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Database: UniProt
Entry: A0A6P8AU65_PYRGI
LinkDB: A0A6P8AU65_PYRGI
Original site: A0A6P8AU65_PYRGI 
ID   A0A6P8AU65_PYRGI        Unreviewed;       668 AA.
AC   A0A6P8AU65;
DT   02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT   02-DEC-2020, sequence version 1.
DT   28-JAN-2026, entry version 23.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=PgNI_08740 {ECO:0000313|RefSeq:XP_030978447.1};
OS   Pyricularia grisea (Crabgrass-specific blast fungus) (Magnaporthe grisea).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX   NCBI_TaxID=148305 {ECO:0000313|Proteomes:UP000515153, ECO:0000313|RefSeq:XP_030978447.1};
RN   [1] {ECO:0000313|Proteomes:UP000515153, ECO:0000313|RefSeq:XP_030978447.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NI907 {ECO:0000313|Proteomes:UP000515153,
RC   ECO:0000313|RefSeq:XP_030978447.1};
RX   PubMed=30835262;
RA   Gomez Luciano L.B., Jason Tsai I., Chuma I., Tosa Y., Chen Y.H., Li J.Y.,
RA   Li M.Y., Jade Lu M.Y., Nakayashiki H., Li W.H.;
RT   "Blast fungal genomes show frequent chromosomal changes, gene gains and
RT   losses, and effector gene turnover.";
RL   Mol. Biol. Evol. 36:1148-1161(2019).
RN   [2] {ECO:0000313|RefSeq:XP_030978447.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NI907 {ECO:0000313|RefSeq:XP_030978447.1};
RG   NCBI Genome Project;
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:XP_030978447.1}
RP   IDENTIFICATION.
RC   STRAIN=NI907 {ECO:0000313|RefSeq:XP_030978447.1};
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
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DR   RefSeq; XP_030978447.1; XM_031128732.1.
DR   AlphaFoldDB; A0A6P8AU65; -.
DR   GeneID; 41963640; -.
DR   KEGG; pgri:PgNI_08740; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000515153; Chromosome V.
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   Reference proteome {ECO:0000313|Proteomes:UP000515153};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          599..648
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          182..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..429
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          539..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        193..203
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..223
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  74784 MW;  8B2CC9A44F541032 CRC64;
     MATVSLIPSP VSFHQTAMSS RSRVPLSSNP NAANSPMRPM AVAHPKPVKR SHASNQREEL
     YGQPPPAKKQ MISNPSTYRV TARSPVKART TTHTITQSRA VGGHRDRDAA SQQHVKAQLA
     DEDVNDFKKW AAAQKQQFVK HVFYFDNLPQ EVLPKIERQI AALGAREDKF FSISISHVVT
     TRPIPQPQTS QKPKLDVSTK TDRDEQEPQT INPSLLSRNL DSTCTKRKLF DTHPAGRRPP
     IQLGEDVVRR PKAPRQQNDI LGRALTMGKK IWSLEKMQRI LDMLTESDPY RAATLGQGGR
     TIKTVEQSNP LQMLNKERVS GPSDRDPTAS TKEMHIFKGP FIYIYDIEQK QRPIMAREYA
     KVADKMKGDW PQFRASGSGR CPFVEDHDQE KHPKKEREVT RQAAVNAAVG SAPKLQPPTQ
     ISRPKPITGK RPLAEMSEVS TNRILFPSKT TTGGNALMDS AQGSKLSKED ALSNAFISTN
     RSRPARIFAG EPVASGLQAS NITSAIRSQM ISSTTGTIAS NKSGVSKEVL GLQRKVLAKS
     GSISQDPSSR RHAEMSVDSG PLSRSTSLGN PRLIFEGEET QHRRTHSVPS KLQPKPKKRD
     PKPGYCENCQ DKFADFEEHI QSRTHRKFAE NDENWEDLDR LLQQLERQPL PHHHLYSDET
     VEQNYDQY
//
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