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Database: UniProt
Entry: P32325
LinkDB: P32325
Original site: P32325 
ID   DBF4_YEAST              Reviewed;         704 AA.
AC   P32325; D6VS39; P32355;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   07-APR-2021, entry version 178.
DE   RecName: Full=DDK kinase regulatory subunit DBF4;
DE   AltName: Full=Dumbbell forming protein 4;
GN   Name=DBF4; Synonyms=DNA52; OrderedLocusNames=YDR052C;
GN   ORFNames=D4205, YD9609.07C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204626 / S288c / A364A;
RX   PubMed=1592236;
RA   Kitada K., Johnston L.H., Sugino T., Sugino A.;
RT   "Temperature-sensitive cdc7 mutations of Saccharomyces cerevisiae are
RT   suppressed by the DBF4 gene, which is required for the G1/S cell cycle
RT   transition.";
RL   Genetics 131:21-29(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1514326; DOI=10.1002/yea.320080405;
RA   Solomon N.A., Wright M.B., Chang S., Buckley A.M., Dumas L.B., Gaber R.F.;
RT   "Genetic and molecular analysis of DNA43 and DNA52: two new cell-cycle
RT   genes in Saccharomyces cerevisiae.";
RL   Yeast 8:273-289(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8789263;
RX   DOI=10.1002/(sici)1097-0061(199601)12:1<85::aid-yea890>3.0.co;2-u;
RA   Brandt P., Ramlow S., Otto B., Bloecker H.;
RT   "Nucleotide sequence analysis of a 32,500 bp region of the right arm of
RT   Saccharomyces cerevisiae chromosome IV.";
RL   Yeast 12:85-90(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=8474449; DOI=10.1128/mcb.13.5.2899;
RA   Jackson A.L., Pahl P.M., Harrison K., Rosamond J., Sclafani R.A.;
RT   "Cell cycle regulation of the yeast Cdc7 protein kinase by association with
RT   the Dbf4 protein.";
RL   Mol. Cell. Biol. 13:2899-2908(1993).
RN   [7]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=8066465; DOI=10.1126/science.8066465;
RA   Dowell S.J., Romanowski P., Diffley J.F.;
RT   "Interaction of Dbf4, the Cdc7 protein kinase regulatory subunit, with
RT   yeast replication origins in vivo.";
RL   Science 265:1243-1246(1994).
RN   [8]
RP   INTERACTION WITH CDC5, AND PHOSPHORYLATION.
RX   PubMed=8943332; DOI=10.1128/mcb.16.12.6775;
RA   Hardy C.F., Pautz A.;
RT   "A novel role for Cdc5p in DNA replication.";
RL   Mol. Cell. Biol. 16:6775-6782(1996).
RN   [9]
RP   INDUCTION.
RX   PubMed=10330168; DOI=10.1128/mcb.19.6.4270;
RA   Cheng L., Collyer T., Hardy C.F.;
RT   "Cell cycle regulation of DNA replication initiator factor Dbf4p.";
RL   Mol. Cell. Biol. 19:4270-4278(1999).
RN   [10]
RP   INDUCTION.
RX   PubMed=10373538; DOI=10.1128/mcb.19.7.4888;
RA   Oshiro G., Owens J.C., Shellman Y., Sclafani R.A., Li J.J.;
RT   "Cell cycle control of Cdc7p kinase activity through regulation of Dbf4p
RT   stability.";
RL   Mol. Cell. Biol. 19:4888-4896(1999).
RN   [11]
RP   FUNCTION, AND INTERACTION WITH ORC2; ORC3 AND RAD53.
RX   PubMed=12441400; DOI=10.1073/pnas.252093999;
RA   Duncker B.P., Shimada K., Tsai-Pflugfelder M., Pasero P., Gasser S.M.;
RT   "An N-terminal domain of Dbf4p mediates interaction with both origin
RT   recognition complex (ORC) and Rad53p and can deregulate late origin
RT   firing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16087-16092(2002).
RN   [12]
RP   FUNCTION IN MEIOTIC REPLICATION.
