UniProtKB - P24279 (MCM3_YEAST)
Protein
DNA replication licensing factor MCM3
Gene
MCM3
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
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. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Necessary for cell growth.2 Publications
Miscellaneous
Present with 35100 molecules/cell in log phase SD medium.1 Publication
Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. The MCM2-7 hexamer is the proposed physiological active complex.
Catalytic activityi
ATP + H2O = ADP + phosphate.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Nucleotide bindingi | 409 – 416 | ATPSequence analysis | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- chromatin binding Source: SGD
- DNA replication origin binding Source: SGD
- helicase activity Source: UniProtKB-KW
- MCM complex binding Source: SGD
GO - Biological processi
- chromatin silencing at silent mating-type cassette Source: SGD
- chromatin silencing at telomere Source: SGD
- DNA duplex unwinding Source: GOC
- DNA replication initiation Source: SGD
- DNA strand elongation involved in DNA replication Source: SGD
- double-strand break repair via break-induced replication Source: SGD
- mitotic DNA replication initiation Source: SGD
- pre-replicative complex assembly involved in nuclear cell cycle DNA replication Source: SGD
Keywordsi
| Molecular function | DNA-binding, Helicase, Hydrolase |
| Biological process | DNA replication |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
| BioCyci | YEAST:G3O-30154-MONOMER |
| Reactomei | R-SCE-68949 Orc1 removal from chromatin R-SCE-68962 Activation of the pre-replicative complex R-SCE-69052 Switching of origins to a post-replicative state |
Names & Taxonomyi
| Protein namesi | Recommended name: DNA replication licensing factor MCM3 (EC:3.6.4.12)Alternative name(s): Minichromosome maintenance protein 3 |
| Gene namesi | Name:MCM3 Ordered Locus Names:YEL032W ORF Names:SYGP-ORF23 |
| Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
| Taxonomic identifieri | 559292 [NCBI] |
| Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
| Proteomesi |
|
Organism-specific databases
| EuPathDBi | FungiDB:YEL032W |
| SGDi | S000000758 MCM3 |
Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 415 | K → A: No effect on MCM2-7 complex helicase activity. Loss of MCM2-7 complex helicase activity; when associated with MCM5 A-422. Reduces MCM2-7 complex helicase activity; when associated with MCM2 A-549. 1 Publication | 1 |
PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000194099 | 1 – 971 | DNA replication licensing factor MCM3Add BLAST | 971 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 761 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 777 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 781 | PhosphoserineCombined sources | 1 | |
| Modified residuei | 868 | PhosphothreonineCombined sources | 1 |
Keywords - PTMi
PhosphoproteinProteomic databases
| MaxQBi | P24279 |
| PaxDbi | P24279 |
| PRIDEi | P24279 |
PTM databases
| iPTMneti | P24279 |
Interactioni
Subunit structurei
Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5; loaded onto DNA, forms a head-head double hexamer. Interacts with CSM1.3 Publications
Binary interactionsi
Protein-protein interaction databases
| BioGridi | 36697, 395 interactors |
| ComplexPortali | CPX-2944 MCM complex |
| DIPi | DIP-2407N |
| IntActi | P24279, 35 interactors |
| MINTi | P24279 |
| STRINGi | 4932.YEL032W |
Structurei
3D structure databases
| ProteinModelPortali | P24279 |
| SMRi | P24279 |
| ModBasei | Search... |
| MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 359 – 566 | MCMAdd BLAST | 208 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Motifi | 541 – 544 | Arginine finger | 4 |
Sequence similaritiesi
Belongs to the MCM family.Curated
Phylogenomic databases
| GeneTreei | ENSGT00900000141082 |
| HOGENOMi | HOG000224126 |
| InParanoidi | P24279 |
| KOi | K02541 |
| OMAi | RNDQNTK |
| OrthoDBi | EOG092C0VUM |
Family and domain databases
| InterProi | View protein in InterPro IPR003593 AAA+_ATPase IPR031327 MCM IPR008046 Mcm3 IPR018525 MCM_CS IPR001208 MCM_dom IPR033762 MCM_OB IPR012340 NA-bd_OB-fold IPR027417 P-loop_NTPase |
| PANTHERi | PTHR11630 PTHR11630, 1 hit |
| Pfami | View protein in Pfam PF00493 MCM, 1 hit PF17207 MCM_OB, 1 hit |
| PRINTSi | PR01657 MCMFAMILY PR01659 MCMPROTEIN3 |
| SMARTi | View protein in SMART SM00382 AAA, 1 hit SM00350 MCM, 1 hit |
| SUPFAMi | SSF50249 SSF50249, 1 hit SSF52540 SSF52540, 2 hits |
| PROSITEi | View protein in PROSITE PS00847 MCM_1, 1 hit PS50051 MCM_2, 1 hit |
Sequencei
Sequence statusi: Complete.
