RPOC2_MANES
ID RPOC2_MANES Reviewed; 1393 AA.
AC B1NWE0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 52.
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 Manihot esculenta (Cassava) (Jatropha manihot).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Manihoteae;
OC Manihot.
OX NCBI_TaxID=3983;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. TME3;
RX PubMed=18214421; DOI=10.1007/s00122-007-0706-y;
RA Daniell H., Wurdack K.J., Kanagaraj A., Lee S.-B., Saski C., Jansen R.K.;
RT "The complete nucleotide sequence of the cassava (Manihot esculenta)
RT chloroplast genome and the evolution of atpF in Malpighiales: RNA editing
RT and multiple losses of a group II intron.";
RL Theor. Appl. Genet. 116:723-737(2008).
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; EU117376; ABV66144.1; -; Genomic_DNA.
DR RefSeq; YP_001718427.1; NC_010433.1.
DR AlphaFoldDB; B1NWE0; -.
DR GeneID; 5999961; -.
DR KEGG; mesc:5999961; -.
DR OrthoDB; 731145at2759; -.
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..1393
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353570"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1393 AA; 158018 MW; E620F1E5F0ADC791 CRC64;
MEVLMAERAN LVFHNKAIDG TAIKRLISRL IDHFGMAYTS HILDQVKTLG FQQATATSIS
LGIDDLLTIP SKGWLVQDAE QQSLILEKHY HYGNVHAVEK LRQSIEIWYA TSEYLRQEMN
LNFRMTEPFN PVHIMSFSGA RGNTSQVHQL VGMRGLMSDP QGQMIDLPIQ SNLREGLSLT
EYIISCYGAR KGVVDTAVRT SDAGYLTRRL VEVVQHIVVR RTDCGTARGI SVSPRNGMMP
ERIFIQTFIG RVLADNIYMG LRCIAIRNQD IGIGLANRFI TFRTQTISIR TPFTCRSTSW
ICRLCYGRSP THGDLVELGE AVGIIAGQSI GEPGTQLTLR TFHTGGVFTG GTAEHVRAPS
NGKIKFNEDL VHPIRTRHGH PAFLCYIDLY VTIKSQDIIH NVTIPPKSFL LVQNDQYVES
EQVIAEIRAG AYTLNFKEKV RKHIYSDSEG EMHWSTDVYH APEFTYSNVH LLPKTSHLWI
LSGSSCRSSI VPFSLHKDQD QMNVHSLSVK RRYISSPSVN NDQVKHKFFS SDFSGKKESG
IPDYSELNRS ICTGHCNLIY STILYKNSDL LAKRRRNKFI IPFQSIQERE KELMTQSAIS
IEIPINGIFR RNSVFAYFDD PQYRKKSSGI TKYGAIGVHS IVKKEDLIEY RGVKEFKPKY
QTKVDRFFFI PEEVYILPES SSLMVRNNSI IGVDTQIALN TRSRVGGLVR VERKKKKMEL
KIFSGDIHFP GETDKISRHS DILIPPGTVK TNSKESKKVK NWIYIQRITP TKKKYFVLVR
PVIIYEIANG INLETLFPQD LLQEKDNLKL RVVNYILYGT GKPIRGISDT SIQLVRTCLV
LNWDQDKKSS SIEEARAAFV EISTNGLIRD FLRINLVKFH ISYIGRKRND PSGSEPISNN
GSDRTNINPF YPIYSKTRVQ QSLKQNQGTI STLLNINKEC QSLIILSSSN CFQMDPFNDV
KHHNVIKESI KRDPIIPIRN SLGPLGTALQ IANFYLFYHL NLITHNQISV TKYSKLYNLK
QTFQVLKYYL MDENGRIVNP DPCSNSVLNP FNLNWYFLHH NYCESFFTII SLGQFICENL
CMAKNGPHLK SGQVIIVHID SVVIRSAKPY LATPGATVHG HYGEILYEGN TLVTFIYEKS
RSGDITQGLP KVEQVLEVRS IDSISINLEK RVEGWNECIT RILGIPWGFL IGTELTIVQS
RISLVNKIQK VYRSQGVQIH NRHIEIIVRQ ITSKVLVSED GMSNVFSPGE LIGLLRAERT
GRALEEAICY GAILLGITRA SLNTQSFISE ASFQETTRVL AKAALRGRID WLKGLKENVV
LGGMIPVGTG FKGLVQGSRQ HKNIPLKTKK KNLFEGEFRD RDILFHHREL FDSCISKNLY
DTSEQSFIGF NDS