MCM9_CHICK
ID MCM9_CHICK Reviewed; 1169 AA.
AC I0IUP4; F1N960;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=DNA helicase MCM9;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 9;
GN Name=MCM9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, IDENTIFICATION IN THE MCM8-MCM9
RP COMPLEX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-360 AND ARG-484.
RX PubMed=22771115; DOI=10.1016/j.molcel.2012.05.047;
RA Nishimura K., Ishiai M., Horikawa K., Fukagawa T., Takata M., Takisawa H.,
RA Kanemaki M.T.;
RT "Mcm8 and Mcm9 form a complex that functions in homologous recombination
RT repair induced by DNA interstrand crosslinks.";
RL Mol. Cell 47:511-522(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
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. {ECO:0000269|PubMed:22771115}.
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:0000269|PubMed:22771115}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22771115}.
CC Note=Localizes to nuclear foci and colocalizes with RAD51.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
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DR EMBL; AB689141; BAM08993.1; -; mRNA.
DR EMBL; AADN02001969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AADN02001970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001292018.1; NM_001305089.1.
DR AlphaFoldDB; I0IUP4; -.
DR SMR; I0IUP4; -.
DR STRING; 9031.ENSGALP00000023968; -.
DR PaxDb; I0IUP4; -.
DR PRIDE; I0IUP4; -.
DR GeneID; 100857742; -.
DR KEGG; gga:100857742; -.
DR CTD; 254394; -.
DR VEuPathDB; HostDB:geneid_100857742; -.
DR eggNOG; KOG0477; Eukaryota.
DR InParanoid; I0IUP4; -.
DR OrthoDB; 266497at2759; -.
DR PRO; PR:I0IUP4; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
DR GO; GO:0097362; C:MCM8-MCM9 complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IDA: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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1169
FT /note="DNA helicase MCM9"
FT /id="PRO_0000419477"
FT DOMAIN 302..507
FT /note="MCM"
FT REGION 685..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 928..946
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 360
FT /note="K->A: Loss of function; when associated with A-484."
FT /evidence="ECO:0000269|PubMed:22771115"
FT MUTAGEN 484
FT /note="R->A: Loss of function; when associated with A-360."
FT /evidence="ECO:0000269|PubMed:22771115"
FT CONFLICT 196
FT /note="S -> T (in Ref. 1; BAM08993)"
FT /evidence="ECO:0000305"
FT CONFLICT 675
FT /note="I -> T (in Ref. 1; BAM08993)"
FT /evidence="ECO:0000305"
FT CONFLICT 689
FT /note="K -> Q (in Ref. 1; BAM08993)"
FT /evidence="ECO:0000305"
FT CONFLICT 1050
FT /note="L -> Q (in Ref. 1; BAM08993)"
FT /evidence="ECO:0000305"
FT CONFLICT 1064
FT /note="P -> H (in Ref. 1; BAM08993)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1169 AA; 129682 MW; 7A7E8732F2531201 CRC64;
MALRADQVSL IGQVFESYLL QHHRDDILGI LRQGDDEAHY PVLVDALTLF ETNMEIGEYF
NAFPSQVLPI FDGALRRAAM AVLQAATPSP ELRMKPNLHA RISGLPICPE LTREHIPKTR
DVGHFLSVTG TVIRTSLVKV LEFERSYICN KCKHVFVAKA DFEQYYAFCR PSACLNEEGC
NSTKFTCLSG TSSSPSSCRD YQEIKIQEQV QRLSVGSIPR CMVVVLEDDL VDSCKSGDDI
TVYGVVMQRW KPFHQDARCD LELVLKANYV KVNNEQLAGV TIDEEVRKEF EDFWEKHRNN
PLAGRNEILA SLCPQVFGLY LVKLAVAMVL AGGVQRIDAT GTRIRGESHL LLVGDPGTGK
SQFLKYAVKI TPRSVLTAGI GSTSAGLTVT AVKDFGEWNL EAGALVLADG GLCCIDEFNS
IKEHDRTSIH EAMEQQTISV AKAGLVCKLN TRTTILAATN PKGHYDPAES VSVNIALGSP
LLSRFDLVLV LLDTKNEEWD RIISSFILQN KGCPSKSEKL WSMEKMKTYF CLIKRIQPKL
SDESNLILVR YYQMQRQSDC RNAARTTIRL LESLIRLAEA HARLMFRDTV TLEDAVTVVS
VMESSMQGGA LLGAINALHT SFPENPMTQY RMQCELILER LELHDLLHKE LQRLDRLQKE
TYCQLQPEET SFSTITGCLN KNTFESKQKS QSEPSDQQKI NSYPQPSLPK SNCEGDKHPE
ALRNPTPGNN ISTKRLSRLN KRSDDGSLGW FDRLEDRNTD AEETFWKTSP LPKTSPDNMA
LKTMSKSSCS EEGNSSVPRK EDGMRGSLRT VTLCAPLEQD KVSEISSKRT EERKCFSSEA
NIQDPTSASA SVQESVITQR VSKSLQRLHT EKSHRFFTST QNSEANALPS VLPVSGLLDL
SSDTDSVVGD ENNSASAAVK HAVISMRKRS KGQAEKEAKA VSSHEPEITD GESPPAAKLA
KFSFRPRTKL DDSSEKKNAE FPLFPSENTV KPGEQPQGEQ LQKDCCPPEK RKMTLTCLGR
KGLEKQSIGS KGNEEQLSQA LGKEMGGNAL IHSDVTLDVV SPPPTEKRRE GEEKLGGPST
VRVCSSTLEN LSKFCFASRP DSKSEAPPTI KTDTNNKESH SPLLKVHVSN PNKRKSFALG
NASKDSVVTR KSLFSIAELD DATLDFDWD
