ID   RPOC1_MARPO             Reviewed;         684 AA.
AC   P06273;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01323};
DE   AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
DE            Short=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01323};
GN   Name=rpoC1 {ECO:0000255|HAMAP-Rule:MF_01323};
OS   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1038/322572a0;
RA   Ohyama K., Fukuzawa H., Kohchi T., Shirai H., Sano T., Sano S., Umesono K.,
RA   Shiki Y., Takeuchi M., Chang Z., Aota S., Inokuchi H., Ozeki H.;
RT   "Chloroplast gene organization deduced from complete sequence of liverwort
RT   Marchantia polymorpha chloroplast DNA.";
RL   Nature 322:572-574(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2974085; DOI=10.1016/0022-2836(88)90002-2;
RA   Umesono K., Inokuchi H., Shiki Y., Takeuchi M., Chang Z., Fukuzawa H.,
RA   Kohchi T., Shirai H., Ohyama K., Ozeki H.;
RT   "Structure and organization of Marchantia polymorpha chloroplast genome.
RT   II. Gene organization of the large single copy region from rps'12 to
RT   atpB.";
RL   J. Mol. Biol. 203:299-331(1988).
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_01323}.
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_01323};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01323};
CC       Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01323};
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_01323}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC       Rule:MF_01323}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X04465; CAA28062.1; -; Genomic_DNA.
DR   PIR; A00697; RNLVC1.
DR   RefSeq; NP_039276.1; NC_001319.1.
DR   AlphaFoldDB; P06273; -.
DR   SMR; P06273; -.
DR   PRIDE; P06273; -.
DR   GeneID; 2702534; -.
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:0000287; F:magnesium ion binding; 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; 1.10.274.100; -; 1.
DR   Gene3D; 4.10.860.120; -; 1.
DR   HAMAP; MF_01323; RNApol_bact_RpoC1; 1.
DR   InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR   InterPro; IPR000722; RNA_pol_asu.
DR   InterPro; IPR006592; RNA_pol_N.
DR   InterPro; IPR007080; RNA_pol_Rpb1_1.
DR   InterPro; IPR007066; RNA_pol_Rpb1_3.
DR   InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR   InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR   InterPro; IPR034678; RNApol_RpoC1.
DR   PANTHER; PTHR19376; PTHR19376; 1.
DR   Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR   Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR   Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR   SMART; SM00663; RPOLA_N; 1.
PE   3: Inferred from homology;
KW   Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT   CHAIN           1..684
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067880"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         489
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         491
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         493
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ   SEQUENCE   684 AA;  78961 MW;  68D53B74958E1EA3 CRC64;
     MTYQKKHQHL RIELASPEQI RNWAERVLPN GEIVGQVTKP YTLHYKTHKP EKDGLFCEKI
     FGPIKSGICA CGKYQGIEKK KENIKFCEQC GVEFIESRIR RYRMGYIKLA CSVTHVWYLK
     RLPSYIANLL AKPLKELESL VYCDLFLARP ITKKPTLLKL QGLFKYEDQS WKDIFPRFFS
     PRGFEVFQNR EIATGGDAIQ KQLTNLNLQN VINLAHLEWK EFAEQKSTGN EWEDRKIQRR
     KDLLVRRIKL AKHFIQTNIK PEWMVLSLLP VLPPELRPMI ELGEGELITS DLNELYRRVI
     YRNNTLLDFL ARSGSTPGGL VVCQKRLVQE AVDALIDNGI RGQPMKDSHN RPYKSFSDLI
     EGKEGRFREN LLGKRVDYSG RSVIVVGPFL PLHQCGLPRE MAIELFQAFV IRGLIGRNFA
     PNLRAAKTMI QNKEPIIWKV LQEVMQGHPI LLNRAPTLHR LGIQAFQPIL VNGRAIHLHP
     LVCGGFNADF DGDQMAVHIP LSLEAQAEAR LLMLSHKNLL SPATGEPISV PSQDMLLGLY
     ILTIENNQGI YGNKYNPSKK YDSKKKFSQI PYFSSYDNVF RALQQKQIYL HSSLWLRWQI
     NLRIITLLNQ EGPIEIQYKS FGNSFQIYEH YQLRKNKNQE IISTYICTTA GRILFNQQIE
     EAIQGTYKAS LKQKTFVQKI EKNG