ID A0A1J0PKA6_PINMU Unreviewed; 1075 AA. AC A0A1J0PKA6; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 07-NOV-2018, entry version 12. 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:APD51969.1}; OS Pinus mugo subsp. x rotundata. OG Plastid; Chloroplast {ECO:0000313|EMBL:APD51969.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Pinidae; Pinales; Pinaceae; Pinus; Pinus. OX NCBI_TaxID=689842 {ECO:0000313|EMBL:APD51969.1}; RN [1] {ECO:0000313|EMBL:APD51969.1} RP NUCLEOTIDE SEQUENCE. RA Celinski K., Kijak H., Barylski J., Grabsztunowicz M., RA Wojnicka-Poltorak A., Chudzinska E.; RT "Characterization of the complete chloroplast genome of Pinus RT uliginosa (Neumann) from the Pinus mugo complex."; RL Conserv Genet Resour 0:0-0(2016). 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: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000256|HAMAP-Rule:MF_01321, CC 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 -!- 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; KX833097; APD51969.1; -; 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: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; 2.40.270.10; -; 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; 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:APD51969.1}; 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:APD51969.1}; 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 17 356 RNA_pol_Rpb2_1. {ECO:0000259|Pfam: FT PF04563}. FT DOMAIN 129 320 RNA_pol_Rpb2_2. {ECO:0000259|Pfam: FT PF04561}. FT DOMAIN 379 447 RNA_pol_Rpb2_3. {ECO:0000259|Pfam: FT PF04565}. FT DOMAIN 585 984 RNA_pol_Rpb2_6. {ECO:0000259|Pfam: FT PF00562}. FT DOMAIN 986 1060 RNA_pol_Rpb2_7. {ECO:0000259|Pfam: FT PF04560}. SQ SEQUENCE 1075 AA; 122610 MW; B9A01D31CA22C6D2 CRC64; MRLDENEGAF TIPEFGKIQF EGFCRFIDQG LMEELHNFPK IEDIDKEIEF RLFGNEYELA EPFIKERDAV YQSLTYYSEL YVPARSIRRN SRKIQKQTVF LGNIPLMNSH GTFVLNGIYR VVVNQILISP GIYYRSELDH NRINYIYTGT LISDWGRRSK LEIDVGERIW ARVSRKQKIS IPVLLSAMGL NLEEILDNTR YPERFLFLLK KKERWEREEY LWSREKAILE FYKKLYCISG DLVFSESLCK ELQKKFFRKR CELGKIGRRN LNQKLNLDIP ENEIFSLPQD VLAAVDYLIG VKFGMGTLDD IDHLRNRRIR SVADLLQNQF RLALGRLEDA VKRTIRRATK RRSTPQNLVT STLLKNTFQD FFGSHPLSQF LDQTNPLTEI AHGRKLSHLG PGGLTGRTAS FRTRDIHPSY YGRICPIDTS EGMNAGLVAS LSIHAKIGDC GSLQSPFYKI SERSREEHMV YLLPGEDEDE YYRIATGNSL ALNQGIQEEQ ITPARYRQEF IVIAWEQIHF RSIFPFQYFS VGVSLIPFLE HNDANRALMG SNMQRQAVPL FRPEKCIAGT GLEGQAALDS GSVAIATQEG RIEYIDAVNI TSSVNGDTVR TESVIYQRSN TNTCTHQKPQ IHQGECVKKG QILADGATTV GGELSLGKNV LVAYMPWEGY NFEDAILISE RLVYEDIYTS FHIVRYRIEI CMTRQGPERI TREIPHLDAH LLRHLDENGL VMLGSWIETG DVLVGKLTPQ TIEESLCTPE GRLLQTIFGI EVSTARENCL RAPIGGRGRV IDVRWINRVD DSGDNAETVH VYISQKRKIQ VGDKVAGRHG NKGIISIVLP RQDMPYLQNG IPVDMVLNPL GVPSRMNVGQ IFECLPGLAG NPMNKHYRIT PFDEKYEREA SRKLVFPELY KASEQTANPW VFEPDHPGKH RLIDGRTGDV FEQPVTIGKA YMSKLSHQVD EKIHARSSGP YARVTQQPLR GKSKRGGQRI GEMEVWALEG FGVAYILQEM LTLKSDHIRT RNEVLGAIIT GGPIPKPDTA PESFRLLIRE LRSLALELNH AIISEKNFQI DREEV //