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Database: UniProt
Entry: A0A165KYI0_9APHY
LinkDB: A0A165KYI0_9APHY
Original site: A0A165KYI0_9APHY 
ID   A0A165KYI0_9APHY        Unreviewed;       583 AA.
AC   A0A165KYI0;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   18-JUN-2025, entry version 32.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0000259|PROSITE:PS51265};
GN   ORFNames=DAEQUDRAFT_679798 {ECO:0000313|EMBL:KZT63759.1};
OS   Daedalea quercina L-15889.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Fomitopsis.
OX   NCBI_TaxID=1314783 {ECO:0000313|EMBL:KZT63759.1, ECO:0000313|Proteomes:UP000076727};
RN   [1] {ECO:0000313|EMBL:KZT63759.1, ECO:0000313|Proteomes:UP000076727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L-15889 {ECO:0000313|EMBL:KZT63759.1,
RC   ECO:0000313|Proteomes:UP000076727};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV429158; KZT63759.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165KYI0; -.
DR   STRING; 1314783.A0A165KYI0; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000076727; 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:UP000076727};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          478..527
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          294..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..22
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  65905 MW;  F970D17DADC0DC94 CRC64;
     MSRKASGSSK RARSPEPSKD GDASQSMKRL KATVAPQPPA PTAREDLREE ARREKERKRA
     EREDEFRIKY TRAFPNWTFH FDLDTMNPDV AALKDTLERR LRQMGAAVED FFSRDITHLI
     TLDAEGSEKE NSTQPAASAM PSLLLSPIKL KGRATGDAPA TASERIAKKA LAFGIKVWTP
     TKLESVLDRC HAPAAYSTRA PARGPAAASR PLTRLLEEER TYGTTSERDP TQKRHGFTYF
     SKGTYFVLVE DMRQELATIA AAEYPIRKGR DGQEKPTWPV LYCHPLARGP FVPYDEREER
     RRERADRMDK EREQERAQRK ARLREEERRR QAQAMAKQHD LRRSASMHNL HRRASLPDAG
     FALDGYIDLD AEFGEGDIPS ANASGYLASG AYMAASGNSV GVTSTTGTTS AAGNTLRNLQ
     LPPGLRGRVQ QQVLTSRRVV SGAEGKEKMG PPPNIPEKPN MLRKSRSTNT LRLPKREEGV
     KPGYCESCRV KFEDFKQHIN GRRHRKYAMD ESNFHALDTI LSRVRRRTRA EVEEEKREWA
     MRYTTTHSDF DDVDEDATML PTVAASSDDD VRWNDWVDDG EEL
//
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