MORC1_ARATH
ID MORC1_ARATH Reviewed; 635 AA.
AC Q84WV6; O23245; O65520; Q56WA8; Q9C5D9;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein MICRORCHIDIA 1 {ECO:0000303|PubMed:22555433};
DE Short=AtMORC1 {ECO:0000303|PubMed:22555433};
DE EC=3.6.-.- {ECO:0000269|PubMed:18191794};
DE AltName: Full=Protein COMPROMISED RECOGNITION OF TCV 1 {ECO:0000303|PubMed:18191794};
GN Name=MORC1 {ECO:0000303|PubMed:22555433};
GN Synonyms=CRT1 {ECO:0000303|PubMed:18191794};
GN OrderedLocusNames=At4g36290 {ECO:0000312|Araport:AT4G36290};
GN ORFNames=C7A10.1020 {ECO:0000312|EMBL:CAB16854.1},
GN F23E13.180 {ECO:0000312|EMBL:CAA18135.1};
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|EMBL:AAN71939.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [2]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 409-635.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP REVIEW.
RX PubMed=18191789; DOI=10.1016/j.chom.2007.12.005;
RA Monaghan J., Li X.;
RT "R protein activation: another player revealed.";
RL Cell Host Microbe 3:9-10(2008).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RPP8; SSI4 AND RPS2, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RX PubMed=18191794; DOI=10.1016/j.chom.2007.11.006;
RA Kang H.-G., Kuhl J.C., Kachroo P., Klessig D.F.;
RT "CRT1, an Arabidopsis ATPase that interacts with diverse resistance
RT proteins and modulates disease resistance to turnip crinkle virus.";
RL Cell Host Microbe 3:48-57(2008).
RN [8]
RP FUNCTION, 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 [9]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RCY1; RPP8; RPM1 AND SNC1.
RX PubMed=20332379; DOI=10.1105/tpc.109.071662;
RA Kang H.-G., Oh C.-S., Sato M., Katagiri F., Glazebrook J., Takahashi H.,
RA Kachroo P., Martin G.B., Klessig D.F.;
RT "Endosome-associated CRT1 functions early in resistance gene-mediated
RT defense signaling in Arabidopsis and tobacco.";
RL Plant Cell 22:918-936(2010).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, COFACTOR, INTERACTION WITH FLS2, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=23250427; DOI=10.1038/ncomms2279;
RA Kang H.-G., Hyong W.C., von Einem S., Manosalva P., Ehlers K., Liu P.-P.,
RA Buxa S.V., Moreau M., Mang H.-G., Kachroo P., Kogel K.-H., Klessig D.F.;
RT "CRT1 is a nuclear-translocated MORC endonuclease that participates in
RT multiple levels of plant immunity.";
RL Nat. Commun. 3:1297-1297(2012).
RN [11]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=22555433; DOI=10.1126/science.1221472;
RA Moissiard G., Cokus S.J., Cary J., Feng S., Billi A.C., Stroud H.,
RA Husmann D., Zhan Y., Lajoie B.R., McCord R.P., Hale C.J., Feng W.,
RA Michaels S.D., Frand A.R., Pellegrini M., Dekker J., Kim J.K.,
RA Jacobsen S.E.;
RT "MORC family ATPases required for heterochromatin condensation and gene
RT silencing.";
RL Science 336:1448-1451(2012).
RN [12]
RP SUBUNIT, AND INTERACTION WITH MORC6; SUVH9 AND SUVH2.
RX PubMed=24465213; DOI=10.1371/journal.pgen.1003948;
RA Liu Z.-W., Shao C.-R., Zhang C.-J., Zhou J.-X., Zhang S.-W., Li L.,
RA Chen S., Huang H.-W., Cai T., He X.-J.;
RT "The SET domain proteins SUVH2 and SUVH9 are required for Pol V occupancy
RT at RNA-directed DNA methylation loci.";
RL PLoS Genet. 10:E1003948-E1003948(2014).
RN [13]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MORC6, GENE FAMILY, AND
RP 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).
CC -!- FUNCTION: Mediator of defense signaling triggered by distinct classes
CC of R proteins. Required during hypersensitive response (HR) that
CC confers disease resistance to turnip crinkle virus (TCV). Exhibits
CC ATPase activity (PubMed:18191794, PubMed:19704828). Contributes to
CC resistance against Pseudomonas syringae and Hyaloperonospora
CC arabidopsidis, at early stages prior to cytosolic calcium ions Ca(2+)
CC accumulation (PubMed:20332379). Required for pathogen-associated
CC molecular pattern (PAMP)-triggered immunity (PTI), basal resistance,
CC non-host resistance and systemic acquired resistance (SAR). Binds
CC DNA/RNA in a non-specific manner and exhibits endonuclease activity.
