ID A0A9P6FJH2_9FUNG Unreviewed; 1313 AA.
AC A0A9P6FJH2;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 18-JUN-2025, entry version 10.
DE RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN ORFNames=EC957_008186 {ECO:0000313|EMBL:KAF9551517.1};
OS Mortierella hygrophila.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mortierellomycotina;
OC Mortierellomycetes; Mortierellales; Mortierellaceae; Mortierella.
OX NCBI_TaxID=979708 {ECO:0000313|EMBL:KAF9551517.1, ECO:0000313|Proteomes:UP000723463};
RN [1] {ECO:0000313|EMBL:KAF9551517.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NRRL 2591 {ECO:0000313|EMBL:KAF9551517.1};
RX PubMed=33364917;
RA Vandepol N., Liber J., Desiro A., Na H., Kennedy M., Barry K.,
RA Grigoriev I.V., Miller A.N., O'Donnell K., Stajich J.E., Bonito G.;
RT "Resolving the Mortierellaceae phylogeny through synthesis of multi-gene
RT phylogenetics and phylogenomics.";
RL Fungal Divers. 104:267-289(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:KAF9551517.1}.
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DR EMBL; JAAAXW010000004; KAF9551517.1; -; Genomic_DNA.
DR Proteomes; UP000723463; 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:UP000723463};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 598..647
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT REGION 138..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 820..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 923..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1018..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1193..1225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..746
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..761
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..836
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..888
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..936
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1033
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1071
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1092
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1157..1175
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1313 AA; 144811 MW; 7FFD741352269C8D CRC64;
MADRPLKPAL QRAPLQESRA YSNINHLRQQ HYGINTFNPH HGLVNKPSQD VSFTRSSSAH
LPVKPTMAPH MDKDTTRQRI ALQQKPFTWN NAQNIKAPPG PARIPSNPMH KTKPVPFPGF
TSTTPSYTRS DANIENQCRS QSQHTDYAQH LPQPQDTEPR SQTKHKNRVN AEYGSPEWTQ
QMANILPRCR FYFDSVDPSM IKKISDVVRR HKGTTTSFFS NEVTHIITTR PVPDESVLER
IRNHDNTEQS PAAQLDPRKT TAKPLNHQVP NAEMGILVKA LSLGIKIWTL DSTLKLLDPL
APGLAKQTDD RKLKDMLQYE KVHGVSTVHI DNSTKPDFYA FQGKYVLVDD TTGYYRTIMA
YDFTAKPSPT GKQPWPRLYI QDSDRSPFCL IEPAIKASER LSGARDDKGQ EIKQDKDLPN
AVQDARPADD QKLSPSAMAS GLVNSITSNI ISTTTSTASK PAAANLQQNR RVEQLEKRAL
NATKVEVGVS TDFVKKQEFA RPLDVARQDK GSATVGGATQ DIVPGRETIA DAESKMQPPT
LPVKHSSGLA ISANNERAVA QGHDNLVPVR REANNALSVH PVLEIPVSHT AKHKEAKDYR
KQRYCENCRG FFENFEKHIE SPAHRKYAHD ASKFAQLDIL LAKLQRKPNI SSGLSELPTT
SPALAESELS DSTSLDAAFG IPVTPALDPV GEVNIQEGMD TTPHTQELSI AVNMPTLHPE
QDVSRGQGEI VQETQETTER PRGRQDVDDE GIVEDMDEEG APGETGDQVT LTLEPPRNAV
EAFDIADELS SEMSQLGLSE RGVDRFSDQL NDAEYVAPFE APEEEQEEQE EEEETVVETV
PPSDLLEDKV AAPTSLQKVL RHEFRLPCSE RSGLSDSNAT SQLETDTTQP DDRFLDRSAS
ATASIDDGLS TPVRLCFDTS STVASPNASR TINQAPFSPE ALNESDREGS DDGVSLVKSP
SAGRGHFGRN QGVGLRDELF TPNRIALDAS MFSPCKDITS GLYKGALKRK LDNVLAEERA
AGRSQSRAGT TVETPDASRY AGQLISRKHL SNTGAPQQLS NSSHAASTPL RSESWVIHSP
SRSSTRTSSP MSPHEPLELL FQTSPPLASQ PHQAAVDPSY QRQAQLASGY FHPSLSSQLE
YESPLLTHWE PRRHGQSTDS QQTPPPLQSQ QRSQQGGVPI APFQDYLMRD ESETHAKPGH
PGPVVTSRRE PEAPSTSQSS PIAFSSPEGL CSPVIYMSQG YGFSSPSQSP SRRAQRKFFP
VMTHAEQEEE RVYQHYHGNQ LPEPAGGQKK MRSSSSLAEA YEEYGEGAMV FIE
//
