MORC5_ARATH
ID MORC5_ARATH Reviewed; 708 AA.
AC F4K2G3; F4K2G2; Q9FY97;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein MICRORCHIDIA 5 {ECO:0000303|PubMed:24799676};
DE Short=AtMORC5 {ECO:0000303|PubMed:24799676};
DE EC=3.6.-.-;
DE AltName: Full=Protein CRT1-homolog 5 {ECO:0000303|PubMed:19704828};
DE Short=CRT1-h5 {ECO:0000303|PubMed:19704828};
GN Name=MORC5 {ECO:0000303|PubMed:24799676};
GN Synonyms=CRH5 {ECO:0000303|PubMed:19704828};
GN OrderedLocusNames=At5g13130 {ECO:0000312|Araport:AT5G13130};
GN ORFNames=T19L5.90 {ECO:0000312|EMBL:CAC05441.1};
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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).
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. {ECO:0000250|UniProtKB:Q84WV6}.
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. {ECO:0000250|UniProtKB:Q84WV6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q56Y74,
CC ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4K2G3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K2G3-2; Sequence=VSP_057992, VSP_057993;
CC -!- SIMILARITY: Belongs to the MORC ATPase protein family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC05441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL391711; CAC05441.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91854.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91855.1; -; Genomic_DNA.
DR RefSeq; NP_001190300.1; NM_001203371.1. [F4K2G3-2]
DR RefSeq; NP_196817.2; NM_121316.2. [F4K2G3-1]
DR AlphaFoldDB; F4K2G3; -.
DR SMR; F4K2G3; -.
DR STRING; 3702.AT5G13130.1; -.
DR PaxDb; F4K2G3; -.
DR PRIDE; F4K2G3; -.
DR ProteomicsDB; 238263; -. [F4K2G3-1]
DR EnsemblPlants; AT5G13130.1; AT5G13130.1; AT5G13130. [F4K2G3-1]
DR EnsemblPlants; AT5G13130.2; AT5G13130.2; AT5G13130. [F4K2G3-2]
DR GeneID; 831152; -.
DR Gramene; AT5G13130.1; AT5G13130.1; AT5G13130. [F4K2G3-1]
DR Gramene; AT5G13130.2; AT5G13130.2; AT5G13130. [F4K2G3-2]
DR KEGG; ath:AT5G13130; -.
DR Araport; AT5G13130; -.
DR TAIR; locus:2179837; AT5G13130.
DR eggNOG; KOG1845; Eukaryota.
DR InParanoid; F4K2G3; -.
DR OMA; NSWKEIT; -.
DR PRO; PR:F4K2G3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K2G3; baseline and differential.
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:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; 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:0031349; P:positive regulation of defense response; IEA:UniProt.
DR GO; GO:0002833; P:positive regulation of response to biotic stimulus; IEA:UniProt.
DR GO; GO:0032103; P:positive regulation of response to external stimulus; IEA:UniProt.
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 3: Inferred from homology;
KW Alternative splicing; ATP-binding; Chromatin regulator; Coiled coil;
KW DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase; Kinase;
KW Nuclease; Nucleotide-binding; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing; Transferase.
FT CHAIN 1..708
FT /note="Protein MICRORCHIDIA 5"
FT /id="PRO_0000434980"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 590..665
FT /evidence="ECO:0000255"
FT MOTIF 672..679
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 406
FT /note="E -> EVLPYLTLVSLFIILKHSQKFLLCFQKILQ (in isoform 2)"
FT /id="VSP_057992"
FT VAR_SEQ 646..686
FT /note="Missing (in isoform 2)"
FT /id="VSP_057993"
SQ SEQUENCE 708 AA; 80919 MW; 4CA54280E1E704EB CRC64;
MAESGSTNPK SPSVVPDSTL GGLKRDLRNY HDGDDSNNLS IKKSKTTKME NNCREIVPLD
VTPLSIVPPD TPKLSRQFWK AGDDDEAAPV PLYCSNDAAV RVHPQFLHAN ATSHKWALGA
LAELLDNSLD EVSNGATYVH VDSTINKRDG KSSILIVEDN GGGMNPSTFR ECLSLGYSRK
RNMANRVGQY GNGFKTSTMR LGADAIVFSR SRGINGNNPT QSIGMLSYTF LYETRKCEAI
VPTVDYELVD NKWKEIVYNS TNEWLDNLET ILRWSPYLSQ QDLLDQFNHL EEQGTRIVIY
NLWEDDEGKM ELDFDTDPHD IQLRGVNRDE KNIDMAKTYP NSRHFLTYRH SLRSYASILY
LKRPDNFRII LRGEDVEHHS VLDDMMKIEE KTYKPMRSPE WPDQEEMVAS LKLGFVKDAH
HHIDIQGFNV YHKNRLIKPF WRVWNAAGSD GRGVIGILEA NFIQPAHNKQ GFERTVVLAK
LESRLVTHQK NYWSSRCHEI GYAPRRKQKN YESSVTETPR PFNNINVVKG SSSSTPVPVR
VFRPNVEPSG RNQIPQVETR ERSFDINPEI GAKNRSYYGL GISSFKETGS VNLEAELQKV
KQESAKLVSE LQRQKQLLEL QLQESKAKIQ NLEKAQREKE VLELQLKESK ARIQNLENRQ
EGVSTIFQQE RARRDVTEDG LRKKLREASD VIDGLRKQVD TFKGKRIL
