ID A0A9P6X0H5_RHIOR Unreviewed; 587 AA.
AC A0A9P6X0H5;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 11.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=G6F64_010735 {ECO:0000313|EMBL:KAG1302666.1};
OS Rhizopus oryzae (Mucormycosis agent) (Rhizopus arrhizus var. delemar).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=64495 {ECO:0000313|EMBL:KAG1302666.1, ECO:0000313|Proteomes:UP000716291};
RN [1] {ECO:0000313|EMBL:KAG1302666.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GL11 {ECO:0000313|EMBL:KAG1302666.1};
RX PubMed=33245689; DOI=10.1099/mgen.0.000473;
RA Nguyen M.H., Kaul D., Muto C., Cheng S.J., Richter R.A., Bruno V.M.,
RA Liu G., Beyhan S., Sundermann A.J., Mounaud S., Pasculle A.W.,
RA Nierman W.C., Driscoll E., Cumbie R., Clancy C.J., Dupont C.L.;
RT "Genetic diversity of clinical and environmental Mucorales isolates
RT obtained from an investigation of mucormycosis cases among solid organ
RT transplant recipients.";
RL Microb. Genom. 6:0-0(2020).
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:KAG1302666.1}.
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DR EMBL; JAANQT010002326; KAG1302666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P6X0H5; -.
DR OrthoDB; 21380at2759; -.
DR Proteomes; UP000716291; 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; 1.
DR Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
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; 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:UP000716291};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 538..587
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..12
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 66758 MW; D78AD5A23F33603B CRC64;
MNFTSNISSN KVANKVDSSQ ASRSAARDAD LRRRLLQKQH QVAQQQQQQP QEITPPPQAN
TSKKISPLEI QKKKKQFQKF RFFLYKLDLD LETKLARKIF LLGATRETFF SAKCTHVITN
SKLLPNSQTN NTSASPEQSN AANKTLEDLT IQNARKWGLQ IWSGEGALKI VNILMESSTA
TAKAHERASR DDKKPHFVEF TGHYVLIEDA TQVHCPVLVK EYTKELITDK PALIPWPTLR
KKRSKAQTDA KATAEDQQND QGSKEKERLG TKAAAQSPAE ENDKAANQKK VKNAERTRGA
QETKQAENTK DQASSPESPN QEKTKKSIVS GQQHRLLNER RNPDKSDVRD YENKQNQITG
EIKAQAIKKQ RCNDEIKYSN KLVVDELKTD RLNREYAVIS TLAGSSTVQT DVGKSTQSDS
NKDEAKTEDS KQPSKEQVKA KGLVQIDLYK RESKVDESKS TGLQEKVEDA DGPKQTDVNK
EQIKMDESKQ ADSIKKEDKD NDSKHPDSNK EERKTDEKKT ELEKLRLEQK QRAAKRKRNA
DLQFCENCNE KFTVLADHIK SSKHAAFVKN SENFYELDQL LKRLKRR
//