RDR2_ARATH
ID RDR2_ARATH Reviewed; 1133 AA.
AC O82504;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=RNA-dependent RNA polymerase 2 {ECO:0000303|PubMed:15024409, ECO:0000303|PubMed:15692015};
DE Short=AtRDRP2 {ECO:0000303|PubMed:15024409, ECO:0000303|PubMed:15692015};
DE EC=2.7.7.48;
DE AltName: Full=Protein SILENCING MOVEMENT DEFICIENT 1;
DE AltName: Full=RNA-directed RNA polymerase 2 {ECO:0000303|PubMed:15024409, ECO:0000303|PubMed:15692015};
GN Name=RDR2 {ECO:0000303|PubMed:15024409, ECO:0000303|PubMed:15692015};
GN Synonyms=RDRP2 {ECO:0000303|PubMed:15024409, ECO:0000303|PubMed:15692015},
GN SMD1; OrderedLocusNames=At4g11130 {ECO:0000312|Araport:AT4G11130};
GN ORFNames=F2P3.11 {ECO:0000312|EMBL:AAC35535.1};
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;
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 FUNCTION.
RX PubMed=15024409; DOI=10.1371/journal.pbio.0020104;
RA Xie Z., Johansen L.K., Gustafson A.M., Kasschau K.D., Lellis A.D.,
RA Zilberman D., Jacobsen S.E., Carrington J.C.;
RT "Genetic and functional diversification of small RNA pathways in plants.";
RL PLoS Biol. 2:E104-E104(2004).
RN [4]
RP FUNCTION.
RX PubMed=15692015; DOI=10.1126/science.1106910;
RA Herr A.J., Jensen M.B., Dalmay T., Baulcombe D.C.;
RT "RNA polymerase IV directs silencing of endogenous DNA.";
RL Science 308:118-120(2005).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=16839878; DOI=10.1016/j.cell.2006.05.031;
RA Pontes O., Li C.F., Nunes P.C., Haag J., Ream T., Vitins A., Jacobsen S.E.,
RA Pikaard C.S.;
RT "The Arabidopsis chromatin-modifying nuclear siRNA pathway involves a
RT nucleolar RNA processing center.";
RL Cell 126:79-92(2006).
RN [6]
RP FUNCTION.
RX PubMed=16798886; DOI=10.1105/tpc.106.042127;
RA Ronemus M., Vaughn M.W., Martienssen R.A.;
RT "MicroRNA-targeted and small interfering RNA-mediated mRNA degradation is
RT regulated by argonaute, dicer, and RNA-dependent RNA polymerase in
RT Arabidopsis.";
RL Plant Cell 18:1559-1574(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17105345; DOI=10.1371/journal.pbio.0040363;
RA Chan S.W., Zhang X., Bernatavichute Y.V., Jacobsen S.E.;
RT "Two-step recruitment of RNA-directed DNA methylation to tandem repeats.";
RL PLoS Biol. 4:E363-E363(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17526749; DOI=10.1105/tpc.107.051540;
RA Smith L.M., Pontes O., Searle I., Yelina N., Yousafzai F.K., Herr A.J.,
RA Pikaard C.S., Baulcombe D.C.;
RT "An SNF2 protein associated with nuclear RNA silencing and the spread of a
RT silencing signal between cells in Arabidopsis.";
RL Plant Cell 19:1507-1521(2007).
RN [9]
RP FUNCTION.
RX PubMed=17785412; DOI=10.1073/pnas.0706701104;
RA Brosnan C.A., Mitter N., Christie M., Smith N.A., Waterhouse P.M.,
RA Carroll B.J.;
RT "Nuclear gene silencing directs reception of long-distance mRNA silencing
RT in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:14741-14746(2007).
RN [10]
RP FUNCTION.
RX PubMed=20548962; DOI=10.1371/journal.pgen.1000986;
RA Vrbsky J., Akimcheva S., Watson J.M., Turner T.L., Daxinger L., Vyskot B.,
RA Aufsatz W., Riha K.;
RT "siRNA-mediated methylation of Arabidopsis telomeres.";
RL PLoS Genet. 6:E1000986-E1000986(2010).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21150311; DOI=10.4161/epi.6.3.14242;
RA Greenberg M.V., Ausin I., Chan S.W., Cokus S.J., Cuperus J.T., Feng S.,
RA Law J.A., Chu C., Pellegrini M., Carrington J.C., Jacobsen S.E.;
RT "Identification of genes required for de novo DNA methylation in
RT Arabidopsis.";
RL Epigenetics 6:344-354(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NRPD1.
RX PubMed=21811420; DOI=10.1371/journal.pgen.1002195;
RA Law J.A., Vashisht A.A., Wohlschlegel J.A., Jacobsen S.E.;
RT "SHH1, a homeodomain protein required for DNA methylation, as well as RDR2,
RT RDM4, and chromatin remodeling factors, associate with RNA polymerase IV.";
RL PLoS Genet. 7:E1002195-E1002195(2011).
