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Database: UniProt
Entry: A0A1E5R2B3_9ASCO
LinkDB: A0A1E5R2B3_9ASCO
Original site: A0A1E5R2B3_9ASCO 
ID   A0A1E5R2B3_9ASCO        Unreviewed;       904 AA.
AC   A0A1E5R2B3;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   18-JUN-2025, entry version 30.
DE   SubName: Full=DDK kinase regulatory subunit DBF4 {ECO:0000313|EMBL:OEJ80703.1};
GN   ORFNames=AWRI3579_g4259 {ECO:0000313|EMBL:OEJ80703.1};
OS   Hanseniaspora osmophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycodales; Saccharomycodaceae; Hanseniaspora.
OX   NCBI_TaxID=56408 {ECO:0000313|EMBL:OEJ80703.1, ECO:0000313|Proteomes:UP000095728};
RN   [1] {ECO:0000313|Proteomes:UP000095728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AWRI3579 {ECO:0000313|Proteomes:UP000095728};
RX   PubMed=27856586; DOI=10.1128/genomea.01287-16;
RA   Sternes P.R., Lee D., Kutyna D.R., Borneman A.R.;
RT   "Genome sequences of three species of Hanseniaspora isolated from
RT   spontaneous wine fermentations.";
RL   Genome Announc. 4:E01287-E01287(2016).
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:OEJ80703.1}.
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DR   EMBL; LPNM01000011; OEJ80703.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E5R2B3; -.
DR   FunCoup; A0A1E5R2B3; 190.
DR   STRING; 56408.A0A1E5R2B3; -.
DR   InParanoid; A0A1E5R2B3; -.
DR   OrthoDB; 3973118at2759; -.
DR   Proteomes; UP000095728; Unassembled WGS sequence.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IEA:TreeGrafter.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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   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; 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   PROSITE; PS51265; ZF_DBF4; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:OEJ80703.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095728};
KW   Transferase {ECO:0000313|EMBL:OEJ80703.1};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00600}.
FT   DOMAIN          853..902
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51265"
FT   REGION          273..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          654..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   904 AA;  99972 MW;  E7364892F4CF7555 CRC64;
     MNNFASTGST RRIPLGETNA NQLSLSQTGS LSQKANLAAS TVTKKHNYQF FKDNWEHTKA
     KPVADPQSNS RDSEHGLANM QEDTEVDVTD AAAENGDGPL HDAPEALQQN QNFQKGDEHD
     ASLLACGVVG QDKNSLVQIT PKDSTSYRKR LSESLDRQTH NNACALEEGA RRKLTTAEFL
     RKNSGQIAVD AIDAEYQEEK KTSVLDDPMY LSKNKHIATP ITKSRRSIGG ASLVNPMYTK
     ILPIQSTVQN IGGKPTLTTV SDKEQTNVEM GKVTNKNTTS GNTTTSRSVG ATGTTGVSGT
     AKNSAAMNLK VWQTNWKNIM KKETVIYFDI QEGVATGGKT GAQEMKTLRE KDSTKALIAL
     ETLRLGYYSL GAAVSKFFDR EVTIVITDRS NDASFIKSLS ESDVLKKASK NDMKIWTLEK
     AERFLTHLDV DISKMKKKAL NSAALGNASK NGLVSKFGNA IVAAQTTTET GTLRRYLQNE
     KLYGPMDRDP LAKRDDMHYF SKDRPHIYIY DLNQQFSPLV IMEWKTNKSN SEPGNDLSKD
     GAGTKNDADL PYPTLKNSTF GRCPFIADNE DETSDKRIFK RLKKDMNQQD QAEFLLRLYS
     TTAVPNPMND IYLLNHDKYN DSGKNFYKKF GYHFDELPFA KNNKNSEKSI GKVKIHEPKT
     PANKNAQQDN QKSNSPKNNS DMGEDGESPK LPQKVVWKRP PLKNKVNIEN LLRMETTGLD
     DSNGFNGVGK NDTATGASFA GKKRPMLSEI KASGVLNNDP INNSSTQPFQ ANNGLAATKS
     TVVGKQMNAL NSKFVVMDPV PANCNVPKTP STHVSVPLKP KERIAGSKIS LGNKSPVTRK
     PNTIAINAAI RDKRMGGGYC ENCRVKYESL RLHIKTEKHL EFAQKDQNFY AIDSLIENLH
     SSMY
//
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