RPOC1_NYMAL
ID RPOC1_NYMAL Reviewed; 684 AA.
AC Q6EW57;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 71.
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 Nymphaea alba (White water-lily) (Castalia alba).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nymphaea.
OX NCBI_TaxID=34301;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15084683; DOI=10.1093/molbev/msh147;
RA Goremykin V.V., Hirsch-Ernst K.I., Woelfl S., Hellwig F.H.;
RT "The chloroplast genome of Nymphaea alba: whole-genome analyses and the
RT problem of identifying the most basal angiosperm.";
RL Mol. Biol. Evol. 21:1445-1454(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 -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01323}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF28584.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ627251; CAF28584.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_053146.1; NC_006050.1.
DR AlphaFoldDB; Q6EW57; -.
DR SMR; Q6EW57; -.
DR GeneID; 2896156; -.
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 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_0000067883"
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; 78718 MW; 7BA54C82F1808C8C CRC64;
MIDQYKHQQL RIGLVSPKQI RAWANKILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
FGPIKSGICA CGNYRVIGGE KEEPKFCEQC GVESVDSRIR RYQMGYIKLA CPVTHVWYLK
RLPSYIANLL DKPLKELEGL VYCDFSFARP IAKKPTFLRL RGSFEYEIQS RKYSIPLFFT
TQGFDTFRNR EISTGATAIR EQLADLDLRI IIDRSLVEWK ELGEEGSTGN DWEDRKIGRR
KDFLVRRMEL AKHFLRTNVE PEWMVLSLLP VLPPELRPII QIDGGKSMSS DINELYRRVI
YRNNTLTDLL TTSRSTPGEL VMCQEKLVQE AVDTLLDNGI RGQPMRDGHN KVYKSFSDVI
EGKEGRFRET LLGKRVDYSG RSVIVVGPSL SLHQCGLPRE IAIELFQTFV IRGLIRQHLA
SNIGLAKSKI REKEPIVWEI LQEVMQGHPV LLNRAPTLHR LGIQAFQPIL VEGRAICLHP
LVCKGFNADF DGDQMAVHVP LSLEAQAEAR LLMFSHTNLL SPAIGDPISV PTQDMLMGLY
VLTMGNRRGI CANRYNPCNP RNHQNERMDH SNYEYRKGKE PYFCSSYDAL GAYRQKGIDL
YSTLWLRWRL DQRVIASINR EVPIEVQYES LGTYHEIYDH YRVVRSVKKG MLCIYIRTTV
GHISFYREIE EAIQGFCRSY SYGT
