RPOC2_CUSRE
ID RPOC2_CUSRE Reviewed; 1379 AA.
AC A7M956;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS Cuscuta reflexa (Southern Asian dodder).
OG Plastid.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Convolvulaceae; Cuscuteae; Cuscuta;
OC Cuscuta subgen. Monogynella.
OX NCBI_TaxID=4129;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17714582; DOI=10.1186/1471-2229-7-45;
RA Funk H.T., Berg S., Krupinska K., Maier U.-G., Krause K.;
RT "Complete DNA sequences of the plastid genomes of two parasitic flowering
RT plant species, Cuscuta reflexa and Cuscuta gronovii.";
RL BMC Plant Biol. 7:45-45(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- CAUTION: Young tissue from this organism is photosynthetic and contains
CC some thylakoids, although the photosynthetic activity does not exceed
CC the light compensation point. {ECO:0000305}.
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DR EMBL; AM711640; CAM98384.1; -; Genomic_DNA.
DR RefSeq; YP_001430098.1; NC_009766.1.
DR AlphaFoldDB; A7M956; -.
DR PRIDE; A7M956; -.
DR GeneID; 5536697; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009536; C:plastid; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; IPR045867; DNA-dir_RpoC_beta_prime.
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 PANTHER; PTHR19376; PTHR19376; 1.
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 DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1379
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353557"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1379 AA; 155934 MW; A0BF91E6C05CCB89 CRC64;
MAERINLVFH NKVLDGTAMK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID
DLLTIPSKGW LVQDAEQQSF VFEKYQHSGN VHAVEKLRQS IEIWYATSEY LRQEMHLNFR
MTDPLNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRADC GTARGISVSP HNGMMPERIF
IQTLIGRVLA DDIYIGPRCI ATRNQNIGVG LVNKLLNFRA QPISIRTPFT CRSTSWICRL
CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRAPSNGKI
RFTEDLVHPT RTRHGYPAFF CSIYLYVTIQ SQDILHHVKI PPKSFILVQN DQYVESEQVI
AETRAGASTL NYKEKIRKHI YSDSGGEMHW STNVYHAPEF TYGNVHLLSK TSHLWILLGE
PCHSSLVSTS IHRDQDQMSA QSLSVKRRYT SKLSETNDEA KQKIASEDLI ADYSDVNPSR
CTDHYNLVYP AILPILDENS YFFSNCLSKR RRNQFIIPLQ SIQEHKNQLM PCSSISMKIP
PNANGIFCAN SILAYFDDPR YRRNNSGSTK YGTLEMYSTI KKEDFIQYRG VNEFRLKSKV
ERFFFIPEEV HILPGSSSIM VRNQSLIGVD TQITLNLRSR VGGLVWVERK KNRIELKIFF
GDIYFPGGAD NLSRHSGVLI PPGTEIKTNY KESKKVKNWI YVQRITLSKK KFFFLVRPLV
TYEIMDGIPL ATLFPPDLLQ QRENAQLRVV NYILHGNGKP IRGNYDASIQ LVRTCLVFKR
NQDKKSSYSE AARASVVEIR TNYLIRHFLR IDFVKAPISY IGKRYDPLGL GLLAEDWTHK
NPYSKARIHQ NLNQNKGTIH TFFNRNKGSQ SLIILSSSNC SRMDPANGAK SNNVIQESKK
EEYPMLQISN SLGPLGTYPP IANCDSFNRL LTHNQILVTN YFHLDNVKPP FQVFKFKYYF
IAENLKICNY NPCSNLRLNA FYLNLNFLHP NSCAETSKIM SLGQFICQNV CIDKTRPPFK
SGQVIFIQVD SVVIRLAKPY LATPGATVHG LYGETFFGGD TVVTFNYEKS RSGDITQGLP
KVEQVLEVRS VDSISMNLEG RVEGWGKCIT GILGIPWGFL IGAELTIVQS RISLVNKIQK
VYRFQGVHIH NRHIEIIVRQ ITSKVLVSED GMSNVFLPGE LIGLLRAERM GRALEEPIHY
RSVFLGITKA SLNTQSFISE ASFQETARVL SKAALGGRID WLKGLKENVV LGGVIPAGTG
FRGLVDPSKQ YNKNNIPLKN NLFEGGMTDL LVHHRKLFDS FLNTLIYHHH RIDRFYNDS