ID A0A290DMP2_9ASPA Unreviewed; 1380 AA. AC A0A290DMP2; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 12-AUG-2020, entry version 12. 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; Magnoliopsida; 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 implication RT on Asparagaceae s.l."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AZL35659.1} RP NUCLEOTIDE SEQUENCE. RA Wang R.-H., Gao J., Li M., Wu X., Shen C., Wu J., Qi Z.-C., Li P.; RT "The complete chloroplast genome sequences of Barnardia japonica (Thunb.) RT Schult. and Schult.f."; RL Mitochondrial DNA Part B Resour 3:697-698(2018). RN [3] {ECO:0000313|EMBL:AZL35659.1} RP NUCLEOTIDE SEQUENCE. RA Wang R., Qi Z., Li P., Gao J.; RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates. CC {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, ChEBI:CHEBI:83400; CC EC=2.7.7.6; Evidence={ECO:0000256|ARBA:ARBA00000097, CC ECO:0000256|HAMAP-Rule:MF_01324}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01324}; CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01324}; 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_01324}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01324}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2 CC 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 EMBL; MH287351; AZL35659.1; -; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.274.100; -; 1. DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1. DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp. DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf. 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|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01324}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01324}; Plastid {ECO:0000313|EMBL:ATB18719.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01324}. FT DOMAIN 95..157 FT /note="RNA_pol_Rpb1_4" FT /evidence="ECO:0000259|Pfam:PF05000" FT DOMAIN 172..388 FT /note="RNA_pol_Rpb1_5" FT /evidence="ECO:0000259|Pfam:PF04998" FT DOMAIN 1184..1271 FT /note="RNA_pol_Rpb1_5" FT /evidence="ECO:0000259|Pfam:PF04998" FT METAL 220 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT METAL 290 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT METAL 297 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT METAL 300 FT /note="Zinc" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" 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 //