RPOC1_SOLTU
ID RPOC1_SOLTU Reviewed; 687 AA.
AC Q2VEI5; Q27S59;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 70.
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 Solanum tuberosum (Potato).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RX PubMed=16835751; DOI=10.1007/s00299-006-0196-4;
RA Chung H.-J., Jung J.D., Park H.-W., Kim J.-H., Cha H.W., Min S.R.,
RA Jeong W.-J., Liu J.R.;
RT "The complete chloroplast genome sequences of Solanum tuberosum and
RT comparative analysis with Solanaceae species identified the presence of a
RT 241-bp deletion in cultivated potato chloroplast DNA sequence.";
RL Plant Cell Rep. 25:1369-1379(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Desiree;
RA Gargano D., Scotti N., Vezzi A., Bilardi A., Valle G., Grillo S., Cardi T.;
RT "Complete chloroplast genome sequences of Solanum tuberosum cultivar
RT Desiree and comparative analyses with other Solanaceae genomes.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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=ABB90034.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=ABD47048.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ231562; ABB90034.1; ALT_INIT; Genomic_DNA.
DR EMBL; DQ386163; ABD47048.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_635630.1; NC_008096.2.
DR AlphaFoldDB; Q2VEI5; -.
DR SMR; Q2VEI5; -.
DR STRING; 4113.PGSC0003DMT400076161; -.
DR GeneID; 4099931; -.
DR KEGG; sot:4099931; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR OrthoDB; 774084at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
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; Reference proteome; Transcription;
KW Transferase; Zinc.
FT CHAIN 1..687
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225325"
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 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT CONFLICT 145..150
FT /note="Missing (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="K -> Q (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="Y -> S (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..263
FT /note="QS -> RT (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..268
FT /note="DPQ -> EPE (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="W -> L (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="R -> Q (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="S -> N (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="K -> R (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="R -> T (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="K -> R (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="H -> N (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
FT CONFLICT 502..504
FT /note="DFK -> AVH (in Ref. 2; ABD47048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 79482 MW; CF1BAE8B15CB1EDC CRC64;
MIDRYKHQQL RIGSVSPQQI SAWATKILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
FGPIKSGICA CGNYRVIGDE KEDPKFCEQC GVEFVDSRIR RYQMGYIKLA CPVTHVWYLK
RLPSYIANLL DKPLKELEGL VYCDIESYPN FSFARPITKK PTFLRLRGLF EYEIQSWKYS
IPLFFTTKGF DTFRNREIYT GAGAIREQLA DLDLRIIIEN SLVEWEELGE EGHTGNEWED
RKVGRRKDFL VRRVELAKHF IQSNIDPQWM VWCLLPVLPP ELRPIIRIDG GKLMSSDISE
LYRKVIYRNN TLTDLLRTSK STPGELVMCQ EKLVQEAVDT LLDNGIRGQP MRDGHNKVYK
SFSDVIEGKE GRFRETLLGK RVDYSGRSVI VVGPSLSLHR CGLPREIAIE LFQTFVIRGL
IRQHLASNIG VAKSKIREKE PIVWEILQEV MQGHPVLLNR APTLHRLGIQ AFQPVLVEGR
AICLHPLVCK GFHADFDGDQ MDFKVPLSLE AQVEARLLMF SHMNLLSPAI GDPISVPTQD
MLIGLYVLTS GNHRGICVNR YNPCNRRNYQ NQKRSDNSYY KYTKEPFFSN SYDAIGAYRQ
KRINLDSPLW LRWRLDQRVI ASRETPIEVH YESLGTFYEI YGHYLIVRSL KKKILFIYIR
TTVGHIALYR EIEEAIQGFS RAYSYAT
