RPOC1_CHAGL
ID RPOC1_CHAGL Reviewed; 661 AA.
AC Q8MA11;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Chaetosphaeridium globosum (Charophycean green alga) (Herposteiron
OS globosum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Coleochaetophyceae; Coleochaetales;
OC Chaetosphaeridiaceae; Chaetosphaeridium.
OX NCBI_TaxID=96477;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12161560; DOI=10.1073/pnas.162203299;
RA Turmel M., Otis C., Lemieux C.;
RT "The chloroplast and mitochondrial genome sequences of the charophyte
RT Chaetosphaeridium globosum: insights into the timing of the events that
RT restructured organelle DNAs within the green algal lineage that led to land
RT plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11275-11280(2002).
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; AF494278; AAM96567.1; -; Genomic_DNA.
DR RefSeq; NP_683775.1; NC_004115.1.
DR AlphaFoldDB; Q8MA11; -.
DR SMR; Q8MA11; -.
DR PRIDE; Q8MA11; -.
DR GeneID; 860723; -.
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..661
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067865"
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 661 AA; 76867 MW; E918994FEFBB33A6 CRC64;
MFDKQKNRYI RVELASPDQI RNWAERTLPN GEIVGKVTKP YTLHYNSHKP EKDGLFCERI
FGPIKSGICA CGKYHGFVKN LPEVKFCKQC GVEFTDSKVR RYRMGYIQLA YPATHIWYLK
RLPSHIATLL KMSLKEVESL VYCDLFLPRP IIKKPNLLKV KKLFNYDDQL WKETLPRFFS
TRSFESFQNR EMATGGDAIH KRLSSLNLQK LIFQSYNEWE KLSLQRSTGN SYEDKKIQRM
KDIIIRRIKL AKQFFENNIK PEWMVLSVLP VLPPELRPMI EINQGELITS DLNELYRRVI
YRNNTLIGFL NKSNSTPAGL IIYQKRLVQE AVDALIDNRI GNQIMKDRNN RPYKSFSEII
EGKEGRFRQD LLGKRVDYSG RSVIVVGPSL SLHQCGIPKD MAIELFQPFI IRDLINCQLA
PNLRAARSMI QNQEPIIFKI LEKIIKNHPI LLNRAPTLHR LGIQAFQPIL VEGLAIRLHP
LVCGGFNADF DGDQMAVHIP LSLEAQAEAR FLMLANSNLL SPANGEPITV PSQDMLLGLY
VLTMSCKQGI YIYNEQKLKK KIPYFCNYID VITAYEKKQI NLHDPIWLKW YGNLRGTSST
KKQKLFEIQC ESRGTRRKIF ENWHFCENIR NRKFTIYLFT TPGRIIFNQL LEQSIQATVR
I
