MCM3_SCHPO
ID MCM3_SCHPO Reviewed; 879 AA.
AC P30666;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=DNA replication licensing factor mcm3;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 3;
GN Name=mcm3; ORFNames=SPCC1682.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SP011;
RX PubMed=9705504; DOI=10.1093/nar/26.17.3955;
RA Sherman D.A., Forsburg S.L.;
RT "Schizosaccharomyces pombe Mcm3p, an essential nuclear protein, associates
RT tightly with Nda4p (Mcm5p).";
RL Nucleic Acids Res. 26:3955-3960(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 359-434.
RX PubMed=1454522; DOI=10.1093/nar/20.21.5571;
RA Coxon A., Maundrell K., Kearsey S.E.;
RT "Fission yeast cdc21+ belongs to a family of proteins involved in an early
RT step of chromosome replication.";
RL Nucleic Acids Res. 20:5571-5577(1992).
RN [4]
RP SUBUNIT.
RC STRAIN=SP011;
RX PubMed=11606526; DOI=10.1093/genetics/159.2.471;
RA Liang D.T., Forsburg S.L.;
RT "Characterization of Schizosaccharomyces pombe mcm7(+) and cdc23(+) (MCM10)
RT and interactions with replication checkpoints.";
RL Genetics 159:471-486(2001).
CC -!- FUNCTION: Acts as component of the mcm2-7 complex (mcm complex) which
CC is the putative replicative helicase essential for 'once per cell
CC cycle' DNA replication initiation and elongation in eukaryotic cells.
CC The active ATPase sites in the mcm2-7 ring are formed through the
CC interaction surfaces of two neighboring subunits such that a critical
CC structure of a conserved arginine finger motif is provided in trans
CC relative to the ATP-binding site of the Walker A box of the adjacent
CC subunit. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Component of the mcm2-7 complex. The complex forms a toroidal
CC hexameric ring with the proposed subunit order mcm2-mcm6-mcm4-mcm7-
CC mcm3-mcm5 (Probable). The heterodimers of mcm4/mcm6 and mcm3/mcm5
CC interact with mcm2 and mcm7. {ECO:0000269|PubMed:11606526,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AF063864; AAC32263.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20668.1; -; Genomic_DNA.
DR EMBL; Z15034; CAA78752.1; -; Genomic_DNA.
DR PIR; S26642; S26642.
DR PIR; T41059; T41059.
DR RefSeq; NP_587795.1; NM_001022788.2.
DR AlphaFoldDB; P30666; -.
DR SMR; P30666; -.
DR BioGRID; 275419; 11.
DR ComplexPortal; CPX-2945; MCM complex.
DR IntAct; P30666; 4.
DR MINT; P30666; -.
DR STRING; 4896.SPCC1682.02c.1; -.
DR SwissPalm; P30666; -.
DR MaxQB; P30666; -.
DR PaxDb; P30666; -.
DR PRIDE; P30666; -.
DR EnsemblFungi; SPCC1682.02c.1; SPCC1682.02c.1:pep; SPCC1682.02c.
DR GeneID; 2538838; -.
DR KEGG; spo:SPCC1682.02c; -.
DR PomBase; SPCC1682.02c; mcm3.
DR VEuPathDB; FungiDB:SPCC1682.02c; -.
DR eggNOG; KOG0479; Eukaryota.
DR HOGENOM; CLU_000995_6_0_1; -.
DR InParanoid; P30666; -.
DR OMA; NVYPQED; -.
DR PhylomeDB; P30666; -.
DR Reactome; R-SPO-176187; Activation of ATR in response to replication stress.
DR Reactome; R-SPO-68867; Assembly of the pre-replicative complex.
DR Reactome; R-SPO-68949; Orc1 removal from chromatin.
DR Reactome; R-SPO-68962; Activation of the pre-replicative complex.
DR Reactome; R-SPO-69052; Switching of origins to a post-replicative state.
DR PRO; PR:P30666; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031261; C:DNA replication preinitiation complex; IC:PomBase.
DR GO; GO:0042555; C:MCM complex; IDA:PomBase.
DR GO; GO:0005656; C:nuclear pre-replicative complex; IC:PomBase.
DR GO; GO:0043596; C:nuclear replication fork; IC:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003688; F:DNA replication origin binding; ISO:PomBase.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; EXP:PomBase.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR008046; Mcm3.
DR InterPro; IPR018525; MCM_CS.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
DR InterPro; IPR027925; MCM_N.
DR InterPro; IPR033762; MCM_OB.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11630; PTHR11630; 1.
DR Pfam; PF00493; MCM; 1.
DR Pfam; PF17855; MCM_lid; 1.
DR Pfam; PF14551; MCM_N; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR PRINTS; PR01659; MCMPROTEIN3.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00847; MCM_1; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..879
FT /note="DNA replication licensing factor mcm3"
FT /id="PRO_0000194100"
FT DOMAIN 306..513
FT /note="MCM"
FT REGION 679..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 488..491
FT /note="Arginine finger"
FT COMPBIAS 692..714
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 879 AA; 97481 MW; 876051CC7DE2504A CRC64;
MTELLADEVF KDRVRIFQEY LEHDTDDANV TLYQEAILRM LNMGQRRLIV NIDELRDYNR
ELADGVLLKP LEYVEPFDEA LRNVVSTLID PVVHKDLKDK LFYVGFRGSF GDHHVNPRTL
RAMHLNKMIS LEGIVTRCSF VRPKVIKSVH YCEATKRHHF KQYADATMNG GLSFQSTVYP
TQDENGNPLS IEFGFSTFRD HQSISLQEMP ERAPPGQLPR SIDILLDDDL VDTVKPGDRV
NIVGQYRSMG SKTSGNTSAT FRTVLLANNV VLLGNKPGLG NVGGGALDIT DADIRNINKL
ARKKNVFELL STSLAPSIYG YEYVKQAILL LLLGGTEKNL TNGTHIRGDI NILMVGDPST
AKSQLLRFVL NTAPLAIATT GRGSSGVGLT AAVTTDKETG ERRLEAGAMV LADRGVVCID
EFDKMSDIDR VAIHEVMEQQ TVTIAKAGIH TSLNARCSVI AAANPIYGQY DIRKDPHQNI
ALPDSMLSRF DLLFIVTDDI DDKKDRALSE HVLRMHRYLP PGVEPGTPVR DSLNSVLNVG
ATNAAGVSTE NVEQEVETPV WETFSSLLHA NARTKKKELL NINFVRKYIQ YAKSRIHPIL
NQATAEYITN IYCGLRNDDL QGNQRRTSPL TARTLETLIR LSTAHAKARL SSVVEVKDAK
AAEKILRYAL FREVVKPKRK KHKKQRLEAG EEFDSEDDNS DDMDIEESEE EMDTNMVIDS
GSRRVTRSQN ATSQSQESGS EIGSSIAGTA GSYNVGTSNT QLSWPSTHST LPATSRELAS
SDRNINTGTS VASEVSASVS EQSTVSLPRE KMSVFMARLA SLTKSELFSE ECASLEDVLE
SINNIEDDVG FSREEAIVAL KEMDAQNKIM FSDNVVYRI
