NRPD1_ARATH
ID NRPD1_ARATH Reviewed; 1453 AA.
AC Q9LQ02;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA-directed RNA polymerase IV subunit 1;
DE AltName: Full=DNA-directed RNA polymerase D subunit 1;
DE Short=AtNRPD1a;
DE Short=Nuclear RNA polymerase D 1a;
DE EC=2.7.7.6;
DE AltName: Full=Protein RNA-DIRECTED DNA METHYLATION DEFECTIVE 3;
DE AltName: Full=Protein SILENCING DEFECTIVE 4;
DE AltName: Full=Protein SILENCING MOVEMENT DEFICIENT 2;
DE AltName: Full=RNA polymerase IV subunit 1a;
DE Short=POL IV 1a;
GN Name=NRPD1; Synonyms=NRPD1a, RMD3, RPD1, SDE4, SMD2;
GN OrderedLocusNames=At1g63020; ORFNames=F16M19.19, F16P17.19;
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], 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10850496; DOI=10.1016/s0092-8674(00)80864-8;
RA Dalmay T., Hamilton A., Rudd S., Angell S., Baulcombe D.C.;
RT "An RNA-dependent RNA polymerase gene in Arabidopsis is required for
RT posttranscriptional gene silencing mediated by a transgene but not by a
RT virus.";
RL Cell 101:543-553(2000).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12198169; DOI=10.1093/emboj/cdf464;
RA Hamilton A., Voinnet O., Chappell L., Baulcombe D.;
RT "Two classes of short interfering RNA in RNA silencing.";
RL EMBO J. 21:4671-4679(2002).
RN [7]
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 [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16377568; DOI=10.1016/j.cell.2005.11.035;
RA Borsani O., Zhu J., Verslues P.E., Sunkar R., Zhu J.-K.;
RT "Endogenous siRNAs derived from a pair of natural cis-antisense transcripts
RT regulate salt tolerance in Arabidopsis.";
RL Cell 123:1279-1291(2005).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16273107; DOI=10.1038/ng1675;
RA Dunoyer P., Himber C., Voinnet O.;
RT "DICER-LIKE 4 is required for RNA interference and produces the 21-
RT nucleotide small interfering RNA component of the plant cell-to-cell
RT silencing signal.";
RL Nat. Genet. 37:1356-1360(2005).
RN [10]
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 [11]
RP FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP NRPD2.
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 [12]
RP 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 [13]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, and cv. No-0;
RX PubMed=17558406; DOI=10.1038/ng2081;
RA Dunoyer P., Himber C., Ruiz-Ferrer V., Alioua A., Voinnet O.;
RT "Intra- and intercellular RNA interference in Arabidopsis thaliana requires
RT components of the microRNA and heterochromatic silencing pathways.";
RL Nat. Genet. 39:848-856(2007).
RN [14]
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 [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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 [16]
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 [17]
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 [18]
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 [19]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=18467467; DOI=10.1104/pp.108.117846;
RA Perez-Hormaeche J., Potet F., Beauclair L., Le Masson I., Courtial B.,
RA Bouche N., Lucas H.;
RT "Invasion of the Arabidopsis genome by the tobacco retrotransposon Tnt1 is
RT controlled by reversible transcriptional gene silencing.";
RL Plant Physiol. 147:1264-1278(2008).
RN [20]
RP INTERACTION WITH NRPD4.
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 [21]
RP FUNCTION, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY, 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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NRPD2; NRPD3; NRPD3B;
RP NRPD4; NRPD5; NRPD5B; NRPD6A; NRPD7; NRPD7B; NRPD9A; NRPD9B; NRPD10;
RP NRPD11; NRPD12; RDR2; RDM4; CLSY1; CLSY2; CLSY3; CLSY4 AND SHH1, AND
RP 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 [23]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SHH1 AND CLSY1.
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 (By similarity). Largest and catalytic component of RNA polymerase IV
CC which mediates 24-nt short-interfering RNAs (siRNA) accumulation.
CC Implicated in siRNA-directed heterochromatin formation through the
CC action of DCL3 and AGO4, and subsequent DNA methylation-dependent
CC silencing of targeted sequences. Essential component of a self-
CC reinforcing loop coupling de novo DNA methylation to siRNA production.
CC Required for intercellular but not intracellular RNA interference
CC (RNAi) leading to systemic post-transcriptional gene silencing.
CC Involved in the maintenance of post-transcriptional RNA silencing.
