ID A0A6F8FN23_9GENT Unreviewed; 685 AA. AC A0A6F8FN23; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 27-NOV-2024, entry version 15. DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01323}; DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01323}; DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; DE Short=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; GN Name=rpoC1 {ECO:0000256|HAMAP-Rule:MF_01323, GN ECO:0000313|EMBL:ATL61741.1}; OS Gaertnera phyllostachya. OG Plastid; Chloroplast {ECO:0000313|EMBL:ATL61741.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Gentianales; Rubiaceae; Rubioideae; Gaertnereae; OC Gaertnera. OX NCBI_TaxID=509943 {ECO:0000313|EMBL:ATL61741.1}; RN [1] {ECO:0000313|EMBL:ATL61741.1} RP NUCLEOTIDE SEQUENCE. RA Wikstrom N.; RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ATL61741.1} RP NUCLEOTIDE SEQUENCE. RA Wikstroem N., Bremer B., Rydin C.; RT "Conflicting phylogenetic signals in genomic data of the coffee family RT (Rubiaceae)."; RL Zhi Wu Fen Lei Xue Bao 0:0-0(2020). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000256|HAMAP-Rule:MF_01323, ECO:0000256|RuleBase:RU004279}. CC -!- CATALYTIC ACTIVITY: CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + CC diphosphate; 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:0000256|ARBA:ARBA00024550, CC ECO:0000256|HAMAP-Rule:MF_01323, ECO:0000256|RuleBase:RU004279}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01323}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323}; CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01323}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01323}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1 CC subfamily. {ECO:0000256|ARBA:ARBA00007207, ECO:0000256|HAMAP- CC Rule:MF_01323}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; KY378695; ATL61741.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6F8FN23; -. 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:DNA-templated transcription; IEA:UniProtKB-UniRule. DR FunFam; 4.10.860.120:FF:000007; DNA-directed RNA polymerase subunit gamma; 1. DR Gene3D; 1.10.40.90; -; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 1. DR SMART; SM00663; RPOLA_N; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ATL61741.1}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01323}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01323}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01323}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01323}; Plastid {ECO:0000313|EMBL:ATL61741.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01323}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01323}; Zinc {ECO:0000256|HAMAP-Rule:MF_01323}. FT DOMAIN 265..547 FT /note="RNA polymerase N-terminal" FT /evidence="ECO:0000259|SMART:SM00663" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 87 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 493 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 495 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 497 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" SQ SEQUENCE 685 AA; 79163 MW; 4BD0E115C41F1894 CRC64; MIDRYKHQQL QIGSVSPQQI SAWATKILPN GEIVGEVKKP YTFHYKTNKP EKDGLFCERI FGPIKSGICA CGNYRVIGEE KGDPKFCEKC GVEFIDSRIR RYQMGYIKLA CPVTHVWYLK RLPSYIANLL DKSLKELEGL VYGDYPNFSF ARHITKKPTF LRLRGLFEYE IQSWKYSIPL FFTTEGFYTF RNREMSTGAI AIREQLADLD LRIILENSLV EWKELGEEGP TGNEWEDRKV GRRKDFLVRR MELTKHFIRT NIEPEWMVLC LLPVLPPELR PIIQIDGGKL MSSDINELYR RVIYRNNTLT DLLTTNRSTP GELVMCQEKL VQEAVDTLLD NGIRRGQPTK DGHNKVYKSF SDVIEGKEGR FRETLLGKRV DYSGRSVIVV GPSLSLHRCG LPREIAIELF QTFVIRGLIG QHLASNIGVA KNKIREKETI VWEILQEVMQ GHPVLLNRAP TLHRLGIQAF QPVLVEGRAI CLHPLVCKGF NADFDGDQMA VHVPLSLEAQ SEARLLMFSH QNLLSPAIGD PISVPTQDML MGLYVLTSGN RRGICVIKYN PRNYRKYENK KTDNNNYKYM KEPFFCSSYD TIGAYRRKGI NLDSPLWLRW RLDRRVITSR EIPVEIQYEC LGTYYEIYGH YLIVRSIIKK EIIFLYTRTT VGHIFLYQKM EEAIQGFSRA CSYGT //