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Database: UniProt
Entry: A0A1Y1YSL8_9FUNG
LinkDB: A0A1Y1YSL8_9FUNG
Original site: A0A1Y1YSL8_9FUNG 
ID   A0A1Y1YSL8_9FUNG        Unreviewed;       676 AA.
AC   A0A1Y1YSL8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   28-JAN-2026, entry version 29.
DE   RecName: Full=DBF4-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=K493DRAFT_405696 {ECO:0000313|EMBL:ORY01011.1};
OS   Basidiobolus meristosporus CBS 931.73.
OC   Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota;
OC   Entomophthoromycotina; Basidiobolomycetes; Basidiobolales; Basidiobolaceae;
OC   Basidiobolus.
OX   NCBI_TaxID=1314790 {ECO:0000313|EMBL:ORY01011.1, ECO:0000313|Proteomes:UP000193498};
RN   [1] {ECO:0000313|EMBL:ORY01011.1, ECO:0000313|Proteomes:UP000193498}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 931.73 {ECO:0000313|EMBL:ORY01011.1,
RC   ECO:0000313|Proteomes:UP000193498};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
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:ORY01011.1}.
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DR   EMBL; MCFE01000075; ORY01011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y1YSL8; -.
DR   FunCoup; A0A1Y1YSL8; 159.
DR   STRING; 1314790.A0A1Y1YSL8; -.
DR   InParanoid; A0A1Y1YSL8; -.
DR   OrthoDB; 21380at2759; -.
DR   Proteomes; UP000193498; 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; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR055116; DBF4_BRCT.
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; PF22437; DBF4_BRCT; 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; PS50172; BRCT; 1.
DR   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193498};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          83..130
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          322..371
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          34..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          281..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          371..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        286..305
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        374..394
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        452..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  75641 MW;  D7AE9D866D9FA85A CRC64;
     MGRSTLSCYG EVAQTSAVWD QPNCNFRTSR KRVVEATSDS GSEQSDSVRV VKKPKRMKPS
     LDKVSPNATP KSSALDVAVW AKAYRKAFPN FLFYFDQIDE NVKQQLAPQI RRLGGRMEPF
     FSSKITHLIT CQSKSNESRY MSPSKSSRAF PMSPTASKTS VASELAQKAS KWGIKVWTTQ
     KLFNVLRHLL KSPMSSLSQP SKPLTDVLRD EKMFGISTHS SLSTNSSNVH FLKQIYLLVE
     DTTKAHRPIA VREYFGGGGG ITWPKIYRNT EGKCPFIKYE EEPKSSKTPQ ISSRHLNSNT
     AATPQPATPI SIATKPSPVI VIPKKPGYCE NCQAKFADLE EHVHSPIHCK YALDNSSYVE
     LDAILESVTR KAAPSLPVES PESDSESTVS SIVSGPAQEY TDVYQTTNDE GDLSDEGYAS
     LKTISDSEPT GDQSATQYDI KEPTPILGDH SGPTEDDPRV SCDHQQHPLE GTLAAEVENF
     DLDPYFTMEQ PQLYNPPQRH DFQSTQFAPE YMAQPFHDQH YAQTDYTLHQ VPTQEEIYAA
     IRDFQQYVQG DECAVPALEE TLYPPSVEPT YDALSAREAL YCPQVNYQPM SGYHEQPLSY
     GTGNDFLPNG GFLKPNQRMS IQELLLTDVG YFLNNGYPTT PQVDTWYPDN NNNNNNHHNH
     QASYLHSYVN SQFSVP
//
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