CC {ECO:0000250, ECO:0000269|PubMed:10850496, ECO:0000269|PubMed:12198169,
CC ECO:0000269|PubMed:15692015, ECO:0000269|PubMed:15766525,
CC ECO:0000269|PubMed:16140984, ECO:0000269|PubMed:16273107,
CC ECO:0000269|PubMed:16377568, ECO:0000269|PubMed:16839878,
CC ECO:0000269|PubMed:17360559, ECO:0000269|PubMed:17526749,
CC ECO:0000269|PubMed:17558406, ECO:0000269|PubMed:17785412,
CC ECO:0000269|PubMed:18287047, ECO:0000269|PubMed:18433438,
CC ECO:0000269|PubMed:18467467, ECO:0000269|PubMed:19110459}.
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 complex. Interacts with
CC NRPD2, NRPD3, NRPD3B, NRPD4, NRPD5, NRPD5B, NRPD6A, NRPD7, NRPD7B,
CC NRPD9A, NRPD9B, NRPD10, NRPD11, NRPD12, RDR2, RDM4, CLSY1, CLSY2,
CC CLSY3, CLSY4 and SHH1. {ECO:0000269|PubMed:16140984,
CC ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:19110459,
CC ECO:0000269|PubMed:19204117, ECO:0000269|PubMed:21811420,
CC ECO:0000269|PubMed:23637343}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16140984,
CC ECO:0000269|PubMed:16839878, ECO:0000269|PubMed:16839879}. Note=Follows
CC a punctate localization pattern.
CC -!- TISSUE SPECIFICITY: Mostly expressed in flowers, and, to a lower
CC extent, in leaves. {ECO:0000269|PubMed:16140984,
CC ECO:0000269|PubMed:17160640}.
CC -!- DISRUPTION PHENOTYPE: Blocked in the perpetuation of CNN, CG and CNG
CC methylation in repeated endogenous DNA accompanied by a reduction in
CC long 24-26 nt siRNAs. Transient loss of post-transcriptional gene
CC silencing (PTGS) in young leaves. Reduction of heterochromatin
CC association into chromocenters, coincident with losses in cytosine
CC methylation at pericentromeric 5S gene clusters and AtSN1
CC retroelements. Altered cell-to-cell movement of siRNAs beyond the
CC vasculature. Release of transposon silencing. Not impaired RNA-directed
CC DNA methylation-dependent (RdDM) silencing. Defective in the
CC maintenance of post-transcriptional RNA silencing.
CC {ECO:0000269|PubMed:10850496, ECO:0000269|PubMed:12198169,
CC ECO:0000269|PubMed:15692015, ECO:0000269|PubMed:15766525,
CC ECO:0000269|PubMed:16140984, ECO:0000269|PubMed:16273107,
CC ECO:0000269|PubMed:16377568, ECO:0000269|PubMed:16839878,
CC ECO:0000269|PubMed:17526749, ECO:0000269|PubMed:17558406,
CC ECO:0000269|PubMed:17785412, ECO:0000269|PubMed:18287047,
CC ECO:0000269|PubMed:18433438, ECO:0000269|PubMed:18467467,
CC ECO:0000269|PubMed:19110459}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; AY826515; AAX12372.1; -; mRNA.
DR EMBL; DQ020657; AAY89363.1; -; mRNA.
DR EMBL; AC010795; AAG51604.1; -; Genomic_DNA.
DR EMBL; AC011000; AAF75815.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34041.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34042.1; -; Genomic_DNA.
DR PIR; D96655; D96655.
DR RefSeq; NP_001185298.1; NM_001198369.1.
DR RefSeq; NP_176490.2; NM_104980.4.
DR AlphaFoldDB; Q9LQ02; -.
DR SMR; Q9LQ02; -.
DR BioGRID; 27826; 32.
DR DIP; DIP-48679N; -.
DR IntAct; Q9LQ02; 1.
DR STRING; 3702.AT1G63020.2; -.
DR PaxDb; Q9LQ02; -.
DR PRIDE; Q9LQ02; -.
DR EnsemblPlants; AT1G63020.1; AT1G63020.1; AT1G63020.
DR EnsemblPlants; AT1G63020.2; AT1G63020.2; AT1G63020.
DR GeneID; 842605; -.
DR Gramene; AT1G63020.1; AT1G63020.1; AT1G63020.
DR Gramene; AT1G63020.2; AT1G63020.2; AT1G63020.
DR KEGG; ath:AT1G63020; -.
DR Araport; AT1G63020; -.
DR TAIR; locus:2015163; AT1G63020.
