MCM8_ARATH
ID MCM8_ARATH Reviewed; 801 AA.
AC Q9SF37; L7UY20;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable DNA helicase MCM8;
DE EC=3.6.4.12;
DE AltName: Full=Minichromosome maintenance 8;
DE Short=AtMCM8;
GN Name=MCM8; OrderedLocusNames=At3g09660; ORFNames=F11F8.25;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23300481; DOI=10.1371/journal.pgen.1003165;
RA Crismani W., Portemer V., Froger N., Chelysheva L., Horlow C.,
RA Vrielynck N., Mercier R.;
RT "MCM8 is required for a pathway of meiotic double-strand break repair
RT independent of DMC1 in Arabidopsis thaliana.";
RL PLoS Genet. 9:E1003165-E1003165(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP GENE FAMILY.
RX PubMed=17556508; DOI=10.1104/pp.107.101105;
RA Shultz R.W., Tatineni V.M., Hanley-Bowdoin L., Thompson W.F.;
RT "Genome-wide analysis of the core DNA replication machinery in the higher
RT plants Arabidopsis and rice.";
RL Plant Physiol. 144:1697-1714(2007).
CC -!- FUNCTION: Probable DNA helicase that plays a role in meiotic double-
CC strand break (DSB) repair, but seems not required for recombination
CC with the homologous chromosome. May be involved with RAD51 in a backup
CC pathway that repairs meiotic DSB without giving meiotic crossover, in
CC parallel to the meiotic homologous recombination which relies on DMC1.
CC {ECO:0000269|PubMed:23300481}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility and seed numbers due to defects
CC in gametogenesis. {ECO:0000269|PubMed:23300481}.
CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23296.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KC109786; AGC54635.1; -; mRNA.
DR EMBL; AC016661; AAF23296.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74794.2; -; Genomic_DNA.
DR RefSeq; NP_001319512.1; NM_001337836.1.
DR AlphaFoldDB; Q9SF37; -.
DR SMR; Q9SF37; -.
DR STRING; 3702.AT3G09660.1; -.
DR PRIDE; Q9SF37; -.
DR ProteomicsDB; 238324; -.
DR EnsemblPlants; AT3G09660.1; AT3G09660.1; AT3G09660.
DR GeneID; 820123; -.
DR Gramene; AT3G09660.1; AT3G09660.1; AT3G09660.
DR KEGG; ath:AT3G09660; -.
DR Araport; AT3G09660; -.
DR TAIR; locus:2074934; AT3G09660.
DR eggNOG; KOG0480; Eukaryota.
DR HOGENOM; CLU_000995_7_2_1; -.
DR InParanoid; Q9SF37; -.
DR OrthoDB; 266497at2759; -.
DR PRO; PR:Q9SF37; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SF37; baseline and differential.
DR Genevisible; Q9SF37; AT.
DR GO; GO:0042555; C:MCM complex; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:TAIR.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:TAIR.
DR GO; GO:0007140; P:male meiotic nuclear division; IMP:TAIR.
DR GO; GO:0009555; P:pollen development; IMP:TAIR.
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; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Meiosis; Metal-binding; Nucleotide-binding; Nucleus; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..801
FT /note="Probable DNA helicase MCM8"
FT /id="PRO_0000426001"
FT DOMAIN 351..558
FT /note="MCM"
FT ZN_FING 180..207
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT MOTIF 534..537
FT /note="Arginine finger"
FT BINDING 403..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 801 AA; 88125 MW; 811B5AA36E2D58C9 CRC64;
MGFYGGGSMA SGRPESTGID SLGIGKILAV YIKDNENLAI DEDKLQLTAE LIRVFSASPG
RDIVSQVNED GGGSFSLSLD LQQFKKISDI ENFFINLEDN PKGVIPCMNA AVHKVLFDQW
ETNEFENVMK INVRLHNYPE SSISLKNLRA AYIGKLVTVH GTVVKVSTVK PLVTQMAFDC
GKCKTGITRE FTDGKFSPPL KCDSHGCKSK TFTPIRSSAQ TIDFQKIRVQ ELQKPEDHEE
GRVPRTVECE LMEDLVDICI PGDVVTVTGI IGVINNYMDI GGGKSKTKNQ GFYYLFIEAV
SVKNTKRQSA FENSEDSSSS AQTADVGDLY SFSQRDLEFI VKFKEEYGSD TFRRILHSVC
PSIYGHEIVK AGITLSLFGG VRKHSMDRNK VPVRGDIHVI IVGDPGLGKS QLLQAAAAIS
PRGIYVCGNA TTRAGLTVAV VKDSMTNDYA FEAGAMVLAD GGLCCIDEFD KMTTEHQALL
EAMEQQCVSV AKAGLVASLS ARTSVIAAAN PVGGHYNRAK TVNENLKMSA ALLSRFDLVF
ILLDKPDELL DKQVSEHIMS LHSASGETSP ALKKFKPVNA ASQNAGYANM HAEGNSLLSR
LRLDSEKDDD FSPVPGQLLR KYISYARNFV NPKMSKDAGE IIQKFYLKLR DHNTSADSTP
ITARQLESLV RLAQARARVD LREEITVQDA MDVVEIMKES LYDKLIDEHG VVDFGRSGGM
SQQKEAKRFL SALDKQSELQ QKDCFSVSEM YSLADRIGLR VPDIDTFLEN LNIAGYLLKK
GPKTYQVLSS SYSRSQSSRS R
