RPOC1_ADICA
ID RPOC1_ADICA Reviewed; 694 AA.
AC Q85FM8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 73.
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 Adiantum capillus-veneris (Maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT "Complete nucleotide sequence of the chloroplast genome from a
RT leptosporangiate fern, Adiantum capillus-veneris L.";
RL DNA Res. 10:59-65(2003).
RN [2]
RP SEQUENCE REVISION, AND RNA EDITING.
RC TISSUE=Frond;
RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA Wolf P.G., Rowe C.A., Hasebe M.;
RT "High levels of RNA editing in a vascular plant chloroplast genome:
RT analysis of transcripts from the fern Adiantum capillus-veneris.";
RL Gene 339:89-97(2004).
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 -!- RNA EDITING: Modified_positions=39 {ECO:0000269|PubMed:15363849}, 43
CC {ECO:0000269|PubMed:15363849}, 55 {ECO:0000269|PubMed:15363849}, 56
CC {ECO:0000269|PubMed:15363849}, 140 {ECO:0000269|PubMed:15363849}, 283
CC {ECO:0000269|PubMed:15363849}, 417 {ECO:0000269|PubMed:15363849}, 486
CC {ECO:0000269|PubMed:15363849}, 490 {ECO:0000269|PubMed:15363849};
CC Note=The nonsense codons at positions 39 and 417 are modified to sense
CC codons.;
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; AY178864; AAP29383.2; -; Genomic_DNA.
DR RefSeq; NP_848051.1; NC_004766.1.
DR AlphaFoldDB; Q85FM8; -.
DR SMR; Q85FM8; -.
DR GeneID; 807354; -.
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; 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 SMART; SM00663; RPOLA_N; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; RNA editing; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..694
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067858"
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 694 AA; 79724 MW; CD061390182F8BF0 CRC64;
MIHRTNYQQL RIGLASPEQI RSWAERELPN GDVIGQVDQP YTLHYKTHKP ERDGLFCERI
FGPTKSGVCA CGNCRSVNDE GESSRFCKHC GVEFTDSRVR RYRMGYIKLA CPVTHVWFLK
RIPSYIANLL AKPLKELESL VYCDLFLARP VAERPALLRL RGLFNYEDRA WRNILPTFFS
TQNYEMLRKN EIVTGGDAIR EGLASLDLQS FLNCAYLEWQ ASVKQKPVGI EWEDRTIRRR
KDLLIRRIKL AKDFLRTNMK PEWMVLYFIP VLPPELRPIV ELHEGELITS DLNELYRKII
YRNNTLREFL SGSEFTPEGL IVCQKRLVQE AVDALIGSGI RGQPMRDIHN RPYKSFSEVI
EGKEGRFREN LLGKRVDYSG RSVIVVGPSL SLHQCGLPRE MAIELFQAFV IRNLIGRHLA
CNLRAAKCMI RKGNPIIWEV LREVMRGHPV LLNRAPTLHR LGIQAFQPLL IEGRAIRLHP
LVRGGFNADF DGDQMAVHVP LSVEAQIEAR LLMFSHLNLL SPATGDPVSV PSQDMLLGLY
ALTIESRQGI YRNRHLGFID RVNVYSTKLL HFSSYCDLLR AKESRQVDSH SLLWLRWKID
LQIISSKIRE LSSESHYESS GTSFHFYENC RIRKCRDGSI SSMYVLTTAG RILFNQQLKE
AMQGVSKNSF SYTTSSTLST STIDRCNTNS NNEE
