MCM8_XENLA
ID MCM8_XENLA Reviewed; 831 AA.
AC Q5F310; Q501Q5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=DNA helicase MCM8;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 8;
GN Name=mcm8;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=15707891; DOI=10.1016/j.cell.2004.12.010;
RA Maiorano D., Cuvier O., Danis E., Mechali M.;
RT "MCM8 is an MCM2-7-related protein that functions as a DNA helicase during
RT replication elongation and not initiation.";
RL Cell 120:315-328(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the MCM8-MCM9 complex, a complex involved in
CC homologous recombination repair following DNA interstrand cross-links
CC and plays a key role during gametogenesis. The MCM8-MCM9 complex
CC probably acts as a hexameric helicase required to process aberrant
CC forks into homologous recombination substrates and to orchestrate
CC homologous recombination with resection, fork stabilization and fork
CC restart (By similarity). In eggs, required for elongation during DNA
CC replication by facilitating the recruitment of rpa2/rpa34 and
CC stimulating the processivity of DNA polymerases at replication foci.
CC Probably not required for DNA replication in other cells. {ECO:0000250,
CC ECO:0000269|PubMed:15707891}.
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 -!- SUBUNIT: Component of the MCM8-MCM9 complex, which forms a hexamer
CC composed of mcm8 and mcm9. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Localizes to nuclear
CC foci and colocalizes with rad51. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AJ867218; CAI29793.1; -; Genomic_DNA.
DR EMBL; BC095919; AAH95919.1; -; mRNA.
DR RefSeq; NP_001089437.1; NM_001095968.1.
DR AlphaFoldDB; Q5F310; -.
DR SMR; Q5F310; -.
DR BioGRID; 592268; 3.
DR IntAct; Q5F310; 1.
DR GeneID; 734487; -.
DR KEGG; xla:734487; -.
DR CTD; 734487; -.
DR Xenbase; XB-GENE-961378; mcm8.L.
DR OrthoDB; 266497at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 734487; Expressed in testis and 19 other tissues.
DR GO; GO:0097362; C:MCM8-MCM9 complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
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:0030174; P:regulation of DNA-templated DNA replication initiation; IEA:UniProt.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..831
FT /note="DNA helicase MCM8"
FT /id="PRO_0000419473"
FT DOMAIN 395..602
FT /note="MCM"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 13
FT /note="R -> RGG (in Ref. 1; CAI29793)"
FT /evidence="ECO:0000305"
FT CONFLICT 130
FT /note="A -> S (in Ref. 1; CAI29793)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="K -> KL (in Ref. 1; CAI29793)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 92300 MW; 1F9AB5787AC29F13 CRC64;
MSQGWRGGSG GWRGGGGGNP YAGAWRGRPW RGRGQGGTWS RNNGRDPVCF APPKPQLTQT
TLDKYIPYKG WKLYFSEAYS DNSPFLEKVR AFEKFFKKQI ELYDKDEIER KGSILVDYKE
LLQDEDLSAA IPLSSELKDM PEKVLECMGL AIHQVLTKDL ETHAADLQQQ EGLRTEEAPI
VNVPFIHARV FNYDTLTSLK NLRASLYGKY VALRGTVVRV GNIKPLCTKM AFSCNMCGDI
QCFPLPDGKY TVPTKCPVPE CRGRSFTANR SSPLTVTVDW QTIKVQELMS DDQREAGRIP
RTVECELIQD LVDSCVPGDM ITVTGIVKVS NTRDGGFKNK NNKCMFLLYI EANSVSNSKG
QKGKSTEDSG NHGASMDFSL KDLYAIQEIQ SQENLFQLIV NSLCPTIYGH ELVKAGLSLA
LFGGCQKYAD DKNRIPIRGD PHILVVGDPG LGKSQMLQAV CNVAPRGVYV CGNTTTTSGL
TVTLSRDTTT GDFGLEAGAL VLGDQGICGI DEFDKMGNQH QALLEAMEQQ SISLAKAGIV
CSLPARTSII AAANPVGGHY NKGKTVSENL KMGSALLSRF DLVFILVDTP NEDHDHLLSE
HVMAMRSGAK EIQSVDITRI NTQNSNTSIL EVPSERPLGE RLKRTGEHFD ALPHQLLRKF
VGYARQYVHP SLSPDAAQIL QDFYLELRKQ NQGIDSTPIT TRQLESLIRL TEARARLELR
EKATKEDAEE VVQIMKYSLL GTFSDEFGKL DFQRSQHGSG MSNRSKAKKF VSALNRVAEQ
TYNNLFEFQQ LRQIARELQI QVIDFEAFIG SLNDQGYLLK KGPRVFQLQT M
