ID A0A9E9ER39_9LAMI Unreviewed; 680 AA. AC A0A9E9ER39; DT 03-MAY-2023, integrated into UniProtKB/TrEMBL. DT 03-MAY-2023, sequence version 1. DT 28-JUN-2023, entry version 2. 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:WAN81454.1}; OS Buddleja sp. GJ53. OG Plastid; Chloroplast {ECO:0000313|EMBL:WAN81454.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Scrophulariaceae; Buddlejeae; Buddleja. OX NCBI_TaxID=2965491 {ECO:0000313|EMBL:WAN81454.1}; RN [1] {ECO:0000313|EMBL:WAN81454.1} RP NUCLEOTIDE SEQUENCE. RA Yang F.; RL Submitted (JUL-2022) 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 {ECO:0000256|HAMAP-Rule:MF_01323, ECO:0000256|RuleBase:RU004279}. 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: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|HAMAP-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; OP007343; WAN81454.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW. 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:SF60; 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:WAN81454.1}; 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:WAN81454.1}; 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 262..543 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 489 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 491 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" 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" SQ SEQUENCE 680 AA; 78413 MW; D9EABCE743163358 CRC64; MIDRYKHQQL RIGLVSPEQI SAWATKILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI FGPIKSGICA CGNYRVIGDE KEDPKFCEQC GVEFVDSRIR RYQMGYIKLA CPVTHVWYLK RLPSYIANLL DKPLKELEGL VYCDFSFARP ITKKPTFLRL RGLFEYEIQS WKYSIPLFFT TQGFDTFRNR EISTGAGAIR EQLADLDLRI ILDNSLVEWK ELGEEGPTGN EWEDRKVGRR KDFLVRRMEL AKHFLRTNIE PEWMVLCLLP VLPPELRPII QIDGGKLMSS DINELYRRVI YRNNTLTDLL TTSRSTPGEL VMCQEKLVQE AVDTLLDNGI RGQPMRDGHN KVYKSFSDVI EGKEGRFRET LLGKRVDYSG RSVIVVGPSL SLHRCGLPRE IAIELFQTFV IRGLIRQHLA SNIGIAKSKI REKEPIVWEI LQEVMQGHPV LLNRAPTLHK LGIQAFQPIL VEGRAICLHP LVCKGFNADF DGDQMAVHVP LSLEAQAEAR LLMFSHMNLL SPAIGDPISV PTQDMLIGLY VLTSGNRRGI CVNRYNPWNR RNYQNKRSDN NNHKYTKEPF FSNSYDAIGA YRQKRINLDS PLWLRWRLDQ RVIASRETPI EVHYESLGTY YEIYGHYLIV RSIKKEILFI YIRTTVGHIS LYREIEEAIQ GFSQACSYGT //