ID A0A8K1HNH0_9MAGN Unreviewed; 1073 AA. AC A0A8K1HNH0; DT 03-AUG-2022, integrated into UniProtKB/TrEMBL. DT 03-AUG-2022, sequence version 1. DT 02-OCT-2024, entry version 6. 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:UBN07738.1}; GN ORFNames=Lod_N6912Cp012 {ECO:0000313|EMBL:UBN07738.1}, GN LorDel_N4678Cp012 {ECO:0000313|EMBL:UBN07673.1}; OS Loranthus delavayi. OG Plastid; Chloroplast {ECO:0000313|EMBL:UBN07738.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC Santalales; Loranthaceae; Lorantheae; Loranthinae; Loranthus. OX NCBI_TaxID=227897 {ECO:0000313|EMBL:UBN07738.1}; RN [1] {ECO:0000313|EMBL:UBN07738.1} RP NUCLEOTIDE SEQUENCE. RA Nickrent D.L., Su H.-J., Lin R.-Z., Devkota M.P., Hu J.-M., Glatzel G.; RT "Examining the Needle in the Haystack: Evolutionary Relationships in the RT Mistletoe Genus Loranthus (Loranthaceae)."; RL Syst. Bot. 46:403-415(2021). 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; MT987625; UBN07673.1; -; Genomic_DNA. DR EMBL; MT987626; UBN07738.1; -; 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:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1100.10; -; 1. DR Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 2. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:UBN07738.1}; 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:UBN07738.1}; 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 128..317 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04561" FT DOMAIN 378..447 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04565" FT DOMAIN 586..982 FT /note="DNA-directed RNA polymerase subunit 2 hybrid- FT binding" FT /evidence="ECO:0000259|Pfam:PF00562" FT DOMAIN 984..1059 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04560" SQ SEQUENCE 1073 AA; 122308 MW; 4CF82B65398FEECE CRC64; MLWDGNEGMY TIPGLNQIQF EGFCRFIDRG LMEKLYKFPK IKDADQEIEF QLFVETYQLV EPLIKERDAV YESLTYSSEL YVYSGLIWKT SRDMEEQTIF IGNIPLMNSL GTSIVNGIYR IVINQILQSP GIYYRSELDH NGISAYTATI ISDWGGRLEL EIDKKERMWA RVSRKQKISI LVLSSAMGSH LRQILENVCY PEIFLSFLNL NEKEKRRIGA KENATLEFYR QFFCISGDPG FSESLCKELQ QKFFQQKCEL GSIGRRNMNQ RLKLDIPQNN LFLLPRDILA AADHLIRMKL EMCTLDNMNH LKNKRIRSVA DLLQDQLGLA LVRLENFVQG TICRAIRHKW TPTPHNLVTS TPLTITYEYF FGLHPLSQVL DRTNPLTQIV HGRKSSHLGP GGLTERAASC FPIRDIHPSH YGRICPIDTS EGINVGLIGS LAIYARIGRW GSLESLFYVY EISAKKMRML YLSSSMDESY MVAAVNSLVL NLSIQEEQLV PARYRQEFLT IAWEQVHLRS IFPFQYFSIG ASLIPFIEHN DANRALMSSN MQRQAVPLSR SERCIVGTGL ERQAALDSGV PVMAERGGKI ISTDTDKILL SDSVETLSIS LIMYQRSNKN TCMYQKPKVW KDKCIKRGHI LADGTATVGG ELALGKNVLV AYMPWGGYNF EDAVLISERL VYKDIYTSFN IQKYEIKTHV TRQGPEKITT KIPHLESHLL RNLDKKGVVM LGSWVEAGDI LVGKLTPQMV KKLSYAPEDK LVRTILGIQV STSKETCLKL PTGGRGKVID VRWYCRKGGY NYNPETICVY ILQKREIKVG DKVAGRHGNK GIISKILPIQ DMLYLQDGRP VDMVFNPLGV PSRMNVGQIF ECSLGLAGSL LDRHYRIGAF DERYEQEASR KLVFSELYEA SRQRVNPWVF EPEYPGKSRI FDGRTGDSFD QPVIIGNPYI FKLIHQVDDK IHGRSSGHYA LVTQQPLRGR AKRGGQRVGE MEVWALEGLG VAHILQEMLT YKSDHIRARQ EVLGTTIVGR TISNPEDAPE SFRLLVRELR SLALEMNHFL VSEKNFRINR KEV //