ID A0A8J8WL76_9EURO Unreviewed; 640 AA.
AC A0A8J8WL76;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=PECM_002663 {ECO:0000313|EMBL:KAF7718279.1};
OS Penicillium ucsense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=2839758 {ECO:0000313|EMBL:KAF7718279.1, ECO:0000313|Proteomes:UP000631181};
RN [1] {ECO:0000313|EMBL:KAF7718279.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S1M29 {ECO:0000313|EMBL:KAF7718279.1};
RA Lenz A.R., Galan-Vasquez E., Balbinot E., De Abreu F.P., De Oliveira N.S.,
RA Da Rosa L.O., De Avila E Silva S., Camassola M., Dillon A.J.P.,
RA Perez-Rueda E.;
RT "Gene regulatory networks of Penicillium echinulatum 2HH and Penicillium
RT oxalicum 114-2 inferred by a computational biology approach.";
RL Front. Microbiol. 0:0-0(2020).
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:KAF7718279.1}.
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DR EMBL; WIWV01000017; KAF7718279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8J8WL76; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000631181; 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 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:UP000631181};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 583..632
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..454
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 569..588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 71634 MW; 2B95B812194BB581 CRC64;
MAAVFVPPSP RTSMNMSTRR PLANVPNATN SPHRTGLVPA KRARSGQVDI PFGQPPPKKH
VMDAVEQDRN RLIVPQGPES KLFARRSNNA NPSAFEKKLV AAREKERVTQ PKTKNDRPAA
DTIDTIRQWQ RHYRKAFPQF VFYFDSIPED VRCKFSRQVV ALGACEEKFF SRLVTHVVTA
RSIPPEAAHT NNPAGDTSNE TNGASGDHTQ TVNPSLLEKN GDGHLQVSLK IEGRRDQGSM
DVLQRARQMG MKIWALEKLQ RMITTINDND IGGQSENVSR SKQVGASTAH GKGENDLSRV
LRQELLNGPS DRDPFASMEM VVFKGPFIYI HDMNEKTKPV MVREYARVNR RQDGAWPQFR
SAPLGKCPFI DEPPSRKEYD RQRLRQAQKE KKIALQTVEE LKTKASTSVK ANTQTQRPTD
KKPLGDVSKA DEPPIKKEVF AKPSLEDINE RKSSESLIPP HFPRTGPFYS GREPAASGVQ
PSNVTSAIRS QMISSTAAAP GAKAGLSKEV HGLKRKVLEK GTGSIVPGSM AAPQRPNHGS
GSFCKQADVK KVSIGETNTQ GDATSTKRRR DDVVAPQKVE RKRDPKPGYC ENCRDKFDDF
EEHTMTRKHR RFAQNSSNWN DLDALLFDIQ RPKEEWDWES
//
