ID MCM6_DICDI Reviewed; 867 AA.
AC Q86B14; Q1ZXM5;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=DNA replication licensing factor mcm6;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P97311};
GN Name=mcm6; ORFNames=DDB_G0272760;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Acts as a component of the MCM2-7 complex (MCM complex) which
CC is the replicative helicase essential for 'once per cell cycle' DNA
CC replication initiation and elongation in eukaryotic cells. Core
CC component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that
CC unwinds template DNA during replication, and around which the replisome
CC is built. The active ATPase sites in the MCM2-7 ring are formed through
CC the interaction surfaces of two neighboring subunits such that a
CC critical structure of a conserved arginine finger motif is provided in
CC trans relative to the ATP-binding site of the Walker A box of the
CC adjacent subunit. The six ATPase active sites, however, are likely to
CC contribute differentially to the complex helicase activity.
CC {ECO:0000250|UniProtKB:Q14566}.
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:0000250}.
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; AAFI02000008; EAS66960.1; -; Genomic_DNA.
DR RefSeq; XP_001134626.1; XM_001134626.1.
DR AlphaFoldDB; Q86B14; -.
DR SMR; Q86B14; -.
DR STRING; 44689.Q86B14; -.
DR PaxDb; 44689-DDB0232357; -.
DR EnsemblProtists; EAS66960; EAS66960; DDB_G0272760.
DR GeneID; 8618624; -.
DR KEGG; ddi:DDB_G0272760; -.
DR dictyBase; DDB_G0272760; mcm6.
DR eggNOG; KOG0480; Eukaryota.
DR HOGENOM; CLU_000995_3_2_1; -.
DR InParanoid; Q86B14; -.
DR OMA; CQTEIRN; -.
DR PhylomeDB; Q86B14; -.
DR Reactome; R-DDI-68867; Assembly of the pre-replicative complex.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-68962; Activation of the pre-replicative complex.
DR Reactome; R-DDI-69052; Switching of origins to a post-replicative state.
DR PRO; PR:Q86B14; -.
DR Proteomes; UP000002195; Chromosome 2.
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:InterPro.
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 CDD; cd17757; MCM6; 1.
DR Gene3D; 1.20.58.870; -; 1.
DR Gene3D; 2.20.28.10; -; 1.
DR Gene3D; 3.30.1640.10; mini-chromosome maintenance (MCM) complex, chain A, domain 1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; DNA REPLICATION LICENSING FACTOR MCM FAMILY MEMBER; 1.
DR PANTHER; PTHR11630:SF43; DNA REPLICATION LICENSING FACTOR MCM6; 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; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..867
FT /note="DNA replication licensing factor mcm6"
FT /id="PRO_0000328208"
FT DOMAIN 420..626
FT /note="MCM"
FT /evidence="ECO:0000255"
FT REGION 51..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 602..605
FT /note="Arginine finger"
FT BINDING 473
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 693
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM2"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 696
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM2"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
SQ SEQUENCE 867 AA; 97772 MW; 42C3797DFE08162C CRC64;
MIYTDAGVDE DKATIRPNQT HQFQKVQDEA KEWTKNKFLE FLNNFKLKKK IDKNNNNNNN
EDNEDNNENE NEYDENGIKK EKIDKSYYRQ QVERMIKNDK SSLYIDFLHL EKFDKGLGKA
LLMEYFRLEP AIRQGLSIFI QKYFPSFMER VNKERIVLSI CCYNVSTFVH IRELRSSRIG
SLCSISGTVT RTSEVRPELV IGSFICKDCN TSSLPIAQQF KYTEPTKCLN PLCSNQRRWK
INLEESTFTD WQKVRVQENN SEIPGGSVPR SLEIILRGDS VETARAGDTC TFVGTMNVIP
DVSKMSIGNN AQIIKGVASS TKEGSNANGK DDFGGVGGLK DLGVREMNYR VCFFSQSVRS
NVSTLSSINR KESGDNHGGH SHSVGIIDED LEPESKESFL DSLPKKEKDS LKKMIKSKKI
YQNLVNSICP SIFGHEEIKR GVLLMLFGGV HKKTPEKIRL RGDINVCIVG DPSTSKSTFL
KYLVSFLPRT VYTSGKASSA AGLTATVVKD QESGDFNIEA GALMLADNGI CCIDEFDKME
PGDQVAIHEA MEQQTISIAK AGIHASLNAR TSILAAANPI GGRYDRNKTL KQNLNIGGPL
MSRFDLFFVV LDECNPESDH RIAEHIVLTH QKREKAFNAP FSATEIKNYI KYTKFICPTI
PDESVQLLVG HYDRLRQMDT SGSKTPAYRI TVRQLESLVR LSESLARLHL DTKVLPKYVN
EAARLLEKSI VHVETNDVIL GDDDDDLVKN VENDNDNHAE EDGDDGIGKL TMNFSKYSQL
SKLLVLQIKQ SGKEKSGIKQ IDLIDWYIKD QLESGIITDD EVTKETKITK MVINKMINKD
NSLVVLVPNQ YPDHRILIIH PNYSFDK
//
