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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//