RPC2B_CHLRE
ID RPC2B_CHLRE Reviewed; 489 AA.
AC Q8HUH0; B7U1K9;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' C-terminal section;
DE EC=2.7.7.6;
DE AltName: Full=PEP;
DE AltName: Full=Plastid-encoded RNA polymerase beta' C-terminal section;
DE Short=RNA polymerase beta' C-terminal section;
GN Name=rpoC1B;
OS Chlamydomonas reinhardtii (Chlamydomonas smithii).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Chlamydomonadaceae; Chlamydomonas.
OX NCBI_TaxID=3055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION, AND COMPLETE
RP PLASTID GENOME.
RX PubMed=12417694; DOI=10.1105/tpc.006155;
RA Maul J.E., Lilly J.W., Cui L., dePamphilis C.W., Miller W., Harris E.H.,
RA Stern D.B.;
RT "The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a
RT sea of repeats.";
RL Plant Cell 14:2659-2679(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC-503;
RX PubMed=19473533; DOI=10.1186/1471-2148-9-120;
RA Smith D.R., Lee R.W.;
RT "Nucleotide diversity of the Chlamydomonas reinhardtii plastid genome:
RT addressing the mutational-hazard hypothesis.";
RL BMC Evol. Biol. 9:120-120(2009).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250}.
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 -!- 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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: In C.reinhardtii the gene for this protein is split in
CC two.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF541870; AAN17821.1; -; Genomic_DNA.
DR EMBL; FJ423446; ACJ50156.1; -; Genomic_DNA.
DR EMBL; BK000554; DAA00969.1; -; Genomic_DNA.
DR RefSeq; NP_958425.1; NC_005353.1.
DR AlphaFoldDB; Q8HUH0; -.
DR SMR; Q8HUH0; -.
DR STRING; 3055.DAA00969; -.
DR PaxDb; Q8HUH0; -.
DR PRIDE; Q8HUH0; -.
DR GeneID; 2717049; -.
DR KEGG; cre:ChreCp069; -.
DR eggNOG; ENOG502QPYA; Eukaryota.
DR HOGENOM; CLU_558214_0_0_1; -.
DR InParanoid; Q8HUH0; -.
DR OrthoDB; 774084at2759; -.
DR Proteomes; UP000006906; 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: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 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 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 2: Evidence at transcript level;
KW Chloroplast; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Plastid; Reference proteome; Transcription;
KW Transferase.
FT CHAIN 1..489
FT /note="DNA-directed RNA polymerase subunit beta' C-terminal
FT section"
FT /id="PRO_0000067867"
FT BINDING 208
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 210
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 212
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
SQ SEQUENCE 489 AA; 55630 MW; 1912E0FB97448C47 CRC64;
MSGQFTISDL NRLYQRIIYR NERLKKFLKD PALSSSFEMK YAQRLLQEAV DNLIQNGKSG
VVPEKDARGR LLKSLSDILK GKQGRFRQYL LGKRVDYSGR SVIVVGPRLR LHECGIPKEM
ALVLYSPFLI KRILNEKLAD TYLSAKKLIR TNPLLVSQLL REIMKSCPVL LNRAPTLHRL
GFQAFQPKLV DGKAILLHPL VCPAFNADFD GDQMAVHVPI TFEARAEAWK LMLARNNLLS
PATGEPLILP SQDMVLGCYY LTTNCAEKWS KLKKGSGMYF HNIHEVLKAY NQHLIHLHAV
IWVNIQGHLE TANNIEQPLE IRIPLNQKYF YSQKGSYTAL AGRPWQLLLR EDAYSSNGLI
AEANAGNLPQ INVAEGEVNK NILDLRYLNL NYMEIYSKTH NLLNVNHSTL VAQRGQIKDN
IHLPQLTTQI IRTTPGKILF NIIVKNAIEK RPKLLSKSNF KGGFIKNKLV NAIDQEIDNY
FIRKNTALS