MORC7_ARATH
ID MORC7_ARATH Reviewed; 707 AA.
AC F4JRS4; Q9SW29;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein MICRORCHIDIA 7 {ECO:0000303|PubMed:24799676};
DE Short=AtMORC7 {ECO:0000303|PubMed:24799676};
DE EC=3.6.-.-;
DE AltName: Full=Protein CRT1-homolog 3 {ECO:0000303|PubMed:19704828};
DE Short=CRT1-h3 {ECO:0000303|PubMed:19704828};
GN Name=MORC7 {ECO:0000303|PubMed:24799676};
GN Synonyms=CRH3 {ECO:0000303|PubMed:19704828};
GN OrderedLocusNames=At4g24970 {ECO:0000312|Araport:AT4G24970};
GN ORFNames=F13M23.110 {ECO:0000312|EMBL:CAB36739.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
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 [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=19704828; DOI=10.4161/psb.3.9.5822;
RA Kang H.-G., Klessig D.F.;
RT "The involvement of the Arabidopsis CRT1 ATPase family in disease
RT resistance protein-mediated signaling.";
RL Plant Signal. Behav. 3:689-690(2008).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=24799676; DOI=10.1073/pnas.1406611111;
RA Moissiard G., Bischof S., Husmann D., Pastor W.A., Hale C.J., Yen L.,
RA Stroud H., Papikian A., Vashisht A.A., Wohlschlegel J.A., Jacobsen S.E.;
RT "Transcriptional gene silencing by Arabidopsis microrchidia homologues
RT involves the formation of heteromers.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:7474-7479(2014).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=27171361; DOI=10.1371/journal.pgen.1005998;
RA Harris C.J., Husmann D., Liu W., Kasmi F.E., Wang H., Papikian A.,
RA Pastor W.A., Moissiard G., Vashisht A.A., Dangl J.L., Wohlschlegel J.A.,
RA Jacobsen S.E.;
RT "Arabidopsis AtMORC4 and AtMORC7 form nuclear bodies and repress a large
RT number of protein-coding genes.";
RL PLoS Genet. 12:E1005998-E1005998(2016).
CC -!- FUNCTION: Exhibits ATPase activity. Binds DNA/RNA in a non-specific
CC manner and exhibits endonuclease activity. Probably involved in DNA
CC repair. Involved in RNA-directed DNA methylation (RdDM) as a component
CC of the RdDM machinery and required for gene silencing. May also be
CC involved in the regulation of chromatin architecture to maintain gene
CC silencing. Together with MORC4, acts to suppress a wide set of non-
CC methylated protein-coding genes, especially involved in pathogen
CC response. Positive regulators of defense against the oomycete
CC Hyaloperonospora arabidopsidis (Hpa) (PubMed:27171361).
CC {ECO:0000250|UniProtKB:Q84WV6, ECO:0000269|PubMed:27171361}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q84WV6};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q84WV6};
CC -!- SUBUNIT: Homodimer and heterodimer. Component of an RNA-directed DNA
CC methylation (RdDM) complex. Forms homomeric complexes
CC (PubMed:27171361). {ECO:0000250|UniProtKB:Q84WV6,
CC ECO:0000269|PubMed:27171361}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:27171361}. Note=Accumulates in discrete nuclear
CC bodies adjacent to chromocenters. {ECO:0000269|PubMed:27171361}.
CC -!- DISRUPTION PHENOTYPE: The double mutant atmorc4 atmorc7 exhibits a
CC pathogen response phenotype with abnormal up-regulation of several
CC genes involved in plant defense. {ECO:0000269|PubMed:27171361}.
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36739.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL035523; CAB36739.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161562; CAB79406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE84983.1; -; Genomic_DNA.
DR PIR; T05518; T05518.
DR RefSeq; NP_194227.2; NM_118629.3.
DR AlphaFoldDB; F4JRS4; -.
DR SMR; F4JRS4; -.
DR STRING; 3702.AT4G24970.1; -.
DR iPTMnet; F4JRS4; -.
DR PaxDb; F4JRS4; -.
DR PRIDE; F4JRS4; -.
DR ProteomicsDB; 238302; -.
DR EnsemblPlants; AT4G24970.1; AT4G24970.1; AT4G24970.
DR GeneID; 828599; -.
DR Gramene; AT4G24970.1; AT4G24970.1; AT4G24970.
DR KEGG; ath:AT4G24970; -.
DR Araport; AT4G24970; -.
DR TAIR; locus:2117358; AT4G24970.
DR eggNOG; KOG1845; Eukaryota.
DR HOGENOM; CLU_011516_6_0_1; -.
DR InParanoid; F4JRS4; -.
DR OMA; AYWSINC; -.
DR OrthoDB; 144359at2759; -.
DR PRO; PR:F4JRS4; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; F4JRS4; baseline and differential.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; ISS:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1902290; P:positive regulation of defense response to oomycetes; IMP:UniProtKB.
DR GO; GO:0044030; P:regulation of DNA methylation; IMP:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0060966; P:regulation of gene silencing by RNA; ISS:UniProtKB.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR045261; MORC_ATPase.
DR InterPro; IPR041006; Morc_S5.
DR PANTHER; PTHR23336; PTHR23336; 1.
DR Pfam; PF17942; Morc6_S5; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Chromatin regulator; Coiled coil; DNA damage; DNA repair;
KW DNA-binding; Endonuclease; Hydrolase; Kinase; Nuclease; Nucleotide-binding;
KW Nucleus; Plant defense; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transferase.
FT CHAIN 1..707
FT /note="Protein MICRORCHIDIA 7"
FT /id="PRO_0000434982"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 620..701
FT /evidence="ECO:0000255"
FT MOTIF 633..640
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 568..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 707 AA; 79573 MW; 63E99890DC1D4803 CRC64;
MDNSIHVKRE IQLPSTSPAG FPGRESVTVV DLCSSDDDSD IGEVAGGLEK VGNNFVGLKR
GRDTFGGSSE VDRNNVKKVT TLAELGVGLP EGFGQSNPPE SLTHPIPANP CNVFRPVPPP
PPPPYAGTSG KIGGCKQFWK AGDYEGAAGD NWDLSSGGFD HVRVHPKFLH SNATSHKWAL
GAFAELLDNA LDEVASGATY VKVDMLENNK GGNRMLLIED NGGGMDPEKM RQCMSLGYSA
KSKLANTIGQ YGNGFKTSTM RLGADVIVFS RCPGKDGKSS TQSIGLLSYT FLRSTGKEDI
VVPMLDYERR DPEWSKIIRS STRDWDKNVE TIIQWSPFSS EEDLLHQFDL MKDRGTRIII
YNLWEDDQGM LELDFDADPY DIQLRGVNRE ERNIKMASQF PNSRHFLTYK HSLRSYVSIL
YLRIPPGFRI ILRGIDVEHH SVVNDMMQTE QITYRPQSES YGVVTNMSAI VIIGFVKDAK
HHVDVQGFNV YHKNRLIKPF WRIWNATGSD GRGVIGVLEA NFVEPAHDKQ GFERTTVLAR
LESRLVQMQK TYWSTNCHKI GYAPRRREKS AYGYDNRDSS PENDREGPSS IKTPTPASDK
FYSSSYPNHN GDNGVSGKDG ARLQEELRRE KERRKALEVE VQLSRQKIEE MKKEQENLIE
IFSEERDRRD GEEEVLRNKL EEASNTIDDL LNKIKKMEGS KVPSWRH
