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RPOC1_PHYPA
ID   RPOC1_PHYPA             Reviewed;         679 AA.
AC   P60288;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004;
RX   PubMed=12954768; DOI=10.1093/nar/gkg726;
RA   Sugiura C., Kobayashi Y., Setsuyuki A., Sugita C., Sugita M.;
RT   "Complete chloroplast DNA sequence of the moss Physcomitrella patens:
RT   evidence for the loss and relocation of rpoA from the chloroplast to the
RT   nucleus.";
RL   Nucleic Acids Res. 31:5324-5331(2003).
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}.
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DR   EMBL; AP005672; BAC85072.1; -; Genomic_DNA.
DR   RefSeq; NP_904222.1; NC_005087.1.
DR   AlphaFoldDB; P60288; -.
DR   SMR; P60288; -.
DR   STRING; 3218.PP1S997_1V6.1; -.
DR   GeneID; 2546751; -.
DR   KEGG; ppp:2546751; -.
DR   eggNOG; ENOG502QPYA; Eukaryota.
DR   HOGENOM; CLU_101590_0_0_1; -.
DR   InParanoid; P60288; -.
DR   OrthoDB; 774084at2759; -.
DR   Proteomes; UP000006727; Chloroplast.
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; Reference proteome; Transcription;
KW   Transferase; Zinc.
FT   CHAIN           1..679
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067889"
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         84
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         486
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         488
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   BINDING         490
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
SQ   SEQUENCE   679 AA;  78272 MW;  564E93A90140D5E5 CRC64;
     MIHREKYHHL RIRLASPEQI RSWAERVLPN GEIVGQVTKP YTLHYKTHKP EKDGLFCERI
     FGPIKSGICA CGKYQIIEKY SKFCEQCGVE FVESRVRRYR MGYIKLACPV THVWYLKRLP
     SYIANLLAKP LKELESLVYC DLFLARPISK KPILLKLRGL FKYEDQSWRE IFPRYFSSRG
     FEAFQNKEIA TGGDAIKKQL SNLDLQGVLD YAYIEWKELV EQKSTGNEWE DRKIQRRKDL
     LVRRIKLAKQ FLQTNIKPEW MVLSLLPVLP PELRPMIELG EGELITSDLN ELYRRVIYRN
     NTLIDFLARS GSTPGGLVVC QIRLVQEAVD GLIDNGIRGQ PMKDSHNRPY KSFSDVIEGK
     EGRFRENLLG KRVDYSGRSV IVVGPFLSLH QCGLPREMAI ELFQAFVIRG LIGRHLAPNL
     RAAKSMIQNK EPIIWKILQE IMQGHPVLLN RAPTLHRLGI QAFQPILIKG RAIRLHPLVC
     GGFNADFDGD QMAVHIPLSL EAQAEARLLM FSHTNLLSPA TGDPVSVPSQ DMLLGLYILT
     IKNHQGIYGN KNHPYKQNNN KIFLNKTPYF SSYDDVIKAY NQKKVRLHSA LWLWWGSKLR
     TITSINREKP IEVQYNSSGI SFKIYEHYQL KKNKNEKNFS VYICTTVGRI IFNQQIEEAI
     QGTLKASLFR NQSLPAITI
 
 
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