MCM9_BOVIN
ID MCM9_BOVIN Reviewed; 1139 AA.
AC F1N2W9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=DNA helicase MCM9;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 9;
GN Name=MCM9;
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 MRN complex,
CC indirectly regulates the recruitment of downstream effector RAD51 to
CC DNA damage sites including DBSs and ICLs. Acts as a helicase in DNA
CC mismatch repair (MMR) following DNA replication errors to unwind the
CC mismatch containing DNA strand. In addition, recruits MLH1, a component
CC of the MMR complex, to chromatin. The MCM8-MCM9 complex is dispensable
CC for DNA replication and S phase progression. Probably by regulating HR,
CC plays a key role during gametogenesis. {ECO:0000250|UniProtKB:Q2KHI9,
CC ECO:0000250|UniProtKB:Q9NXL9}.
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:Q9NXL9};
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 MLH1; the interaction recruits MLH1 to chromatin. Interacts with
CC MSH2; the interaction recruits MCM9 to chromatin. Interacts with MSH6.
CC Interacts with the MRN complex composed of MRE11, RAD50 and NBN/NBS1;
CC the interaction recruits the MRN complex to DNA damage sites. Interacts
CC with RAD51; the interaction recruits RAD51 to DNA damage sites.
CC {ECO:0000250|UniProtKB:Q9NXL9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NXL9}.
CC Chromosome {ECO:0000250|UniProtKB:Q9NXL9}. Note=Colocalizes to nuclear
CC foci with RPA1 following DNA damage. Localizes to double-stranded DNA
CC breaks. Recruited to chromatin by MSH2. {ECO:0000250|UniProtKB:Q9NXL9}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DAAA02025730; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_001789594.4; XM_001789542.5.
DR RefSeq; XP_002690126.3; XM_002690080.5.
DR AlphaFoldDB; F1N2W9; -.
DR SMR; F1N2W9; -.
DR STRING; 9913.ENSBTAP00000002665; -.
DR PaxDb; F1N2W9; -.
DR PRIDE; F1N2W9; -.
DR GeneID; 100139498; -.
DR KEGG; bta:100139498; -.
DR CTD; 254394; -.
DR eggNOG; KOG0477; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; F1N2W9; -.
DR OrthoDB; 266497at2759; -.
DR TreeFam; TF329421; -.
DR Proteomes; UP000009136; Unplaced.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
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:0007276; P:gamete generation; ISS:UniProtKB.
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; Chromosome; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1139
FT /note="DNA helicase MCM9"
FT /id="PRO_0000419475"
FT DOMAIN 299..504
FT /note="MCM"
FT REGION 671..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1060..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..879
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..903
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1011
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 351..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXL9"
FT MOD_RES 1105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NXL9"
SQ SEQUENCE 1139 AA; 126508 MW; FEFFF2D5438DDE8E CRC64;
MNSDQVTLVG QVFESYVSEY HKNDILLILK ERDEDAHYPV VVNAMTLFET NMEIGEYFNA
FPNEVLTIFD NALRRSALTI LQSLSQPEGL SMKQNLHARI SGLPVCPELV REHIPKTKDV
GHFLSVTGTV IRTSLVKILE FERDYMCNKC KHVFVVQADF EQYYTFFRPS SCPSLENCDS
SKFTCLSDLS SPTRCRDYQE IKIQEQVQRL SVGSIPRSMQ VILEDDLVDS CKSGDDITIY
GVVMQRWKPF KQDVRCEVEI VLKANYIQVN NEESAGVNMD EEVRKEFEDF WEHYKSDPFA
GRNEILASLC PQVFGMYLVK LAVAMVLAGG IQRTDATGTR VRGESHLLLV GDPGTGKSQF
LKYAAKITPR SVLTTGIGST SAGLTVTAVK DSGEWNLEAG ALVLADAGLC CIDEFNSLKE
HDRTSIHEAM EQQTISVAKA GLVCKLNTRT TILAATNPKG QYDPRESVSV NIALSSPLLS
RFDLILVLLD TKNEDWDRII SSFILENKGY PSKSEKLWSM EKMKSYFCLI RKLQPTLSDE
GNQVLLRYYQ MQRQSDSRNA ARTTIRLLES LIRLAEAHAR LMFRDTVTLE DAVTVVSVME
SSMQGGALLG GVNALHTSFP ENPLQQYQTQ CELILEKLEL PNLLSEELRR LERLQNWSVD
QSQPQAMEAE TIPGSLGGDA RKESNFRTST QQEVNCSAHR FSIGGSFGGS PLLGPSSHLG
PKGPASGKHS EEHRNSQDGS LDWFDSVATH PIEPKNTAPV SPSPKTSRGA MALKICNNRS
QGKEDREAGQ RSKLETEPLP AAGETETPLR PGNREGERPR KAATVSEAAV SADEPDSVLT
HHVPRKLHKL HKARAQELCR NPTRPPLQPT SPSHPQPTPI QSPERVLETP KRKRQKSHAQ
AQEPHQESVE SLGAPVAKLA KFTFKQKSKL THSPEDRGPV SPGTSKPVVQ SPENPQRRAK
RGAALPGKGP EKLASRIRSS AQPQDETRGV SPQPPYKDRP EEKRERAPAK GTVQPELELG
NDMGRFFLAS ERVRKEEVSC SNKSSKVHAC TLAKLANFSF TSPSESKSES PPPPQSKNPS
EGGPSCVATA TALGRKRKTF QLDTSTEKLS LSKTSLFTLP ELDDEPLDFD WDEEMRKKP
