ID A0A481ZMT9_9POAL Unreviewed; 1075 AA. AC A0A481ZMT9; DT 05-JUN-2019, integrated into UniProtKB/TrEMBL. DT 05-JUN-2019, sequence version 1. DT 31-JUL-2019, entry version 3. 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:QBL02632.1}; OS Eriachne agrostidea. OG Plastid; Chloroplast {ECO:0000313|EMBL:QBL02632.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; OC PACMAD clade; Micrairoideae; Eriachneae; Eriachne. OX NCBI_TaxID=2546637 {ECO:0000313|EMBL:QBL02632.1}; RN [1] {ECO:0000313|EMBL:QBL02632.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Teisher34 {ECO:0000313|EMBL:QBL02632.1}; RA Teisher J.K., McKain M.R., Schaal B.A., Kellogg E.A.; RT "Plastome Phylogenetics of Tribe Eriachneae and Evolution of C4 RT Photosynthesis in Subfamily Micrairoideae (Poaceae)."; RL Syst. Bot. 44:32-40(2019). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {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:11128, Rhea:RHEA- CC COMP:11129, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, CC ChEBI:CHEBI:83400; EC=2.7.7.6; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01321, ECO:0000256|RuleBase:RU363031}; CC -!- SUBUNIT: In plastids the minimal PEP RNA polymerase catalytic core CC is composed of four subunits: alpha, beta, beta', and beta''. When CC a (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 ECO:0000256|SAAS:SAAS01158605}. 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|HAMAP-Rule:MF_01321, 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; MH036233; QBL02632.1; -; Genomic_DNA. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. 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: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; 1. 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:QBL02632.1}; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_01321, KW ECO:0000256|RuleBase:RU363031}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01321, KW ECO:0000256|RuleBase:RU363031}; KW Plastid {ECO:0000313|EMBL:QBL02632.1}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_01321, KW ECO:0000256|RuleBase:RU363031}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01321, KW ECO:0000256|RuleBase:RU363031}. FT DOMAIN 19 356 RNA_pol_Rpb2_1. {ECO:0000259|Pfam: FT PF04563}. FT DOMAIN 127 315 RNA_pol_Rpb2_2. {ECO:0000259|Pfam: FT PF04561}. FT DOMAIN 380 448 RNA_pol_Rpb2_3. {ECO:0000259|Pfam: FT PF04565}. FT DOMAIN 588 984 RNA_pol_Rpb2_6. {ECO:0000259|Pfam: FT PF00562}. FT DOMAIN 986 1061 RNA_pol_Rpb2_7. {ECO:0000259|Pfam: FT PF04560}. SQ SEQUENCE 1075 AA; 121462 MW; A5A177246D7E3142 CRC64; MLRNGNEGMS TIPGFSQVQF EGFCRFINQG LAEELEKFPT IKDPDQKIAF QLFAKGYQLL EPAIKERDAV YESLTYSSEF YVPARLILGF DVQKQTISIG NIPIMNSLGT FIINGIYRIV INQILLSPGI YYRSELDHKG ISIYTGTIIS DWGGRSELAI DKKERIWARV SRKQKISILV LLSAMGLNLR EILDNVSYPE IFLSFLNAKE KKRIESKEKA ILEFYQQFAC VGGDLVFSGS LCEELQKKFF QQKCELGRVG RRNMNRRLNL DIPQNNTFLL PRDVLTATDH LIGMKFETGI LDDDDMNHLK NKRIRSVADL LQDQFGLALG RLQHAVQKTI RRVFIRQSKP TPQTLVTPTS TSILLITTYE TFFGTYPLSQ VFDQTNPLTQ TVHGRKVSCL GPGGLTGRTA SFRSRDIHPS HYGRICPIDT SEGINVGLTG SLAIHARIDH WWGSIESPFY EISEKAKEKK ERQVVYLSPN RDEYYMIAAG NSLSLNQGIQ EDQVVPARYR QEFLTIAWEQ IHVRSIFPFQ YFSIGGSLIP FIEHNDANRA LMSSNMQRQA VPLSRSEKCI VGTGLEPQTA LDSRVSIIAE REGKVISSES HKILLSSSGK IISIPLVAHQ RSNKNTCMHQ KPQVTRGKSI KKGQILAEGA ATVGGELALG KNILVAYMPW EGYNFEDAVL ISERLVCEDI YTSFHIRKYE IQTDTTSQGS AEKITKEIPH LEEHLLRNLD RNGVVRLGSW VETGDILVGK LTPQVASESS YIAEAGLLRA IFGLEVSTSK ETSLKLPIGG RGRVIDVKWI QRDPLDIMIR VYILQKREIK VGDKVAGRHG NKGIISKILP RQDMPYLQDG TPVDMVFNPL GVPSRMNVGQ IFESSLGLAG DLLKKHYRIA PFDERYEQEA SRKLVFSELY EASKQTKNPW VFEPEYPGKS RIFDGRTGDP FEQPVLIGKS YILKLIHQVD EKIHGRSTGP YSLVTQQPVR GRAKQGGQRV GEMEVWALEG FGVAHILQEI LTYKSDHLIA RQEILNATIW GKRVPNHEDP PESFRVLVRE LRSLALELNH FLVSEKNFQV NREDV //