CC Probably involved in DNA repair (PubMed:23250427). Required for both
CC RPP8- and SSI4-mediated resistance responses, thus being involved in
CC both TIR- and CC-NB-LRR pathways (PubMed:18191794). Involved in RNA-
CC directed DNA methylation (RdDM) as a component of the RdDM machinery
CC and required for gene silencing (PubMed:24799676). May also be involved
CC in the regulation of chromatin architecture to maintain gene silencing
CC (PubMed:22555433, PubMed:24799676). {ECO:0000269|PubMed:18191794,
CC ECO:0000269|PubMed:19704828, ECO:0000269|PubMed:20332379,
CC ECO:0000269|PubMed:22555433, ECO:0000269|PubMed:23250427,
CC ECO:0000269|PubMed:24799676}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:23250427};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:23250427};
CC Note=Uses preferentially Mn(2+) and, to a lesser extent, Mg(2+) as
CC cofactors. {ECO:0000269|PubMed:23250427};
CC -!- SUBUNIT: Homodimer and heterodimer with MORC6. Component of an RNA-
CC directed DNA methylation (RdDM) complex that contains at least MORC6,
CC MORC1/CRT1, MORC2, SWI3D and SUVH9. Binds directly to SUVH2 and SUVH9
CC (PubMed:24465213, PubMed:24799676). Interacts with the resistance
CC proteins RCY1, RPM1, SNC1, RPP8, SSI4 and RPS2 (PubMed:18191794,
CC PubMed:20332379). The interactions with various resistance proteins are
CC disrupted when these resistance proteins are activated
CC (PubMed:20332379). Interacts with the PAMP recognition receptor FLS2
CC (PubMed:23250427). {ECO:0000269|PubMed:18191794,
CC ECO:0000269|PubMed:20332379, ECO:0000269|PubMed:23250427,
CC ECO:0000269|PubMed:24465213, ECO:0000269|PubMed:24799676}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768,
CC ECO:0000269|PubMed:22555433, ECO:0000269|PubMed:23250427}. Endosome
CC {ECO:0000269|PubMed:20332379}. Note=Present in nuclear bodies near
CC chromocenters (PubMed:22555433). Localized in endosome-like vesicles
CC displaying rapid cytosolic streaming (PubMed:20332379). Accumulates in
CC the nucleus following pathogen-associated molecular pattern (PAMP)
CC treatment or infection with an avirulent pathogen (PubMed:23250427).
CC {ECO:0000269|PubMed:20332379, ECO:0000269|PubMed:22555433,
CC ECO:0000269|PubMed:23250427}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively.
CC {ECO:0000269|PubMed:18191794}.
CC -!- DISRUPTION PHENOTYPE: Loss of ATPase activity. Increased sensitivity to
CC turnip crinkle virus (TCV) leading to spreading hypersensitive response
CC (HR) and impaired control of viral replication and spread. Suppression
CC of HR-like cell death induced by Pseudomonas syringae avrRpt2.
CC Suppression of lesion formation and partial suppression of stunted
CC growth of ssi4 mutant (PubMed:18191794). In the double mutant crt1-2
CC crh1-1, compromised resistance to avirulent Pseudomonas syringae and
CC Hyaloperonospora arabidopsidis associated with compromised cytosolic
CC calcium accumulation upon infection (PubMed:20332379). Impaired gene
CC silencing due to decondensation of chromocenters leading to the
CC derepression of DNA-methylated genes and transposable elements (TEs);
CC DNA and histone methylation seems normal (PubMed:22555433,
CC PubMed:24799676). The double mutant crt1-2 crh1-1 exhibits also an
CC increased sensitivity to turnip crinkle virus (TCV), and reduced
CC defense mediated by flg22 against Pseudomonas syringae (Pst). Impaired
CC non-host resistance toward P. infestans and altered systemic acquired
CC resistance (SAR) triggered by P. syringae pv. maculicola (Psm) AvrRpt2
CC cor(-). Reduced sensitivity to the DNA-damaging agent mitomycin C
CC (PubMed:23250427). {ECO:0000269|PubMed:18191794,
CC ECO:0000269|PubMed:20332379, ECO:0000269|PubMed:22555433,
CC ECO:0000269|PubMed:23250427, ECO:0000269|PubMed:24799676}.
