RPOC2_CYACA
ID RPOC2_CYACA Reviewed; 1269 AA.
AC Q9TM34;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
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 Cyanidium caldarium (Red alga).
OG Plastid; Chloroplast.
OC Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae; Cyanidium.
OX NCBI_TaxID=2771;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RK-1;
RX PubMed=11040290; DOI=10.1007/s002390010101;
RA Gloeckner G., Rosenthal A., Valentin K.-U.;
RT "The structure and gene repertoire of an ancient red algal plastid
RT genome.";
RL J. Mol. Evol. 51:382-390(2000).
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; AF022186; AAF13013.1; -; Genomic_DNA.
DR RefSeq; NP_045033.1; NC_001840.1.
DR AlphaFoldDB; Q9TM34; -.
DR SMR; Q9TM34; -.
DR GeneID; 800295; -.
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; IPR007066; RNA_pol_Rpb1_3.
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; 4.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
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..1269
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067921"
FT BINDING 226
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 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1269 AA; 143047 MW; 37AA6642C3EBD564 CRC64;
MVIDKKKVKN RTPYFLNRII EKSELREIIE VVFHKNGIAK ASLIADNLKE IGFGFATKAG
ISISIEDLKI PPNKSRILQI TNQELRKTEI SFKRAEITTI EKSQKSTDTW NNASEALKDE
IIKYYRLTDP LNPVYMMAFS GARGNLSQVK QLVGMRGLMA DPNGQIIELP ILSNFREGLN
VTEYLISSYG ARKGLVDTSL RTADSGYLTR RLVDVAQDII VREIDCKTNN GITFSNIQNN
EKIIIPLYKR LIGRILADDV KNPITPQVNI ASKNTLITGN LIKEFKKNNI QKIKLRSPLT
CQSYRSICQK CYGASLSDGK LVDIGEAIGI IAAQSIGEPG TQLTMRTFHT GGVFTAEFSK
PIKTLFEGVI KYPSNLKFHH VRTRHGDDAI IIEKSATFDI RTTQSERKIT LETGTTLLVK
DNSFIKKNQV IAETSTSGRL ITEKSTKDLI SNSAGEIYFS DITIEERVDR HGNLTKISKQ
HGLIWILSGE VYNFPMGANL VVQNSFEVNK GCLLAKALIK SRHSGISRIR CAANYYAIDI
ILGTVTIRNA NLYKDSKLFN NNYLLKTSNK KNFVVKALVG QKLSHSDIIA ELIDDQYLTN
TGGIVKYVNL KLAKTHKDDS EYTLSGIGYI FFIPQETHQI NKDASILLAN SGDYVNKNTE
IAKGVFCKCS GLLEIIKSNN IIKEIIIKPG VVYPVSNNLS TFTNKIFYPG EKIIDNIVTN
KIVYVEHIKL INKSCILIRP VNQYKVSNTE SLFDFVTKGE NKDLISLKVV NKSFFKDGEV
IKSVKGVSLV NIQLIFYTKP SATAVTTKME FVKDLDKSTN STSEIKLRIT ATETTKIKYK
QQKNIISQIL IKEGQYITKD FPIIETLFLS RHDGRVVIKS NFKQKNNACL IIISPSNKKE
IYINKKEHKL KIGDFIRVGD HLGTNKNFKS PYSGEVLDIN DKLITIRIAE PYLISPGTLI
HVNHGELIRK GDYLALLVFD KIKTGDIIQG LPRIEEILEA RKPRETCHLA KFDGKIYVHY
NDKGESLISL ESQKKEKYVY ILRLNQRVLV QSGTEVTIGE PITDGLINPH EMLEIFFEYF
LTQTSPIQAT KASFEKIRLE LLKEIQQVYQ SQKIEINDKH IEVIIRQMTS KVLIQERGDT
TLFPGELVTI NQIEKINSAI IAVNKKEAKY KPVLLGITKA SLNTDSFISA ASFQETTRIL
TEAAIEGKVD WLKGLKENVI IGRLIPGGTG LISLDNKDSI KMRLALRHKK NFLNKTFKKK
NNKFLNKTY
