MCM6_DROPS
ID MCM6_DROPS Reviewed; 815 AA.
AC Q29JI9;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=DNA replication licensing factor Mcm6;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P97311};
GN Name=Mcm6; ORFNames=GA17904;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL32312.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(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. The six ATPase active sites, however, are likely to contribute
CC differentially to the complex helicase activity Required for DNA
CC replication and cell proliferation. Required for mitotic cycles,
CC endocycles, and the special S phase associated with the amplification
CC of chorion genes; has a role in origin unwinding or fork elongation at
CC chorion loci (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. The heterodimers of mcm4/mcm6 and mcm3/mcm5 interact with
CC mcm2 and mcm7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Associated with
CC chromatin during cell cycles. {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:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL32312.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH379063; EAL32312.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001355255.1; XM_001355219.3.
DR AlphaFoldDB; Q29JI9; -.
DR SMR; Q29JI9; -.
DR STRING; 7237.FBpp0273188; -.
DR EnsemblMetazoa; FBtr0274750; FBpp0273188; FBgn0077913.
DR GeneID; 4816084; -.
DR KEGG; dpo:Dpse_GA17904; -.
DR eggNOG; KOG0480; Eukaryota.
DR HOGENOM; CLU_000995_3_2_1; -.
DR InParanoid; Q29JI9; -.
DR OMA; KYYIAQI; -.
DR PhylomeDB; Q29JI9; -.
DR Proteomes; UP000001819; Chromosome X.
DR Bgee; FBgn0077913; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0071162; C:CMG complex; IEA:EnsemblMetazoa.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:EnsemblMetazoa.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISS:UniProtKB.
DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR GO; GO:0007307; P:eggshell chorion gene amplification; IEA:EnsemblMetazoa.
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; Cell division; DNA replication; DNA-binding;
KW Helicase; Hydrolase; Metal-binding; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..815
FT /note="DNA replication licensing factor Mcm6"
FT /id="PRO_0000233316"
FT DOMAIN 338..544
FT /note="MCM"
FT /evidence="ECO:0000255"
FT ZN_FING 152..179
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 672..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 520..523
FT /note="Arginine finger"
FT COMPBIAS 677..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 815 AA; 91994 MW; 932D6C1BDA572D33 CRC64;
MDVADAQIGQ LRVKDDVGIR TQKLFQDFLE EFKENGEIKY TRPAANLESP DRCTLEVSFE
DVEKYDQNLA TAIIEEYYHV YPFLCQSVSN YVKDRIGLKT NKDCYVAFTE VPTRHKVRDL
TTSKIGTLIR ISGQVVRTHP VHPELVSGTF MCLDCQTEIR NVEQQFKFTN PTICRNPVCS
NRRRFMLDVE KSLFLDFQKI RIQETQAELP RGCIPRAVEI ILRSELVETV QAGDRYDFTG
TLIVVPDVSV LAMPGTRAES GSRHKPGEGM EGVTGLKALG MRELNYRMAF LACSVQATTA
RFGGTDLPMS EVTAEDMKKQ MTDAEWHKIY EMSKDRNLYQ NLITCLFPSI YGNDEVKRGI
LLQLFGGVAK TTIEKTSLRG DVNVCIVGDP STAKSQFLKQ VSDFSPRAIY TSGKASSAAG
LTAAVVRDEE SFDFVIEAGA LMLADNGICC IDEFDKMDLR DQVAIHEAME QQTISIARAG
VRATLNARTS ILAAANPING RYDRSKSLQQ NIQLSAPIMS RFDLFFILVD ECNEVVDYAI
ARKIVDLHSN IEESVERAYS REEVLRYVTF ARQFKPIIGQ EAGKMLVENY GHLRQRDTGT
AGRSTWRITV RQLESMIRLS EAMAKLECSN RVLERHVKEA FRLLNKSIIR VEQPDIHLDD
DDDLDVDDGI QDDIDMENNG SAANTETDTL DTSGASTVQK KKFTLSFEDY KNLSTMLVLH
MRGEEARCEV EGSDSGMKRS DVVTWYLEQV ADQIESEDEL ISRKNLIEKL IDRLIYHDQV
IIPLKTSNLS RIKGPAEEQV DNDPLLVVHP NYVVD
