NRPC1_ARATH
ID NRPC1_ARATH Reviewed; 1376 AA.
AC F4JXF9; Q9LVH0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=DNA-directed RNA polymerase III subunit 1 {ECO:0000305};
DE AltName: Full=DNA-directed RNA polymerase III subunit RPC1 {ECO:0000305};
DE Short=DNA polymerase I subunit C1 {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000305};
DE AltName: Full=Nuclear RNA polymerase C1 {ECO:0000312|EMBL:AED97269.1};
GN Name=NRPC1 {ECO:0000312|EMBL:AED97269.1}; Synonyms=RPC1 {ECO:0000305};
GN OrderedLocusNames=At5g60040 {ECO:0000312|Araport:AT5G60040};
GN ORFNames=MGO3.2 {ECO:0000312|EMBL:BAA96933.1};
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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 core component of RNA polymerase III which
CC synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase
CC active center together with the second largest subunit. A single-
CC stranded DNA template strand of the promoter is positioned within the
CC central active site cleft of Pol III. A bridging helix emanates from
CC NRPC1 and crosses the cleft near the catalytic site and is thought to
CC promote translocation of Pol III by acting as a ratchet that moves the
CC RNA-DNA hybrid through the active site by switching from straight to
CC bent conformations at each step of nucleotide addition.
CC {ECO:0000250|UniProtKB:P04051}.
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; Evidence={ECO:0000305};
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000250|UniProtKB:P04051}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P04051}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences. {ECO:0000305};
CC Name=1;
CC IsoId=F4JXF9-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK229965; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AK230117; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA96933.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB019231; BAA96933.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97269.1; -; Genomic_DNA.
DR EMBL; AK229965; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK230117; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_200812.2; NM_125397.3. [F4JXF9-1]
DR AlphaFoldDB; F4JXF9; -.
DR SMR; F4JXF9; -.
DR STRING; 3702.AT5G60040.2; -.
DR iPTMnet; F4JXF9; -.
DR PaxDb; F4JXF9; -.
DR PRIDE; F4JXF9; -.
DR ProteomicsDB; 249451; -. [F4JXF9-1]
DR EnsemblPlants; AT5G60040.1; AT5G60040.1; AT5G60040. [F4JXF9-1]
DR GeneID; 836126; -.
DR Gramene; AT5G60040.1; AT5G60040.1; AT5G60040. [F4JXF9-1]
DR KEGG; ath:AT5G60040; -.
DR Araport; AT5G60040; -.
DR eggNOG; KOG0261; Eukaryota.
DR HOGENOM; CLU_000487_3_0_1; -.
DR OMA; AVCPPYN; -.
DR PRO; PR:F4JXF9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4JXF9; baseline and differential.
DR Genevisible; F4JXF9; AT.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
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:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_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; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 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 Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1376
FT /note="DNA-directed RNA polymerase III subunit 1"
FT /id="PRO_0000434010"
FT REGION 845..857
FT /note="Bridging helix"
FT /evidence="ECO:0000305"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 118
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
SQ SEQUENCE 1376 AA; 153006 MW; 12B86B2A04751C4E CRC64;
METKMEIEFT KKPYIEDVGP LKIKSINFSV LSDLEVMKAA EVQVWNIGLY DHSFKPYENG
LLDPRMGPPN KKSICTTCEG NFQNCPGHYG YLKLDLPVYN VGYFNFILDI LKCICKRCSN
MLLDEKLYED HLRKMRNPRM EPLKKTELAK AVVKKCSTMA SQRIITCKKC GYLNGMVKKI
AAQFGIGISH DRSKIHGGEI DECKSAISHT KQSTAAINPL TYVLDPNLVL GLFKRMSDKD
CELLYIAYRP ENLIITCMLV PPLSIRPSVM IGGIQSNEND LTARLKQIIL GNASLHKILS
QPTSSPKNMQ VWDTVQIEVA RYINSEVRGC QNQPEEHPLS GILQRLKGKG GRFRANLSGK
RVEFTGRTVI SPDPNLKITE VGIPILMAQI LTFPECVSRH NIEKLRQCVR NGPNKYPGAR
NVRYPDGSSR TLVGDYRKRI ADELAIGCIV DRHLQEGDVV LFNRQPSLHR MSIMCHRARI
MPWRTLRFNE SVCNPYNADF DGDEMNMHVP QTEEARTEAI TLMGVQNNLC TPKNGEILVA
STQDFLTSSF LITRKDTFYD RAAFSLICSY MGDGMDSIDL PTPTILKPIE LWTGKQIFSV
LLRPNASIRV YVTLNVKEKN FKKGEHGFDE TMCINDGWVY FRNSELISGQ LGKATLGNGN
KDGLYSILLR DYNSHAAAVC MNRLAKLSAR WIGIHGFSIG IDDVQPGEEL SKERKDSIQF
GYDQCHRKIE EFNRGNLQLK AGLDGAKSLE AEITGILNTI REATGKACMS GLHWRNSPLI
MSQCGSKGSP INISQMVACV GQQTVNGHRA PDGFIDRSLP HFPRMSKSPA AKGFVANSFY
SGLTATEFFF HTMGGREGLV DTAVKTASTG YMSRRLMKAL EDLLVHYDNT VRNASGCILQ
FTYGDDGMDP ALMEGKDGAP LNFNRLFLKV QATCPPRSHH TYLSSEELSQ KFEEELVRHD
KSRVCTDAFV KSLREFVSLL GVKSASPPQV LYKASGVTDK QLEVFVKICV FRYREKKIEA
GTAIGTIGAQ SIGEPGTQMT LKTFHFAGVA SMNITQGVPR INEIINASKN ISTPVISAEL
ENPLELTSAR WVKGRIEKTT LGQVAESIEV LMTSTSASVR IILDNKIIEE ACLSITPWSV
KNSILKTPRI KLNDNDIRVL DTGLDITPVV DKSRAHFNLH NLKNVLPNII VNGIKTVERV
VVAEDMDKSK QIDGKTKWKL FVEGTNLLAV MGTPGINGRT TTSNNVVEVS KTLGIEAART
TIIDEIGTVM GNHGMSIDIR HMMLLADVMT YRGEVLGIQR TGIQKMDKSV LMQASFERTG
DHLFSAAASG KVDNIEGVTE CVIMGIPMKL GTGILKVLQR TDDLPKLKYG PDPIIS
