ID MCM6_BOVIN Reviewed; 821 AA.
AC Q2KIZ8;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE RecName: Full=DNA replication licensing factor MCM6;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P97311};
GN Name=MCM6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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:Q14566};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q14566};
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. Component of the CMG helicase complex, a hexameric ring of
CC related MCM2-7 subunits stabilized by CDC45 and the tetrameric GINS
CC complex. May interact with MCM10. Interacts with TIPIN. Interacts with
CC CDT1. Interacts with MCMBP. Interacts with DDI2.
CC {ECO:0000250|UniProtKB:Q14566}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q14566}.
CC Chromosome {ECO:0000250|UniProtKB:Q14566}. Note=Binds to chromatin
CC during G1 and detaches from it during S phase.
CC {ECO:0000250|UniProtKB:Q14566}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000250|UniProtKB:Q14566}.
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; BC112448; AAI12449.1; -; mRNA.
DR RefSeq; NP_001039699.1; NM_001046234.1.
DR AlphaFoldDB; Q2KIZ8; -.
DR BMRB; Q2KIZ8; -.
DR SMR; Q2KIZ8; -.
DR STRING; 9913.ENSBTAP00000048625; -.
DR PaxDb; 9913-ENSBTAP00000048625; -.
DR GeneID; 517812; -.
DR KEGG; bta:517812; -.
DR CTD; 4175; -.
DR eggNOG; KOG0480; Eukaryota.
DR InParanoid; Q2KIZ8; -.
DR OrthoDB; 5476523at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0071162; C:CMG complex; ISS:UniProtKB.
DR GO; GO:0042555; C:MCM complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031090; C:organelle membrane; IEA:UniProt.
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:SF73; 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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Chromosome; DNA replication;
KW DNA-binding; Glycoprotein; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..821
FT /note="DNA replication licensing factor MCM6"
FT /id="PRO_0000239660"
FT DOMAIN 346..553
FT /note="MCM"
FT REGION 676..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 528..531
FT /note="Arginine finger"
FT BINDING 359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 399
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 400
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 401
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared with MCM4"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 619
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM2"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT BINDING 622
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="ligand shared with MCM2"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT MOD_RES 278
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT MOD_RES 643
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97311"
FT MOD_RES 689
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97311"
FT MOD_RES 762
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
FT MOD_RES 791
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14566"
SQ SEQUENCE 821 AA; 92930 MW; B0F7841B9DCFD7AC CRC64;
MDLAAAAEPG AGSQHLEVRD EVAEKCQKLF LDFLEEFQNS DGEIKYLQLA EELIRPERNT
LVVSFVDLEQ FNQQLSTTIQ EEFYRVYPYL CRALKTFVKD RKEIPLAKDF YVAFQDLPTR
HKIRELTSSR IGLLTRISGQ VVRTHPVHPE LVSGTFLCLD CQTVIKDVEQ QFKYTQPNIC
RNPVCANRRR FLLDTNKSRF VDFQKVRIQE TQAELPRGSI PRSLEVILRA EAVESAQAGD
KCDFTGTLIV VPDVSKLSTP GARAETDSRV SGVDGYETEG VRGLRALGVR DLSYRLVFLA
CCVAPTNPRF GGKELRDEEQ TAESIKNQMT VKEWEKVFEM SQDKNLYHNL CTSLFPTIHG
NDEVKRGVLL MLFGGVPKTT GEGTSLRGDI NVCIVGDPST AKSQFLKHVE EFSPRAVYTS
GKASIAAGLT AAVVRDEESH EFVIEAGALM LADNGVCCID EFDKMDVRDQ VAIHEAMEQQ
TISITKAGVK ATLNARTSIL AAANPISGHY DRSKSLKQNI NLSAPIMSRF DLFFILVDEC
NEVTDYAIAR RIVDLHSRIE DSIDRVYSLD EIRRYLLFAR QFKPKISKES EDFIVEQYKR
LRQRDGSGVT KSSWRITVRQ LESMIRLSEA MARMHCCDEV QPKHVKEAFR LLNKSIIRVE
TPDVNLDQEE DAQMEVDEGP DGINGHADSP APASGINGHS EDMNQDSVPK ASLRLGFSEY
CRISNLIVLH LRKMEEEEDE SALKRSELVN WYLKEIESEI DSEEELINKK RIIEKVIYRL
THYDHVLIEL TQAGLKGSTE GSESYEEDPY LVVNPNYLLE D
//
