ID A0A135LGK0_PENPA Unreviewed; 649 AA.
AC A0A135LGK0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 18-JUN-2025, entry version 34.
DE SubName: Full=Regulatory subunit Dfp1/Him1, central region {ECO:0000313|EMBL:KXG48075.1};
GN ORFNames=PGRI_019450 {ECO:0000313|EMBL:KXG48075.1};
OS Penicillium patulum (Penicillium griseofulvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5078 {ECO:0000313|EMBL:KXG48075.1, ECO:0000313|Proteomes:UP000070168};
RN [1] {ECO:0000313|EMBL:KXG48075.1, ECO:0000313|Proteomes:UP000070168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG3 {ECO:0000313|EMBL:KXG48075.1,
RC ECO:0000313|Proteomes:UP000070168};
RX PubMed=26729047; DOI=10.1186/s12864-015-2347-x;
RA Banani H., Marcet-Houben M., Ballester A.R., Abbruscato P.,
RA Gonzalez-Candelas L., Gabaldon T., Spadaro D.;
RT "Genome sequencing and secondary metabolism of the postharvest pathogen
RT Penicillium griseofulvum.";
RL BMC Genomics 17:19-19(2016).
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:KXG48075.1}.
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DR EMBL; LHQR01000065; KXG48075.1; -; Genomic_DNA.
DR RefSeq; XP_040646611.1; XM_040789658.1.
DR AlphaFoldDB; A0A135LGK0; -.
DR STRING; 5078.A0A135LGK0; -.
DR GeneID; 63704958; -.
DR OMA; GMKIWAI; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000070168; 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; 2.
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:UP000070168};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 591..640
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 182..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 541..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 649 AA; 73226 MW; DFAAFF6EE1A6A2E4 CRC64;
MATVFVSPSP RTSMTMATRR PLANVPNATN SPRRAELVLK RARPTKVEMP YGQPPPKRQA
MENMEYEPRS TTCQTTTTDS KLFARRSNNG NPSAFEKKLV AAREKERQPV VKNVRVEKAP
ADTMDSIRQW QRHYRKAFPQ FVFYFDSIPE DVRRRFSRQV SALGAREEKF FSRLVTHVVT
SRTIPPESAT PTEPESTENA TNGDGNVQTV NPSLLERNGE THLHASLKTE TRRDQATMDI
LQRARQMGMK IWALEKLQRM ITTINDSDIG AQYEQAARNK AAGGNAANGR GENDLSRVLR
QELLNGPSDR DPLTSMEMII FKGPFVYIHD MNEKTKPVMV REYSRVARRQ DGSWPQFRSA
PLGKCPFIDE PPSRKEYDRH RLRQLHKEKK AASQKADGTR DAKTKAAVPV QVPESVTTTE
IAHSQPSVKQ EERVSPPIQN DIQRPSLEET HERKSSESFI PPHFPRTGPF YAGHEPAASG
VQPSNMTSAI RSQMISSTAA APGAKAGLSK EVHGLKRKVL EKGTGGFAVG SMAAPQRRGD
VTMTVPTKNN INPAGKSNIP HNEDELKQAE VAGSKRQRDD KDEQKKPERR RDPKPGYCEN
CRDKFDDFEE HTLTRKHRRF ATNSTNWAEL DALLAEIQRP LKGDYEYDE
//
