RPOC2_CHAVU
ID RPOC2_CHAVU Reviewed; 1412 AA.
AC Q1ACN4;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 49.
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 Chara vulgaris (Common stonewort).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Charophyceae; Charales; Characeae;
OC Chara.
OX NCBI_TaxID=55564;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16611644; DOI=10.1093/molbev/msk018;
RA Turmel M., Otis C., Lemieux C.;
RT "The chloroplast genome sequence of Chara vulgaris sheds new light into the
RT closest green algal relatives of land plants.";
RL Mol. Biol. Evol. 23:1324-1338(2006).
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; DQ229107; ABA61978.1; -; Genomic_DNA.
DR RefSeq; YP_635713.1; NC_008097.1.
DR AlphaFoldDB; Q1ACN4; -.
DR SMR; Q1ACN4; -.
DR GeneID; 4100201; -.
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..1412
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000277185"
FT BINDING 220
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 1412 AA; 162967 MW; 7AE51DA5FF9EB6DE CRC64;
MRQFKEIPFY NQIVDKGTIK QLIGRLVAHF GSTYTSHILD KLKELGFEYG TKTGISLGID
DLLITPSKKW LIQDAEQQAQ ASDSHYNSGN LHAVEKLRQL IETWHTTSEY LKQEMNPNFR
ITDPFNPVHM MAFSGARGTT SQVHQLVGMR GLMSDPHGQI IDLPIQSNFR EGLSLAEYII
SCYGARKGVV DTAIRTSDSG YLTRRLVDVA QHIVVRKTDC KTHKCISIQP FLEEWKMNIH
LYVQQKLIGR ILADYVLKDN RCIASRNQDI SFDLAIRLLS FKFQSIWVRS PLTCESTRWI
CQMCYGWSIG YRNLIEVGEA VGIIAAQSIG EPGTQLTLRT FHTGGVFTGD IAQQIRSPLN
GIIQLNNSKI RSIRNRYGQP AFVCLDNIHI KVKGKDTYQS IIPTESLLFV KNNQKVQAKQ
VIAEIRSTIR QSKEEVNKNI NSELAGEVFW SNKYYFKEQN LHDLQKNNFF VKNNHNFRNC
PTSDSQNEND SNRSNHFLTI NSIKYSQEKT NWPISNTGHI WILSGQVYKF HNIQSIFYKQ
QDKVRIKNIL AQKELLVNNG GRYHNFHSQR LSYFQENLMN NSYTHSKKKT KSLSSNFVNN
AICGLTILKE KKGKFSFLKN SSFCKKTRTN LQFILEVKNY SRIKHNDLLA TLHNPAHRTS
TAGMVKYGFL LINSQLDKNL KSYNKNSRKK KISLYQNNQI QPGQSLFWIP EEIHEIYKPF
SFLHVKNGEI IQKGTYISED IQCGTSGLVE INKRNRNHYE ISIQPGSLYF LKDKQIALQK
DQILIAPGEK IDNTNISDEW LYLKYLKTDQ GVSVLFARPA KEYKIDLINH LEHASSLETL
YMKKCFDVRI SHYTPYEDGQ KIRNNAGAQL ISASLVFKLN NQNLAHKAEI SWTRIKFQRK
ISYYLQINLR DKILPYSYSL SELKKLKFNS HFSNKNKQIN NIDEVILGDT IFHTPLLTKN
YGCIRTFSRR RQDNKTSFVL LSSSDQLELP LPIIFFAFIS YKRFFNKKLG LIGNLYTKKT
KLRNSNQNLF LNLFFISWYI IDEYSCNFLF WGAFSQLIKD ARNKYSHNCF PIIIKKAFFS
LGKFLSKIEM KILGNLETEL GQVISLCNKK IILRIGKPYL ATRGAIVHPR NGETIREGDT
LMTLIYERLK AGDIIQGLPK IEQLLEARRE NVVELIVNRY FLDCTNLLTE ELGMLLGSLW
GFQFSAWASM ERSKLDLVFE IQQVYRSQGV YICDKHIEII VRQMTSKIII LGDGMTDGFL
PGELVEIPRA RKTNRAMKSI MFYKPILVGI TRASLNTRSF ISEASFQETT RVLTKAAIKG
RTDWLKGLKE NVILGRLIPA GTGSEEIILQ RLMNLQKIEK LRKGKSKKYT TSKLDSLLFS
KCKSAFLKRH PLNPYCRETF HFILKQQITN SF