RX   PubMed=16319063; DOI=10.1074/jbc.m510626200;
RA   Valentin G., Schwob E., Della Seta F.;
RT   "Dual role of the Cdc7-regulatory protein Dbf4 during yeast meiosis.";
RL   J. Biol. Chem. 281:2828-2834(2006).
RN   [13]
RP   FUNCTION.
RX   PubMed=17018296; DOI=10.1016/j.molcel.2006.07.033;
RA   Sheu Y.-J., Stillman B.;
RT   "Cdc7-Dbf4 phosphorylates MCM proteins via a docking site-mediated
RT   mechanism to promote S phase progression.";
RL   Mol. Cell 24:101-113(2006).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59 AND SER-84, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [15]
RP   FUNCTION IN MEIOTIC SPINDLE ORIENTATION.
RX   PubMed=19013276; DOI=10.1016/j.cell.2008.10.026;
RA   Matos J., Lipp J.J., Bogdanova A., Guillot S., Okaz E., Junqueira M.,
RA   Shevchenko A., Zachariae W.;
RT   "Dbf4-dependent CDC7 kinase links DNA replication to the segregation of
RT   homologous chromosomes in meiosis I.";
RL   Cell 135:662-678(2008).
RN   [16]
RP   FUNCTION IN MEIOTIC RECOMBINATION.
RX   PubMed=18245450; DOI=10.1101/gad.1626408;
RA   Wan L., Niu H., Futcher B., Zhang C., Shokat K.M., Boulton S.J.,
RA   Hollingsworth N.M.;
RT   "Cdc28-Clb5 (CDK-S) and Cdc7-Dbf4 (DDK) collaborate to initiate meiotic
RT   recombination in yeast.";
RL   Genes Dev. 22:386-397(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-623, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [18]
RP   FUNCTION, AND INTERACTION WITH MCM2.
RX   PubMed=19692334; DOI=10.1074/jbc.m109.039123;
RA   Bruck I., Kaplan D.;
RT   "Dbf4-Cdc7 phosphorylation of Mcm2 is required for cell growth.";
RL   J. Biol. Chem. 284:28823-28831(2009).
RN   [19]
RP   FUNCTION, AND INTERACTION WITH CDC5.
RX   PubMed=19478884; DOI=10.1371/journal.pgen.1000498;
RA   Miller C.T., Gabrielse C., Chen Y.-C., Weinreich M.;
RT   "Cdc7p-Dbf4p regulates mitotic exit by inhibiting Polo kinase.";
RL   PLoS Genet. 5:E1000498-E1000498(2009).
RN   [20]
RP   FUNCTION, AND MUTAGENESIS OF CYS-661; CYS-664; HIS-674 AND HIS-680.
RX   PubMed=20436286; DOI=10.4161/cc.9.10.11752;
RA   Jones D.R., Prasad A.A., Chan P.K., Duncker B.P.;
RT   "The Dbf4 motif C zinc finger promotes DNA replication and mediates
RT   resistance to genotoxic stress.";
RL   Cell Cycle 9:2018-2026(2010).
RN   [21]
RP   FUNCTION, INTERACTION WITH CDC5, AND MUTAGENESIS OF ARG-83; SER-84; ILE-85;
RP   GLU-86; GLY-87 AND ALA-88.
RX   PubMed=21036905; DOI=10.1074/jbc.m110.155242;
RA   Chen Y.-C., Weinreich M.;
RT   "Dbf4 regulates the Cdc5 polo-like kinase through a distinct non-canonical
RT   binding interaction.";
RL   J. Biol. Chem. 285:41244-41254(2010).
RN   [22]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=20170732; DOI=10.1016/j.ymeth.2010.02.013;
RA   Kaplan D.L., Bruck I.;
RT   "Methods to study kinase regulation of the replication fork helicase.";
RL   Methods 51:358-362(2010).
RN   [23]
RP   FUNCTION IN REPLICATION INITIATION.
RX   PubMed=20054399; DOI=10.1038/nature08647;
RA   Sheu Y.-J., Stillman B.;
RT   "The Dbf4-Cdc7 kinase promotes S phase by alleviating an inhibitory
RT   activity in Mcm4.";
RL   Nature 463:113-117(2010).
