NRPE1_ARATH
ID NRPE1_ARATH Reviewed; 1976 AA.
AC Q5D869; O04206; O04207; Q1L5X4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=DNA-directed RNA polymerase V subunit 1;
DE AltName: Full=DNA-directed RNA polymerase D subunit 1b;
DE Short=AtNRPD1b;
DE Short=Nuclear RNA polymerase D 1b;
DE AltName: Full=DNA-directed RNA polymerase E subunit 1;
DE Short=Nuclear RNA polymerase E 1;
DE EC=2.7.7.6;
DE AltName: Full=Protein DEFECTIVE IN MERISTEM SILENCING 5;
DE AltName: Full=Protein DEFECTIVE IN RNA-DIRECTED DNA METHYLATION 3;
DE AltName: Full=Protein RNA-DIRECTED DNA METHYLATION DEFECTIVE 1;
DE AltName: Full=RNA polymerase IV subunit 1;
DE Short=POL IV 1;
GN Name=NRPE1; Synonyms=DMS5, DRD3, NRPD1b, RMD1, RPE1;
GN OrderedLocusNames=At2g40030; ORFNames=T28M21.19;
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, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=17160640; DOI=10.1007/s00239-006-0093-z;
RA Luo J., Hall B.D.;
RT "A multistep process gave rise to RNA polymerase IV of land plants.";
RL J. Mol. Evol. 64:101-112(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NRPD2A.
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 [8]
RP INTERACTION WITH AGO4, AND SUBCELLULAR LOCATION.
RX PubMed=16839879; DOI=10.1016/j.cell.2006.05.032;
RA Li C.F., Pontes O., El-Shami M., Henderson I.R., Bernatavichute Y.V.,
RA Chan S.W.-L., Lagrange T., Pikaard C.S., Jacobsen S.E.;
RT "An ARGONAUTE4-containing nuclear processing center colocalized with Cajal
RT bodies in Arabidopsis thaliana.";
RL Cell 126:93-106(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.
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 [11]
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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18433438; DOI=10.1111/j.1365-313x.2008.03525.x;
RA Eamens A., Vaistij F.E., Jones L.;
RT "NRPD1a and NRPD1b are required to maintain post-transcriptional RNA
RT silencing and RNA-directed DNA methylation in Arabidopsis.";
RL Plant J. 55:596-606(2008).
RN [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=18287047; DOI=10.1073/pnas.0709632105;
RA Mosher R.A., Schwach F., Studholme D., Baulcombe D.C.;
RT "PolIVb influences RNA-directed DNA methylation independently of its role
RT in siRNA biogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3145-3150(2008).
RN [14]
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 [15]
RP INTERACTION WITH NRPD4, AND SUBCELLULAR LOCATION.
RX PubMed=19204117; DOI=10.1101/gad.1765209;
RA He X.-J., Hsu Y.-F., Pontes O., Zhu J., Lu J., Bressan R.A., Pikaard C.,
RA Wang C.-S., Zhu J.-K.;
RT "NRPD4, a protein related to the RPB4 subunit of RNA polymerase II, is a
RT component of RNA polymerases IV and V and is required for RNA-directed DNA
RT methylation.";
RL Genes Dev. 23:318-330(2009).
RN [16]
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 [17]
RP FUNCTION, AND MUTAGENESIS OF ASP-451.
RX PubMed=19141635; DOI=10.1073/pnas.0810310106;
RA Lahmy S., Pontier D., Cavel E., Vega D., El-Shami M., Kanno T.,
RA Lagrange T.;
RT "PolV(PolIVb) function in RNA-directed DNA methylation requires the
RT conserved active site and an additional plant-specific subunit.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:941-946(2009).
RN [18]
RP WG/GW REPEATS.
RX PubMed=20338883; DOI=10.1093/nar/gkq162;
RA Karlowski W.M., Zielezinski A., Carrere J., Pontier D., Lagrange T.,
RA Cooke R.;
RT "Genome-wide computational identification of WG/GW Argonaute-binding
RT proteins in Arabidopsis.";
RL Nucleic Acids Res. 38:4231-4245(2010).
