MCM8_BOVIN
ID MCM8_BOVIN Reviewed; 816 AA.
AC E1BPX4;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=DNA helicase MCM8;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9UJA3};
DE AltName: Full=Minichromosome maintenance 8;
GN Name=MCM8;
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 GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
CC -!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in the
CC repair of double-stranded DNA breaks (DBSs) and DNA interstrand cross-
CC links (ICLs) by homologous recombination (HR). Required for DNA
CC resection by the MRE11-RAD50-NBN/NBS1 (MRN) complex by recruiting the
CC MRN complex to the repair site and by promoting the complex nuclease
CC activity. Probably by regulating the localization of the MNR complex,
CC indirectly regulates the recruitment of downstream effector RAD51 to
CC DNA damage sites including DBSs and ICLs. The MCM8-MCM9 complex is
CC dispensable for DNA replication and S phase progression. However, may
CC play a non-essential for DNA replication: may be involved in the
CC activation of the prereplicative complex (pre-RC) during G(1) phase by
CC recruiting CDC6 to the origin recognition complex (ORC). Probably by
CC regulating HR, plays a key role during gametogenesis. Stabilizes MCM9
CC protein. {ECO:0000250|UniProtKB:Q9CWV1, ECO:0000250|UniProtKB:Q9UJA3}.
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:Q9UJA3};
CC -!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
CC composed of MCM8 and MCM9. Interacts with the DNA mismatch repair (MMR)
CC complex composed at least of MSH2, MSH3, MSH6, PMS1 and MLH1. Interacts
CC with RAD51; the interaction recruits RAD51 to DNA damage sites.
CC Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1.
CC Interacts with CDC6 and ORC2. Interacts with HROB; the interaction
CC recruits the MCM8-MCM9 complex to DNA damage sites (By similarity).
CC {ECO:0000250|UniProtKB:Q9UJA3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UJA3}.
CC Chromosome {ECO:0000250|UniProtKB:Q9UJA3}. Note=Localizes to nuclear
CC foci. Localizes to double-stranded DNA breaks. Binds chromatin
CC throughout the cell cycle. {ECO:0000250|UniProtKB:Q9UJA3}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; DAAA02036045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001179965.1; NM_001193036.1.
DR AlphaFoldDB; E1BPX4; -.
DR SMR; E1BPX4; -.
DR STRING; 9913.ENSBTAP00000019471; -.
DR PaxDb; E1BPX4; -.
DR PRIDE; E1BPX4; -.
DR Ensembl; ENSBTAT00000019471; ENSBTAP00000019471; ENSBTAG00000014623.
DR GeneID; 507507; -.
DR KEGG; bta:507507; -.
DR CTD; 84515; -.
DR VEuPathDB; HostDB:ENSBTAG00000014623; -.
DR VGNC; VGNC:31314; MCM8.
DR eggNOG; KOG0480; Eukaryota.
DR GeneTree; ENSGT01050000244972; -.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; E1BPX4; -.
DR OMA; THTVDWQ; -.
DR OrthoDB; 266497at2759; -.
DR TreeFam; TF323155; -.
DR Reactome; R-BTA-68689; CDC6 association with the ORC:origin complex.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000014623; Expressed in semen and 104 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0097362; C:MCM8-MCM9 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:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0032406; F:MutLbeta complex binding; IEA:Ensembl.
DR GO; GO:0032407; F:MutSalpha complex binding; IEA:Ensembl.
DR GO; GO:0032408; F:MutSbeta complex binding; IEA:Ensembl.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0007292; P:female gamete generation; ISS:UniProtKB.
DR GO; GO:0048232; P:male gamete generation; ISS:UniProtKB.
DR GO; GO:0071168; P:protein localization to chromatin; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0036298; P:recombinational interstrand cross-link repair; IEA:Ensembl.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR031327; MCM.
DR InterPro; IPR001208; MCM_dom.
DR InterPro; IPR041562; MCM_lid.
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; PF17855; MCM_lid; 1.
DR Pfam; PF17207; MCM_OB; 1.
DR PRINTS; PR01657; MCMFAMILY.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00350; MCM; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50051; MCM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Chromosome; DNA damage; DNA repair;
KW DNA replication; DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..816
FT /note="DNA helicase MCM8"
FT /id="PRO_0000419470"
FT DOMAIN 378..585
FT /note="MCM"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 430..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJA3"
SQ SEQUENCE 816 AA; 90768 MW; 6ED33F4C4CA79319 CRC64;
MNGKYRGRGF GQGRFQSWKS GRGGRGFSGK WREREHRPDL NKATGKHPEQ TPQSLLLQST
LDHFIPYKGW KLYFSEVYSD SIPFIEKIEA FESFFTERIE LYDKDEIERK GSILVDFKEL
INDDEIIKLI PNIANELRDT PEKTLACMGL AIHQVLTKDL ERHAAELQAQ EGLSRNGETV
VNVPHIHARV YNYEPLTQLK NVRANYYGKY IALRGTVVRV SNTKPLCTKM AFLCAACGEI
QSLSLPDGKY NLPTKCPVPA CRGKSFTALR SSPLTVTMDW QSIKIQELMS DDQREAGRIP
RTIECELVHD LVDSCVPGDT VTITGVVKVS NAEEANSVSN NKGQKTKASE DGCKHGALME
FSLKDLYAIQ EIQSEENLFK LIVNSLCPVI FGHELVKAGL ALALFGGSQK YADDKNRIPI
RGDPHVLVVG DPGLGKSQML QAVCSVAPRG VYVCGNTTTT SGLTVTLSKD SSSGDFALEA
GALVLGDQGI CGIDEFDKMG NQHQALLEAM EQQSISLAKA GMVCSLPART SIIAAANPVG
GHYNKAKTVS ENLKMGSALL SRFDLVFILL DTPNEDHDHL LSEHVIAIRA GKQRAVSSAT
VARMNSQDSN TSILEVVSDK PLSERLKVVP GETIDPIPHQ LLRKYIGYSR QYVYPRLSTE
AAQILQNFYL ELRKQSQRLS SSPITTRQLE SLIRLTEARA RLELREEATK EDAEDIVEIM
KYSMLGTYSD EFGNLDFERS QHGSGMSNRS AAKRFISALN KIAERTYNNL FQFHQLQQIA
KELNIQVADF ENFIGSLNDQ GYLLKKGPKV YQLQTM
