ID RPOC2_POPAL Reviewed; 1390 AA.
AC Q14FG7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 56.
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 Populus alba (White poplar).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX NCBI_TaxID=43335;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Okumura S., Yamashita A., Kanamoto H., Hattori M., Takase H., Tomizawa K.;
RT "Complete structure of the chloroplast genome of Populus alba.";
RL Submitted (MAR-2005) 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: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; AP008956; BAE97195.1; -; Genomic_DNA.
DR RefSeq; YP_665548.1; NC_008235.1.
DR AlphaFoldDB; Q14FG7; -.
DR SMR; Q14FG7; -.
DR GeneID; 4178256; -.
DR KEGG; palz:4178256; -.
DR OrthoDB; 806648at2759; -.
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..1390
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277199"
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 1390 AA; 158141 MW; CF27A94D3114D0A6 CRC64;
MAERANLFFH NKVIDGTAIK RIISRFIDHF GMAYTSHILD QVKTLGFHQA TATSISLGID
DLLTIPSKGW LVQDAEQQSL ILEKHHHYGN VHAIEKLRQS IEIWYATSEY LRQEMNPNFR
MTEPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTTRGISVSS RNGMIPERIF
IQTLIGRVLA DNIYMGLRCI ATRNQDIGIG LVNRFITFRT QPISIRTPFT CRSTSWICRL
CYGRSPTHGD LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE HVRAPSNGKI
KFNKGLVHPT RTRHGHPAFL CSMDLYVTIE SQDIIHNVTI PPKSFLLVQN DQYVESEQVI
AEIRSGTYTL NFTERVRKHI YSDSEGEMHW STDVYHASEF TYSNVHLLPK TSHLWILSGG
SCRSSIVPFS LHKDQDQINV HSLSVERGYI SNPSENNDKV KHKFFSSYLS SKSKKKSRIL
DYSDLNRIIC TGFIYPTILH ENSDLLAKRR KNRFIIPFQS IQEKELMSHS DILIEIPING
IFRRNSIFAY FDDPQYRRKS SGITKYVAIG VHSIVKKEDL VEYRGVKEFQ PKYQMKVDRF
FFIPEEVYIL PESSSLMVRN NSIIGVDTQI TLNTKSRVGG LIRIERKKKK MELKIFSGDI
HFPRATDKIS RYSGILIPPG TVKTNSKESK KVKNWIYVQR ITPTKKKSFV LVRPVLIYER
GDGINLERLF PPDLLQEKEN LKLRIVNYIL YGNGKPIQGI SNTSIQLVRT CLVLNWNQDK
KSSSIEEARV YFVEVSINGL IRDFLRIHLG KSRISYISRK RNDPSGLGLI SDNGPDRTNI
NPFYSIYSKT RIPQSLKQNQ GTISISTLLN RNMECQSLII LSSSNCFRMD PSNGVKSYNV
IKESTKRDPI IPIRNLLGPL GTTLQIANFY SFYHLLTHNQ ISVIKYLKLD NLKLKQTSKV
LKYYLMDENG RIVNHDPYSN NVLNPFKLNW YFLHHNYHHN YCEETFTIIN LGQFICENVC
MTKNGPRLKS GQVLIVHADS VILRLAKPYL ATPGATVHGH YGEILYEGDT LVTFIYEKSR
SGDITQGLPK VEQVLEVRSI DSISINLEKR VENWNECITR IVGIPWGFLI GAELTIVQSR
ISLVNKIQKV YRSQGVQIHN RHIEIIVRQI TSKVLVSEDG MSNVFSPGEL IGLLRAERAM
RALEEAICYR TVFLGITRAS LSTQSFISEA SFQETARVLA KAALRGRIDW LKGLKENVVL
GGMIPVGTGF KGLAHRSSQH KIIPFKIKKK NLFAGEMRDI LFHHRELFDS CISKNFYNIS
EQSFIGFNDS
//
