ID RPOC2_RANMC Reviewed; 1383 AA.
AC A1XGM8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 55.
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 Ranunculus macranthus (Large buttercup).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae;
OC Ranunculeae; Ranunculus.
OX NCBI_TaxID=334596;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17573971; DOI=10.1186/1471-2164-8-174;
RA Raubeson L.A., Peery R., Chumley T.W., Dziubek C., Fourcade H.M.,
RA Boore J.L., Jansen R.K.;
RT "Comparative chloroplast genomics: analyses including new sequences from
RT the angiosperms Nuphar advena and Ranunculus macranthus.";
RL BMC Genomics 8:174-174(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, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; DQ359689; ABC70746.1; -; Genomic_DNA.
DR RefSeq; YP_001004176.1; NC_008796.1.
DR AlphaFoldDB; A1XGM8; -.
DR SMR; A1XGM8; -.
DR GeneID; 4712081; -.
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; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR PANTHER; PTHR48355: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; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1383
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353583"
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 1383 AA; 156581 MW; 7CDA9824B9859EF0 CRC64;
MAERADLVFH NKAIDGTAMK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TTTSISLGID
DLLTIPSKGW LVQDAEQQSL ILEKHHNYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR
MTDPSNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTTRGISVSP RNGMITERIF
IQTLIGRVLA DDLYMGSRCI AIRNQDIGVG LVNRFITFRS QPISIRTPFT CRSTSWICRL
CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRAPDNGKI
KFNEGLVYPT RTRHGYPAFL CYIDLSVTIE GPDILHNVNI PPKSFILVKN DQYVESEQVI
AEIRAEASTL NFKERVRKHI YSDSEGEMHW STAVYHAPEY TYGNVHLLPK TSHLWILSGV
PQRSSIVPFS LHKDQDQINI HSLSAKQKFI SNLSLSMTND QVIKKLFRSD SSVKKGGWVL
DYSGPAEVLC NGHCNLIYSA ILDENSDLLA KRRRNRFTIP LQSNQEKEQK PRSGISIEIP
INGLFRINSI LAYFEDPRYR RKSSGITKYG TIEVDSIVKK EDLIEYRRTK EFRPKYQMKI
DRFFFIPEEV HILPGSSSIM IRNNSIIGVD TRITFNIRSQ VGGLVRVEKK KKKIELKIFS
GNIYFPGETD PISWHSGILI PPGAGKKNSK ESKKLKNGIY VQRITPTKKK YFVLVRPVVT
YERADGINLA ALFPQDPLQE RDNVQLRVVN YILYGNGKPI RRISHTNIQL VRTCLVLNWD
QDKKGSSIEE VRASFVEIKI NALIRDFIKM DLVKYPISYT RKRNDPVGSG LIPVNGSDHT
NLNPFYSKAS IKQSLIRHQG TIRTLLNKNK ECQSLITLSS SNCSRIDPFN RLKYHNNMIK
KSNKRDILPP IRNLLGPLGI IPKITNFFSF YYLITHNQIL VKKNSQLDNL KRTSPVLKYY
LIDENGRIFN PDPSINMILN PFNWNWYFIH HDYCEETSTI INLGQFFCEN VCISKSGPHL
KSGQVLIVDV DSLVIRSAKP YLATPGATVH GHYGEILYEG DTLVTFIYEK SRSGDITQGL
PKVEQVLEVR SIDSISMNLE NRVEGWNERI TRTLGIPWGF LIGAELTIAQ SRISLVNKIQ
KVYRSQGVQI HNRHIEIIVR QITSKVLVSE DGMSNVFSPG ELIGLLRAER TGRALEEAIC
YRAVLLGITR ASLNTQSFIS EASFQETARV LAKAALRGRI DWLKGLKENV VLGGMIPVGT
GFKGLVHRLS NISLEIEKKN LFKGGMRDIL FHHKELFDSC IPRNFPDTSE QLFTKQSFTR
FTD
//
