ID   MCM9_XENTR              Reviewed;        1117 AA.
AC   F6RIX4;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=DNA helicase MCM9;
DE            EC=3.6.4.12;
DE   AltName: Full=Minichromosome maintenance 9;
GN   Name=mcm9;
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).
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 MCM2-7 loading onto chromatin during DNA
CC       replication. Probably not required for DNA replication in other cells
CC       (By similarity). {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. Interacts with cdt1 (By similarity).
CC       {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; AAMC01008549; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; F6RIX4; -.
DR   SMR; F6RIX4; -.
DR   STRING; 8364.ENSXETP00000028127; -.
DR   PaxDb; F6RIX4; -.
DR   PRIDE; F6RIX4; -.
DR   eggNOG; KOG0477; Eukaryota.
DR   HOGENOM; CLU_000995_7_2_1; -.
DR   InParanoid; F6RIX4; -.
DR   OMA; LESKGCP; -.
DR   TreeFam; TF329421; -.
DR   Proteomes; UP000008143; Genome assembly.
DR   Proteomes; UP000790000; Unplaced.
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: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   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA replication; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT   CHAIN           1..1117
FT                   /note="DNA helicase MCM9"
FT                   /id="PRO_0000419479"
FT   DOMAIN          301..506
FT                   /note="MCM"
FT   REGION          686..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..704
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        868..886
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   1117 AA;  123826 MW;  D8224F4DE6897B49 CRC64;
     MYLSPEQVAL VGQVFESFVL EHHQKEIAQI LTEKYEDAHY SLVVNAMTLF EANMEIGEYF
     NAFPNEVLPI FDNALRRAAM SFLQSCSEKQ TLVMKQNFHA RITGLPVCPE LTREHIPRTR
     DVGHFLSVTG TVIRTSLVKV LEYEQDFMCN KCKHVVTVKA DFEQYYTFKP PITCSNEEGC
     NSSKFTCLSD SSTPASCRDY QEIKIQEQVQ RLSVGSIPRS MIVVLEDDLV DSCKSGDDVT
     VYGVVMQRWK PLYIDTRCDL EIVLKANYIA VNNEQPCGVV INEEVRKEYE GFWEKYRNSP
     LEGRNEILAS LCPQVFGMFV VKLAVAMVLA GGVQRIDSAG TRVRGESHLL LVGDPGTGKS
     QFLKYAVKIT PRSVLTAGIG STSAGLTVTA VKDSGEWNLE AGALVLADGG LCCIDEFNSI
     KEHDRTSIHE AMEQQTISVA KAGLVCKLNT RTTILAATNP KGQYDPEESI SVNVALASPL
     LSRFDLVLVL LDTKNEDWDR IISSFILESK GCPRKSDKLW SMEKMKTYFC LIKNLQPKMS
     QDANVILVRY YQLQRQSSCR NAARTTIRLL ESLIRLAEAH ARLMYRDVVT TEDAITVVSI
     MESSMQGGAL LGGVNALHTS FPENPREQYR MQCELLLERL GLQKLLDKEL QRLDRQQNED
     SLESDHGESA SNISCNLVGH KVHSDSAMEE TCSTNETFSS PDATRKTIPD ILDMTKSDDT
     ISKGTITPAE QNRAIRTQSK SSSKHNTQSL AGGHLSENHL TRCSDKSLGW FDSLQSVQMS
     PISKLGEGCT AEKLQPAVLP VLAEGSCHPD KEVVDLVGNK SEVLQKSGSS PVGTERHLSN
     RIVTEHVSKK WQNLNKNSLC GKTGSNMTSL QSENSGSHTV CSSGPLHSTP GAPWKRKKII
     AQVEKETKAE LLDPDTQARL VQLARFSFKQ HSKLVHLPGG KTDIASIAQN HEDQPDQKLT
     PSDRLNKLDR ILNNVDKASN SVKGLKQQDT LAQENPPKQT VLAQQSNSIS NAATACVHEK
     KLNEGSDSRK VSSSTLAKLA RFSFSPPPEN KALEASKETL ISSRAAAPSS KRKCFQLEPS
     SDKTTMSSKF LFSTDLDDDE LDVDWEVEIK RNKRTAT