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Database: UniProt
Entry: A0AAD9HNT5_9PEZI
LinkDB: A0AAD9HNT5_9PEZI
Original site: A0AAD9HNT5_9PEZI 
ID   A0AAD9HNT5_9PEZI        Unreviewed;       641 AA.
AC   A0AAD9HNT5;
DT   29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2024, sequence version 1.
DT   28-JAN-2026, entry version 8.
DE   SubName: Full=Dfp1/Him1 {ECO:0000313|EMBL:KAK2031447.1};
GN   ORFNames=LX32DRAFT_661868 {ECO:0000313|EMBL:KAK2031447.1};
OS   Colletotrichum zoysiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1216348 {ECO:0000313|EMBL:KAK2031447.1, ECO:0000313|Proteomes:UP001232148};
RN   [1] {ECO:0000313|EMBL:KAK2031447.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MAFF235873 {ECO:0000313|EMBL:KAK2031447.1};
RG   DOE Joint Genome Institute;
RA   Baroncelli R., Diaz J.F., Benocci T., Peng M., Battaglia E., Haridas S.,
RA   Andreopoulos W., Labutti K., Pangilinan J., Floch G.L., Makela M.R.,
RA   Henrissat B., Grigoriev I.V., Crouch J.A., De Vries R.P., Sukno S.A.,
RA   Thon M.R.;
RT   "Comparative genomics, transcriptomics and evolutionary studies reveal
RT   genomic signatures of adaptation to plant cell wall in hemibiotrophic
RT   fungi.";
RL   Submitted (JUN-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:KAK2031447.1}.
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DR   EMBL; MU842840; KAK2031447.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0AAD9HNT5; -.
DR   Proteomes; UP001232148; 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:UP001232148};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          575..624
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          163..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          622..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        58..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..94
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..391
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        530..540
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        557..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  72229 MW;  B026B4CC2FCF3972 CRC64;
     MSARRTPLSS NPNVANSPLR AASAMAQAKQ KRSHANIQRE ELYAQPPPYK KQAIENAGSR
     QLRSPSKVTK ASQLPQRVGR PVTKERSTHH DDASVERIRQ WQAEYRGRFP KMVFYFDSVP
     EDQRAKLSRH AQSLGARDER FFSSSITHVV TARPIPAQED VQATAHDTGP EEQPQTINPS
     LLDRSTDARR RLLLETTSRR AHAHMQPQDD RTRRTRSTQS NDVLHKARDM GKKIWSVEKF
     QRMLQFLLEP DPHVVAAYGA KGEPVRNLGT KRTTEEPGLL QLLQHERLNG PSDAVTSREM
     INFKGPYIYV YDIDEKQKPI MVREYPKVNN KYDGEWPQFR TVTDGRCPFV EEPEPAERPG
     RKPSTQQKEK NEPKEQKERP ATKAAAEERQ SLHPPEIPAP KAVIGKRTLS EMQDEQHRAG
     SAAKPMDVFN PPKAVVSNPI DFGRTQNAFT GRTGSGRFFA GEPVASGVQP SNITSAIRSQ
     MISSTSGING AKAGTSKEVH GLQRKVLQRG APTPPDASSR RLTEMSLEAT STRSTSVSRT
     TSRRMELIEE DPDKQSSKLS RTSSKTAAPA PKNRRDLKPG YCENCQDKFK DFDEHILTRK
     HRKFAENSDN WAELDELLSQ LGRAPRYSKH SHHDGYADES L
//
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