RPOB_NYMAL
ID RPOB_NYMAL Reviewed; 1071 AA.
AC Q6EW56;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
OS Nymphaea alba (White water-lily) (Castalia alba).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Nymphaeales; Nymphaeaceae; Nymphaea.
OX NCBI_TaxID=34301;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15084683; DOI=10.1093/molbev/msh147;
RA Goremykin V.V., Hirsch-Ernst K.I., Woelfl S., Hellwig F.H.;
RT "The chloroplast genome of Nymphaea alba: whole-genome analyses and the
RT problem of identifying the most basal angiosperm.";
RL Mol. Biol. Evol. 21:1445-1454(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; AJ627251; CAF28585.1; -; Genomic_DNA.
DR RefSeq; YP_053147.1; NC_006050.1.
DR AlphaFoldDB; Q6EW56; -.
DR SMR; Q6EW56; -.
DR GeneID; 2896155; -.
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; 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; 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_0000048033"
SQ SEQUENCE 1071 AA; 120572 MW; 94701268EBDA8616 CRC64;
MLRDGGDEGM FTIPGFSQIQ FEGFCRFIDQ GLMEELHQFP KIEDTDQEIE FQLFGESYQL
VEPLIKERDA VYESITYSSE LYVPAGLIWR TGRNMQEQTV LLGNIPLMNS LGTSIVNGIY
RIVINQILQS PGIYYSTGLD HNGISVYTGT IISDWGGRSE LEIDRKERIW ARVSRKQKIS
ILVLSSAMGS SLREILDNVC YPEIFLSFPN EKEKKKIGSK ENAILEFYQK FACVGGDPVF
SESLCKELQK KFFQQRCELG RIGRRNMNQR LNLDIPPNNT FLLPRDVLAA ADHLIGMKFG
MGTLDDMNHL KNKRIRSVAD LLQDQFGLAL VRLENVVRGT ICGAIRHKLI PTPRNLVTST
PLTTTYESFF GLHPLSQVLD RTNPLTQIVH GRKSSYLGPG GLTGRTASFR IRDIHPSHYG
RICPIDTSEG INVGLIGSLA IHARVGDWGS IETPFYEISE RSKEEQMVYL SPSRDEYYMV
AAGNSLALTR GIQEEEVGPA RYRQEFLTIA WEQIHLRNIY PFQYFSIGAS LIPFIEHNDA
NRALMSSNMQ RQAVPLSQSE KCIVGTGLER QAALDSGGSA IAEREGKIIY TDAEKIVLSG
NGDTISIPLV MYQRSNKNTW MHQKPQVHRG KYLKKGQILA DGAATVGGEL ALGKNVSVAY
MPWEGYNSED AVLISERLVY DDIYTSFHIR KYEIQTHVTS QGPERITNEI PHLEPYLLRN
LDRNGIVMLG SWVETGDVLV GKLTPQTAKE SSYAPEDRLL RAILGIQVST AKETCLKLPI
GGRGRVIDVR WGQKKGGSIY NPEMIRVYIS QKRKIKVGDK VAGRHGNKGI ISKILPRQDM
PYLQDGTPVD MVFNPLGVPS RMNVGQMFEC SLGLAGDLLG RHYRITPFDE RYEQEASRKL
VFSELYEASK QTANPWVFEP EYPGKSRIFD GRTGDPFEQP VIIGKSYMLK LIHQVDDKIH
GRSSGHYALV TQQPLRGRAK QGGQRVGEME VWALEGFGVA HILQEMLTYK SDHIRARQEV
LGTTIVGGTI PNPEGAPESF RLLVRELRSL SLELNHFLVS EKNFQINRKE V