ID   MCM8_XENTR              Reviewed;         843 AA.
AC   Q0V9Q6;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=DNA helicase MCM8;
DE            EC=3.6.4.12;
DE   AltName: Full=Minichromosome maintenance 8;
GN   Name=mcm8;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20431018; DOI=10.1126/science.1183670;
RA   Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J.,
RA   Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., Blitz I.L.,
RA   Blumberg B., Dichmann D.S., Dubchak I., Amaya E., Detter J.C., Fletcher R.,
RA   Gerhard D.S., Goodstein D., Graves T., Grigoriev I.V., Grimwood J.,
RA   Kawashima T., Lindquist E., Lucas S.M., Mead P.E., Mitros T., Ogino H.,
RA   Ohta Y., Poliakov A.V., Pollet N., Robert J., Salamov A., Sater A.K.,
RA   Schmutz J., Terry A., Vize P.D., Warren W.C., Wells D., Wills A.,
RA   Wilson R.K., Zimmerman L.B., Zorn A.M., Grainger R., Grammer T.,
RA   Khokha M.K., Richardson P.M., Rokhsar D.S.;
RT   "The genome of the Western clawed frog Xenopus tropicalis.";
RL   Science 328:633-636(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2006) 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. In eggs, required for elongation during DNA replication by
CC       facilitating the recruitment of rpa2/rpa34 and stimulating the
CC       processivity of DNA polymerases at replication foci. Probably not
CC       required for DNA replication in other cells (By similarity).
CC       {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   -!- 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; AAMC01063807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01063808; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01063809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01063810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01063811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01063812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01063813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAMC01063814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC121433; AAI21434.1; -; mRNA.
DR   RefSeq; NP_001072344.1; NM_001078876.1.
DR   AlphaFoldDB; Q0V9Q6; -.
DR   SMR; Q0V9Q6; -.
DR   STRING; 8364.ENSXETP00000060047; -.
DR   PaxDb; Q0V9Q6; -.
DR   DNASU; 779797; -.
DR   Ensembl; ENSXETT00000061843; ENSXETP00000060047; ENSXETG00000004500.
DR   GeneID; 779797; -.
DR   KEGG; xtr:779797; -.
DR   CTD; 84515; -.
DR   Xenbase; XB-GENE-961372; mcm8.
DR   eggNOG; KOG0480; Eukaryota.
DR   InParanoid; Q0V9Q6; -.
DR   OMA; THTVDWQ; -.
DR   OrthoDB; 266497at2759; -.
DR   PhylomeDB; Q0V9Q6; -.
DR   TreeFam; TF323155; -.
DR   Reactome; R-XTR-176187; Activation of ATR in response to replication stress.
DR   Reactome; R-XTR-68689; CDC6 association with the ORC:origin complex.
DR   Reactome; R-XTR-68962; Activation of the pre-replicative complex.
DR   Proteomes; UP000008143; Chromosome 5.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000004500; Expressed in testis and 11 other tissues.
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: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: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..843
FT                   /note="DNA helicase MCM8"
FT                   /id="PRO_0000419474"
FT   DOMAIN          394..601
FT                   /note="MCM"
FT   REGION          1..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         446..453
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   843 AA;  93575 MW;  29D2046FFDCDA998 CRC64;
     MSQGWRGGWS GGRGGNPYAG GWRGRPWRGR GQGGSWSRNS GRDPVCFSTA PPKPQLTQTT
     LDKYIPYKGW KLYFSEAYSD SSPFLEKVRA FEKFFTKQIE LYDKDEIERK GSILVDYKDL
     LQDEDLSASI PMSSELKEMP EKILECMGLA IHQVLTKDLE RHAAELQEQE GLRTEEAPIV
     NVPFIHARVF NYDPLTPLKN LRASLYGKYV ALRGTVVRVS NIKPLCVKMA FSCNMCGDIQ
     SFPFPDGKYA VPTKCPVPEC RGRSFTANRS SPLTVTVDWQ TIKVQELMSD DQREAGRIPR
     TVECELIQDL VDSCVPGDMV TVTGIVKVSN TRDGGFKNKN NKCMFLLYIE ANSVSNSKGH
     KIKSTDDSES HGASMDFSLK DLYAIQEIQA QENLFQLIVN SLCPTIYGHE LVKAGLSLAL
     FGGCQKYADD KNRIPIRGDP HILVVGDPGL GKSQMLQAVC NVAPRGVYVC GNTTTTSGLT
     VTLSRDSATG DFGLEAGALI LGDQGICGID EFDKMGNQHQ ALLEAMEQQS ISLAKAGIVC
     SLPARTSIIA AANPVGGHYN KGKTVSENLK MGSALLSRFD LVFILLDTPN EDHDHLLSEH
     VMAMRAGAKE MQSADLTCPT TQNSNTSVLE EPSERPLGER LKLRPGEHFD PIPHQLLRKY
     VGYARQYVHP TLSPDAAQVL QDFYLELRKQ NQGIDSTPIT TRQLESLIRL TEARARLELR
     EKATKDDAEE VVQIMKYSLL GTFSDEFGKL DFHRSQHGSG MSNRSKAKKF ISALNRIAEQ
     TYNNLFEFQQ LRQIAKELQI QLLGKFNHSD KMATEIPNLR AAPGNQLRPK GSVSVLITTW
     DCA