ID   RPOC2_CYAPA             Reviewed;        1265 AA.
AC   P48120;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Cyanophora paradoxa.
OG   Plastid; Cyanelle.
OC   Eukaryota; Glaucocystophyceae; Cyanophoraceae; Cyanophora.
OX   NCBI_TaxID=2762;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Stirewalt V.L., Michalowski C.B., Loeffelhardt W., Bohnert H.J.,
RA   Bryant D.A.;
RT   "Nucleotide sequence of the cyanelle DNA from Cyanophora paradoxa.";
RL   Plant Mol. Biol. Rep. 13:327-332(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTEX LB 555 / Pringsheim;
RA   Loeffelhardt W., Stirewalt V.L., Michalowski C.B., Annarella M.,
RA   Farley J.Y., Schluchter W.M., Chung S., Newmann-Spallart C., Steiner J.M.,
RA   Jakowitsch J., Bohnert H.J., Bryant D.A.;
RT   "The complete sequence of the cyanelle genome of Cyanophora paradoxa: the
RT   genetic complexity of a primitive plastid.";
RL   (In) Schenk H.E.A., Herrmann R., Jeon K.W., Mueller N.E., Schwemmler W.
RL   (eds.);
RL   Eukaryotism and symbiosis, pp.40-48, Springer-Verlag, Heidelberg (1997).
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, cyanelle.
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; U30821; AAA81259.1; -; Genomic_DNA.
DR   PIR; T06916; T06916.
DR   RefSeq; NP_043228.1; NC_001675.1.
DR   AlphaFoldDB; P48120; -.
DR   GeneID; 801650; -.
DR   GO; GO:0009842; C:cyanelle; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; 3.
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   Cyanelle; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..1265
FT                   /note="DNA-directed RNA polymerase subunit beta''"
FT                   /id="PRO_0000067922"
FT   BINDING         223
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT   BINDING         297
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"
FT   BINDING         307
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ   SEQUENCE   1265 AA;  142137 MW;  D28D4A926A7CA911 CRC64;
     MSENLFSKKK IFFNQTIGKK EVKNVIAWAF TSYGAARTAY LVEQLKDLGF HYATKAGISL
     SVEDLLIPPL KDSLLQTAEN EIKATLNRYL LGEITEVERF QKVIDIWHRT SETLKDEVVD
     YFKSTDPLNS LYMMSFSGAR GNLSQVHQLV GMRGLMADPQ GEIIDFPIRS NFKEGLTTTE
     YLISSYGARK GVVDTALRTA DSGYLTRRLV DIAQEVIIRE IDCETPRGVI LTALKENGKI
     LISLKDRLVG RVLLHNLYHP KTHSLIAQKN ESISVLLADD IIKAGLKEVW IRSPLTCKAT
     RSVCQYCYGW NLAHGRLVEL GEAVGIIAAQ SIGEPGTQLT MRTFHTGGVF TAEVAKQITA
     PFPGRIYYPL NTTFREIRTR YGDNAWWVEN NAKLRLEGEN GKRVSFNLTQ GSIIRIKDQS
     WVETNDLLAE IASTAPNTRR AKEKTTRELR TDIAGEVYFQ NLEIDEAGGQ VDTAGGSIWI
     LGGNVYNLSS NFDVILKNGD FILNGSILAR TQFISQYGGY VRLTDDNLTV EVIPASLKIQ
     NAKIFIDETD QPCLHFKNNE TFELKIQNET QLKHGQVVAE RYLTTEMGGI IRYADLDAKT
     TNKNGYEITK SGSLLWIPEE THEVNTEAKN VLVKNGQYIP SGTQLIKNKK IRNKHSGVVE
     LVHKKNFVIE IIIKPGIVLK IKNNVSFSKK AKRFIQPGEY LFSKFVVEDL RYLDYIITST
     GIILLLRPVV EYKVESPKTI IRDDKNHLKI SSIQSILYKD GERIKSVQGI ELFKIQLKLQ
     VRKGLKHLPI KTNFIPSSQN SFELEFLIIE SILPKNDKYF DSTVLESLAK AQTKILVKNN
     QLVKKGELIA QIEIISINQG EIRWIGDNTA KQIRRLLLIT EKQIVTIPIQ NLTKLKNKNL
     NLGNFIRAGE EIEETIKIPN SGQIIEITST YIRLRISRPY LISARAIIRV LTGDLVQSGE
     SLALLVFERA KTGDIIQGLP RIEELLEARK PKDNCVLSTH PGFTQLYYSE TIELKIKSLD
     KINTLLELQP GVFPTVTNNQ FIEAGAPLSE GDISVHEILE IFFNLYFKNR VNCLSLADAI
     HLSLQKIQQF LVSEVQSVYQ SQGIDISDKH IEIIIKQMTN KVKIEEGGDT TLLPNELIEF
     QQIEKMNEKF STSNGQLASY TPILLGITKS SLNTQSFISA ASFQETTRVL AKAAVEGKID
     QLRGLKENVI IGNLIPAGTG FSAYNDNAVF QNEDIESIEV KTSVLNSPAE SDTNSDLDDI
     ILNKD