RPOB_PANGI
ID RPOB_PANGI Reviewed; 1071 AA.
AC Q68S14;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; ORFNames=PSC0250;
OS Panax ginseng (Korean ginseng).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15500250; DOI=10.1093/dnares/11.4.247;
RA Kim K.-J., Lee H.-L.;
RT "Complete chloroplast genome sequence from Korea ginseng (Panax schinseng
RT Nees) and comparative analysis of sequence evolution among 17 vascular
RT plants.";
RL DNA Res. 11:247-261(2004).
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_01321}.
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_01321};
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_01321}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; AY582139; AAT98501.1; -; Genomic_DNA.
DR RefSeq; YP_086958.1; NC_006290.1.
DR AlphaFoldDB; Q68S14; -.
DR SMR; Q68S14; -.
DR GeneID; 3021561; -.
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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 3.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 1.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW Chloroplast; DNA-directed RNA polymerase; Nucleotidyltransferase; Plastid;
KW Transcription; Transferase.
FT CHAIN 1..1071
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000048038"
SQ SEQUENCE 1071 AA; 120830 MW; 84A1BEBD3A6BB42B CRC64;
MLRDGKNEGM STIPGFNQIQ FEGFCRFIDQ GLTEELYKFP KIEDTDQEIE FQLFVETYQL
VEPLIKERDA VYESLTYSSE LYVSAGLIWK TGRDMQEQTI FFGNIPLMNS LGTSIVNGIY
RIVINQVLQS PGIYYRSELD HNGISVYTGT IISDWGGRSE LEIDRKARIW ARVSRKQKIS
ILVLSSAMGS NLREILENVC YPEIFLSFLT DKEKKKIGSK ENAILEFYQQ FACVGGDPVF
SESLCKELQK KFFQQRCELG RIGRRNMNRR LNLDISQNNT FLLPRDILAA ADHLIGMKFG
MGTLDDMNHL KNKRIRSVAD LLQDQFGLAL VRLENVVRGT ICGALRHKLI PTPQNLVTST
PLTTTYESFF GLHPLSQVLD RTNPLTQIVH GRKLSYLGPG GLTGRTASFR IRDIHPSHYG
RICPIDTSEG INVGLIGSLA IHARIGRWGS LESPFYEISE RSKGARMLYL SPGKDEYYMV
AAGNSLALNQ GIQEEQVVPA RYRQEFLTIA WEQVHLRSIF SFQYFSIGAS LIPFIEHNDA
NRALMSSNMQ RQAVPLSRSE KCIVGTGLER QAAIDSGALA IAEHEGKIIY TDTDKILLSG
NGNTLSIPLV IYQRSNKNTC MHQKPQVQRG KCIKKGQILA HGAATVGGEL ALGKNVLVAY
MPWEGYNFED AVLISERLVY EDIYTSFHIR KYEIKTHVTS QGPERVTNEI PHLEAHLLRN
LDKNGIVMLG SWVETGDILV GKLTPQMVKE SSYAPEDRLL RAILGIQVST SKETCLKLPI
GGRGRVIDVR WIQKRGGSSY NPEMIRVYIS QKREIKVGDK VAGRHGNKGI ISKILPRQDM
PYLQDGRPVD MVFNPLGVPP RMNVGQIFEC SLGLAGGLLD RHYRIAPFDE RYEQEASRKL
VFSELYEAGK QTANPWVFEP EYPGKSRIFD GRTGDPFEQP VIIGKPYILK LIHQVDDKIH
GRSSGHYALV TQQPLRGRAK QGGQRVGEME VWALEGFGVA HILQEMLTYK SDHIRARQEV
LGTTIIGGTI PNPQDAPESF RLLVRELRSL ALELNHFFVS EKNFQINRKE A