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RPOC1_AMBTC
ID   RPOC1_AMBTC             Reviewed;         680 AA.
AC   P60287;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2004, sequence version 1.
DT   03-AUG-2022, entry version 79.
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   Amborella trichopoda.
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12832641; DOI=10.1093/molbev/msg159;
RA   Goremykin V.V., Hirsch-Ernst K.I., Wolfl S., Hellwig F.H.;
RT   "Analysis of the Amborella trichopoda chloroplast genome sequence suggests
RT   that Amborella is not a basal angiosperm.";
RL   Mol. Biol. Evol. 20:1499-1505(2003).
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; AJ506156; CAD45098.1; -; Genomic_DNA.
DR   RefSeq; NP_904090.1; NC_005086.1.
DR   AlphaFoldDB; P60287; -.
DR   SMR; P60287; -.
DR   GeneID; 2546589; -.
DR   KEGG; atr:2546589; -.
DR   OrthoDB; 774084at2759; -.
DR   Proteomes; UP000017836; Chloroplast.
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..680
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000067859"
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   680 AA;  78630 MW;  AD43DEC4F189BA06 CRC64;
     MIDRYKHQQL RIGLVSPQQI TAWANKILPN GEMVGEVTKP YTFHYKSNKP EKDGLFCERI
     FGPIKSGICA CGNYRVIGDE KEDPKFCEQC GVESVDSRIR RYQMGYIKLA CPVTHVWYLK
     RLPSYIANLS DRPLKELEGL VYCDFSFARP IAKKPTFLRL RGSFEYEIQS RKYSIPLFFT
     TQCFNLFRNR EISTGAGAIR EQLADPDLRI ITDRSLVEWK ELGEERSAEN EWEDKKIVRR
     KDFLVRRMEL AKHLLRTNVE PERMVLCLLP VLPPELRPII QIDGGKPMSS DINELYRRVI
     YRNNTLIDPL TTSRSTPGES VMCQEKLVQE AVDTLLDNGI RGQPMRDGHN KVYKSFSDVI
     EGKEGRFRET LLGKRVDYSG RSVIVVGPSL SLHRCGLPRE IAIELFQTFV IRGLIRQHVA
     SNIGIAKSKI REKEPIVWEI LQKVMEGHPV LLNRAPTLHR LGIQAFQPIL VEGRAICLHP
     LVRKGFNADF DGDQMAVHVP LSLEAQAEAR LLMFSHMNLL SPAIGDPISV PTQDMLIGLY
     VLTIGNRRGI CTNRYNPCNY RNYQNEIVDD NNYKYTKEKE PYFCSSYDAL GAYRQKRIDL
     YSPLWLRWRL DQCVIASINR EVPIEVQYES LGIYHEIHEH YRIVKSVKKE IVCIYIRTTV
     GHISFYREIE EAIQGFCRTY
 
 
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