ID A0A0N9LME3_BETVV Unreviewed; 1365 AA. AC A0A0N9LME3; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 13-SEP-2023, entry version 31. 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:ALG63279.1}; OS Beta vulgaris subsp. vulgaris (Beet). OG Plastid; Chloroplast {ECO:0000313|EMBL:ALG63279.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Caryophyllales; Chenopodiaceae; Betoideae; Beta. OX NCBI_TaxID=3555 {ECO:0000313|EMBL:ALG63279.1}; RN [1] {ECO:0000313|EMBL:ALG63279.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Leaf {ECO:0000313|EMBL:ALG63279.1}; RX PubMed=26377912; DOI=10.1186/s12859-015-0726-6; RA Stadermann K.B., Weisshaar B., Holtgrawe D.; RT "SMRT sequencing only de novo assembly of the sugar beet (Beta vulgaris) RT chloroplast genome."; RL BMC Bioinformatics 16:295-295(2015). 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: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_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; KR230391; ALG63279.1; -; Genomic_DNA. 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd02655; RNAP_beta'_C; 1. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.150.390; -; 1. DR Gene3D; 1.10.1790.20; -; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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 NCBIfam; TIGR02388; rpoC2_cyan; 1. DR PANTHER; PTHR34995; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR PANTHER; PTHR34995:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 2. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ALG63279.1}; 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:ALG63279.1}; 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 polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF05000" FT DOMAIN 172..364 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF04998" FT DOMAIN 1176..1263 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF04998" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 291 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 298 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 301 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" SQ SEQUENCE 1365 AA; 155236 MW; 8F2AD5DD50B24094 CRC64; MAERANLVFH NKAIDGTAMK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID DLLTIPSKGW LVQDAEQQSL ILEKHHHYGN VHAVEKLRQS IEIWYSTSEY LRQEMNPNFR MTDPYNPVHI MSFSGARGNV SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTIRGISVSP RNGMIPERIW IQTLIGRVLA DDIYIGSRCI ATRNQDIGVG LVNRFITLRA QPISIRTPFT CRSASWICRL CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRAPSNGKI QFNEDLVHPT RTRHGHPAFL CYIDLYVTIE SEDILHNVNI PPKSFLLVQN DQYVESEQVI AEIRAGTSTL NFKERVRKHI YSDAEGEMHW STDVYHAPEF TYGNVHLLPK TSHLWILSGR PYRSSVVPFS LSKDQDQMNT HSLSFDQIYI SNPSVTNDQV KEKLSDSFSK KEDRILNYSE LNRIGHYTLI YSAKNSDLLA KKRRNRFIIP FQSSQEREKE LMSPSGISIE IPINGIFRRN SIFAYYDDPR YRRKSSGITK YGTIEMHSIV KKEDLIEYRG VKEFRPKYQM KVDRFFFIPE EVHILPGSSS IMVRNNSIIG VDTQITLNTR SRVGGVVRVE RKKKKIELKI FSGDIHFPGE TDKISRHSGI LIPPSRTNSK DSKNLKNWIY VQRITPTKKK YFVLVRPVVP YEITDGINLT TLFPQDLLQE RDNVQLRVVN YILYGNGKAT RGISDTSIQL VRTCLVLNWN QDQKSSSMEE ARASFVEVRT NGMIRDFLRI DLVKSAISYI GKRNDPSLEK NEGSDHTNMN PFYSIYSKTK PQESFNKNQG TVRTLLGINK ECPFFIILSS SNCFRIGPFI SKGVKYHKES IKKDPLSPIR NSLGPLGTAL QIANFFSFYH LITHNQILVT NYLQLDNLKQ TFQLLKFQYY LMDENGRIYN PDPCSNIILN PFKLNWYFLH YNFCEETSTK IYLGQFVCEN VCITKNGPHL KSGQVLIVQS DYVVIRSAKP YLATPGATVH GHYGEIIYEG DTLVTFIYEK SRSGDITQGL PKVEQVLEVR SINSISMNLK KRIDGWNERI TRILGIPWGF FIGAELTIAQ SRISLVNKIQ KVYRSQGVQI HNRHIEIIVR QITSKVLVSE DGMSNVFLPG ELIGLFRAER TGRALEEAIC YRATLLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV VLGGMIPVGT GFKGFVHHSS QHKGIPLKTK KKNLFEGEMG DILFYHRELF DSFLSKNFCD RSKQQ //