RPOC1_MAIZE
ID RPOC1_MAIZE Reviewed; 683 AA.
AC P16024;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS Zea mays (Maize).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2381419; DOI=10.1007/bf00259403;
RA Igloi G.L., Meinke A., Doery I., Koessel H.;
RT "Nucleotide sequence of the maize chloroplast rpo B/C1/C2 operon:
RT comparison between the derived protein primary structures from various
RT organisms with respect to functional domains.";
RL Mol. Gen. Genet. 221:379-394(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2308853; DOI=10.1093/nar/18.3.663;
RA Igloi G.L., Meinke A., Doery I., Koessel H.;
RT "Nucleotide and derived amino acid sequence of rps2 from maize
RT chloroplasts.";
RL Nucleic Acids Res. 18:663-663(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. B73;
RX PubMed=7666415; DOI=10.1006/jmbi.1995.0460;
RA Maier R.M., Neckermann K., Igloi G.L., Koessel H.;
RT "Complete sequence of the maize chloroplast genome: gene content, hotspots
RT of divergence and fine tuning of genetic information by transcript
RT editing.";
RL J. Mol. Biol. 251:614-628(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX PubMed=2304916; DOI=10.1073/pnas.87.4.1531;
RA Hu J., Bogorad L.;
RT "Maize chloroplast RNA polymerase: the 180-, 120-, and 38-kilodalton
RT polypeptides are encoded in chloroplast genes.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:1531-1535(1990).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
RX PubMed=2062657; DOI=10.1093/nar/19.12.3431;
RA Hu J., Troxler R.F., Bogorad L.;
RT "Maize chloroplast RNA polymerase: the 78-kilodalton polypeptide is encoded
RT by the plastid rpoC1 gene.";
RL Nucleic Acids Res. 19:3431-3434(1991).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01323}.
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:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01323}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01323}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
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DR EMBL; X17318; CAA35196.1; -; Genomic_DNA.
DR EMBL; X86563; CAA60277.1; -; Genomic_DNA.
DR EMBL; M31207; AAA84488.1; -; Genomic_DNA.
DR PIR; S12801; RNZMB1.
DR RefSeq; NP_043016.1; NC_001666.2.
DR AlphaFoldDB; P16024; -.
DR SMR; P16024; -.
DR STRING; 4577.GRMZM5G899366_P01; -.
DR PaxDb; P16024; -.
DR PRIDE; P16024; -.
DR GeneID; 845226; -.
DR KEGG; zma:845226; -.
DR MaizeGDB; 69581; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR HOGENOM; CLU_030022_2_0_1; -.
DR OMA; WGERTLP; -.
DR OrthoDB; 774084at2759; -.
DR Proteomes; UP000007305; Chloroplast.
DR ExpressionAtlas; P16024; baseline and differential.
DR Genevisible; P16024; ZM.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01323; RNApol_bact_RpoC1; 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; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR034678; RNApol_RpoC1.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..683
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067879"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ SEQUENCE 683 AA; 78323 MW; FDBF04DEB555B30A CRC64;
MIDQYKHKQL QIGLVSPQQI KAWAKKILPN GEVVGEVTRP STFHYKTDKP EKDGLFCERI
FGPIKSGICA CGNSRASVRE NEDERFCQKC GVEFVDSRIR RYQMGYIKLA CPVTHVWYLK
GLPSYIANLL DKPLKKLEGL VYGDFSFARP SAKKPTFLRL RGLFEDEISS CNHSISPFFS
TPGFATFRNR EIATGAGAIR EQLADLDLRI IIENSLVEWK ELEDEGYSGD EWEDRKRRIR
KVFLIRRMQL AKHFIQTNVE PEWMVLCLLP VLPPELRPIV YRSGDKVVTS DINELYKRVI
RRNNNLAYLL KRSELAPADL VMCQEKLVQE AVDTLLDSGS RGQPTRDGHN KVYKSLSDVI
EGKEGRFRET LLGKRVDYSG RSVIVVGPSL SLHQCGLPLE IAIKLFQLFV IRDLITKRAT
SNVRIAKRKI WEKEPIVWEI LQEVMRGHPV LLNRAPTLHR LGIQAFQPTL VEGRTICLHP
LVCKGFNADF DGDQMAVHLP LSLEAQAEAR LLMFSHMNLL SPAIGDPICV PTQDMLIGLY
VLTIGNRLGI CANRYNSCGN SPNKKVNYNN NNYYKYTKDK EPHFSSSYDA LGAYRQKRIG
LNSPLWLRWK LDQRIVGSRE VPIEVQYESF GTYHEIYAHY LVVGNRKKEI RSIYIRTTLG
HISFYREIEE AIQGFSRAYS YTI
