DBF4_YEAST
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 03-AUG-2022, entry version 183.
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; DOI=10.1093/genetics/131.1.21;
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.13.5.2899-2908.1993;
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 PDB; 7P5Z; EM; 3.30 A; G=1-704.
DR PDB; 7V3V; EM; 2.90 A; I=1-704.
DR PDBsum; 3OQ0; -.
DR PDBsum; 3OQ4; -.
DR PDBsum; 3QBZ; -.
DR PDBsum; 5T2F; -.
DR PDBsum; 5T2S; -.
DR PDBsum; 6MF6; -.
DR PDBsum; 7P5Z; -.
DR PDBsum; 7V3V; -.
DR AlphaFoldDB; P32325; -.
DR SMR; P32325; -.
DR BioGRID; 32106; 832.
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 BioCyc; YEAST:G3O-29662-MON; -.
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:0005813; C:centrosome; IDA:ComplexPortal.
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; IDA:ComplexPortal.
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; IDA:ComplexPortal.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; 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:1905561; P:positive regulation of kinetochore assembly; IDA:ComplexPortal.
DR GO; GO:0060903; P:positive regulation of meiosis I; IDA:ComplexPortal.
DR GO; GO:1903343; P:positive regulation of meiotic DNA double-strand break formation; IDA:ComplexPortal.
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:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:1901987; P:regulation of cell cycle phase transition; IBA:GO_Central.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 6.10.250.3410; -; 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 REGION 397..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 83..88
FT /note="POLO box domain (PBD)-binding"
FT COMPBIAS 397..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 674
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
FT BINDING 680
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00600"
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:0007829|PDB:6MF6"
FT HELIX 106..122
FT /evidence="ECO:0007829|PDB:5T2S"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:3OQ4"
FT HELIX 138..157
FT /evidence="ECO:0007829|PDB:3OQ4"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:3OQ4"
FT STRAND 172..177
FT /evidence="ECO:0007829|PDB:3OQ4"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:3OQ4"
FT HELIX 190..196
FT /evidence="ECO:0007829|PDB:3OQ4"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3OQ4"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:3OQ4"
FT HELIX 218..221
FT /evidence="ECO:0007829|PDB:3OQ4"
FT HELIX 233..241
FT /evidence="ECO:0007829|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