RN [13]
RP FUNCTION, AND INTERACTION WITH POL IV COMPLEX.
RX PubMed=23142082; DOI=10.1016/j.molcel.2012.09.027;
RA Haag J.R., Ream T.S., Marasco M., Nicora C.D., Norbeck A.D., Pasa-Tolic L.,
RA Pikaard C.S.;
RT "In vitro transcription activities of Pol IV, Pol V, and RDR2 reveal
RT coupling of Pol IV and RDR2 for dsRNA synthesis in plant RNA silencing.";
RL Mol. Cell 48:811-818(2012).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SHH1.
RX PubMed=23637343; DOI=10.1073/pnas.1300585110;
RA Zhang H., Ma Z.Y., Zeng L., Tanaka K., Zhang C.J., Ma J., Bai G., Wang P.,
RA Zhang S.W., Liu Z.W., Cai T., Tang K., Liu R., Shi X., He X.J., Zhu J.K.;
RT "DTF1 is a core component of RNA-directed DNA methylation and may assist in
RT the recruitment of Pol IV.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:8290-8295(2013).
RN [15]
RP DISRUPTION PHENOTYPE, INTERACTION WITH JMJ24, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26119694; DOI=10.1111/tpj.12924;
RA Deng S., Xu J., Liu J., Kim S.-H., Shi S., Chua N.-H.;
RT "JMJ24 binds to RDR2 and is required for the basal level transcription of
RT silenced loci in Arabidopsis.";
RL Plant J. 83:770-782(2015).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH
RP MAGNESIUM, AND FUNCTION.
RX PubMed=34903670; DOI=10.1073/pnas.2115899118;
RA Fukudome A., Singh J., Mishra V., Reddem E., Martinez-Marquez F.,
RA Wenzel S., Yan R., Shiozaki M., Yu Z., Wang J.C.-Y., Takagi Y.,
RA Pikaard C.S.;
RT "Structure and RNA template requirements of Arabidopsis RNA-DEPENDENT RNA
RT POLYMERASE 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.16 ANGSTROMS) IN COMPLEX WITH MAGNESIUM
RP AND POL IV, FUNCTION, AND SUBUNIT.
RX PubMed=34941388; DOI=10.1126/science.abj9184;
RA Huang K., Wu X.-X., Fang C.-L., Xu Z.-G., Zhang H.-W., Gao J., Zhou C.-M.,
RA You L.-L., Gu Z.-X., Mu W.-H., Feng Y., Wang J.-W., Zhang Y.;
RT "Pol IV and RDR2: A two-RNA-polymerase machine that produces double-
RT stranded RNA.";
RL Science 374:1579-1586(2021).
CC -!- FUNCTION: RNA-dependent direct polymerase involved in the production of
CC small interfering RNAs (siRNAs). Binds to single-stranded RNA (ssRNA);
CC engages ssRNAs longer than 7 nucleotides and initiates internal to
CC their 3' ends (PubMed:34903670). Able to transcribe the RNA of an
CC RNA/DNA hybrid, the transcript produced by Pol IV, if its 3' end is
CC accessible, to generate double-stranded small interfering RNAs (dsRNAs)
CC precursor essential for establishing and maintaining DNA methylation
CC (PubMed:34903670, PubMed:34941388). Required for the biogenesis of
CC endogenous siRNAs of 24 nucleotide which derive from heterochromatin
CC and DNA repeats such as transposons or endogenous gene tandem repeats,
CC such as repeats present in FWA gene. Involved in transcriptional gene
CC silencing (TGS). Component of the RNA-directed DNA methylation (RdDM)
CC silencing pathway that utilizes siRNAs to guide DNA methyltransferases
CC to asymmetric cytosines. Involved in control of flowering time through
CC RdDM of FWA locus. Required for reception of long-distance mRNA
CC silencing in the shoot. Required for the formation of telomeric siRNAs
CC and the RNA-dependent DNA methylation of asymmetric cytosines in
CC telomeric (5'-CCCTAAA-3') repeats. {ECO:0000269|PubMed:15024409,
CC ECO:0000269|PubMed:15692015, ECO:0000269|PubMed:16798886,
CC ECO:0000269|PubMed:17105345, ECO:0000269|PubMed:17526749,
CC ECO:0000269|PubMed:17785412, ECO:0000269|PubMed:20548962,
CC ECO:0000269|PubMed:21150311, ECO:0000269|PubMed:23142082,
CC ECO:0000269|PubMed:34903670, ECO:0000269|PubMed:34941388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.48;
CC -!- SUBUNIT: Interacts with NRPD1 and SHH1. Associates with Pol IV complex,
CC forming an interpolymerase channel bridging their active sites, through
CC which the Pol IV-generated transcript is handed over to the RDR2 active
CC site after being backtracked, where it is used as the template for
CC double-stranded RNA (dsRNA) synthesis (PubMed:34941388). Interacts with
CC JMJ24 (PubMed:26119694). {ECO:0000269|PubMed:21811420,
CC ECO:0000269|PubMed:23142082, ECO:0000269|PubMed:23637343,
CC ECO:0000269|PubMed:26119694, ECO:0000269|PubMed:34941388}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:17526749}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:17526749}.