CC   -!- FUNCTION: Regulatory subunit of the CDC7-DBF4 kinase, also called DBF4-
CC       dependent kinase (DDK), which is involved in cell cycle regulation of
CC       premitotic and premeiotic chromosome replication and in chromosome
CC       segregation. DDK plays an essential role in initiating DNA replication
CC       at replication origins by phosphorylating the MCM2 and MCM4 subunits of
CC       the MCM2-7 helicase complex. DBF4 recruits the catalytic subunit CDC7
CC       to MCM2 and to origins of replication. DDK has also postreplicative
CC       functions in meiosis. DDK phosphorylates the meiosis-specific double-
CC       strand break protein MER2 for initiation of meiotic recombination.
CC       Interacts with CDC5 during meiosis to promote double-strand breaks and
CC       monopolar spindle orientation. Inhibits CDC5 activity during mitosis
CC       through direct binding to its PBD. {ECO:0000269|PubMed:12441400,
CC       ECO:0000269|PubMed:16319063, ECO:0000269|PubMed:17018296,
CC       ECO:0000269|PubMed:18245450, ECO:0000269|PubMed:19013276,
CC       ECO:0000269|PubMed:19478884, ECO:0000269|PubMed:19692334,
CC       ECO:0000269|PubMed:20054399, ECO:0000269|PubMed:20170732,
CC       ECO:0000269|PubMed:20436286, ECO:0000269|PubMed:21036905,
CC       ECO:0000269|PubMed:8066465}.
CC   -!- SUBUNIT: Heterodimer with CDC7 to form the DBF4-dependent kinase (DDK)
CC       complex. Interacts (via PBD-binding motif) with CDC5 (via POLO box
CC       domains). Interacts (via N-terminus) with ORC2, ORC3 and RAD53. Binds
CC       to ARS1 origin DNA. {ECO:0000269|PubMed:12441400,
CC       ECO:0000269|PubMed:19478884, ECO:0000269|PubMed:19692334,
CC       ECO:0000269|PubMed:20170732, ECO:0000269|PubMed:21036905,
CC       ECO:0000269|PubMed:8943332}.
CC   -!- INTERACTION:
CC       P32325; P06243: CDC7; NbExp=8; IntAct=EBI-5575, EBI-4451;
CC   -!- INDUCTION: Cell cycle-regulated. Protein levels increase as cells begin
CC       S phase and remain high through late mitosis.
CC       {ECO:0000269|PubMed:10330168, ECO:0000269|PubMed:10373538}.
CC   -!- PTM: Phosphorylated by CDC7 and by CDC5. {ECO:0000269|PubMed:8943332}.
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DR   EMBL; X60279; CAA42819.1; -; Genomic_DNA.
DR   EMBL; M83539; AAA34573.1; -; Genomic_DNA.
DR   EMBL; X84162; CAA58969.1; -; Genomic_DNA.
DR   EMBL; Z49209; CAA89082.1; -; Genomic_DNA.
DR   EMBL; Z74348; CAA98869.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11899.1; -; Genomic_DNA.
DR   PIR; S25371; S25371.
DR   RefSeq; NP_010337.3; NM_001180360.3.
DR   PDB; 3OQ0; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J=120-250.
DR   PDB; 3OQ4; X-ray; 2.40 A; A/B/C/D/E=120-250.
DR   PDB; 3QBZ; X-ray; 2.69 A; A=66-221.
DR   PDB; 5T2F; X-ray; 2.66 A; A/B/C/D=105-220.
DR   PDB; 5T2S; X-ray; 2.40 A; A/C=105-220.
DR   PDB; 6MF6; X-ray; 3.40 A; C/D=76-96.
DR   PDBsum; 3OQ0; -.
DR   PDBsum; 3OQ4; -.
DR   PDBsum; 3QBZ; -.
DR   PDBsum; 5T2F; -.
DR   PDBsum; 5T2S; -.
DR   PDBsum; 6MF6; -.
DR   SMR; P32325; -.
