MCM6_DICDI
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 03-AUG-2022, entry version 115.
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 (Slime mold).
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 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 (By similarity). {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: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.DDB0232357; -.
DR PaxDb; Q86B14; -.
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; KYYIAQI; -.
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: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..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"
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
