RPOC2_GUITH
ID RPOC2_GUITH Reviewed; 1286 AA.
AC O78483;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG Plastid; Chloroplast.
OC Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX NCBI_TaxID=55529;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9929392; DOI=10.1007/pl00006462;
RA Douglas S.E., Penny S.L.;
RT "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT sequence and conserved synteny groups confirm its common ancestry with red
RT algae.";
RL J. Mol. Evol. 48:236-244(1999).
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_01324}.
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_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
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_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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; AF041468; AAC35674.1; -; Genomic_DNA.
DR RefSeq; NP_050740.1; NC_000926.1.
DR AlphaFoldDB; O78483; -.
DR GeneID; 857045; -.
DR HOGENOM; CLU_000524_1_0_1; -.
DR OMA; IEGKSDW; -.
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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 4.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1286
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000067926"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1286 AA; 145045 MW; BEFF46FEF5522C73 CRC64;
MKEKYLFVPP KPKFTNKVID KKELKKLMAW AFSNYGTGRA SFMADKIKDL GFHYATKAGL
SLSVEDLRVP PIKRDLLLQA NREIQQTEQL YERGEITTIE RFQKVIDTWN NTSEQLKDEV
IKYFKQNDPL NPIYIMAFSG ARGNISQVRQ LVGMRGLMAD PQGQIIDLPI KSNFREGLTV
TEYLISSYGA RKGLVDTALR TADSGYLTRR LVDVAQDIII REIDCGTQRG IVLRDMVDNN
QILVSLKNRL IGRVLFETLY LPNDASVIGH INQDLDHDIT NSIIKCGIKS VIVRSPLTCE
APRSVCQFCY GWNLAHGSLV DLGEAVGIIA AQSIGEPGTQ LTMRTFHTGG VFTGELAEQI
RAPFNGIIRY PKNLKIRIIR TRHGNEGVIL DENYKLNILN QRGEKTRLEF KQGTTLFISD
NEEFKKGQII GETKSRSTLV TEKATRDLVT ETSGEVIYTN LNIENKIDRQ GNSTLITNKG
GLLWILKGDV YNIPYNTDIQ LKIGDKIAKD TIISTFKTIS EYNGIVRLNE KNEEIQILTD
FISLENAEIE YNELDVNIEC PINLRFEDGK ILNLLCVPGN KITNSQVIGE YIEDNYKTTT
GGIIKYKNYA ELKKEKNKKG YEINDNEVIY WIPEETHEIN KDLSLLLIKN NTLINSGTEI
IKDVYCLNSG YVEIIQEDEI VKEVIIKPGI IYDSSELNTK RNIGTICDIK EVISTSTENK
QIFLDVIGEK LFLRPVESYN IKMSHINLKT KRLTNLEDIL NLKVVNRSLY KDGEKIKSVY
GLDLVKTYLI VNFNSNKPYA SADIEFAPIE NSTKYKLNLT ITESIQLNYD IFGAINNEDV
KTSLVIKDGQ RIKKEDLIAE THLVARNKGI LKNILISSQS TKKLLIMREE DTFRVPTNNA
TIQVSRGDLV KYGDQLAGSV IASESGQVFE ITKNEIILRK AYPYLVSAGA ILQIKDHELV
QRNDTLAILV FERSKTGDIV QGLPRIEEIL EARKPKEPCK LSQKPGKINT TNSNDETEVI
QLIDTDGYTT DYIINNNQKL IISNGENVLL AEPLTDGAPN PHEMLNLYFN FYTSIITLYE
SAKLSLQKVQ TYLVDEVQKV YQSQNVDISD KHIEVIVRQM TSKVKVEDGG DTTLLPGELV
ELQQIENINE AMMLTKGVPA TYCPILLGIT KASLNTDSFI SAASFQETTR VLTEAAIEGK
ADWLRGLKEN VIIGRLIPAG TGFNAYNEQH KSSKSMKLTG IPDTYYLSSS LEVEDSKLST
IIEDNNLEQY NSIDSFDNIE KENPNN