DR   BioGRID; 32106; 825.
DR   ComplexPortal; CPX-867; DBF4-dependent CDC7 kinase complex.
DR   DIP; DIP-2290N; -.
DR   IntAct; P32325; 5.
DR   MINT; P32325; -.
DR   STRING; 4932.YDR052C; -.
DR   MoonDB; P32325; Predicted.
DR   iPTMnet; P32325; -.
DR   MaxQB; P32325; -.
DR   PaxDb; P32325; -.
DR   PRIDE; P32325; -.
DR   EnsemblFungi; YDR052C_mRNA; YDR052C; YDR052C.
DR   GeneID; 851623; -.
DR   KEGG; sce:YDR052C; -.
DR   SGD; S000002459; DBF4.
DR   VEuPathDB; FungiDB:YDR052C; -.
DR   eggNOG; KOG4139; Eukaryota.
DR   GeneTree; ENSGT00530000063909; -.
DR   HOGENOM; CLU_023948_0_0_1; -.
DR   InParanoid; P32325; -.
DR   OMA; PIITLEW; -.
DR   Reactome; R-SCE-68962; Activation of the pre-replicative complex.
DR   EvolutionaryTrace; P32325; -.
DR   PRO; PR:P32325; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P32325; protein.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0031431; C:Dbf4-dependent protein kinase complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR   GO; GO:0043539; F:protein serine/threonine kinase activator activity; IMP:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   GO; GO:0006270; P:DNA replication initiation; IPI:SGD.
DR   GO; GO:0033314; P:mitotic DNA replication checkpoint; IGI:SGD.
DR   GO; GO:0001100; P:negative regulation of exit from mitosis; IMP:SGD.
DR   GO; GO:1903468; P:positive regulation of DNA replication initiation; IGI:SGD.
DR   GO; GO:0060903; P:positive regulation of meiosis I; IMP:SGD.
DR   GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; IBA:GO_Central.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:SGD.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:SGD.
DR   GO; GO:0006279; P:premeiotic DNA replication; IMP:SGD.
DR   GO; GO:1901987; P:regulation of cell cycle phase transition; IBA:GO_Central.
DR   Gene3D; 3.30.160.680; -; 1.
DR   Gene3D; 3.40.50.10190; -; 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   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   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Chromosome partition;
KW   DNA replication; DNA-binding; Meiosis; Metal-binding; Mitosis;
KW   Phosphoprotein; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..704
FT                   /note="DDK kinase regulatory subunit DBF4"
FT                   /id="PRO_0000079791"
FT   ZN_FING         654..703
FT                   /note="DBF4-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT   REGION          10..19
FT                   /note="D box 1"
FT   REGION          62..70
FT                   /note="D box 2"
FT   MOTIF           83..88
FT                   /note="POLO box domain (PBD)-binding"
FT   MOD_RES         59
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         84
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         623
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MUTAGEN         83
FT                   /note="R->A,E: Defective for interaction with CDC5."
FT                   /evidence="ECO:0000269|PubMed:21036905"
FT   MUTAGEN         84
FT                   /note="S->A: No effect."
FT                   /evidence="ECO:0000269|PubMed:21036905"
FT   MUTAGEN         85
FT                   /note="I->A: Defective for interaction with CDC5."
FT                   /evidence="ECO:0000269|PubMed:21036905"
FT   MUTAGEN         86
FT                   /note="E->K: No effect."
FT                   /evidence="ECO:0000269|PubMed:21036905"
FT   MUTAGEN         87
FT                   /note="G->A: Defective for interaction with CDC5."
FT                   /evidence="ECO:0000269|PubMed:21036905"
FT   MUTAGEN         88
FT                   /note="A->V: Defective for interaction with CDC5."
FT                   /evidence="ECO:0000269|PubMed:21036905"
FT   MUTAGEN         661
FT                   /note="C->A: In DBF4-AAHH; weakens interaction with ARS1
FT                   origin DNA and MCM2, but not other known ligands; when
FT                   associated with A-664."
