ID   MCM6_CAEBR              Reviewed;         810 AA.
AC   Q61J08; A8XA47;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=DNA replication licensing factor mcm-6;
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:P97311};
GN   Name=mcm-6 {ECO:0000250|UniProtKB:P34647}; ORFNames=CBG09994;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255}.
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:0000255}.
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DR   EMBL; HE601459; CAP29514.1; -; Genomic_DNA.
DR   RefSeq; XP_002641666.1; XM_002641620.1.
DR   AlphaFoldDB; Q61J08; -.
DR   SMR; Q61J08; -.
DR   STRING; 6238.CBG09994; -.
DR   PRIDE; Q61J08; -.
DR   EnsemblMetazoa; CBG09994.1; CBG09994.1; WBGene00031483.
DR   GeneID; 8583659; -.
DR   KEGG; cbr:CBG_09994; -.
DR   CTD; 8583659; -.
DR   WormBase; CBG09994; CBP02437; WBGene00031483; Cbr-mcm-6.
DR   eggNOG; KOG0480; Eukaryota.
DR   HOGENOM; CLU_000995_3_2_1; -.
DR   InParanoid; Q61J08; -.
DR   OMA; KYYIAQI; -.
DR   OrthoDB; 266497at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
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   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   3: Inferred from homology;
KW   ATP-binding; Cell cycle; DNA replication; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..810
FT                   /note="DNA replication licensing factor mcm-6"
FT                   /id="PRO_0000232398"
FT   DOMAIN          346..553
FT                   /note="MCM"
FT                   /evidence="ECO:0000255"
FT   REGION          685..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           529..532
FT                   /note="Arginine finger"
FT   COMPBIAS        686..705
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         397..404
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   810 AA;  90983 MW;  C4200A75154A45A1 CRC64;
     MDNIISGQAQ KVEDVDGTRV QNEFSKFLKS FKGDKNELQY KTAMKELVQP EKNTIFVDMQ
     HLYKFSNNLA TTIELQYYRV YPFMCEALHL ATLDGCDENE RQQMFKKQLY VSLYNLDAKT
     KVRELSADKV GGLVRIAGQI VRTHPVHPEL SRACFVCEDC GVSTRDVQQQ FRYTQPTKCA
     NPQCMNRTRF SLDVNSSTFV DFQKIRIQET QAELPRGSIP RTVDVIVRGE MVETVQPGDK
     CDIVGTLIVI PDIAQLSTPG LRAETSNQNR GRATDKSEGI TGLKALGVRD LTYKMAFLAC
     HIQQTESLVG GDASGAMEEN DYLELWTKMS PEDRSVLKQM SDDKKIEKNI VDSLFPNIYG
     NHEVKLGVLL MLLGGVAKKS KDEGTSLRGD INVCLVGDPS TAKSQVLKAV EEFSPRAIYT
     SGKASSAAGL TAAVVKDEES FEFVIEAGAL MLADNGVCCI DEFDKMDVKD QVAIHEAMEQ
     QTISITKAGV KATLNARASI LAAANPVGGR YDRSRPLKYN VQMSAPIMSR FDLFFVLVDE
     CNEVTDYAIA RRILDNHRSI SEHTERNTVY KIDDIKKYIA FARCFKPKIS DKAAEALVRE
     YKKLRMSDSN NAATSSWRIT VRQLESLVRL SEALARLHCG KEVLEQHVEK AAELLNKSIV
     RVEQPDIALD EDDFDNNIVI VEANKENQGG DDDMEHDGEK DETAKVDPAK LKISFKEYKQ
     LSDVLVLHMR ADEESQGEEE YDGVKQSALV EWYLTTIEGE METEEDFNVQ KTVCERVIHR
     LVHQDHILLE VEPGEDPTLC VHPNYVVSDE