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RPOC1_PHAVU
ID   RPOC1_PHAVU             Reviewed;         684 AA.
AC   A4GGA6; A8W811;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
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   Phaseolus vulgaris (Kidney bean) (French bean).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Negro Jamapa;
RX   PubMed=17623083; DOI=10.1186/1471-2164-8-228;
RA   Guo X., Castillo-Ramirez S., Gonzalez V., Bustos P.,
RA   Fernandez-Vazquez J.L., Santamaria R.I., Arellano J., Cevallos M.A.,
RA   Davila G.;
RT   "Rapid evolutionary change of common bean (Phaseolus vulgaris L) plastome,
RT   and the genomic diversification of legume chloroplasts.";
RL   BMC Genomics 8:228-228(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Moore M.J., Triplett E.W., Broughton W.J., Soltis P.S., Soltis D.E.;
RT   "Complete nucleotide sequence of the plastid genome of the common bean,
RT   Phaseolus vulgaris.";
RL   Submitted (OCT-2007) 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}.
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DR   EMBL; DQ886273; ABH88087.1; -; Genomic_DNA.
DR   EMBL; EU196765; ABW22781.1; -; Genomic_DNA.
DR   RefSeq; YP_001122807.1; NC_009259.1.
DR   AlphaFoldDB; A4GGA6; -.
DR   SMR; A4GGA6; -.
DR   STRING; 3885.XP_007135456.1; -.
DR   PRIDE; A4GGA6; -.
DR   GeneID; 4961811; -.
DR   KEGG; pvu:PhvuCp23; -.
DR   eggNOG; ENOG502QPYA; Eukaryota.
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_0000353510"
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         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"
FT   BINDING         495
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01323"
FT   CONFLICT        145
FT                   /note="V -> F (in Ref. 2; ABW22781)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   684 AA;  79179 MW;  B61342C38B4B68EC CRC64;
     MIDQYKHQQL RIGSVSPQQM SAWAKRILPN GEIVGEVTKP YTFHYKTNKP EKDGLFCERI
     FGPIKSGICA CGNYRVIRDK KDDPKFCEQC GVEFIDSRIR RYQMGYIKLA CLVTHAWYLK
     RLPSYIANLL DKPLKELESL VYGDVSFARP VVKKPTFLRL RGSFEYEIQS WKHSIPLFFT
     TRGFDIFRNR EISSGAVAIR EQLADLDLRI IMDYSLIEWK ELGKEGSPDN ENEWEDRKVG
     RRKNFLVRRI ELAKHFIRTN IEPEWMVLCL LPVLPPELRP IIQVDGGKLM SSDINELYRR
     VIYRNNTLID LLTTSRSTPG ELVICQEKLV QEAVDTLLDN GIRGQPMRDG HNKVYKSFSD
     IIEGKEGRFR ETLLGKRVDY SGRSVIIVGP SLSLHRCGLP GEIAIELFQT FLIRGLIRKH
     FASNIGIAKS KIRQKEPIVW EILQEVMQGH PVLLNRAPTL HRLGIQAFQP ILVEGRAICL
     HPLVCKGFNA DFDGDQMAVH VPLSLEAQAE ARLLMFSHTN LLSPAIADPI SVPTQDMLIG
     LYILTSGNRR GIYSNRYNPR NCRNLKNERI PNNNYKYTKK KEPFFCNSYD AIGAYQQKRI
     TFDSPLWLRW RLDLRIISSR EVPIEVHYES LGTYHEIYGH YLVVRSIKKQ MRSIYIRTNV
     GHISFYREIE EAVQGFCRAY SYDI
 
 
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