NRPA1_ARATH
ID NRPA1_ARATH Reviewed; 1670 AA.
AC Q9SVY0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA-directed RNA polymerase I subunit 1 {ECO:0000305};
DE AltName: Full=DNA-directed RNA polymerase I subunit RPA1 {ECO:0000305};
DE Short=DNA polymerase I subunit A1 {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000305};
DE AltName: Full=Nuclear RNA polymerase A1 {ECO:0000312|EMBL:AEE79684.1};
GN Name=NRPA1 {ECO:0000312|EMBL:AEE79684.1}; Synonyms=RPA1 {ECO:0000305};
GN OrderedLocusNames=At3g57660 {ECO:0000312|Araport:AT3G57660};
GN ORFNames=F15B8.150 {ECO:0000312|EMBL:CAB41189.1};
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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).
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 I which
CC synthesizes ribosomal RNA precursors. Forms the polymerase active
CC center together with the second largest subunit. A single stranded DNA
CC template strand of the promoter is positioned within the central active
CC site cleft of Pol I. A bridging helix emanates from NRPA1 and crosses
CC the cleft near the catalytic site and is thought to promote
CC translocation of Pol I by acting as a ratchet that moves the RNA-DNA
CC hybrid through the active site by switching from straight to bent
CC conformations at each step of nucleotide addition.
CC {ECO:0000250|UniProtKB:P10964}.
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 I (Pol I) complex consisting
CC of at least 13 subunits. {ECO:0000250|UniProtKB:P10964}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P10964}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; AL049660; CAB41189.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79684.1; -; Genomic_DNA.
DR PIR; T06754; T06754.
DR RefSeq; NP_191325.1; NM_115626.1.
DR AlphaFoldDB; Q9SVY0; -.
DR SMR; Q9SVY0; -.
DR IntAct; Q9SVY0; 1.
DR STRING; 3702.AT3G57660.1; -.
DR iPTMnet; Q9SVY0; -.
DR PaxDb; Q9SVY0; -.
DR PRIDE; Q9SVY0; -.
DR ProteomicsDB; 250600; -.
DR EnsemblPlants; AT3G57660.1; AT3G57660.1; AT3G57660.
DR GeneID; 824935; -.
DR Gramene; AT3G57660.1; AT3G57660.1; AT3G57660.
DR KEGG; ath:AT3G57660; -.
DR Araport; AT3G57660; -.
DR TAIR; locus:2076661; AT3G57660.
DR eggNOG; KOG0262; Eukaryota.
DR HOGENOM; CLU_000487_2_4_1; -.
DR InParanoid; Q9SVY0; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; Q9SVY0; -.
DR PRO; PR:Q9SVY0; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SVY0; baseline and differential.
DR Genevisible; Q9SVY0; AT.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005736; C:RNA polymerase I 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR015699; DNA-dir_RNA_pol1_lsu.
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; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR PANTHER; PTHR19376:SF11; PTHR19376:SF11; 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 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Ribosome biogenesis;
KW Transcription; Transferase; Zinc.
FT CHAIN 1..1670
FT /note="DNA-directed RNA polymerase I subunit 1"
FT /id="PRO_0000434008"
FT REGION 154..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1017
FT /note="Bridging helix"
FT /evidence="ECO:0000305"
FT REGION 1318..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1336..1351
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1406..1426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 602
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 604
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
FT BINDING 606
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P04050"
SQ SEQUENCE 1670 AA; 187576 MW; 2F43F2907D4B2C8F CRC64;
MAHAQTTEVC LSFHRSLLFP MGASQVVESV RFSFMTEQDV RKHSFLKVTS PILHDNVGNP
FPGGLYDLKL GPKDDKQACN SCGQLKLACP GHCGHIELVF PIYHPLLFNL LFNFLQRACF
FCHHFMAKPE DVERAVSQLK LIIKGDIVSA KQLESNTPTK SKSSDESCES VVTTDSSEEC
EDSDVEDQRW TSLQFAEVTA VLKNFMRLSS KSCSRCKGIN PKLEKPMFGW VRMRAMKDSD
VGANVIRGLK LKKSTSSVEN PDGFDDSGID ALSEVEDGDK ETREKSTEVA AEFEEHNSKR
DLLPSEVRNI LKHLWQNEHE FCSFIGDLWQ SGSEKIDYSM FFLESVLVPP TKFRPPTTGG
DSVMEHPQTV GLNKVIESNN ILGNACTNKL DQSKVIFRWR NLQESVNVLF DSKTATVQSQ
RDSSGICQLL EKKEGLFRQK MMGKRVNHAC RSVISPDPYI AVNDIGIPPC FALKLTYPER
VTPWNVEKLR EAIINGPDIH PGATHYSDKS STMKLPSTEK ARRAIARKLL SSRGATTELG
KTCDINFEGK TVHRHMRDGD IVLVNRQPTL HKPSLMAHKV RVLKGEKTLR LHYANCSTYN
ADFDGDEMNV HFPQDEISRA EAYNIVNANN QYARPSNGEP LRALIQDHIV SSVLLTKRDT
FLDKDHFNQL LFSSGVTDMV LSTFSGRSGK KVMVSASDAE LLTVTPAILK PVPLWTGKQV
ITAVLNQITK GHPPFTVEKA TKLPVDFFKC RSREVKPNSG DLTKKKEIDE SWKQNLNEDK
LHIRKNEFVC GVIDKAQFAD YGLVHTVHEL YGSNAAGNLL SVFSRLFTVF LQTHGFTCGV
DDLIILKDMD EERTKQLQEC ENVGERVLRK TFGIDVDVQI DPQDMRSRIE RILYEDGESA
LASLDRSIVN YLNQCSSKGV MNDLLSDGLL KTPGRNCISL MTISGAKGSK VNFQQISSHL
GQQDLEGKRV PRMVSGKTLP CFHPWDWSPR AGGFISDRFL SGLRPQEYYF HCMAGREGLV
DTAVKTSRSG YLQRCLMKNL ESLKVNYDCT VRDADGSIIQ FQYGEDGVDV HRSSFIEKFK
ELTINQDMVL QKCSEDMLSG ASSYISDLPI SLKKGAEKFV EAMPMNERIA SKFVRQEELL
KLVKSKFFAS LAQPGEPVGV LAAQSVGEPS TQMTLNTFHL AGRGEMNVTL GIPRLQEILM
TAAANIKTPI MTCPLLKGKT KEDANDITDR LRKITVADII KSMELSVVPY TVYENEVCSI
HKLKINLYKP EHYPKHTDIT EEDWEETMRA VFLRKLEDAI ETHMKMLHRI RGIHNDVTGP
IAGNETDNDD SVSGKQNEDD GDDDGEGTEV DDLGSDAQKQ KKQETDEMDY EENSEDETNE
PSSISGVEDP EMDSENEDTE VSKEDTPEPQ EESMEPQKEV KGVKNVKEQS KKKRRKFVRA
KSDRHIFVKG EGEKFEVHFK FATDDPHILL AQIAQQTAQK VYIQNSGKIE RCTVANCGDP
QVIYHGDNPK ERREISNDEK KASPALHASG VDFPALWEFQ DKLDVRYLYS NSIHDMLNIF
GVEAARETII REINHVFKSY GISVSIRHLN LIADYMTFSG GYRPMSRMGG IAESTSPFCR
MTFETATKFI VQAATYGEKD TLETPSARIC LGLPALSGTG CFDLMQRVEL
