ID A0A9P6YU11_9FUNG Unreviewed; 587 AA.
AC A0A9P6YU11;
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=G6F50_010980 {ECO:0000313|EMBL:KAG1564486.1};
OS Rhizopus delemar.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=936053 {ECO:0000313|EMBL:KAG1564486.1, ECO:0000313|Proteomes:UP000740926};
RN [1] {ECO:0000313|EMBL:KAG1564486.1, ECO:0000313|Proteomes:UP000740926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GL24 {ECO:0000313|EMBL:KAG1564486.1,
RC ECO:0000313|Proteomes:UP000740926};
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:KAG1564486.1}.
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DR EMBL; JAANIU010002603; KAG1564486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9P6YU11; -.
DR Proteomes; UP000740926; 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:UP000740926};
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..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..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 290..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 337..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..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..523
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 587 AA; 66520 MW; 1C2C7405EC30BEFE CRC64;
MNFTSNISSN KVANKVDSSQ ASRSAARDAD LRRRLLQKQH QVAQQQQQQP QESTPPPQPN
TSKKISPLEI QKKKKQFQKF RFFLYKLDLD LETKLARKIF LLGATRETFF SAKCTHVITN
SKLLPNSQTN STSACPEQSN ATNKTPEDLT IQNARKWGLQ IWSGEGALKI VNILMESSTA
TAKAHERASR DDKKPHFVEF TGHYVLIEDA TQVHCPVLVK EYTKELITDK PALIPWPTLR
KKRSKAQTDA KAAAEDQQNG QESKEKEKLG TTTAAQSPAE GNDKTVNQKK AKDAERTRGA
QETKQEENTK DQASSPESPD QETTKKSIVS GQQHGLLNER RDPDKSVVRD CENKQNQTSG
EIKAQAIKKQ WCNDENKYSN ELAVYELKTD RLNREYAVIS TLAGSSTVQT DVGKSTQPDS
NKDEAKTNDS KQPSKEQAKA KDLVQINSYR RESKVDESNS TGLQEKDEDA DGSKQTDVNK
EQIKIDEAKQ ADSIKKEDKN NDSNHPDSNK EDRKTDEKKA ELEKLKLEQK QRVAKRKRHA
DLQFCENCNE KFTVLADHIK SPKHAAFVKN SENFYELDQL LKRLKRR
//
