RPOC1_EUGGR
ID RPOC1_EUGGR Reviewed; 586 AA.
AC P23580;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000305};
DE EC=2.7.7.6 {ECO:0000250|UniProtKB:P0A8T7};
DE AltName: Full=PEP;
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000305};
DE Short=RNA polymerase subunit beta';
GN Name=rpoC1 {ECO:0000305};
OS Euglena gracilis.
OG Plastid; Chloroplast.
OC Eukaryota; Discoba; Euglenozoa; Euglenida; Spirocuta; Euglenophyceae;
OC Euglenales; Euglenaceae; Euglena.
OX NCBI_TaxID=3039;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=2110656; DOI=10.1093/nar/18.7.1869;
RA Yepiz-Plascencia G.M., Radebaugh C.A., Hallick R.B.;
RT "The Euglena gracilis chloroplast rpoB gene. Novel gene organization and
RT transcription of the RNA polymerase subunit operon.";
RL Nucleic Acids Res. 18:1869-1878(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z / UTEX 753;
RX PubMed=8346031; DOI=10.1093/nar/21.15.3537;
RA Hallick R.B., Hong L., Drager R.G., Favreau M.R., Monfort A., Orsat B.,
RA Spielmann A., Stutz E.;
RT "Complete sequence of Euglena gracilis chloroplast DNA.";
RL Nucleic Acids Res. 21:3537-3544(1993).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000305}.
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:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
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. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000305}.
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DR EMBL; X17191; CAA35053.1; -; Genomic_DNA.
DR EMBL; X70810; CAA50137.1; -; Genomic_DNA.
DR PIR; S19258; RNEGB1.
DR RefSeq; NP_041950.1; NC_001603.2.
DR AlphaFoldDB; P23580; -.
DR SMR; P23580; -.
DR PRIDE; P23580; -.
DR GeneID; 807501; -.
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: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; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 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 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..586
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067872"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 448
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ SEQUENCE 586 AA; 68142 MW; D346474567910763 CRC64;
MKDYVRIKIA SPQQVLSWTE RSLPDGRLIG RLTNFDMLHF ETKKPVFGGL LCERIFGSTK
TNQCFCGKYK KMFQKGYANN FVLVCANCFV EINNCNRRRF RMGYIDLVFP LIHTWYLKSR
PCYLAIMLGK KVKNIKKMCF MDSYIKIRNN DGQTVGILTG AEAIYSRLSK IDLESLIEFL
YKRLVGIEKL KEYNFEKYLW LRKKFINRIK LVNAFIQTNT KPIWIMIHFL PVLPPDIRPV
VKLQDGTVIM TDLNFLYIDI IYGNNKIIKL RKFLLPEEFM LNEKRSLQVK VDAFINNENI
SENPYEQNDK KLKSITEGLK GKKGRFRENL LGKTVDYSGR SVIVVEPKLL LHECGMPLDI
ALELFHPILI KMLIRFKFSV GIREAKRHIY NASNFVIPVL EKVLNSYFIL LNRAPTLHRL
GIQSFQPKVT FEKAILLHPL VCSAFNADFD GDQMGIHIPL SLKSLAEARS MLISINNCVL
PANGLPSILP SQDMVLGCYY VTLENCNLDF ILTNLKIYAN IEKVKSAYHK GEILIQTFVW
LICQKFPNIL KNSKIRIKKK RMVKKLVFFR TTIGRIFFDD MIKEFL
