MCM9_DANRE
ID MCM9_DANRE Reviewed; 1133 AA.
AC F1QDI9;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=DNA helicase MCM9;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 9;
GN Name=mcm9;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
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). {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; AL845301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F1QDI9; -.
DR SMR; F1QDI9; -.
DR STRING; 7955.ENSDARP00000115879; -.
DR PaxDb; F1QDI9; -.
DR PRIDE; F1QDI9; -.
DR ZFIN; ZDB-GENE-041014-310; mcm9.
DR eggNOG; KOG0477; Eukaryota.
DR InParanoid; F1QDI9; -.
DR PRO; PR:F1QDI9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; 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:0000724; P:double-strand break repair via homologous recombination; 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; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1133
FT /note="DNA helicase MCM9"
FT /id="PRO_0000419478"
FT DOMAIN 304..509
FT /note="MCM"
FT REGION 656..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 922..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1059
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..850
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1028..1047
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356..363
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1133 AA; 125662 MW; ABA9BECBBA761074 CRC64;
MMLSPDQVSL IGLVFETYVM EHHKSDIQQI LQENTEDLHY PVVVNAMTLF EDNMEVGECF
NAFPSKVLPI FDNALQRAAQ AISQSSSSSP QDTFRLKHNM HVRISGLPVC PELTRDHIPK
ARDVGHFLSV TGTVIRTSVT KVLEYERDYM CNKCRHVFSV QASFEQFYTF TPPTSCPSEE
GCGSFKFTCL SGSDAPPAAC KDYQEIKIQE QVQKLSVGSI PRSMLIILED DLVDSCKSGD
DITVYGVVCQ RWKPMFQDCR CDVEIVLKAN YIEVNNEQST TALVLEDIQK EFEEFWDSHK
HDPIAGRNEI LMSLCPQVFG MYVVKLAVAM VLAGGVQRID ASGTKVRGES HLLLVGDPGT
GKSQFLKYAA KITPRSVLTA GIGSTNAGLT VAAVKDSGEW HLEAGALVLS DGGLCCIDEF
NSIKEHDRTS IHEAMEQQTI SVAKAGMVCK LDTRTTILAA TNPKGQYDPN VSVSVNVALA
SPLLSRFDLV LVLLDTKNPD WDKIISSFIL QNKGAPSESL CLWSMEKMRA YFCLIKTLKP
RITPEANTIL SRYYQLQRQS DSRNAARTTI RMLESLSRLA EAHARLMFRE TVTVEDAVVV
VSVMECSMQG GALLGNVNAL HTSFPDEPCE QYKTQCEIVL ERLGLSDLLQ RELQRLSGLQ
NGRPGSPKSP QSHSEHRNEN TTSTNHSNQE LGLNWFHSLS SSSNITSNNP PTPVITSTQN
ATTPPDMTSR NQQQQASVWA KSADVSVEEA VQETVSKKLR GKRLKEMKET LLLSKDDDLE
DIFSHSTPMK NSKRKNMADT YQESGEDLHD KFTNFTFKPR EKMSHANAST STSAPEKQKR
KIETDSHPPA EGGRANKTLR METHSKNKTC IESEKDAIIP EAPKKQGVKK NNSSLRPPAE
GSRAYKILRM ETQNTNLTPI ESVRDSMKPE APKKQDVKKN ESILCPPAEG SRADKTLRME
MYNTPKDVSS QLLNDDSSAQ KQMFEDKEHP QQLLSRLNAL SPGENDDGSN KKPLKTDHPK
AKVASSTLAK LSRFSFTGSS EEQAGHKTVQ TPPVAANGGV NVVATGSEKQ ENMTNMSMRR
EISDRQEDDG ETAGRKRRCF ELGSGGSAGL IKGFSLFSSS VLDDEDFDDV WNW
