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Database: UniProt
Entry: A0A0P1BBY1_9BASI
LinkDB: A0A0P1BBY1_9BASI
Original site: A0A0P1BBY1_9BASI 
ID   A0A0P1BBY1_9BASI        Unreviewed;       908 AA.
AC   A0A0P1BBY1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Protein kinase essential for the initiation of DNA replication {ECO:0000313|EMBL:CEH13241.1};
OS   Ceraceosorus bombacis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX   NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH13241.1, ECO:0000313|Proteomes:UP000054845};
RN   [1] {ECO:0000313|EMBL:CEH13241.1, ECO:0000313|Proteomes:UP000054845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA   Brescovit A.D., Santos A.J.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CCYA01000206; CEH13241.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P1BBY1; -.
DR   STRING; 401625.A0A0P1BBY1; -.
DR   OrthoDB; 1342482at2759; -.
DR   Proteomes; UP000054845; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 6.10.250.3410; DBF zinc finger; 1.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR013939; Regulatory_Dfp1/Him1.
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   Kinase {ECO:0000313|EMBL:CEH13241.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW   Transferase {ECO:0000313|EMBL:CEH13241.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00600}.
FT   DOMAIN          722..771
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..305
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          376..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          813..908
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..305
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..406
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..856
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        861..886
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   908 AA;  99680 MW;  D670423839A52C28 CRC64;
     MTGRRPAPVP RQAPRRPLAE KNTIANTNPT QQDTAAAGPS KPRIAGARWA PATRSASVAP
     TENKEPSPAA DVQRAVCMTR SPQWPSVDLA ASSSTKRIHA DQEAAITPAA ASAERPVSRL
     PKPIISEKRQ KLATLQPAPT PVHPVPRTPR KRAVPQDDVH CRNRVQAGQH DEMDDLATAT
     GESPNKRSRS SKEDSDSSSH RRRMATDESQ KNSESTTASV TGHLVEVTMH DQPQELVQPS
     SNAQHGSRIH SQLARTLADV KQQEAARSPK TSQPAPVTTS RFLKQSGAKT HDSASREASK
     READGEWRRK YAKSFPTFIL YFDELSPSDL VEASTNAKRF GAIVAPFFSK DVTHLVSAHK
     HQSRRAPEPL RQALLKATPG DSFETRANHE AERSTRSAHR PGATKLARES RQQPLHSGSN
     PFEEATPAPP ESSIVKKARD FNIRVWSHEK FCSIIAALDG AQVPAQAHDP DKRRRNLSQM
     LQQEKLQGTS ERDPTAPRSD YHYFDKNSCY ILVEDATCEH RVLFTQEFKR PRADEDPPWP
     KLYGQREGRC PFTRWESRPN ARATANRHET LRRTRSMTDV ARGAVSSRLK HGSHSPQPVP
     FNLEKARPEA ASMRGASPYP MASGNSIALT SNIHSTTSTA AGTHTIGFAG QGALDRRLVT
     LTDRGLPSPL AGPAGSAVAS ALPRHMTFAS HISPRGIMRR AVSTATGLAQ RQALAAKDKE
     APKSKPGNCE NCRTKYDDFD EHVASNKHRR FALNDSNFVE LDEFLAGVER QSALWCVEMM
     EEAERYREDT GEYTDELQED VMDVSESFGT SWPVAEDDYM TDGTSGTNQY TNIMEDPSMD
     NTDNTSTSTH TSPDAQRSRG VPEPKMSRDA GDRPTSRIEH ADVHDSLGLH GTGVPSAPGS
     DSKSDSCG
//
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