MCM6_SCHPO
ID MCM6_SCHPO Reviewed; 892 AA.
AC P49731; Q9P7R7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=DNA replication licensing factor mcm6;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance protein 6;
GN Name=mcm6; Synonyms=mis5; ORFNames=SPBC211.04c;
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].
RX PubMed=7865880; DOI=10.1091/mbc.5.10.1145;
RA Takahashi K., Yamada H., Yanagida M.;
RT "Fission yeast minichromosome loss mutants mis cause lethal aneuploidy and
RT replication abnormality.";
RL Mol. Biol. Cell 5:1145-1158(1994).
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 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).
RN [4]
RP INTERACTION WITH SLD3.
RX PubMed=12006645; DOI=10.1091/mbc.02-01-0006;
RA Nakajima R., Masukata H.;
RT "SpSld3 is required for loading and maintenance of SpCdc45 on chromatin in
RT DNA replication in fission yeast.";
RL Mol. Biol. Cell 13:1462-1472(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-98, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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. Interacts with sld3.
CC {ECO:0000269|PubMed:11606526, ECO:0000269|PubMed:12006645,
CC ECO:0000305}.
CC -!- INTERACTION:
CC P49731; O94450: SPAC1687.04; NbExp=2; IntAct=EBI-913838, EBI-7492115;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA06729.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D31960; BAA06729.1; ALT_FRAME; Genomic_DNA.
DR EMBL; CU329671; CAB75412.1; -; Genomic_DNA.
DR PIR; T43423; T43423.
DR PIR; T50339; T50339.
DR RefSeq; NP_596614.1; NM_001022535.2.
DR AlphaFoldDB; P49731; -.
DR SMR; P49731; -.
DR BioGRID; 277303; 27.
DR ComplexPortal; CPX-2945; MCM complex.
DR IntAct; P49731; 9.
DR MINT; P49731; -.
DR STRING; 4896.SPBC211.04c.1; -.
DR iPTMnet; P49731; -.
DR MaxQB; P49731; -.
DR PaxDb; P49731; -.
DR EnsemblFungi; SPBC211.04c.1; SPBC211.04c.1:pep; SPBC211.04c.
DR GeneID; 2540784; -.
DR KEGG; spo:SPBC211.04c; -.
DR PomBase; SPBC211.04c; mcm6.
DR VEuPathDB; FungiDB:SPBC211.04c; -.
DR eggNOG; KOG0480; Eukaryota.
DR HOGENOM; CLU_000995_3_2_1; -.
DR InParanoid; P49731; -.
DR OMA; KYYIAQI; -.
DR PhylomeDB; P49731; -.
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:P49731; -.
DR Proteomes; UP000002485; Chromosome II.
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:0097373; C:MCM core 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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006268; P:DNA unwinding 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:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:1902969; P:mitotic DNA replication; IMP:PomBase.
DR GO; GO:1902975; P:mitotic DNA replication initiation; EXP:PomBase.
DR GO; GO:0006279; P:premeiotic DNA replication; IC: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; IPR031327; MCM.
DR InterPro; IPR008049; MCM6.
DR InterPro; IPR041024; Mcm6_C.
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; PF18263; MCM6_C; 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; PR01662; MCMPROTEIN6.
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; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..892
FT /note="DNA replication licensing factor mcm6"
FT /id="PRO_0000194118"
FT DOMAIN 426..633
FT /note="MCM"
FT REGION 748..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 608..611
FT /note="Arginine finger"
FT COMPBIAS 757..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 476..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 892 AA; 99550 MW; 3A00DB55B2EE08B7 CRC64;
MSSLASQGNN ASTPAYRYGF QTSEVGDRPT VSMPSQPESS AMLEDDGMVK RKPFAAIGEA
IPKVIDTTGE SVREAFEEFL LSFSDDRVAG GDALPSASQE KYYVQQIHGL AMYEIHTVYV
DYKHLTSYND VLALAIVEQY YRFSPFLLRA LQKLIEKFEP EYYRSSLSRE NASLSPNFKA
SDKTFALAFY NLPFRSTIRD LRTDRIGRLT TITGTVTRTS EVRPELAQGT FICEECHTVV
SNVEQAFRYT EPTQCPNELC ANKRSWRLNI SQSSFQDWQK VRIQENSNEI PTGSMPRTLD
VILRGDIVER AKAGDKCAFT GILIAVPDVS QLGIPGVKPE AYRDSRNFGG RDADGVTGLK
SLGVRDLTYK LSFLACMVQP DDANDKSGAD VRGDGSQGIE EQDEFLQSLS QEEIDDLRAM
VHSDHIYSRL TNSLAPSVYG HEIIKKGILL QLMGGVHKLT PEGINLRGDL NICIVGDPST
SKSQFLKYVC NFLPRAIYTS GKASSAAGLT AAVVKDEETG DFTIEAGALM LADNGICAID
EFDKMDLSDQ VAIHEAMEQQ TISIAKAGIQ ATLNARTSIL AAANPIGGRY NRKTTLRNNI
NMSAPIMSRF DLFFVVLDEC NESVDRHLAK HIVDIHRLRD DAMQPEFSTE QLQRYIRYAR
TFKPKLNTES CAEIVKKYKQ LRMDDAQGAG KNSYRITVRQ LESMIRLSEA IARANCVDDI
TPAFVNEAYS LLRQSIIHVE RDDIEVEEDD AEAQELENDN TNTTNGNDNV SSEEALQKPK
VKITYDKYVS IMNGILQVLR QRSTEGVDGV PAGDLVQSYL ELREDQFHTE EDIIYEVGLV
RKVLTRLVHE SIIMEIQNLT DSAVRLPFEE RVFSIHPNCD IDALLSNGDV PN
