| IED ID | IndEnz0002010364 |
| Enzyme Type ID | protease010364 |
| Protein Name |
DNA replication licensing factor MCM2 EC 3.6.4.12 Minichromosome maintenance protein 2 |
| Gene Name | MCM2 YBL023C YBL0438 |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces Saccharomyces cerevisiae (Baker's yeast) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Enzyme Sequence | MSDNRRRRREEDDSDSENELPPSSPQQHFRGGMNPVSSPIGSPDMINPEGDDNEVDDVPDIDEVEEQMNEVDLMDDNMYEDYAADHNRDRYDPDQVDDREQQELSLSERRRIDAQLNERDRLLRNVAYIDDEDEEQEGAAQLDEMGLPVQRRRRRRQYEDLENSDDDLLSDMDIDPLREELTLESLSNVKANSYSEWITQPNVSRTIARELKSFLLEYTDETGRSVYGARIRTLGEMNSESLEVNYRHLAESKAILALFLAKCPEEMLKIFDLVAMEATELHYPDYARIHSEIHVRISDFPTIYSLRELRESNLSSLVRVTGVVTRRTGVFPQLKYVKFNCLKCGSILGPFFQDSNEEIRISFCTNCKSKGPFRVNGEKTVYRNYQRVTLQEAPGTVPPGRLPRHREVILLADLVDVSKPGEEVEVTGIYKNNYDGNLNAKNGFPVFATIIEANSIKRREGNTANEGEEGLDVFSWTEEEEREFRKISRDRGIIDKIISSMAPSIYGHRDIKTAVACSLFGGVPKNVNGKHSIRGDINVLLLGDPGTAKSQILKYVEKTAHRAVFATGQGASAVGLTASVRKDPITKEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCSIIAAANPNGGRYNSTLPLAQNVSLTEPILSRFDILCVVRDLVDEEADERLATFVVDSHVRSHPENDEDREGEELKNNGESAIEQGEDEINEQLNARQRRLQRQRKKEEEISPIPQELLMKYIHYARTKIYPKLHQMDMDKVSRVYADLRRESISTGSFPITVRHLESILRIAESFAKMRLSEFVSSYDLDRAIKVVVDSFVDAQKVSVRRQLRRSFAIYTLGH |
| Enzyme Length | 868 |
| Uniprot Accession Number | P29469 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; |
| DNA Binding | |
| EC Number | 3.6.4.12 |
| Enzyme Function | FUNCTION: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity; specifically the MCM2-MCM5 association is proposed to be reversible and to mediate a open ring conformation which may facilitate DNA loading. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth. {ECO:0000269|PubMed:19896182, ECO:0000269|PubMed:19910535}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 543..550; /note=ATP; /evidence=ECO:0000255 |
| Features | Beta strand (12); Chain (1); Compositional bias (4); Domain (1); Helix (16); Modified residue (5); Motif (1); Mutagenesis (4); Natural variant (1); Nucleotide binding (1); Region (3); Sequence conflict (8); Turn (5); Zinc finger (1) |
| Keywords | 3D-structure;ATP-binding;Cell cycle;DNA replication;DNA-binding;Helicase;Hydrolase;Metal-binding;Nucleotide-binding;Nucleus;Phosphoprotein;Reference proteome;Zinc;Zinc-finger |
| Interact With | P09119; Q08496; P30665; Q12306 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Nucleus. |
| Modified Residue | MOD_RES 14; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 16; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 23; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 164; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198; MOD_RES 170; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:19779198 |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | Electron microscopy (22) |
| Cross Reference PDB | 3JA8; 3JC5; 3JC6; 3JC7; 5BK4; 5U8S; 5U8T; 5V8F; 5XF8; 6EYC; 6F0L; 6HV9; 6PTJ; 6PTN; 6PTO; 6RQC; 6SKL; 6SKO; 6U0M; 6WGF; 6WGG; 6WGI; |
| Mapped Pubmed ID | 10373538; 10520598; 10577390; 10656992; 10704410; 10757793; 10783164; 10834843; 10872463; 10902566; 10964916; 10980206; 11163153; 11168584; 11171369; 11237870; 11266441; 11283351; 11290706; 11429609; 11431544; 11694596; 11741544; 11756674; 11805826; 11805837; 11836525; 11967159; 12045100; 12072451; 12381663; 12480933; 12526763; 12694535; 12801628; 12963835; 13679365; 1421579; 14636567; 14660704; 15004237; 15007098; 15020055; 15282291; 15353274; 15353275; 15380092; 15496876; 15610739; 15755447; 16045748; 16085704; 16093348; 16427002; 16429126; 16531994; 16554755; 16824194; 16943325; 17006448; 17018296; 17062629; 17118266; 17314407; 17347517; 17401409; 17630848; 17895243; 18208397; 18211918; 18439895; 18591250; 18662997; 18719252; 19270162; 19318354; 19482523; 19536198; 19540846; 19633981; 19661920; 19692334; 19767190; 19819872; 19856119; 19904620; 19910927; 19914158; 19917723; 19934224; 20012578; 20097898; 20124702; 20126453; 20130679; 20178629; 20203697; 20205354; 20484375; 20489023; 20516198; 20551170; 20581440; 20647475; 20686781; 20811343; 20885784; 21037857; 21160097; 21179020; 21306447; 21362622; 21460226; 21502406; 21508040; 21554750; 21596784; 21647941; 21855008; 21868389; 21963686; 22045335; 22118461; 22194009; 22433841; 22564307; 22615576; 22738223; 22842922; 23075259; 23332289; 23474987; 23499444; 23549044; 23549174; 23603117; 23803736; 23818500; 23838438; 23881938; 23881943; 23974098; 24001138; 24106087; 24234446; 24336748; 24349215; 24566989; 24692448; 24794003; 24811316; 24875627; 25085418; 25087873; 25313033; 25319829; 25835602; 25870112; 25892223; 25921072; 26030591; 26222030; 26255844; 26305410; 26305950; 26359232; 26524492; 26582917; 26656162; 26686640; 26710261; 26719337; 26777405; 26854664; 26854665; 27003891; 27273866; 27298353; 27375603; 27384026; 27416360; 27635237; 27751725; 28025497; 28096349; 28191893; 28191894; 28510759; 29078375; 29269875; 29405332; 29872003; 30244834; 30498216; 31589141; 31748745; 32369734; 32669428; 32701054; 33753149; 33772005; 7701565; 7788724; 8224843; 8542275; 8720069; 8722178; 8756666; 8867732; 8882583; 8939847; 9115430; 9154825; 9285827; 9335335; 9407029; 9407030; 9442876; 9554851; |
| Motif | MOTIF 675..678; /note=Arginine finger |
| Gene Encoded By | |
| Mass | 98,780 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:13065 |
| Cross Reference Brenda |