NRPD2_ARATH
ID NRPD2_ARATH Reviewed; 1172 AA.
AC Q9LK40; Q67ZK6;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA-directed RNA polymerases IV and V subunit 2;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase D subunit 2a;
DE Short=AtNRPD2a;
DE Short=Nuclear RNA polymerase D 2a;
DE AltName: Full=Nuclear RNA polymerase E 2;
DE AltName: Full=Protein DEFECTIVE IN MERISTEM SILENCING 2;
DE AltName: Full=Protein DEFECTIVE IN RNA-DIRECTED DNA METHYLATION 2;
DE AltName: Full=RNA polymerase IV subunit 2a;
DE Short=POL IV 2a;
GN Name=NRPD2; Synonyms=DMS2, DRD2, NRPD2a, NRPE2, RPD2a;
GN OrderedLocusNames=At3g23780; ORFNames=MYM9.13;
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, DISRUPTION PHENOTYPE, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=15766525; DOI=10.1016/j.cell.2005.02.007;
RA Onodera Y., Haag J.R., Ream T., Nunes P.C., Pontes O., Pikaard C.S.;
RT "Plant nuclear RNA polymerase IV mediates siRNA and DNA methylation-
RT dependent heterochromatin formation.";
RL Cell 120:613-622(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, FUNCTION, DISRUPTION
RP PHENOTYPE, AND SUBUNIT.
RX PubMed=16140984; DOI=10.1101/gad.348405;
RA Pontier D., Yahubyan G., Vega D., Bulski A., Saez-Vasquez J., Hakimi M.-A.,
RA Lerbs-Mache S., Colot V., Lagrange T.;
RT "Reinforcement of silencing at transposons and highly repeated sequences
RT requires the concerted action of two distinct RNA polymerases IV in
RT Arabidopsis.";
RL Genes Dev. 19:2030-2040(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 498-1172.
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 (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=15924141; DOI=10.1038/ng1580;
RA Kanno T., Huettel B., Mette M.F., Aufsatz W., Jaligot E., Daxinger L.,
RA Kreil D.P., Matzke M., Matzke A.J.M.;
RT "Atypical RNA polymerase subunits required for RNA-directed DNA
RT methylation.";
RL Nat. Genet. 37:761-765(2005).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [8]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NRPD1 AND NRPE1.
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 [9]
RP REVIEW.
RX PubMed=17449119; DOI=10.1016/j.bbaexp.2007.03.001;
RA Huettel B., Kanno T., Daxinger L., Bucher E., van der Winden J.,
RA Matzke A.J.M., Matzke M.;
RT "RNA-directed DNA methylation mediated by DRD1 and Pol IVb: a versatile
RT pathway for transcriptional gene silencing in plants.";
RL Biochim. Biophys. Acta 1769:358-374(2007).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [11]
RP FUNCTION.
RC STRAIN=cv. Columbia;
RX PubMed=17360559; DOI=10.1073/pnas.0611456104;
RA Zhang X., Henderson I.R., Lu C., Green P.J., Jacobsen S.E.;
RT "Role of RNA polymerase IV in plant small RNA metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4536-4541(2007).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18425128; DOI=10.1038/ng.119;
RA Kanno T., Bucher E., Daxinger L., Huettel B., Boehmdorfer G., Gregor W.,
RA Kreil D.P., Matzke M., Matzke A.J.;
RT "A structural-maintenance-of-chromosomes hinge domain-containing protein is
RT required for RNA-directed DNA methylation.";
RL Nat. Genet. 40:670-675(2008).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=18667720; DOI=10.1104/pp.108.125229;
RA Borges F., Gomes G., Gardner R., Moreno N., McCormick S., Feijo J.A.,
RA Becker J.D.;
RT "Comparative transcriptomics of Arabidopsis sperm cells.";
RL Plant Physiol. 148:1168-1181(2008).
RN [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE, GENE
RP FAMILY, SUBUNIT, AND NOMENCLATURE.