FT                   /evidence="ECO:0000269|PubMed:20436286"
FT   MUTAGEN         664
FT                   /note="C->A: In DBF4-AAHH; weakens interaction with ARS1
FT                   origin DNA and MCM2, but not other known ligands; when
FT                   associated with A-661."
FT                   /evidence="ECO:0000269|PubMed:20436286"
FT   MUTAGEN         674
FT                   /note="H->A: In DBF4-CCAA; weakens interaction with ARS1
FT                   origin DNA and MCM2, but not other known ligands; when
FT                   associated with A-680."
FT                   /evidence="ECO:0000269|PubMed:20436286"
FT   MUTAGEN         680
FT                   /note="H->A: Weakens interaction with ARS1 origin DNA and
FT                   MCM2, but not other known ligands. In DBF4-CCAA; weakens
FT                   interaction with ARS1 origin DNA and MCM2, but not other
FT                   known ligands; when associated with A-674."
FT                   /evidence="ECO:0000269|PubMed:20436286"
FT   MUTAGEN         680
FT                   /note="H->C: Weakens interaction with ARS1 origin DNA and
FT                   MCM2, but not other known ligands."
FT                   /evidence="ECO:0000269|PubMed:20436286"
FT   CONFLICT        159..160
FT                   /note="GA -> NT (in Ref. 1; CAA42819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        177
FT                   /note="R -> RR (in Ref. 1; CAA42819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        197
FT                   /note="N -> K (in Ref. 1; CAA42819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="D -> G (in Ref. 1; CAA42819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416..425
FT                   /note="Missing (in Ref. 1; CAA42819)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="Q -> R (in Ref. 1; CAA42819)"
FT                   /evidence="ECO:0000305"
FT   STRAND          86..90
FT                   /evidence="ECO:0007744|PDB:6MF6"
FT   HELIX           106..122
FT                   /evidence="ECO:0007744|PDB:5T2S"
FT   STRAND          125..128
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   HELIX           138..157
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   STRAND          161..165
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   STRAND          172..177
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   HELIX           179..184
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   HELIX           190..196
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   STRAND          200..203
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   HELIX           204..213
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   HELIX           218..221
FT                   /evidence="ECO:0007744|PDB:3OQ4"
FT   HELIX           233..241
FT                   /evidence="ECO:0007744|PDB:3OQ4"
SQ   SEQUENCE   704 AA;  80690 MW;  BDB93E72EF2ABC0B CRC64;
     MVSPTKMIIR SPLKETDTNL KHNNGIAAST TAAGHLNVFS NDNNCNNNNT TESFPKKRSL
     ERLELQQQQH LHEKKRARIE RARSIEGAVQ VSKGTGLKNV EPRVTPKELL EWQTNWKKIM
     KRDSRIYFDI TDDVEMNTYN KSKMDKRRDL LKRGFLTLGA QITQFFDTTV TIVITRRSVE
     NIYLLKDTDI LSRAKKNYMK VWSYEKAARF LKNLDVDLDH LSKTKSASLA APTLSNLLHN
     EKLYGPTDRD PRTKRDDIHY FKYPHVYLYD LWQTWAPIIT LEWKPQELTN LDELPYPILK
     IGSFGRCPFI GDRNYDESSY KRVVKRYSRD KANKKYALQL RALFQYHADT LLNTSSVNDQ
     TKNLIFIPHT CNDSTKSFKK WMQEKAKNFE KTELKKTDDS AVQDVRNEHA DQTDEKNSIL
     LNETETKEPP LKEEKENKQS IAEESNKYPQ RKELAATPKL NHPVLATFAR QETEEVPDDL
     CTLKTKSRQA FEIKASGAHQ SNDVATSFGN GLGPTRASVM SKNMKSLSRL MVDRKLGVKQ
     TNGNNKNYTA TIATTAETSK ENRHRLDFNA LKKDEAPSKE TGKDSAVHLE TNRKPQNFPK
     VATKSVSADS KVHNDIKITT TESPTASKKS TSTNVTLHFN AQTAQTAQPV KKETVKNSGY
     CENCRVKYES LEQHIVSEKH LSFAENDLNF EAIDSLIENL RFQI
//
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