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Database: UniProt
Entry: A0A9P1HB96_9PEZI
LinkDB: A0A9P1HB96_9PEZI
Original site: A0A9P1HB96_9PEZI 
ID   A0A9P1HB96_9PEZI        Unreviewed;       488 AA.
AC   A0A9P1HB96;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=PPNO1_LOCUS9013 {ECO:0000313|EMBL:CAI4219452.1};
OS   Parascedosporium putredinis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Microascales; Microascaceae; Parascedosporium.
OX   NCBI_TaxID=1442378 {ECO:0000313|EMBL:CAI4219452.1, ECO:0000313|Proteomes:UP000838763};
RN   [1] {ECO:0000313|EMBL:CAI4219452.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Scott C., Bruce N.;
RL   Submitted (NOV-2022) to the EMBL/GenBank/DDBJ databases.
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:CAI4219452.1}.
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DR   EMBL; CALLCH030000020; CAI4219452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9P1HB96; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000838763; 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:UP000838763};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          423..472
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          42..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        70..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  54869 MW;  5989BA784400598A CRC64;
     MVFFFDSVPD DIRAKLVKHI TYLGAREEKF FSIDVTHVVT TRSLPQPNPS TELDASRATR
     SKRGDDAEEQ PQTINPSLLD CSSESRRRML FELGNRRAQP QDDLARLKPA RNNDVLCKAR
     DLGKRIYTLE KLQRILDSLL EGDPYASRSA HPREQSRGDD LAKLLRRERL NGPSDRDPKA
     VTKELNYFRG PYIYVYDMDE KTKPIMVREY PKVADKTDGE WPQFKTVSQG RCPFVDESLA
     EAKLVRRAME RKAAKEAAAK AAAVAERDVT QKPTEPLALR VPGKRTREEY GDPLAETKDG
     QNRMVYSVRP TDIFNPPKDL SSVKHIDFTS QKFFTGRAGT GRIFAGEPVA SGVQPSNVTS
     AIRSQAISSN AGMPGAKAGT SKELHNLQKK VLQKAAPAAR ANDADSHRVG ASLSMDAPSS
     QQKDMKPGYC ENCMDKFDDF DEHIVSRKHR KFADSLDNWA ELDELLKALK RPVKYSHLDD
     GEINVHPW
//
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