RX PubMed=19110459; DOI=10.1016/j.molcel.2008.12.015;
RA Ream T.S., Haag J.R., Wierzbicki A.T., Nicora C.D., Norbeck A.D., Zhu J.K.,
RA Hagen G., Guilfoyle T.J., Pasa-Tolic L., Pikaard C.S.;
RT "Subunit compositions of the RNA-silencing enzymes Pol IV and Pol V reveal
RT their origins as specialized forms of RNA polymerase II.";
RL Mol. Cell 33:192-203(2009).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19825650; DOI=10.1093/mp/ssp006;
RA Pontes O., Costa-Nunes P., Vithayathil P., Pikaard C.S.;
RT "RNA polymerase V functions in Arabidopsis interphase heterochromatin
RT organization independently of the 24-nt siRNA-directed DNA methylation
RT pathway.";
RL Mol. Plant 2:700-710(2009).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21070421; DOI=10.1111/j.1365-313x.2010.04358.x;
RA Mlotshwa S., Pruss G.J., Gao Z., Mgutshini N.L., Li J., Chen X.,
RA Bowman L.H., Vance V.;
RT "Transcriptional silencing induced by Arabidopsis T-DNA mutants is
RT associated with 35S promoter siRNAs and requires genes involved in siRNA-
RT mediated chromatin silencing.";
RL Plant J. 64:699-704(2010).
RN [17]
RP FUNCTION, AND MUTAGENESIS OF ARG-629.
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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NRPD1, AND SUBUNIT.
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 [19]
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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Second largest component of RNA polymerases IV and V which mediate
CC short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed
CC DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS)
CC of endogenous repeated sequences, including transposable elements.
CC Proposed to contribute to the polymerase catalytic activity and forms
CC the polymerase active center together with the largest subunit. Also
CC required for full erasure of methylation when the RNA trigger is
CC withdrawn. Required for intercellular RNA interference (RNAi) leading
CC to systemic post-transcriptional gene silencing. Involved in the
CC maintenance of post-transcriptional RNA silencing. During interphase,
CC mediates siRNA-independent heterochromatin association and methylation
CC into chromocenters and condensation and cytosine methylation at
CC pericentromeric major repeats. Required for complete maintenance of the
CC 35S promoter homology-dependent TGS in transgenic plants and for the
CC initial establishment of DNA methylation. {ECO:0000269|PubMed:15692015,
CC ECO:0000269|PubMed:15766525, ECO:0000269|PubMed:15924141,
CC ECO:0000269|PubMed:16140984, ECO:0000269|PubMed:16839878,
CC ECO:0000269|PubMed:17360559, ECO:0000269|PubMed:17526749,
CC ECO:0000269|PubMed:18425128, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:19825650, ECO:0000269|PubMed:21070421,
CC ECO:0000269|PubMed:21150311}.
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=2.7.7.6;
CC -!- SUBUNIT: Component of the RNA polymerase IV and V complexes. Interacts
CC with SSH1, NRPD1 and NRPE1. {ECO:0000269|PubMed:16140984,
CC ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:21811420, ECO:0000269|PubMed:23637343}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15766525,
CC ECO:0000269|PubMed:16140984, ECO:0000269|PubMed:16839878}.
CC Note=Concentrated in numerous distinct foci around chromocenters.
CC -!- TISSUE SPECIFICITY: Mostly expressed in seedlings, flowers and roots,
CC present ubiquitously, except in sperm cells.
CC {ECO:0000269|PubMed:15766525, ECO:0000269|PubMed:18667720}.
CC -!- DISRUPTION PHENOTYPE: Blocked in the perpetuation of CNN, CG and CNG
CC methylation in repeated endogenous DNA. Reduction of heterochromatin
CC association and methylation into chromocenters, coincident with
CC decondensation and losses in cytosine methylation at pericentromeric
CC major repeats such as 5S gene clusters and AtSN1 retroelements during
CC interphase, independently of siRNA accumulation. Altered cell-to-cell
CC movement of siRNA beyond the vasculature. Reduced 35S promoter
CC homology-dependent transcriptional gene silencing (TGS) in transgenic
CC plants. {ECO:0000269|PubMed:15692015, ECO:0000269|PubMed:15766525,
CC ECO:0000269|PubMed:15924141, ECO:0000269|PubMed:16140984,
CC ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:17526749,
CC ECO:0000269|PubMed:18425128, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:19825650, ECO:0000269|PubMed:21070421}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD43874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY862891; AAW56422.1; -; mRNA.
