ID A0A089X8G0_CERBC Unreviewed; 744 AA. AC A0A089X8G0; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 27-MAR-2024, entry version 36. 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:AIR75954.1}; OS Cerataulina bicornis (Diatom) (Cerataulina daemon). OG Plastid; Chloroplast {ECO:0000313|EMBL:AIR75954.1}. OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae; OC Biddulphiophycidae; Hemiaulales; Hemiaulaceae; Cerataulina. OX NCBI_TaxID=1527800 {ECO:0000313|EMBL:AIR75954.1}; RN [1] {ECO:0000313|EMBL:AIR75954.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25233465; RA Sabir J.S., Yu M., Ashworth M.P., Baeshen N.A., Baeshen M.N., Bahieldin A., RA Theriot E.C., Jansen R.K.; RT "Conserved gene order and expanded inverted repeats characterize plastid RT genomes of Thalassiosirales."; RL PLoS ONE 9:E107854-E107854(2014). RN [2] {ECO:0000313|EMBL:AIR75954.1} RP NUCLEOTIDE SEQUENCE. RA Sabir J.S.M., Yu M., Ashworth M.P., Baeshen N.A., Baeshen M.N., RA Bahieldin A., Theriot E.C., Jansen R.K.; RL Submitted (JUN-2014) 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|HAMAP-Rule:MF_01323, CC 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; KJ958484; AIR75954.1; -; Genomic_DNA. DR RefSeq; YP_009093281.1; NC_025313.1. DR AlphaFoldDB; A0A089X8G0; -. DR GeneID; 20834008; -. 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 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; IPR007066; RNA_pol_Rpb1_3. 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; 2. DR Pfam; PF04983; RNA_pol_Rpb1_3; 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:AIR75954.1}; 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:AIR75954.1}; 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 362..641 FT /note="RNA polymerase N-terminal" FT /evidence="ECO:0000259|SMART:SM00663" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 72 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 85 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 587 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 589 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 591 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" SQ SEQUENCE 744 AA; 87159 MW; 0C67BFBE64B90F16 CRC64; MIRSEKEFDY IKIKLASPVR ILQWSHRRLP NGQFIGEVQK SETINYRTFK PEMDGLFCER IFGPSKSLEC ACGKYKRVRY EGLICERCGV ELTESRVRRH RMGHINLIYP VTHVWYINSR PNYMALLLEV EQCEKRLDTG LLYDYPTFFE LLQWQLGFEF DIEIKSILAQ IRKNPDQLEN FEQSLKTYYE QFYQLNRKKF AIRSGKVNLR DGRIKRIKLA SLAYFIAEDE ISFYGLHWDL QQYRRSREYG FTGYPLKPYP KPKLQNRRRN TPKYLLRTTP NYLIGAVLIK RELEKLNLER EIWKTRRFIT ICSKVLHKEK PTYNSSRWFR KWEHQRIYKL RDQSIKRIRI LENLLATGSN PAWMIITILP VIPPALRPMI QLEGGRFATS DLNELYRRII TRNNRLLRLL EIDAPQLIIR NEKRMLQEAV DTLIDNGKRG KIALSANNRP LKSLSDIIKG KHGRFRQNLL GKRVDYSGRS VIVVGPSLKL NQCGLPYEMA IELFQPFIIR ELINQGLASN MKVAKNLIQQ SEPIIDPVLE KVLANHPIFL NRAPTLHRLG IQAFEPILVQ GRAIKLHPLV CSAFNADFDG DQMAVHVPLS LESQAECYML MLAPYNFLSP ANGEPIIMPS QDMVLGCYYL TVNNINGLLG SNHYFANLED VVLGYNQDQI ELHTSIWVRY NETVDESKSL RKKVILKDNS YIEYYDNLQV RKDANNNVIV QYIQTTTGRV IFNYTIQKIL KLIR //