ID R1GN73_BOTPV Unreviewed; 547 AA.
AC R1GN73;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 28-JAN-2026, entry version 49.
DE SubName: Full=Putative g1 s regulator protein {ECO:0000313|EMBL:EOD47424.1};
GN ORFNames=UCRNP2_5847 {ECO:0000313|EMBL:EOD47424.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD47424.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
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DR EMBL; KB916331; EOD47424.1; -; Genomic_DNA.
DR AlphaFoldDB; R1GN73; -.
DR STRING; 1287680.R1GN73; -.
DR KEGG; npa:UCRNP2_5847; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_0_0_1; -.
DR OMA; ARFPKMV; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000013521; 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; 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 PROSITE; PS51265; ZF_DBF4; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 496..545
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..302
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 61289 MW; 0CE245BFAED7B028 CRC64;
MASRRVPLAN VPNATNSPYR PNAATATKRS RSHASEQRES AYNGQPPAKK QFFEENDTEA
RRQALLKKAG QTQSVQKKLD AARDVRPSQK PVERTQKSAQ DNYDTIRQWQ KHYRKVFPHV
FQDAETRTRS SNNGDILIKA REMGMKIWAL EKLERILNTM FNTETGEQPP AYNTRGNTAV
NASKTRGADL SQLLKNEKVN GPADRDLAVS TKDMAHFRGY YVYIHCMNEK YRPVIMRDYP
KTATKEDGKW PQFRLTAAGR CPFVEDPQHL RKLQFQDQQK TTQQRADRAA SAAPRTRSAS
AALEAAKQRI APKTEERRAL TESKNTTRRT SATEESTDTI VSKPLEPPKL IPAKRREPDG
MPPLFGSAQA SLRGIPRYAG GEPVASGVQP SNITSAIKSQ MISSTAAAPG ARAGTSKELH
QLSRKVLEKN SAPNSTTSSY MTDIRAAING DRAPPPRAAK RKAQETITGA QDNSEEAEKQ
STRRVIIARS KKPIEKDPKP GYCENCREKF DDFDTHIIGR KHRKFATTPD NWKDLDSLLS
ELTRPLL
//