P24279-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEGSTGFDGD ATTFFAPDAV FGDRVRRFQE FLDTFTSYRD SVRSIQVYNS
60 70 80 90 100
NNAANYNDDQ DDADERDLLG DDDGDDLEKE KKAASSTSLN ILPHRIIISL
110 120 130 140 150
DDLREFDRSF WSGILVEPAY FIPPAEKALT DLADSMDDVP HPNASAVSSR
160 170 180 190 200
HPWKLSFKGS FGAHALSPRT LTAQHLNKLV SVEGIVTKTS LVRPKLIRSV
210 220 230 240 250
HYAAKTGRFH YRDYTDATTT LTTRIPTPAI YPTEDTEGNK LTTEYGYSTF
260 270 280 290 300
IDHQRITVQE MPEMAPAGQL PRSIDVILDD DLVDKTKPGD RVNVVGVFKS
310 320 330 340 350
LGAGGMNQSN SNTLIGFKTL ILGNTVYPLH ARSTGVAARQ MLTDFDIRNI
360 370 380 390 400
NKLSKKKDIF DILSQSLAPS IYGHDHIKKA ILLMLMGGVE KNLENGSHLR
410 420 430 440 450
GDINILMVGD PSTAKSQLLR FVLNTASLAI ATTGRGSSGV GLTAAVTTDR
460 470 480 490 500
ETGERRLEAG AMVLADRGVV CIDEFDKMTD VDRVAIHEVM EQQTVTIAKA
510 520 530 540 550
GIHTTLNARC SVIAAANPVF GQYDVNRDPH QNIALPDSLL SRFDLLFVVT
560 570 580 590 600
DDINEIRDRS ISEHVLRTHR YLPPGYLEGE PVRERLNLSL AVGEDADINP
610 620 630 640 650
EEHSNSGAGV ENEGEDDEDH VFEKFNPLLQ AGAKLAKNKG NYNGTEIPKL
660 670 680 690 700
VTIPFLRKYV QYAKERVIPQ LTQEAINVIV KNYTDLRNDD NTKKSPITAR
710 720 730 740 750
TLETLIRLAT AHAKVRLSKT VNKVDAKVAA NLLRFALLGE DIGNDIDEEE
760 770 780 790 800
SEYEEALSKR SPQKSPKKRQ RVRQPASNSG SPIKSTPRRS TASSVNATPS
810 820 830 840 850
SARRILRFQD DEQNAGEDDN DIMSPLPADE EAELQRRLQL GLRVSPRRRE
860 870 880 890 900
HLHAPEEGSS GPLTEVGTPR LPNVSSAGQD DEQQQSVISF DNVEPGTIST
910 920 930 940 950
GRLSLISGII ARLMQTEIFE EESYPVASLF ERINEELPEE EKFSAQEYLA
960 970
GLKIMSDRNN LMVADDKVWR V
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X53540 Genomic DNA Translation: CAA37616.1 U18779 Genomic DNA Translation: AAB65010.1 BK006939 Genomic DNA Translation: DAA07621.1 |
| PIRi | A36376 |
| RefSeqi | NP_010882.1, NM_001178847.1 |
Genome annotation databases
| EnsemblFungii | YEL032W; YEL032W; YEL032W |
| GeneIDi | 856680 |
| KEGGi | sce:YEL032W |
Similar proteinsi
Entry informationi
| Entry namei | MCM3_YEAST | |
| Accessioni | P24279Primary (citable) accession number: P24279 Secondary accession number(s): D3DLL7 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | March 1, 1992 |
| Last sequence update: | March 1, 1992 | |
| Last modified: | September 12, 2018 | |
| This is version 185 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Fungal Protein Annotation Program | |