RN [19]
RP FUNCTION, MUTAGENESIS OF GLY-49, 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 [20]
RP FUNCTION, AND INTERACTION WITH SUVH2.
RX PubMed=24463519; DOI=10.1038/nature12931;
RA Johnson L.M., Du J., Hale C.J., Bischof S., Feng S., Chodavarapu R.K.,
RA Zhong X., Marson G., Pellegrini M., Segal D.J., Patel D.J., Jacobsen S.E.;
RT "SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to
RT DNA methylation.";
RL Nature 507:124-128(2014).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic component of RNA polymerase V involved in RNA-
CC directed DNA methylation-dependent (RdDM) silencing of endogenous
CC repeated sequences, including transposable elements. Also required for
CC full erasure of methylation when the RNA trigger is withdrawn. Seems
CC also involved in the synthesis of short-interfering RNAs (siRNA).
CC Essential component of a self-reinforcing loop coupling de novo DNA
CC methylation to siRNA production. Involved in the maintenance of post-
CC transcriptional RNA silencing. {ECO:0000269|PubMed:15766525,
CC ECO:0000269|PubMed:15924141, ECO:0000269|PubMed:16140984,
CC ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:17360559,
CC ECO:0000269|PubMed:18287047, ECO:0000269|PubMed:18425128,
CC ECO:0000269|PubMed:18433438, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:19141635, ECO:0000269|PubMed:21150311,
CC ECO:0000269|PubMed:24463519}.
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 V complex. Interacts with
CC NRPD4, NRPD2A, and (via C-terminus) with AGO4. Interacts with SUVH2.
CC {ECO:0000269|PubMed:16140984, ECO:0000269|PubMed:16839878,
CC ECO:0000269|PubMed:16839879, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:19204117, ECO:0000269|PubMed:24463519}.
CC -!- INTERACTION:
CC Q5D869; Q9ZVD5: AGO4; NbExp=3; IntAct=EBI-2352263, EBI-2352199;
CC Q5D869; Q9M1J2: NRPE5A; NbExp=2; IntAct=EBI-2352263, EBI-15751359;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16140984,
CC ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:16839879,
CC ECO:0000269|PubMed:19204117}. Note=Clustered within heterochromatic
CC regions and colocalized with RDR2, DCL3, NRPD4, AGO4, and siRNAs within
CC the nucleolus. Recruited to chromatin via its interaction with SUVH2.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, and, to a lower
CC extent, in leaves. Present in sperm cells.
CC {ECO:0000269|PubMed:16140984, ECO:0000269|PubMed:17160640,
CC ECO:0000269|PubMed:18667720}.
CC -!- DOMAIN: WG/GW repeats are involved in AGO4 binding.
CC -!- DISRUPTION PHENOTYPE: Blocked in the perpetuation of CNN, CG and CNG
CC methylation in repeated endogenous DNA accompanied by a reduction in
CC 24-nt siRNAs. Reduction of heterochromatin association into
CC chromocenters, coincident with losses in cytosine methylation at
CC pericentromeric 5S gene clusters and AtSN1 retroelements. Impaired RNA-
CC directed DNA methylation-dependent (RdDM) silencing. Defective in the
CC maintenance of post-transcriptional RNA silencing.
CC {ECO:0000269|PubMed:15766525, ECO:0000269|PubMed:15924141,
CC ECO:0000269|PubMed:16140984, ECO:0000269|PubMed:16839878,
CC ECO:0000269|PubMed:18287047, ECO:0000269|PubMed:18425128,
CC ECO:0000269|PubMed:18433438, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:21150311}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB95288.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAB95289.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY826516; AAX12373.1; -; mRNA.
DR EMBL; AY927744; AAY15198.1; -; mRNA.
DR EMBL; DQ020656; AAY89362.1; -; mRNA.
DR EMBL; AF002109; AAB95288.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF002109; AAB95289.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09767.1; -; Genomic_DNA.
DR PIR; D84824; D84824.
DR PIR; E84824; E84824.
DR RefSeq; NP_181532.2; NM_129561.4.
DR AlphaFoldDB; Q5D869; -.
DR SMR; Q5D869; -.
DR BioGRID; 3929; 30.
DR DIP; DIP-48678N; -.
