ID S3BZR9_OPHP1 Unreviewed; 824 AA.
AC S3BZR9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 18-JUN-2025, entry version 39.
DE SubName: Full=G1 s regulator {ECO:0000313|EMBL:EPE06022.1};
GN ORFNames=F503_02851 {ECO:0000313|EMBL:EPE06022.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE06022.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE06022.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE06022.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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DR EMBL; KE148154; EPE06022.1; -; Genomic_DNA.
DR AlphaFoldDB; S3BZR9; -.
DR STRING; 1262450.S3BZR9; -.
DR VEuPathDB; FungiDB:F503_02851; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_0_0_1; -.
DR OMA; DRKHRKF; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000016923; 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; 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:UP000016923};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 766..815
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..26
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..162
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..692
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..708
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 91005 MW; 5AE3646AE55267AE CRC64;
MAAVSLSPTP HVPYTAAMSS SMSSRRVPLS VNSNAANSPL RTGNGNGNGS GTASNSLTAA
LYAKQHQQRR SHASMQREDS YGQAPPAKKQ MVEKADLHVS ATVTNARVSG LRSPTLSRRV
PQVQRASTST RAYHQAERVS SHQQQQQQQQ SHAHQQQSQQ QSHHNRRQEY QKISEREAEE
VRRWQESQRL RFPKLVFYFD NLPEDQSARL SKQVNHLGAR EDKFFSIDIT HVVTTRSIPP
EEKAAPKQQQ QQQALRTKEA NAEHAPEANH EHVQTINPSL LSRNHVNELG ITTTSLPVKR
KLFDTAPGRR MPLAPFGAVE DAIRKPKPTR STDILQRARE MGKKIWSLEK LQKVLDMLLE
PDPYRSAELG QRMRNGSTTN GAAVSQQGNS RFTGDQALLQ MLDKERHTGP SDRDPTVATR
ELIYFKGYYL YVYDIEEKQR PIMVREYAKV ADREEGDWPQ LRPSADARCP FIEDTDQLEL
RAEKKRARMR STATNSRDAA VAGTASGGTS MQKTLASRYA ATANGSVAAK QATGKRTLAE
MEDGHNRQMT STGTNALAGA PSLRPVEGVF GGSNAAASAG SMSSVASANP PTKAISTSRA
GSVEFQAQHA FTSRSKAGRY FAGEPVASGL QAAGITSAIR SQMISSATGT LGARAGTSKE
IHGLQRKVLQ KSTAIPTTST SQQHDHSSRR MTDSMGTDQQ QQQAQQPQRH NYSRSTSLAT
GTVVAAQLSA KLNQALDDSA TSTDDRQKRR TLSAPVVAQV ARAKKRDPKP GYCENCQDKF
DDFEVHIGTH KHRKFAEDER NWTDLDDLLG QLTRRTKYGF DEWQ
//
