ID A0A9X0C8T4_9EURO Unreviewed; 646 AA.
AC A0A9X0C8T4;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE SubName: Full=Regulatory subunit Dfp1/Him1 central region {ECO:0000313|EMBL:KAJ5513257.1};
GN ORFNames=N7463_002809 {ECO:0000313|EMBL:KAJ5513257.1};
OS Penicillium fimorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1882269 {ECO:0000313|EMBL:KAJ5513257.1, ECO:0000313|Proteomes:UP001149954};
RN [1] {ECO:0000313|EMBL:KAJ5513257.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 29495 {ECO:0000313|EMBL:KAJ5513257.1};
RA Petersen C.;
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAJ5513257.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IBT 29495 {ECO:0000313|EMBL:KAJ5513257.1};
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:KAJ5513257.1}.
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DR EMBL; JAPWDS010000002; KAJ5513257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9X0C8T4; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP001149954; 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:UP001149954};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 588..637
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 646 AA; 72721 MW; 504EAE17F0C52B8F CRC64;
MATVFVPPSP RTSMTMATRR PLANVPNATN SPRRAELVLK RARPTRVEIP HGQPPPKRQA
MENIEYEPRS TTCQTTNTDS KLFARRSNNG NPSAFEKKLV AAREKERQPP VKHVRVEKAP
VDTMDSIRQW QRHYRKAFPQ FVFYFDSIPE DVRRRFSRQV IALGAREEKF FSRLVTHVVT
SRAIPPESAT PTEPESTTDA TNGDSNVQTV NPSLLERNGE THLHASLKTE TRRDQVTMDI
LQRARQMGMK IWALEKLQRM ITTINDSDIG AQYEQAARNK AAGGTAANGR GENDLSRVLR
QELLNGPSDR DPLTAMEMII FKGPFVYIHD MNEKTKPVMV REYSRVARRQ DGSWPQFRSA
PLGKCPFIDE PPSRKEYDRH RLRQLHKEKK AASLRADGTT KTKTAVPVQA PESVATEIAH
SQPLAKQEER VSPPIQNEVQ KPSVDETHER KSSESFIPPH FPRTGPFYAG HEPAASGVQP
SNMTSAIRSQ MISSTAAAPG AKAGLSKEVH GLKRKVLEKG TGGFAVGSMA APQRRGDGLA
PVPTKNNINP PGKANVPHNE DEAKQSEVAG SKRQREDKDE QKKPERRRDP KPGYCENCRD
KFDDFEEHTL TRKHRRFAAN STNWAELDAL LAEIQRPLKA DYEYDE
//
