ID A0A5J6CIW1_9MAGN Unreviewed; 1378 AA. AC A0A5J6CIW1; DT 11-DEC-2019, integrated into UniProtKB/TrEMBL. DT 11-DEC-2019, sequence version 1. DT 07-APR-2021, entry version 5. DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324}; DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324}; DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324, GN ECO:0000313|EMBL:QEQ14900.1}; OS Epimedium mikinorii. OG Plastid; Chloroplast {ECO:0000313|EMBL:QEQ14900.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Ranunculales; Berberidaceae; Berberidoideae; OC Epimedium. OX NCBI_TaxID=402160 {ECO:0000313|EMBL:QEQ14900.1}; RN [1] {ECO:0000313|EMBL:QEQ14900.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=31426439; RA Guo M., Ren L., Xu Y., Liao B., Song J., Li Y., Mantri N., Guo B., Chen S., RA Pang X.; RT "Development of Plastid Genomic Resources for Discrimination and RT Classification of Epimedium wushanense (Berberidaceae)."; RL Int. J. Mol. Sci. 20:0-E4003(2019). RN [2] {ECO:0000313|EMBL:QEQ13942.1} RP NUCLEOTIDE SEQUENCE. RA Ren L., Guo M., Pang X.; RT "The complete chloroplast genome sequences of Epimedium."; RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:QOI13935.1} RP NUCLEOTIDE SEQUENCE. RA Wen C.C., Liu X.X., Yao Y.Y., Luo Y.Y., Liu T.T., Yang Q.Q., Shen G.G., RA Guo B.B., Ge F.F.; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|EMBL:QOI13935.1} RP NUCLEOTIDE SEQUENCE. RA Wen C., Liu X., Yao Y., Luo Y., Liu T., Yang Q., Guo B., Xu C., Suo F., RA Shen G., Ge F.; RT "The complete chloroplast genome of Epimedium mikinorii Stearn. RT (Berberidaceae)."; RL Mitochondrial DNA B Resour 5:806-807(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_01324}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:83400; CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00000097, CC ECO:0000256|HAMAP-Rule:MF_01324}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324}; CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01324}; 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_01324}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01324}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}. 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; MK408752; QEQ13942.1; -; Genomic_DNA. DR EMBL; MK992918; QEQ14900.1; -; Genomic_DNA. DR EMBL; MN857416; QOI13935.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.274.100; -; 1. DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1. DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp. DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR038120; Rpb1_funnel_sf. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 2. DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QEQ14900.1}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01324}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01324}; Plastid {ECO:0000313|EMBL:QEQ14900.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}. FT DOMAIN 95..157 FT /note="RNA_pol_Rpb1_4" FT /evidence="ECO:0000259|Pfam:PF05000" FT DOMAIN 172..358 FT /note="RNA_pol_Rpb1_5" FT /evidence="ECO:0000259|Pfam:PF04998" FT DOMAIN 1186..1274 FT /note="RNA_pol_Rpb1_5" FT /evidence="ECO:0000259|Pfam:PF04998" FT METAL 220 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT METAL 291 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT METAL 298 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT METAL 301 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" SQ SEQUENCE 1378 AA; 155757 MW; 334DA73A55024FFE CRC64; MAERADLVFH NQKMDGTAMK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID DLLTIPSKGW LVQDAEQQSF LLEKHHQYGS VHAVEKLRQS IEIWYSTSEY LRQEMNLNFR MTDPSNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII SCYGARKGVV DTAVRTADAG YLTRRLVEVV QHIVVRRTDC GTLRGISLSP RNGMIRERFF IQTLIGRVLA DDVYIGSRCI AIRNQDIGRG LVNRFIACGA QPISIRTPFT CKSTSWICRL CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE YVRAPSNGKI KFNQDLLHPT RTCHGHPAFL CYIALYVTIE DQDILHNVTI PPKSFLLVQN DQYVESEQVI AEIRAGTSTL NLKDRVRKHI YSDSEGEMHW STAVYHAPDY TYGNVHLLPK TSHLWIVSGV PYRSSMLSVS LHKDQDQMNV HSLSAEGKSI SNSNLLVPND QARYNTFLSS EPFGKHGERI LDYLGPGRII PNGPCNLTYT AILHGNSDFF FLSKRRRNRF IIPFQYNQGQ EKELITPSGL SIEIPINGIF HRNSILAYFD DPRYRRKSSG ITKYGTIEAR SSVKKEDLIE YRRMPKYQTK IDQIFCIPEE VHILPGSSSV MVRNNSIIGV DTEITFKTRS RVGGLVQVEK KTKKIELKIF SGDIYFPGET DKISWQSGIL IPPGREKKNS KESKKVKNWS YVERIAPAKK RYFVLVRPVV RYEIADGINF ATLFPQDPLQ ERDNVQLRVV NYILCGNGKP IRGISHTNIQ LVRTCLVLNW CQEKKGSSME EIHASFVEIR VNDLIQDFIR MDLVKSPISY TRKRNAPAES ELILVNGADR TNPFYSKARI QQLLTQQQGT IRTLLNRNKE CKSLIILSSS NCFRIGPFDD FKYKNLTKKS NTNKGDSVLP IRNSFGPLGV VPKIANFYSF YYLITHNQIL INKYLLLDNL KADFQILQYF LMDENGRIYN PDPCSNRIWN PFNSNWYCLH HDYCDERSTI ISLGQFFCEN LSISQYGTPL KSGQVLIIHV DFLVIRSAKP YLAIPGATVH GHYGEIMYGG DPLLTFLYEK SRSSDITQGL PKVEQVLEAR SVDSISMNLE KRVEGWNESI TRILGIPWGF LIGAELTISQ SRISLVNKIQ RVYRSQGVQI HNRHIEIIVR QITSKVLVSE EGMSNVFSPG ELIGLLRAER TGRALEEAAC YRAVFLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV VLGGMIPVGT GFKGLVHPSS QHGDISLETK TKNLFEGGMR DILFYHKDFF SSCIPIPKNF HEIDISEQ //