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Database: UniProt
Entry: A0A9P6X0H5_RHIOR
LinkDB: A0A9P6X0H5_RHIOR
Original site: A0A9P6X0H5_RHIOR 
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
//
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