKGEKPS ADTLDNIRQW
     QRHYRKAFPQ FVFYFDTIPE DVRRKFSRQV VALGAREEKF FSRLVTHVVT SRPIPAETVT
     SPTEEANPAT EANGDANVQT VNPSLLDKSA GRRDQGNMDV LQRARQMGMK IWALEKLQRM
     ITTINDNDLG GQHDAVSRGK TAGGNATHGK GDNDLSRVLR QELLNGPSDR DPLSSMEMLV
     FKGPFIYIHD MNEKTKPVMV REYSRVARRQ DGVWPQFRSA PLGKCPFIDE PPSRKELDRH
     RMRQAQKEKK AGRKNTEETQ LQPPAAHENT VETKVSTELA KPQKSVEEPT RPPTQAEFPA
     KPSFDETRER KSSESLIPPH FPRTGPFYTG REPAASGVQP SNVTSAIRSQ MISSTAAAPG
     AKAGLSKEVH GLKRKVLEKG TGTVVTGSMA APQRPGNGSS LNPARAQSTE SNKSAAPEKN
     GQHEEDGNQS EGGGAKRRRD ERRDSQPKKT EQRRRDPKPG YCENCRDKFD DFEEHTLTRK
     HRRFAQNSSN WAELDALLFE IQRPLKEEYE F
//
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