ID A0A9P9WDV3_9PEZI Unreviewed; 670 AA.
AC A0A9P9WDV3;
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=JX265_010545 {ECO:0000313|EMBL:KAI1859068.1};
OS Neoarthrinium moseri.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Amphisphaeriales; Apiosporaceae; Neoarthrinium.
OX NCBI_TaxID=1658444 {ECO:0000313|EMBL:KAI1859068.1, ECO:0000313|Proteomes:UP000829685};
RN [1] {ECO:0000313|EMBL:KAI1859068.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TUCIM 5799 {ECO:0000313|EMBL:KAI1859068.1};
RA Vignolle G.A., Hochenegger N., Mach R.L., Mach-Aigner A.R.,
RA Javad Rahimi M., Salim K.A., Chan C.M., Lim L.B.L., Cai F.,
RA Druzhinina I.S., U'Ren J.M., Derntl C.;
RT "Revisited historic fungal species revealed as producer of novel bioactive
RT compounds through whole genome sequencing and comparative genomics.";
RL Submitted (MAR-2021) 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:KAI1859068.1}.
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DR EMBL; JAFIMR010000035; KAI1859068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P9WDV3; -.
DR Proteomes; UP000829685; 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:UP000829685};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 602..651
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 38..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 529..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..426
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 670 AA; 75729 MW; A235ACFAC2A70D85 CRC64;
MSSRRMPLSS NQNVANSPIR ASAAAHAIVK PKRSLATLQR EEAYAHPPPA KKQALESGIP
RPLKSPSQQQ RLARTQLSLQ TRRNANSYET KLARERAGHH HGEATTTTTT TTSKYTERDL
EEIRQWQRHH RARFPNMVFY FDNIAEDVRG KLVKQITALG AREEKFFSIE ITHVVTTRSI
PVESRSSRQR QEDNTATTET HDDQEQLQTI NPSLLNRVSG QSVKRKLFDT TSTTQAPSRG
TFAQIQDARP KRSTDVLSRA REMNKKIWSL DKLQRMLSML LEQDLNVSAA IAYGSRSAAS
QSAHAQSRTA DEKSLLQLLH NERVNGPSDR DPTVATRELH YFKGPYIYVY DFEEKQKPIM
AREYNKVTDK SDGDWPQFRT APLGRCPFVE DYDHREVAKP KKREVVAKPA TGSKPVLQPP
EAPPSKPVTG KRSLSEMESA HNRGSSVAST EFNPPKLLAG KKFDFRPNAF SSRAGTARTL
FGGEPVASGV QPSHMTSAIR SQMISSTAAT PGTITGLSKE VHGLQRKVLQ RNSSHDLSSR
RTFGSVETSF KEDNDTKRSG TLARTSSRKL ELVDEKLAAE EEERDAKARR EMEKRLVKPK
KKDPKPGYCE NCADKFDDFD DHILSRKHRK FADNPENWGE LDELLSQLER EPKHKHYSAW
TPTLPEYPVY
//
