ID A0A290DMP2_9ASPA Unreviewed; 1380 AA. AC A0A290DMP2; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 16-JAN-2019, entry version 6. DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01324}; DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01324}; DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; DE Short=RNA polymerase subunit beta'' {ECO:0000256|HAMAP-Rule:MF_01324}; GN Name=rpoC2 {ECO:0000256|HAMAP-Rule:MF_01324, GN ECO:0000313|EMBL:ATB18719.1}; OS Barnardia japonica. OG Plastid; Chloroplast {ECO:0000313|EMBL:ATB18719.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Asparagales; Hyacinthaceae; OC Hyacinthoideae; Hyacintheae; Barnardia. OX NCBI_TaxID=2033023 {ECO:0000313|EMBL:ATB18719.1}; RN [1] {ECO:0000313|EMBL:ATB18719.1} RP NUCLEOTIDE SEQUENCE. RA Park H., Kim C., Kim J.-H.; RT "The comparative plastid genome analysis and its phylogenetic RT implication on Asparagaceae s.l."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. 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_01324}. 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_01324}; 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_01324}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01324}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC RpoC2 subfamily. {ECO:0000256|HAMAP-Rule:MF_01324}. 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; KX822775; ATB18719.1; -; 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 Gene3D; 1.10.132.30; -; 1. DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1. DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR038120; Rpb1_funnel_sf. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 2. DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ATB18719.1}; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_01324}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01324}; KW Plastid {ECO:0000313|EMBL:ATB18719.1}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_01324}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01324}. FT DOMAIN 95 157 RNA_pol_Rpb1_4. {ECO:0000259|Pfam: FT PF05000}. FT DOMAIN 172 388 RNA_pol_Rpb1_5. {ECO:0000259|Pfam: FT PF04998}. FT DOMAIN 1184 1271 RNA_pol_Rpb1_5. {ECO:0000259|Pfam: FT PF04998}. SQ SEQUENCE 1380 AA; 156695 MW; B1E8D9BAFDF784E5 CRC64; MAERADLVFH NKVIDGAAMK RLISRLIDHF GMAYTSHILD QVKTLGFQQA TATSISLGID DLLTIPSKGW LVQDAEQQSF ILEKHHHYGN VHAVEKLRQS IEIWYATSEY LRQEMNPNFR MTDPSNPVHL MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIIVRRTDC GTIRGISVSP WSGVTEKIFV QTLIGRVLAD DIYMGIRCIA TRNQDIGIGL ANRFITFRAQ PIYIRTPFTC RNTSWICQLC YGRSPTHGDL VELGGAVGII AGQSIGEPGT QLTLRTFHTG GVFTGGTAEH VRAPSNGKIK FNEYLVHPTR TRHGHPAFLC SIDLYVTIES RDIIHNVNIP PKSLILVQND QYVESEQVIA EIRAGASTFH LKEKVRKHIY SESQGEMHWS TDVYHAPEYT YSNVHLLPKT SHLWILAGSP CRSSIVSFSL HKDQDQMNVH SFSVDEIDIS DLSITNDRVR HKLLGPSGKK DREILDYSRL DRSISNGHSN FMYPSILQEN SDFLAKRRRN RFLIPLQYDQ EREKELIPSF GISIEIPING ILRRKSILAY FDDPRYRRKS SGITKYGTVE VDSIVKKEDL IEHRGAKEFS PKYQMKVDRF FFIPEEVHIL PGSSSIMVRN NSIIGVDTQL ALNTNTRSRV VGLVRVERKK KSIELKIFSG DIHFPGETDK ISRHSGILIP PGTEKKNSNE SKKWKNWIYV QRITPTKKKY FVLVRPVVTY EIADGINLAK LFTQDLLQEK DNVQLRVVNY ILYGNGKSIR GIYHTSIQLV RTCLVLNWDQ EKNGSIEEVH ASFVEVRAND LIFDFIRIEL VKFTISYTGK RYDTAGSGLI PDNGLDRTNI NPFYSKAKIP LVTQHQGTIG TLLNRNKECQ SLRILSSVNC FRVGPFNGSK YNNVAKESNP VTPIRDLLGP LGTIVPKTVN FYSSYHLITH NKILLNKYWL FDIHNFKQTF QVLEILKYCL IDENRSIYNP GPCIILNPFR LNWCFLHHNY CEETFTIISI GQFICENICL FKYGPHIKKS GQILIVHIDS LIIRSAKPYL ATPGATVHGH YGETLSEGDT LVTFIYEKSR SGDITQGLPK VEQILEVRSI GSISMNLERR VEGWNERIPR ILGIPWRFLI GAELTIAQSR TSLVNKIQKV YRSQGVQIHN RHIEIIVRQV TSKVLVSEDG MSNVFLPGEL IVLLRAERAG RALDEAICYR AILLGITRAS LNTQSFISEA SFQETARVLA KAALRGRIDW LKGLKENVVL GGIIPVGTGF KKLVHRSRQD KNICLEIKKK SLFELEMRDI LLYHREFFCS CAPSNFYDTP EKSFTRIHNS //