ID   MCM9_XENLA              Reviewed;        1143 AA.
AC   Q6NRM6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=DNA helicase MCM9;
DE            EC=3.6.4.12;
DE   AltName: Full=Minichromosome maintenance 9;
GN   Name=mcm9;
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 [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION.
RX   PubMed=16226853; DOI=10.1016/j.gene.2005.07.031;
RA   Lutzmann M., Maiorano D., Mechali M.;
RT   "Identification of full genes and proteins of MCM9, a novel, vertebrate-
RT   specific member of the MCM2-8 protein family.";
RL   Gene 362:51-56(2005).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH CDT1.
RX   PubMed=18657502; DOI=10.1016/j.molcel.2008.07.001;
RA   Lutzmann M., Mechali M.;
RT   "MCM9 binds Cdt1 and is required for the assembly of prereplication
RT   complexes.";
RL   Mol. Cell 31:190-200(2008).
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 MCM2-7 loading onto
CC       chromatin during DNA replication. Probably not required for DNA
CC       replication in other cells. {ECO:0000250, ECO:0000269|PubMed:18657502}.
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 (By similarity). Interacts with cdt1.
CC       {ECO:0000250, ECO:0000269|PubMed:18657502}.
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}.
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; BC070720; AAH70720.1; -; mRNA.
DR   EMBL; BN000881; CAJ70647.1; -; mRNA.
DR   RefSeq; NP_001084773.1; NM_001091304.1.
DR   AlphaFoldDB; Q6NRM6; -.
DR   SMR; Q6NRM6; -.
DR   BioGRID; 101175; 2.
DR   MaxQB; Q6NRM6; -.
DR   DNASU; 431809; -.
DR   GeneID; 431809; -.
DR   KEGG; xla:431809; -.
DR   CTD; 431809; -.
DR   Xenbase; XB-GENE-949289; mcm9.L.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 431809; Expressed in egg cell and 14 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: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   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..1143
FT                   /note="DNA helicase MCM9"
FT                   /id="PRO_0000304145"
FT   DOMAIN          301..506
FT                   /note="MCM"
FT   REGION          721..767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          838..864
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..915
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          998..1022
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..767
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         353..360
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1143 AA;  126594 MW;  873807828F991D83 CRC64;
     MYLGFEQVAL VGQVFESFVL EHHKNEIAQI LTEKEEHAHY SLVVNAMTLF EANMEIGEYF
     NAFPNEVLPV FDNALRCAAM SFLQSCSEKY TFLMKQNLHA RITGLPVCPE LTREHIPRTR
     DVGHFLSVTG TVIRTSLVKV LEYEQDFMCN KCKHVVTVKA DFEQHYTFKP PIACSNEEGC
     NSTKFTCLSD SSSPASCRDY QEIKIQEQVQ RLSVGSIPRS MIVVLEDDLV DSCKSGDDIT
     VYGVVMQRWK PLYIDMRCDL EIVLKANYIS VNNEQPCGVV INEEVRKEYE DFWVKYRNNP
     LEGRNEILAS LCPQVFGMFV VKLAVAMVLA GGVQRIDSAG TRVRGESHLL LVGDPGTGKS
     QFLKYAAKIT PRSVLTAGIG STSAGLTVTA VKDSGEWNLE AGALVLADGG LCCIDEFNSI
     KEHDRTSIHE AMEQQTISVA KAGLVCKLNT RTTILAATNP KGQYDPDESI SVNVALASPL
     LSRFDLVLVL LDTKNEDWDR IISSFILESK GCPRKSDKLW SMEKMKTYFC LIKNLQPKMS
     QDANVILVRY YQLQRQSSCR NAARTTIRLL ESLIRLAEAH ARIMYRDVVT TEDAITVVSI
     MESSMQGGAL LGGVNALHTS FPENPREQYR LQCELLLDKL GLQKLLEEEL QRLERQQSED
     SLESDLGESA TNLVGHKVVH SECVMEETFS TFEASSLPDE THLGVTGSAA FIQTPKKTIS
     DMTKSDDTIR KGTITPAEQN RGISTDAESS LKQGNAQPLA GGHLSENNLT KCTDNSLGWF
     DTLQSIQMSP ITKQREGCTA EKLQQEVLPV STESSCHPAD KKVVNLGGRN KLEVLQASGS
     SPGGNGRDLS NHTVTCGSSP ERNKRDLSNH IVTEHVSKKW RRINKDSLCG KNVPSFQPQS
     ENTDSAPVCS SVPLHSTPDV AQRRKRIIAQ VEKQSKAEVE DPDTKARLAQ LAKFSFKRHS
     KLVHSPAGDT DTASNAQKHD HPVQKITLSE KLNNLGRTVN NVDKSSNSVN GSKQQKHVEN
     TSKQTVITQK SNFESNTLNA PVHETKLNEG CDSRKVSSST LAKLARFSFS PPPENQAAET
     SKETLILPRA VAPGSKRKCF ELNPSTDKTT MSSKSLFSTT DLDDEELDVD WEAEIKGNQR
     IAT