DR EMBL; AY935711; AAX73261.1; -; mRNA.
DR EMBL; AP000377; BAB01854.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76812.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76813.1; -; Genomic_DNA.
DR EMBL; AK176111; BAD43874.1; ALT_INIT; mRNA.
DR RefSeq; NP_001189957.1; NM_001203028.2.
DR RefSeq; NP_189020.2; NM_113282.3.
DR PDB; 7EU0; EM; 3.16 A; B=1-1172.
DR PDB; 7EU1; EM; 3.86 A; B=1-1172.
DR PDBsum; 7EU0; -.
DR PDBsum; 7EU1; -.
DR AlphaFoldDB; Q9LK40; -.
DR SMR; Q9LK40; -.
DR BioGRID; 7292; 39.
DR STRING; 3702.AT3G23780.2; -.
DR PaxDb; Q9LK40; -.
DR PRIDE; Q9LK40; -.
DR ProteomicsDB; 250570; -.
DR EnsemblPlants; AT3G23780.1; AT3G23780.1; AT3G23780.
DR EnsemblPlants; AT3G23780.2; AT3G23780.2; AT3G23780.
DR GeneID; 821960; -.
DR Gramene; AT3G23780.1; AT3G23780.1; AT3G23780.
DR Gramene; AT3G23780.2; AT3G23780.2; AT3G23780.
DR KEGG; ath:AT3G23780; -.
DR Araport; AT3G23780; -.
DR TAIR; locus:2095233; AT3G23780.
DR eggNOG; KOG0214; Eukaryota.
DR HOGENOM; CLU_000524_5_2_1; -.
DR InParanoid; Q9LK40; -.
DR OMA; CWLHKLQ; -.
DR OrthoDB; 42570at2759; -.
DR PhylomeDB; Q9LK40; -.
DR PRO; PR:Q9LK40; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LK40; baseline and differential.
DR Genevisible; Q9LK40; AT.
DR GO; GO:0000792; C:heterochromatin; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030880; C:RNA polymerase complex; IDA:TAIR.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
DR GO; GO:0000418; C:RNA polymerase IV complex; IDA:UniProtKB.
DR GO; GO:0000419; C:RNA polymerase V complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISS:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006306; P:DNA methylation; IDA:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:TAIR.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:TAIR.
DR GO; GO:0050776; P:regulation of immune response; IMP:TAIR.
DR GO; GO:0030422; P:siRNA processing; IMP:TAIR.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007646; RNA_pol_Rpb2_4.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1172
FT /note="DNA-directed RNA polymerases IV and V subunit 2"
FT /id="PRO_0000407924"
FT ZN_FING 1108..1136
FT /note="C4-type"
FT /evidence="ECO:0000250"
FT BINDING 786
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with RPB1"
FT /evidence="ECO:0000250"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 1136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MUTAGEN 629
FT /note="R->Q: In nrpd/e2-19; decreased DNA methylation."