CC Nucleus {ECO:0000269|PubMed:26119694}. Note=In the nucleolus, localized
CC in a ring or crescent around the inner periphery and to a distinctive
CC nucleolar dot. {ECO:0000269|PubMed:16839878,
CC ECO:0000269|PubMed:17526749}.
CC -!- DISRUPTION PHENOTYPE: Late flowering and absence of siRNAs derived from
CC FWA tandem repeat regions. Loss of de novo methylation. Increased
CC expression of retrotransposon-derived solo long terminal repeat (solo
CC LTR) and SDC due to their derepression; levels are even higher in the
CC double mutant rdr2-1 jmj24-1 (PubMed:26119694).
CC {ECO:0000269|PubMed:17105345, ECO:0000269|PubMed:21150311,
CC ECO:0000269|PubMed:26119694}.
CC -!- MISCELLANEOUS: RDR2 is non-functional in the absence of associated Pol
CC IV. {ECO:0000305|PubMed:23142082}.
CC -!- SIMILARITY: Belongs to the RdRP family. {ECO:0000305}.
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DR EMBL; AF080120; AAC35535.1; -; Genomic_DNA.
DR EMBL; AL049876; CAB43048.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81214.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82976.1; -; Genomic_DNA.
DR PIR; T01920; T01920.
DR RefSeq; NP_192851.1; NM_117183.3.
DR PDB; 7EU0; EM; 3.16 A; M=1-1133.
DR PDB; 7EU1; EM; 3.86 A; M=1-1133.
DR PDB; 7ROZ; EM; 3.10 A; A=1-1133.
DR PDB; 7RQS; EM; 3.57 A; A=1-1133.
DR PDBsum; 7EU0; -.
DR PDBsum; 7EU1; -.
DR PDBsum; 7ROZ; -.
DR PDBsum; 7RQS; -.
DR AlphaFoldDB; O82504; -.
DR SMR; O82504; -.
DR BioGRID; 12013; 4.
DR STRING; 3702.AT4G11130.1; -.
DR iPTMnet; O82504; -.
DR PaxDb; O82504; -.
DR PRIDE; O82504; -.
DR ProteomicsDB; 235077; -.
DR EnsemblPlants; AT4G11130.1; AT4G11130.1; AT4G11130.
DR GeneID; 826714; -.
DR Gramene; AT4G11130.1; AT4G11130.1; AT4G11130.
DR KEGG; ath:AT4G11130; -.
DR Araport; AT4G11130; -.
DR TAIR; locus:2136068; AT4G11130.
DR eggNOG; KOG0988; Eukaryota.
DR HOGENOM; CLU_001366_3_0_1; -.
DR InParanoid; O82504; -.
DR OMA; RVEFWVW; -.
DR OrthoDB; 63910at2759; -.
DR PhylomeDB; O82504; -.
DR BRENDA; 2.7.7.48; 399.
DR PRO; PR:O82504; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; O82504; baseline and differential.
DR Genevisible; O82504; AT.
DR GO; GO:0031380; C:nuclear RNA-directed RNA polymerase complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0071667; F:DNA/RNA hybrid binding; IDA:UniProtKB.
DR GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IBA:GO_Central.
DR GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0062103; P:double-stranded RNA biosynthetic process; IDA:UniProtKB.
DR GO; GO:0030422; P:siRNA processing; IMP:TAIR.
DR GO; GO:0010495; P:siRNA-mediated long-distance post-transcriptional gene silencing; IMP:TAIR.
DR GO; GO:0001172; P:transcription, RNA-templated; IDA:UniProtKB.
DR InterPro; IPR007855; RNA-dep_RNA_pol_euk-typ.
DR PANTHER; PTHR23079; PTHR23079; 1.
DR Pfam; PF05183; RdRP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; RNA-binding; RNA-directed RNA polymerase;
KW RNA-mediated gene silencing; Transferase.