DR IntAct; Q5D869; 3.
DR MINT; Q5D869; -.
DR STRING; 3702.AT2G40030.1; -.
DR iPTMnet; Q5D869; -.
DR PaxDb; Q5D869; -.
DR PRIDE; Q5D869; -.
DR ProteomicsDB; 250480; -.
DR EnsemblPlants; AT2G40030.1; AT2G40030.1; AT2G40030.
DR GeneID; 818591; -.
DR Gramene; AT2G40030.1; AT2G40030.1; AT2G40030.
DR KEGG; ath:AT2G40030; -.
DR Araport; AT2G40030; -.
DR TAIR; locus:2061151; AT2G40030.
DR eggNOG; KOG0260; Eukaryota.
DR eggNOG; KOG2992; Eukaryota.
DR HOGENOM; CLU_002449_2_0_1; -.
DR InParanoid; Q5D869; -.
DR OrthoDB; 106128at2759; -.
DR PhylomeDB; Q5D869; -.
DR PRO; PR:Q5D869; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5D869; baseline and differential.
DR Genevisible; Q5D869; AT.
DR GO; GO:0016604; C:nuclear body; IDA:TAIR.
DR GO; GO:0005730; C:nucleolus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030880; C:RNA polymerase complex; IDA:TAIR.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0000418; C:RNA polymerase IV complex; IDA:TAIR.
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:0050832; P:defense response to fungus; IMP:TAIR.
DR GO; GO:0006306; P:DNA methylation; IMP:TAIR.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:TAIR.
DR GO; GO:0030422; P:siRNA processing; IMP:TAIR.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd02737; RNAP_IV_NRPD1_C; 1.
DR CDD; cd10506; RNAP_IV_RPD1_N; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR040402; NRPD1_C.
DR InterPro; IPR040403; NRPD1_N.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..1976
FT /note="DNA-directed RNA polymerase V subunit 1"
FT /id="PRO_0000407923"
FT REPEAT 1215..1216
FT /note="1"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1329..1330
FT /note="2"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1378..1379
FT /note="3"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1415..1416
FT /note="4"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1430..1431
FT /note="5"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1439..1440
FT /note="6"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1447..1448
FT /note="7"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1464..1465
FT /note="8"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1498..1499
FT /note="9"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1528..1529
FT /note="10"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1545..1546
FT /note="11"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1562..1563
FT /note="11"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1596..1597
FT /note="12"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1604..1605
FT /note="13"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1621..1622
FT /note="14"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1638..1639
FT /note="15"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1641..1642
FT /note="16"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1680..1681
FT /note="17"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REPEAT 1692..1693
FT /note="18"
FT /evidence="ECO:0000269|PubMed:20338883"
FT REGION 751..763
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT REGION 1215..1693
FT /note="18 X 2 AA repeats of [WG]-[GW] repeats"
FT REGION 1272..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1298..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1389..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1459..1473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1486..1508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1524..1538
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1649..1681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1857..1976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT MUTAGEN 49
FT /note="G->R: In nrpe1-12; decreased DNA methylation."
FT /evidence="ECO:0000269|PubMed:21150311"
FT MUTAGEN 451
FT /note="D->N: In nrpe1-3/drd3-3; loss of CNN DNA
FT methylation, but no effect on interaction with NRPE5A."