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD95165.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA18135.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB16854.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80300.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z99708; CAB16854.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL022141; CAA18135.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161589; CAB80300.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86644.1; -; Genomic_DNA.
DR EMBL; AF360314; AAK26024.1; -; mRNA.
DR EMBL; BT001940; AAN71939.1; -; mRNA.
DR EMBL; AK222136; BAD95165.1; ALT_INIT; mRNA.
DR PIR; T04598; T04598.
DR RefSeq; NP_568000.1; NM_119797.4.
DR AlphaFoldDB; Q84WV6; -.
DR SMR; Q84WV6; -.
DR DIP; DIP-59357N; -.
DR IntAct; Q84WV6; 4.
DR STRING; 3702.AT4G36290.1; -.
DR PaxDb; Q84WV6; -.
DR PRIDE; Q84WV6; -.
DR ProteomicsDB; 250881; -.
DR DNASU; 829786; -.
DR EnsemblPlants; AT4G36290.1; AT4G36290.1; AT4G36290.
DR GeneID; 829786; -.
DR Gramene; AT4G36290.1; AT4G36290.1; AT4G36290.
DR KEGG; ath:AT4G36290; -.
DR Araport; AT4G36290; -.
DR TAIR; locus:2122264; AT4G36290.
DR eggNOG; KOG1845; Eukaryota.
DR HOGENOM; CLU_011516_4_1_1; -.
DR OMA; QENSMEP; -.
DR OrthoDB; 378346at2759; -.
DR PhylomeDB; Q84WV6; -.
DR PRO; PR:Q84WV6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84WV6; baseline and differential.
DR GO; GO:0005768; C:endosome; IDA:TAIR.
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; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IMP:UniProtKB.
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:0009626; P:plant-type hypersensitive response; IMP:TAIR.
DR GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:UniProtKB.
DR GO; GO:0034052; P:positive regulation of plant-type hypersensitive response; IMP:UniProtKB.
DR GO; GO:1901672; P:positive regulation of systemic acquired resistance; IMP:UniProtKB.
DR GO; GO:0006282; P:regulation of DNA repair; IMP: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; Endosome; Hydrolase; Hypersensitive response;
KW Nuclease; Nucleotide-binding; Nucleus; Plant defense; Reference proteome;
KW RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..635
FT /note="Protein MICRORCHIDIA 1"
FT /id="PRO_0000434976"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 588..635
FT /evidence="ECO:0000255"
FT COMPBIAS 495..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 77
FT /note="T -> I (in Ref. 4; AAK26024)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 635 AA; 70807 MW; 0889A04DBCFBAB8D CRC64;
MAKNYTVADV VNIDSDSDSD DDNGGVIGMV PSLASLIENQ KVSIADAATV APRETLECRS
FWKAGENFVI PSSVTLTAIG MVEHARVHPK FLHSNATSHK WAFGAIAELL DNAVDEIQNG
ATVVKIDKIN IVKDNTPALV FQDNGGGMDP NGIRKCMSLG YSSKKSNTTI GQYGNGFKTS
TMRLGADAMV FSRSTRGGKS TQSIGLLSYT FLRKTGQDDV IVPMIDFDIS SDSPQPIIYG
SPGDWSTNLN ILLKWSPFST MVELLQQFED IGTHGTKVII YNLWLNDEGI YELSFDDDDV
DIRLRDENAQ DGKRLHAKTL EVRSHISYRY RHSLRAYISM LYLKKFKNFK IILRGVSVAQ
FNIADEFRHP ETIMYKPQAA AVDYAATGIK VGFIKEAPKL PICGFNVYHK NRLIRPFWKV
VLEGSTRGNG VMGVLEANFI EPAHDKQDFE RSSLFLRLEA RLKRITSDYW QNHCHIFGYQ
TAQIPADKSK RTVIPDQPPT VNTYNPSPLP SDRISHGGPI IREINLSNAT SSRTAAVAAP
HLRNYTGLRN NFQPVQLNPQ PPAAGDTGNN LVGKLAAEIR EENLQLFMRC EEYVKKENEV
EQTVKSLEKE LEEIKSKCAQ LALLVDAKKK EMQQV