FT CHAIN 1..1133
FT /note="RNA-dependent RNA polymerase 2"
FT /id="PRO_0000404673"
FT BINDING 830
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:34903670,
FT ECO:0000269|PubMed:34941388, ECO:0007744|PDB:7EU0,
FT ECO:0007744|PDB:7EU1, ECO:0007744|PDB:7ROZ"
FT BINDING 832
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:34903670,
FT ECO:0000269|PubMed:34941388, ECO:0007744|PDB:7EU0,
FT ECO:0007744|PDB:7EU1, ECO:0007744|PDB:7ROZ,
FT ECO:0007744|PDB:7RQS"
FT BINDING 834
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:34903670,
FT ECO:0000269|PubMed:34941388, ECO:0007744|PDB:7EU0,
FT ECO:0007744|PDB:7EU1, ECO:0007744|PDB:7ROZ,
FT ECO:0007744|PDB:7RQS"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 64..69
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 105..114
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 127..137
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 230..233
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 247..251
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 310..314
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 327..339
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 371..375
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 378..386
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 391..400
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 403..407
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 409..414
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 415..421
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 440..446
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 449..460
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 467..473
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 476..481
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 483..488
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 495..502
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 511..520
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 543..546
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 552..560
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 562..572
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 590..594
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 600..604
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 610..612
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 617..623
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 633..642
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 646..661
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 667..670
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 671..677
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 685..691
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 696..698
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 700..719
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 729..732
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 745..751
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 754..758
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 766..774
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 777..785
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 793..797
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 803..806
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 810..814
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 816..820
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 822..825
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 831..833
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 835..839
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 842..844
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 863..865
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 869..881
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 885..896
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 899..905
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 906..920
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 921..923
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 937..943
FT /evidence="ECO:0007829|PDB:7ROZ"
FT STRAND 946..948
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 954..958
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 959..968
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 982..988
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 999..1016
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 1025..1028
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 1037..1039
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 1049..1052
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 1053..1055
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 1056..1066
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 1075..1077
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 1078..1088
FT /evidence="ECO:0007829|PDB:7ROZ"
FT TURN 1089..1094
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 1102..1105
FT /evidence="ECO:0007829|PDB:7ROZ"
FT HELIX 1107..1120
FT /evidence="ECO:0007829|PDB:7ROZ"
SQ SEQUENCE 1133 AA; 129325 MW; 32B72C4E429B20B9 CRC64;
MVSETTTNRS TVKISNVPQT IVADELLRFL ELHLGEDTVF ALEIPTTRDN WKPRDFARVQ
FTTLEVKSRA QLLSSQSKLL FKTHNLRLSE AYDDIIPRPV DPRKRLDDIV LTVGFPESDE
KRFCALEKWD GVRCWILTEK RRVEFWVWES GDCYKIEVRF EDIIETLSCC VNGDASEIDA
FLLKLKYGPK VFKRVTVHIA TKFKSDRYRF CKEDFDFMWI RTTDFSGSKS IGTSTCFCLE
VHNGSTMLDI FSGLPYYRED TLSLTYVDGK TFASAAQIVP LLNAAILGLE FPYEILFQLN
ALVHAQKISL FAASDMELIK ILRGMSLETA LVILKKLHQQ SSICYDPVFF VKTQMQSVVK
KMKHSPASAY KRLTEQNIMS CQRAYVTPSK IYLLGPELET ANYVVKNFAE HVSDFMRVTF
VEEDWSKLPA NALSVNSKEG YFVKPSRTNI YNRVLSILGE GITVGPKRFE FLAFSASQLR
GNSVWMFASN EKVKAEDIRE WMGCFRKIRS ISKCAARMGQ LFSASRQTLI VRAQDVEQIP
DIEVTTDGAD YCFSDGIGKI SLAFAKQVAQ KCGLSHVPSA FQIRYGGYKG VIAVDRSSFR
KLSLRDSMLK FDSNNRMLNV TRWTESMPCF LNREIICLLS TLGIEDAMFE AMQAVHLSML
GNMLEDRDAA LNVLQKLSGE NSKNLLVKML LQGYAPSSEP YLSMMLRVHH ESQLSELKSR
CRILVPKGRI LIGCMDEMGI LEYGQVYVRV TLTKAELKSR DQSYFRKIDE ETSVVIGKVV
VTKNPCLHPG DIRVLDAIYE VHFEEKGYLD CIIFPQKGER PHPNECSGGD LDGDQFFVSW
DEKIIPSEMD PPMDYAGSRP RLMDHDVTLE EIHKFFVDYM ISDTLGVIST AHLVHADRDP
EKARSQKCLE LANLHSRAVD FAKTGAPAEM PYALKPREFP DFLERFEKPT YISESVFGKL
YRAVKSSLAQ RKPEAESEDT VAYDVTLEEA GFESFIETAK AHRDMYGEKL TSLMIYYGAA
NEEEILTGIL KTKEMYLARD NRRYGDMKDR ITLSVKDLHK EAMGWFEKSC EDEQQKKKLA
SAWYYVTYNP NHRDEKLTFL SFPWIVGDVL LDIKAENAQR QSVEEKTSGL VSI
