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Database: UniProt
Entry: A0A9P8VI57_9PEZI
LinkDB: A0A9P8VI57_9PEZI
Original site: A0A9P8VI57_9PEZI 
ID   A0A9P8VI57_9PEZI        Unreviewed;       630 AA.
AC   A0A9P8VI57;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 12.
DE   SubName: Full=Dfp1/Him1 {ECO:0000313|EMBL:KAH6690712.1};
GN   ORFNames=F5X68DRAFT_221216 {ECO:0000313|EMBL:KAH6690712.1};
OS   Plectosphaerella plurivora.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Plectosphaerella.
OX   NCBI_TaxID=936078 {ECO:0000313|EMBL:KAH6690712.1, ECO:0000313|Proteomes:UP000770015};
RN   [1] {ECO:0000313|EMBL:KAH6690712.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MPI-SDFR-AT-0117 {ECO:0000313|EMBL:KAH6690712.1};
RA   Mesny F., Miyauchi S., Thiergart T., Pickel B., Atanasova L., Karlsson M.,
RA   Huettel B., Barry K.W., Haridas S., Chen C., Bauer D., Andreopoulos W.,
RA   Pangilinan J., LaButti K., Riley R., Lipzen A., Clum A., Drula E.,
RA   Henrissat B., Kohler A., Grigoriev I.V., Martin F.M., Hacquard S.;
RT   "Genetic determinants of endophytism in the Arabidopsis root mycobiome.";
RL   Nat. Commun. 0:0-0(2021).
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:KAH6690712.1}.
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DR   EMBL; JAGSXJ010000006; KAH6690712.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9P8VI57; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000770015; 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; 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:UP000770015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          552..601
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          349..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          603..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..74
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..188
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        189..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        364..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        603..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   630 AA;  71734 MW;  728886DCB69FBAA9 CRC64;
     MSTRRTPLTN NPNVVNSPLR TAALPQVKGK RSYATVQRED IYGQPPPLKK QTLEAFPQRP
     PRSPSKSSRA SGLPQRTARP VVRERTQQPQ QHQVQHENAE RIRQWQVEYQ SRFPKMVFYF
     ESISEELRAK LSKQAISLGA REERFFSNAI THVVTTRPIP TSNEEAHATH EEPAPEEQPQ
     TINPSLLDRS TDTRRRLFDA VTRRATPLQS HEDSTRRPRP VRNNDILHKA RDMGKRIWPL
     EKFQRMLDIL LEPEAYVNRT ESSRNGAGVK RAAEEPKLSQ LLQHERINGP SDRDQTVTAR
     ELVPFKGPYL YVYDIEEKYK PIMLREYPKV NNKYEGEWPQ FRTVADGRCP FVEEPDNDRR
     KARAEKEKEK ERAAKAAAES RPTLQPPEVA APKPVVGKRS LTEMQDGQNQ LRTGVKPMDM
     FHATKPLSKQ VDLSGFTSRA PAARLFAGEP VASGVQPSHL TSAIRSQMIS SASGMGAIKA
     GTSKEILGLQ RRVLQRTTNS QDPSSRRPEA ELDPSSRSTS MGRVASRRLE LIEEGTDKAS
     SKPQPAPQKS RRDLKSGYCE NCQDKFKDFD EHVLSRKHRK FADNDDNWAE LDGLLSQLSR
     APKWEPAPRW ETDATSVEFD HNSSGEYQPW
//
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