DR eggNOG; KOG0260; Eukaryota.
DR HOGENOM; CLU_002449_0_1_1; -.
DR InParanoid; Q9LQ02; -.
DR OrthoDB; 106128at2759; -.
DR PhylomeDB; Q9LQ02; -.
DR PRO; PR:Q9LQ02; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LQ02; baseline and differential.
DR Genevisible; Q9LQ02; AT.
DR GO; GO:0005654; C:nucleoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:0000418; C:RNA polymerase IV complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:TAIR.
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: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; 1.10.132.30; -; 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; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 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; Transcription;
KW Transcription regulation; Transferase; Zinc.
FT CHAIN 1..1453
FT /note="DNA-directed RNA polymerase IV subunit 1"
FT /id="PRO_0000407922"
FT REGION 806..818
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 447
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
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"
SQ SEQUENCE 1453 AA; 162521 MW; 0128E71297295F1F CRC64;
MEDDCEELQV PVGTLTSIGF SISNNNDRDK MSVLEVEAPN QVTDSRLGLP NPDSVCRTCG
SKDRKVCEGH FGVINFAYSI INPYFLKEVA ALLNKICPGC KYIRKKQFQI TEDQPERCRY
CTLNTGYPLM KFRVTTKEVF RRSGIVVEVN EESLMKLKKR GVLTLPPDYW SFLPQDSNID
ESCLKPTRRI ITHAQVYALL LGIDQRLIKK DIPMFNSLGL TSFPVTPNGY RVTEIVHQFN
GARLIFDERT RIYKKLVGFE GNTLELSSRV MECMQYSRLF SETVSSSKDS ANPYQKKSDT
PKLCGLRFMK DVLLGKRSDH TFRTVVVGDP SLKLNEIGIP ESIAKRLQVS EHLNQCNKER
LVTSFVPTLL DNKEMHVRRG DRLVAIQVND LQTGDKIFRS LMDGDTVLMN RPPSIHQHSL
IAMTVRILPT TSVVSLNPIC CLPFRGDFDG DCLHGYVPQS IQAKVELDEL VALDKQLINR
QNGRNLLSLG QDSLTAAYLV NVEKNCYLNR AQMQQLQMYC PFQLPPPAII KASPSSTEPQ
WTGMQLFGML FPPGFDYTYP LNNVVVSNGE LLSFSEGSAW LRDGEGNFIE RLLKHDKGKV
LDIIYSAQEM LSQWLLMRGL SVSLADLYLS SDLQSRKNLT EEISYGLREA EQVCNKQQLM
VESWRDFLAV NGEDKEEDSV SDLARFCYER QKSATLSELA VSAFKDAYRD VQALAYRYGD
QSNSFLIMSK AGSKGNIGKL VQHSMCIGLQ NSAVSLSFGF PRELTCAAWN DPNSPLRGAK
GKDSTTTESY VPYGVIENSF LTGLNPLESF VHSVTSRDSS FSGNADLPGT LSRRLMFFMR
DIYAAYDGTV RNSFGNQLVQ FTYETDGPVE DITGEALGSL SACALSEAAY SALDQPISLL
ETSPLLNLKN VLECGSKKGQ REQTMSLYLS EYLSKKKHGF EYGSLEIKNH LEKLSFSEIV
STSMIIFSPS SNTKVPLSPW VCHFHISEKV LKRKQLSAES VVSSLNEQYK SRNRELKLDI
VDLDIQNTNH CSSDDQAMKD DNVCITVTVV EASKHSVLEL DAIRLVLIPF LLDSPVKGDQ
GIKKVNILWT DRPKAPKRNG NHLAGELYLK VTMYGDRGKR NCWTALLETC LPIMDMIDWG
RSHPDNIRQC CSVYGIDAGR SIFVANLESA VSDTGKEILR EHLLLVADSL SVTGEFVALN
AKGWSKQRQV ESTPAPFTQA CFSSPSQCFL KAAKEGVRDD LQGSIDALAW GKVPGFGTGD
QFEIIISPKV HGFTTPVDVY DLLSSTKTMR RTNSAPKSDK ATVQPFGLLH SAFLKDIKVL
DGKGIPMSLL RTIFTWKNIE LLSQSLKRIL HSYEINELLN ERDEGLVKMV LQLHPNSVEK
IGPGVKGIRV AKSKHGDSCC FEVVRIDGTF EDFSYHKCVL GATKIIAPKK MNFYKSKYLK
NGTLESGGFS ENP
