ID A0A0G4P9W6_PENC3 Unreviewed; 649 AA.
AC A0A0G4P9W6;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE SubName: Full=BRCT {ECO:0000313|EMBL:CRL23095.1};
GN ORFNames=PCAMFM013_S009g000035 {ECO:0000313|EMBL:CRL23095.1};
OS Penicillium camemberti (strain FM 013).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1429867 {ECO:0000313|EMBL:CRL23095.1, ECO:0000313|Proteomes:UP000053732};
RN [1] {ECO:0000313|EMBL:CRL23095.1, ECO:0000313|Proteomes:UP000053732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM 013 {ECO:0000313|Proteomes:UP000053732};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
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DR EMBL; HG793142; CRL23095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4P9W6; -.
DR STRING; 1429867.A0A0G4P9W6; -.
DR Proteomes; UP000053732; 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:UP000053732};
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 186..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 386..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..201
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..522
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; 73004 MW; 1FE397BDE112DB83 CRC64;
MATVFVPPSP RNSMAMATRR PLANVPNATN SPHRAGLLPV KRARSNQMEI PYGQPPPKKQ
VMENTEYETR TTTCQNTNTE SKLFARRSNN GNPSAFEKKL VAAREKERQP LVKHVKAEKA
TADTMDSIRQ WQRHYRKAFP QFVFYFDSIP EDVRRRFSRQ VIALGAREEK FFSRLVTHVV
TSRAIPPESA TPAEPEAAAD ASNGDSNVQT VNPSLLERNG ETHLHASLKT ETRRDQGTMD
ILQRARQMGM KIWALEKLQR MITTINDSDI GAQYEQAARN KAAGGNAVNG RGENDLSRVL
RQELLNGPSD RDPLASMEMI MFKGPFVYIH DMNEKTKPVM VREYSRVARR QDGSWPQFRS
APLGKCPFID EPPSRKEYDR HRLRQLHKEK KAASHRADGT RDAKPKAAPP VQAPESVTTT
EIAHSQPLTK QEDRVSPPIQ NEIQKPTFDE THERKSSESF IPPHFPRTGP FYTGREPAAS
GVQPSNMTSA IRSQMISSTA AAPGAKAGLS KEVHGLKRKV LEKGTGGFAA GSMAAPQRRG
DGFTTVPMKT NINPPGKPSL VNENEAKQSE GAGTKRQRDD KDEQKKPERR RDPKPGYCEN
CRDKFDDFEE HTLTRKHRRF AANSTNWAEL DALLSEIQRP LKGEYEYDE
//
