ID A0A010Q574_9PEZI Unreviewed; 635 AA.
AC A0A010Q574;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 28-JAN-2026, entry version 43.
DE SubName: Full=Dfp1/Him1 {ECO:0000313|EMBL:EXF74987.1};
GN ORFNames=CFIO01_05131 {ECO:0000313|EMBL:EXF74987.1};
OS Colletotrichum fioriniae PJ7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum acutatum species complex.
OX NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF74987.1, ECO:0000313|Proteomes:UP000020467};
RN [1] {ECO:0000313|EMBL:EXF74987.1, ECO:0000313|Proteomes:UP000020467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PJ7 {ECO:0000313|EMBL:EXF74987.1,
RC ECO:0000313|Proteomes:UP000020467};
RA Baroncelli R., Thon M.R.;
RT "The genome sequence of Colletotrichum fioriniae PJ7.";
RL Submitted (FEB-2014) 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:EXF74987.1}.
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DR EMBL; JARH01000934; EXF74987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A010Q574; -.
DR STRING; 1445577.A0A010Q574; -.
DR KEGG; cfj:CFIO01_05131; -.
DR eggNOG; KOG4139; Eukaryota.
DR HOGENOM; CLU_017715_0_0_1; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000020467; 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:UP000020467};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 568..617
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 23..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 56..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..635
FT /note="Disordered"
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..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..533
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 635 AA; 71772 MW; 4FE391FDF762E6DD CRC64;
MSTRRTPLSS NPNVVNSPLR AASALAHAKQ KRSHANIQRE ELYAQPPPFK KQVVENVGSR
QLRSPSKVTK ASQLPQRVGR PITKERSTHH DDSSNVERIR QWQAEYRGRF PKMVFYFDSV
PEDQRAKLAR QAQSLGARDE RFFSSSITHI VTARPIPAQE DVQAAAHDTE LEEQPQTINP
SLLDRSTDAR RRLLLETTSR RAQAHDDRTR RTRSTQSNDV LHKARDMGKK IWSVEKFQRI
LQFLLEPDPH VVAAYGANRD SARNVGTKKA TEEPGLLQLL QHERLNGPSD AVTSREMINF
KGPYIYIYDI DEKQKPIMVR EYPKVNNKYH GEWPQFRTVT EGRCPFVEEP EPVERPSRKP
STQQKDPKEH KEHVAKPAAE ESPSLQPPEV PAPKAAVGKR SLSEMQEGQN KLRAAMKPMD
VFNPPKAVVS NPIDFGRTQH AFTGRTGNGR FLAGEPVASG LQPSNVTSAI RSNMISSTSG
INGAKAGTSK EVHGLQRKVL QRGAPVPQDA SSRRLTEMSL EATSTRSTSV SRTTSRRMEL
IEEDAEKQSS KLSRTSSKTQ APPAKSKRDL KPGYCENCQD KFKDFDEHIL TRKHRKFAEN
TDNWAELDDL LSQLGRVPRY RSKHSRDDEY TDDSL
//
