ID A0A8E8U488_9ROSI Unreviewed; 1070 AA. AC A0A8E8U488; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 24-JAN-2024, entry version 7. 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:QWE50297.1}; OS Oxalis corymbosa. OG Plastid; Chloroplast {ECO:0000313|EMBL:QWE50297.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Oxalidales; Oxalidaceae; Oxalis. OX NCBI_TaxID=210382 {ECO:0000313|EMBL:QWE50297.1}; RN [1] {ECO:0000313|EMBL:QWE50297.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cujiang_4 {ECO:0000313|EMBL:QWE50297.1}; RA Li X.-P.; RL Submitted (MAY-2020) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QWE50297.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Cujiang_4 {ECO:0000313|EMBL:QWE50297.1}; RA Li X., Zhao Y., Tu X., Li C., Zhu Y., Zhong H., Liu Z.-J., Wu S., Zhai J.; RT "Comparative analysis of plastomes in Oxalidaceae: Phylogenetic RT relationships and potential molecular markers."; RL Plant Divers 0:0-0(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; MT522018; QWE50297.1; -; 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:QWE50297.1}; 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:QWE50297.1}; 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..315 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04561" FT DOMAIN 376..444 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04565" FT DOMAIN 581..979 FT /note="DNA-directed RNA polymerase subunit 2 hybrid- FT binding" FT /evidence="ECO:0000259|Pfam:PF00562" FT DOMAIN 981..1056 FT /note="RNA polymerase Rpb2" FT /evidence="ECO:0000259|Pfam:PF04560" SQ SEQUENCE 1070 AA; 120806 MW; EF1BF7B1F73F24D4 CRC64; MLLDGNEGMS TIPGFNQIQF EGFYRFIDQG LTEELYKFPK MEDTEQEIEF QLFVETHQLV EPVIKERDAV YKSLTYSSEL YVSAGLIWKT CRDMQEQTIF IGNIPLMNSL GTSIVNGIYR IVINQILQSP GIYYRSELDH NGISVYTGTI ISDWGGRVEL EIDRKARIWA RVSRKQKISI LVLSSAMGSN LREILENVCY PEIFLSFLND KEKKKIGSKE NAILEFYQQF TCVGGDPVFS ESLCKELQKK FFQQRCELGR IGRRNMNQRL NLDIPQNNTF LLPRDILAAA DRLIGMKFGM GTLDDMNHLK NKRIRSVADL LQDQFGLALV RLENVVRGTI CGAIRHKLIP TPQNLVTSTP LTSTYESFFG LHPLSQVLDR TNPLTQIVHG RKLSYLGPGG LTGRTASFRI RDIHPSHYGR ICPIDTSEGI NVGLIGSLSI HARIGRWGSL ESPFYKISEG SNKVRMLYLS PNRDEYYMVA AGNSLALNRG IQEEQVVPAR YRQEFLTVAW EQVHLRSIFP FQYFSIGASL IPFIEHNDAN RALMSSNMQR QAVPLSRSEK CIVGTGLERQ VALDSGVLAI AEHGGRVVYT DTEKIILSEN GNTFSIPLVM YQRSNKNTCM HQKPQAQLGK CIKKGQILAD GAATVGGELA LGKNVLVAYM PWEGYNFEDA VLVSERLVYG DIYTSFHIRK YEIQTHVTSQ GPERITNEIP HLEAHLLRNL DKNGIVVLGS WVETGDILVG KLTPQMSKES SYAPEDRLLR AILGIQVSTS KETCLKLPIG GRGRVIDIRW IQKKGGSSYN PEKISVYISQ KREIKVGDKV AGRHGNKGII SKILPRQDMP YLQDGRPIDM VFNPLGVPSR MNVGQIFECS LGLAGVLLDR HYRIAPFDER YEQEASRKLV FSELYEASKQ TANPWVFEPE YPGKSRIFDG RTGDPFEQPL IIGKPYILKL IHQVDDKIHG RSSGHYALVT QQPLRGRAKQ GGQRIGEMEV WALEGFGVSH ILQEMLTYKS DHIRARQEVL GTTIIGGTIS KPEDAPESFR LLVRELRSLA LELNHFLVSE KNFQINKKEV //