FT /evidence="ECO:0000269|PubMed:21150311"
FT CONFLICT 1170
FT /note="K -> E (in Ref. 5; BAD43874)"
FT /evidence="ECO:0000305"
FT STRAND 24..26
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 30..45
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 63..69
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 279..284
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 291..297
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 305..321
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 323..326
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 327..329
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 330..340
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 350..356
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 367..383
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 404..407
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 408..418
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 420..426
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 439..442
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 446..458
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 474..477
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 483..489
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 511..513
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 526..530
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 549..552
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 553..556
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 564..566
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 572..576
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 588..598
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 608..612
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 613..616
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 617..621
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 628..632
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 635..638
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 650..655
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 658..663
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 664..669
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 676..678
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 693..696
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 699..703
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 705..709
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 712..720
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 722..725
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 740..747
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 752..754
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 756..760
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 764..766
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 769..776
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 780..786
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 788..791
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 792..795
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 796..800
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 802..812
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 846..848
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 859..861
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 881..890
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 896..906
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 913..916
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 923..928
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 930..932
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 943..946
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 950..954
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 959..970
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 991..993
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 997..1006
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1013..1015
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 1020..1022
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1034..1039
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 1044..1046
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1051..1053
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 1058..1060
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1067..1069
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1073..1075
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 1077..1084
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 1085..1087
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 1090..1094
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 1095..1098
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1105..1111
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1134..1145
FT /evidence="ECO:0007829|PDB:7EU0"
FT HELIX 1149..1158
FT /evidence="ECO:0007829|PDB:7EU0"
FT TURN 1159..1162
FT /evidence="ECO:0007829|PDB:7EU0"
FT STRAND 1163..1169
FT /evidence="ECO:0007829|PDB:7EU0"
SQ SEQUENCE 1172 AA; 132654 MW; F007A39F04D19365 CRC64;
MPDMDIDVKD LEEFEATTGE INLSELGEGF LQSFCKKAAT SFFDKYGLIS HQLNSYNYFI
EHGLQNVFQS FGEMLVEPSF DVVKKKDNDW RYATVKFGEV TVEKPTFFSD DKELEFLPWH
ARLQNMTYSA RIKVNVQVEV FKNTVVKSDK FKTGQDNYVE KKILDVKKQD ILIGSIPVMV
KSILCKTSEK GKENCKKGDC AFDQGGYFVI KGAEKVFIAQ EQMCTKRLWI SNSPWTVSFR
SENKRNRFIV RLSENEKAED YKRREKVLTV YFLSTEIPVW LLFFALGVSS DKEAMDLIAF
DGDDASITNS LIASIHVADA VCEAFRCGNN ALTYVEQQIK STKFPPAESV DECLHLYLFP
GLQSLKKKAR FLGYMVKCLL NSYAGKRKCE NRDSFRNKRI ELAGELLERE IRVHLAHARR
KMTRAMQKHL SGDGDLKPIE HYLDASVITN GLSRAFSTGA WSHPFRKMER VSGVVANLGR
ANPLQTLIDL RRTRQQVLYT GKVGDARYPH PSHWGRVCFL STPDGENCGL VKNMSLLGLV
STQSLESVVE KLFACGMEEL MDDTCTPLFG KHKVLLNGDW VGLCADSESF VAELKSRRRQ
SELPREMEIK RDKDDNEVRI FTDAGRLLRP LLVVENLQKL KQEKPSQYPF DHLLDHGILE
LIGIEEEEDC NTAWGIKQLL KEPKIYTHCE LDLSFLLGVS CAVVPFANHD HGRRVLYQSQ
KHCQQAIGFS STNPNIRCDT LSQQLFYPQK PLFKTLASEC LKKEVLFNGQ NAIVAVNVHL
GYNQEDSIVM NKASLERGMF RSEQIRSYKA EVDAKDSEKR KKMDELVQFG KTHSKIGKVD
SLEDDGFPFI GANMSTGDIV IGRCTESGAD HSIKLKHTER GIVQKVVLSS NDEGKNFAAV
SLRQVRSPCL GDKFSSMHGQ KGVLGYLEEQ QNFPFTIQGI VPDIVINPHA FPSRQTPGQL
LEAALSKGIA CPIQKEGSSA AYTKLTRHAT PFSTPGVTEI TEQLHRAGFS RWGNERVYNG
RSGEMMRSMI FMGPTFYQRL VHMSEDKVKF RNTGPVHPLT RQPVADRKRF GGIKFGEMER
DCLIAHGASA NLHERLFTLS DSSQMHICRK CKTYANVIER TPSSGRKIRG PYCRVCVSSD
HVVRVYVPYG AKLLCQELFS MGITLNFDTK LC