FT /evidence="ECO:0000269|PubMed:19141635"
SQ SEQUENCE 1976 AA; 218228 MW; C16F6B0BBDC40617 CRC64;
MEEESTSEIL DGEIVGITFA LASHHEICIQ SISESAINHP SQLTNAFLGL PLEFGKCESC
GATEPDKCEG HFGYIQLPVP IYHPAHVNEL KQMLSLLCLK CLKIKKAKGT SGGLADRLLG
VCCEEASQIS IKDRASDGAS YLELKLPSRS RLQPGCWNFL ERYGYRYGSD YTRPLLAREV
KEILRRIPEE SRKKLTAKGH IPQEGYILEY LPVPPNCLSV PEASDGFSTM SVDPSRIELK
DVLKKVIAIK SSRSGETNFE SHKAEASEMF RVVDTYLQVR GTAKAARNID MRYGVSKISD
SSSSKAWTEK MRTLFIRKGS GFSSRSVITG DAYRHVNEVG IPIEIAQRIT FEERVSVHNR
GYLQKLVDDK LCLSYTQGST TYSLRDGSKG HTELKPGQVV HRRVMDGDVV FINRPPTTHK
HSLQALRVYV HEDNTVKINP LMCSPLSADF DGDCVHLFYP QSLSAKAEVM ELFSVEKQLL
SSHTGQLILQ MGSDSLLSLR VMLERVFLDK ATAQQLAMYG SLSLPPPALR KSSKSGPAWT
VFQILQLAFP ERLSCKGDRF LVDGSDLLKF DFGVDAMGSI INEIVTSIFL EKGPKETLGF
FDSLQPLLME SLFAEGFSLS LEDLSMSRAD MDVIHNLIIR EISPMVSRLR LSYRDELQLE
NSIHKVKEVA ANFMLKSYSI RNLIDIKSNS AITKLVQQTG FLGLQLSDKK KFYTKTLVED
MAIFCKRKYG RISSSGDFGI VKGCFFHGLD PYEEMAHSIA AREVIVRSSR GLAEPGTLFK
NLMAVLRDIV ITNDGTVRNT CSNSVIQFKY GVDSERGHQG LFEAGEPVGV LAATAMSNPA
YKAVLDSSPN SNSSWELMKE VLLCKVNFQN TTNDRRVILY LNECHCGKRF CQENAACTVR
NKLNKVSLKD TAVEFLVEYR KQPTISEIFG IDSCLHGHIH LNKTLLQDWN ISMQDIHQKC
EDVINSLGQK KKKKATDDFK RTSLSVSECC SFRDPCGSKG SDMPCLTFSY NATDPDLERT
LDVLCNTVYP VLLEIVIKGD SRICSANIIW NSSDMTTWIR NRHASRRGEW VLDVTVEKSA
VKQSGDAWRV VIDSCLSVLH LIDTKRSIPY SVKQVQELLG LSCAFEQAVQ RLSASVRMVS
KGVLKEHIIL LANNMTCSGT MLGFNSGGYK ALTRSLNIKA PFTEATLIAP RKCFEKAAEK
CHTDSLSTVV GSCSWGKRVD VGTGSQFELL WNQKETGLDD KEETDVYSFL QMVISTTNAD
AFVSSPGFDV TEEEMAEWAE SPERDSALGE PKFEDSADFQ NLHDEGKPSG ANWEKSSSWD
NGCSGGSEWG VSKSTGGEAN PESNWEKTTN VEKEDAWSSW NTRKDAQESS KSDSGGAWGI
KTKDADADTT PNWETSPAPK DSIVPENNEP TSDVWGHKSV SDKSWDKKNW GTESAPAAWG
STDAAVWGSS DKKNSETESD AAAWGSRDKN NSDVGSGAGV LGPWNKKSSE TESNGATWGS
SDKTKSGAAA WNSWDKKNIE TDSEPAAWGS QGKKNSETES GPAAWGAWDK KKSETEPGPA
GWGMGDKKNS ETELGPAAMG NWDKKKSDTK SGPAAWGSTD AAAWGSSDKN NSETESDAAA
WGSRNKKTSE IESGAGAWGS WGQPSPTAED KDTNEDDRNP WVSLKETKSR EKDDKERSQW
GNPAKKFPSS GGWSNGGGAD WKGNRNHTPR PPRSEDNLAP MFTATRQRLD SFTSEEQELL
SDVEPVMRTL RKIMHPSAYP DGDPISDDDK TFVLEKILNF HPQKETKLGS GVDFITVDKH
TIFSDSRCFF VVSTDGAKQD FSYRKSLNNY LMKKYPDRAE EFIDKYFTKP RPSGNRDRNN
QDATPPGEEQ SQPPNQSIGN GGDDFQTQTQ SQSPSQTRAQ SPSQAQAQSP SQTQSQSQSQ
SQSQSQSQSQ SQSQSQSQSQ SQSQSQSPSQ TQTQSPSQTQ AQAQSPSSQS PSQTQT
