MCM6_CAEEL
ID MCM6_CAEEL Reviewed; 810 AA.
AC P34647; Q5FC84;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=DNA replication licensing factor mcm-6;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P97311};
GN Name=mcm-6; ORFNames=ZK632.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Bristol N2;
RA Kohara Y., Shin-i T., Suzuki Y., Sugano S., Potdevin M., Thierry-Mieg Y.,
RA Thierry-Mieg D., Thierry-Mieg J.;
RT "The Caenorhabditis elegans transcriptome project, a complementary view of
RT the genome.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000250|UniProtKB:P97311};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:P97311};
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 (By simililarity).
CC -!- INTERACTION:
CC P34647; P34638: cya-1; NbExp=4; IntAct=EBI-2006759, EBI-2421605;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=P34647-1; Sequence=Displayed;
CC Name=b;
CC IsoId=P34647-2; Sequence=VSP_017896;
CC -!- MISCELLANEOUS: Early fractionation of eukaryotic MCM proteins yielded a
CC variety of dimeric, trimeric and tetrameric complexes with unclear
CC biological significance. Specifically a MCM467 subcomplex is shown to
CC have in vitro helicase activity which is inhibited by the MCM2 subunit.
CC The MCM2-7 hexamer is the proposed physiological active complex.
CC {ECO:0000250|UniProtKB:P97311}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; Z22181; CAA80191.1; -; Genomic_DNA.
DR EMBL; Z29095; CAA80191.1; JOINED; Genomic_DNA.
DR EMBL; Z22181; CAI46590.1; -; Genomic_DNA.
DR EMBL; AF326940; AAG49390.1; -; mRNA.
DR PIR; H88565; H88565.
DR PIR; S40933; S40933.
DR RefSeq; NP_001023011.1; NM_001027840.3. [P34647-1]
DR RefSeq; NP_001023012.1; NM_001027841.4.
DR AlphaFoldDB; P34647; -.
DR SMR; P34647; -.
DR BioGRID; 41579; 13.
DR ComplexPortal; CPX-4482; MCM complex.
DR IntAct; P34647; 10.
DR STRING; 6239.ZK632.1a; -.
DR EPD; P34647; -.
DR PaxDb; P34647; -.
DR PeptideAtlas; P34647; -.
DR EnsemblMetazoa; ZK632.1a.1; ZK632.1a.1; WBGene00003158. [P34647-1]
DR EnsemblMetazoa; ZK632.1b.1; ZK632.1b.1; WBGene00003158. [P34647-2]
DR GeneID; 176385; -.
DR KEGG; cel:CELE_ZK632.1; -.
DR UCSC; ZK632.1a; c. elegans. [P34647-1]
DR CTD; 176385; -.
DR WormBase; ZK632.1a; CE00415; WBGene00003158; mcm-6. [P34647-1]
DR WormBase; ZK632.1b; CE38018; WBGene00003158; mcm-6. [P34647-2]
DR eggNOG; KOG0480; Eukaryota.
DR GeneTree; ENSGT01050000244824; -.
DR InParanoid; P34647; -.
DR OMA; KYYIAQI; -.
DR OrthoDB; 266497at2759; -.
DR PhylomeDB; P34647; -.
DR Reactome; R-CEL-68867; Assembly of the pre-replicative complex.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-68962; Activation of the pre-replicative complex.
DR Reactome; R-CEL-69052; Switching of origins to a post-replicative state.
DR PRO; PR:P34647; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00003158; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
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:1902969; P:mitotic DNA replication; IBA:GO_Central.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IC: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 Alternative splicing; ATP-binding; Cell cycle; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..810
FT /note="DNA replication licensing factor mcm-6"
FT /id="PRO_0000194116"
FT DOMAIN 346..554
FT /note="MCM"
FT MOTIF 529..532
FT /note="Arginine finger"
FT BINDING 397..404
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..294
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_017896"
SQ SEQUENCE 810 AA; 91130 MW; 214B65CFCE76EEB1 CRC64;
MDNIIGGQAQ QVEDTDGTRV QNEFSKFLKS FKDQKNEFIY KSAMKELVQP EKNTIFINMQ
HLYKFSNNLA TTIELQYYRV YPFMCEALHL ATLDACDESE RQQMFKKQLY VSLFNLDAKT
KVRELSADKV GGLVRIAGQI VRTHPVHPEL SRACFVCEDC GVTTRDVQQQ FRYTQPTKCA
NPQCMNRTRF SLDVNSSTFV DFQKIRIQET QAELPRGSIP RTVDVIVRGE MVETVQPGDK
CDIVGTLIVI PDIAQLSTPG LRAETSNQNR GRATDKSEGI TGLKALGVRD LTYKMAFLAC
HIQQTESLVG GDASGAVEET DYLDLWSKMS TEDRATLKKM SDDKKIEKNI VDSLFPNIYG
NHEVKLGVLL MLLGGVAKKS RDEGTSLRGD INVCLVGDPS TAKSQVLKAV EEFSPRAIYT
SGKASSAAGL TAAVVKDEES FEFVIEAGAL MLADNGVCCI DEFDKMDLKD QVAIHEAMEQ
QTISITKAGV KATLNARASI LAAANPVNGR YDRSRPLKYN VQMSAPIMSR FDLFFVLVDE
CNEVTDYAIA RRILDNHRAI SEHTERDSVY KIDDIKKYIA FARCFKPKIS DKAAETLVRE
YKKLRMSDSN NAATSSWRIT VRQLESLVRL SEALARLHCG KEVLVEHVEK AAELLNKSIV
RVEQPDIALD DDDFDNNIMV VEADKENQRG DDSMDHDGEK ENAPKIDIAK LKISFKEYKQ
LSDVLVLHMR SDEDNQGEDE YDGVKQSALV EWYLSTIEAD LETEEDFNVQ KTICERVIHR
LIHQDHVLLE VEQGEDPTLC VHPNYVIADE
