ID A0A2H4V2N5_9MAGN Unreviewed; 1089 AA. AC A0A2H4V2N5; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 03-AUG-2022, entry version 17. DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01321}; DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01321}; DE AltName: Full=Plastid-encoded RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321}; DE Short=RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321}; GN Name=rpoB {ECO:0000256|HAMAP-Rule:MF_01321, GN ECO:0000313|EMBL:AUB29863.1}; OS Aconitum reclinatum. OG Plastid; Chloroplast {ECO:0000313|EMBL:AUB29863.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Ranunculoideae; OC Delphinieae; Aconitum. OX NCBI_TaxID=1905858 {ECO:0000313|EMBL:AUB29863.1}; RN [1] {ECO:0000313|EMBL:AUB29863.1} RP NUCLEOTIDE SEQUENCE. RA Kong H., Liu W., Yao G., Gong W.; RT "Characterization of the whole chloroplast genome of a rare and endangered RT species Aconitum reclinatum (Ranunculaceae) in the United States."; RL Conserv Genet Resour 0:0-0(2017). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {ECO:0000256|ARBA:ARBA00004026, ECO:0000256|HAMAP-Rule:MF_01321, CC ECO:0000256|RuleBase:RU363031}. 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:0000256|ARBA:ARBA00024550, CC ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}; 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:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01321}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000256|ARBA:ARBA00006835, ECO:0000256|HAMAP-Rule:MF_01321, CC ECO:0000256|RuleBase:RU000434}. 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; MF186593; AUB29863.1; -; Genomic_DNA. 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; -; 2. 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 {ECO:0000313|EMBL:AUB29863.1}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01321}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01321}; Plastid {ECO:0000313|EMBL:AUB29863.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01321}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01321}. FT DOMAIN 35..366 FT /note="RNA_pol_Rpb2_1" FT /evidence="ECO:0000259|Pfam:PF04563" FT DOMAIN 148..334 FT /note="RNA_pol_Rpb2_2" FT /evidence="ECO:0000259|Pfam:PF04561" FT DOMAIN 395..463 FT /note="RNA_pol_Rpb2_3" FT /evidence="ECO:0000259|Pfam:PF04565" FT DOMAIN 600..998 FT /note="RNA_pol_Rpb2_6" FT /evidence="ECO:0000259|Pfam:PF00562" FT DOMAIN 1000..1075 FT /note="RNA_pol_Rpb2_7" FT /evidence="ECO:0000259|Pfam:PF04560" SQ SEQUENCE 1089 AA; 122708 MW; 4DB63F923D52A385 CRC64; MKNEPWGMNG IFSINGKLKM LRDGNEGMST IPGFSQIQFE GFCRFIDQGL TEELYKFPKI EDTDQEIEFQ LFVETYQLVE PLIKEKDAVY ESLTYSSELY VPAGLIWKTG RDTQEQTIFI GKIPLMNSLG TSIVNGIYRI VINQILQSPG IYYRSELDHN GISVYTGTII SDWGGRSELE IDRKARIWAR VSRKQKISIL VPSSAMGSNL REIIDNVCYP EIFLSFPNDK EKKKIGSKEN AILEFYQQFA CVGGDPVFSE SLCKELQKKF FQQRCELGRI GRRNMNRRLN LDIPQNITFL LPRDILAAAD HLIRMKFGMG TLDDMNHLKN KRIRSVADLL QDQFGLALVR LENTVRGTIG GAIRHKLIPT PHNLVTSTPL TTTFESFFGL HPLSQVLDRT NPLTQIVHGR KLSYLGPGGL TGRTASFRIR DIHPSHYGRI CPIDTSEGIN VGLIGSLAIH ARIGHWGSLE RPFYEISEKS KEVRVVYLSP SRDEYYMVAA GNSLALNQGI QEEQVVPARY RQEFLTIAWE QIHLRSILPF QYFSIGASLI PFIEHNDANR ALMSSNMQRQ AVPLSRSEKC IVGTGLERQA ALDSGVPAIA EQEGKIIYTD TNKIMLSGNG GTLSIPLVMY QRSNKNTCMH QKPRVPQGFC IKKGQILADG AATVGGELAL GKNVLVAYMP WEGYNFEDAV LISERLVYGD FYTSFHIRKY EIQTHVTSQG PERITNEIPH LEAHLLRNLD INGIVMLGSW VETGDILVGK LTPQMAKESS YAPEDRLLRA ILGIQVSTAK ETCLKLPIGG RGRVIDVRWI QKRGGSSYNP ETIRVYISQK REIKVGDKVA GRHGNKGIIS KILPRQDMPY LQDGTPVDMV FNPLGVPSRM NVGQIFECSL GLAGDLLDRH YRISPFDERY EQEASRKLVF SELYEASTQT ANPWVFEPEY PGKSRIFDGR TGDPFEQPVI IGKSYILKLI HQVDDKIHGR SSGHYALVTQ QPLRGRAKQG GQRVGEMEVW ALEGFGVAHI LQEMLTYKSD HIRARQEVLG TTIIGGTISN PEDAPESFRL LVRELRSLAL ELNHFLVSEK NFQINRKEA //