RPOC2_CALFG
ID RPOC2_CALFG Reviewed; 1377 AA.
AC Q7YJY0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 73.
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 Calycanthus floridus var. glaucus (Eastern sweetshrub) (Calycanthus
OS fertilis var. ferax).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Calycanthaceae;
OC Calycanthus.
OX NCBI_TaxID=212734;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Goremykin V., Hirsch-Ernst K.I., Woelfl S., Hellwig F.H.;
RT "The chloroplast genome of the 'basal' angiosperm Calycanthus fertilis
RT -- structural and phylogenetic analyses.";
RL Plant Syst. Evol. 242:119-135(2003).
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; AJ428413; CAD28711.1; -; Genomic_DNA.
DR RefSeq; NP_862744.2; NC_004993.1.
DR AlphaFoldDB; Q7YJY0; -.
DR GeneID; 2598034; -.
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: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; 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 Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1377
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067917"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 294
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"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1377 AA; 156094 MW; 1ECD65E171FFC56A CRC64;
MEVLMAERAD LVFHNKVIDG AAMKRLISRL IDHFGMAYTS HILDQVKTLG FQQATTTSIS
LGIDDLLTIP SKGWLVQDAE QQSLILEKHH HYGNVHAVEK LRQSIEIWYA TSEYLRQEMH
PNFRMTDPSN PVHIMSFSGA RGNASQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTIRGI SVSPRNGMTE
RIWIQTLIGR VLAYDIYMGP RCIAARNQDI GIGLVNRFIT FRAQPIYIRT PFLCRSTSWI
CRLCYGRSPA HGDLVELGEA VGIIAGQSIG EPGTQLTLRT FHTGGVFTGG TAEHVRAPFN
GKIQFNEDLV HPTRTRHGHP AFLCYTDLYV TIESHDILHN VNIPQKSFLL VQNDQYVESE
QVIAEIRAGT STFNLKVKEK VRKHIYSDSE GEMHWSTDVY HAPEYTYGNV HLLPKTSHLW
ILSGGLCRSS IVPFSLHKDQ DQMNVHSLSV EQRYISDLSV TNVRVRHKLF SSDSSGKKGG
RAPDYSGPDR IISNGHWNFI YPAILHENSD LLAKRRRNRF IIPFQSDQER EKELMPRSGI
SIEIPINGIL RRNSILAYFD DPRYRRSSSG ITKYGTIGVD SIVKKEDLIE YRRAKEFRPK
YQMKVDRFFF IPEEVHILPA SSPVMVRNNS IIGVNTRIAL NTRSRVGGLV RVERKKKRIE
LKIFSGDIHF PGETDKISRH SGILIPPGTG KKNVKESKKW KNWIYVQRIT PTKKKYFVLV
RPVVTYEIAD GINLETLFPQ DPLQERDNVQ LRVVNYILYG NGKPIRGISH TSLQLVRTCL
VLNWDQDRNG SIEEVHASFV EVRANGLIRD FLKIDLVKSP ILYSGKRNDT TSSGFIPNNG
SDRTNINPFY FKARIQSLTQ HQGTIRTLLN RNKECQSFLI LSSSDCSRIG SFNGSKSHKV
TKESITIKED PTIPIRNSLG PLGTVPKIAN FDSSYYLITH NQILLNKYLS LDNLKQTFQV
LKYYLMDENG RIYNPDPRSN IIFNPFDLNW CFLPHDYCEE TSTIINPGQF ICENVCISKY
GPHIKSGQIL IVRVDSLVIR SAKPHLATPG ATVHGHCGEI LYEGDTLVTF IYEKSRSGDI
TQGLPKVEQV LEARSIDSIS MNLEKRVEGW NERITKILGI PWGFLIGAEL TIAQSRISLV
NKIQKVYRSQ GVQIHNRHIE IIVRQITSRV LVSEDGMSNV FSPGELIGLL RAERTGRALE
EAICYRAILL GITRASLNTQ SFISEASFQE TARVLAKAAL RGRIDWLKGL KENVVLGGMM
PVGTGFKGLV RRSRQHNNIP LEIKKKNLFE GEMRDILFHH RELFDSCIPN NFPDTLE
