ID A0A5Q2MMF6_9MAGN Unreviewed; 1385 AA. AC A0A5Q2MMF6; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 27-NOV-2024, entry version 15. 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:QGG43788.1}; GN ORFNames=LiagCp011 {ECO:0000313|EMBL:QGG43788.1}; OS Lindera aggregata. OG Plastid; Chloroplast {ECO:0000313|EMBL:QGG43788.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Magnoliidae; Laurales; Lauraceae; Lindera. OX NCBI_TaxID=545644 {ECO:0000313|EMBL:QGG43788.1}; RN [1] {ECO:0000313|EMBL:QGG43788.1} RP NUCLEOTIDE SEQUENCE. RA Jo S., Kim Y.-K., Cheon S.-H., Fan Q., Kim K.-J.; RT "Characterization of 20 complete plastomes from the tribe Laureae RT (Lauraceae) and distribution of small inversions."; RL PLoS ONE 14:0-e0224622(2019). RN [2] {ECO:0000313|EMBL:QXP99429.1} RP NUCLEOTIDE SEQUENCE. RA yuan x.L.; RT "The complete chloroplast genome of Lindera aggregate (Sims) Kosterm."; RL Submitted (APR-2021) 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=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + CC diphosphate; 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|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; MG581437; QGG43788.1; -; Genomic_DNA. DR EMBL; MZ027676; QXP99429.1; -; 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:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd02655; RNAP_beta'_C; 1. DR FunFam; 1.10.132.30:FF:000002; DNA-directed RNA polymerase subunit beta; 1. DR FunFam; 1.10.1790.20:FF:000002; DNA-directed RNA polymerase subunit beta; 1. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.150.390; -; 1. DR Gene3D; 1.10.1790.20; -; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1. DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1. DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp. DR InterPro; IPR050254; RNA_pol_beta'_chain. 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 NCBIfam; TIGR02388; rpoC2_cyan; 1. DR PANTHER; PTHR48355; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR PANTHER; PTHR48355:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 2. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:QGG43788.1}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01324}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01324}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01324}; KW Plastid {ECO:0000256|ARBA:ARBA00022640, ECO:0000313|EMBL:QGG43788.1}; 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 94..157 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF05000" FT DOMAIN 172..364 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF04998" FT DOMAIN 1184..1269 FT /note="RNA polymerase Rpb1" FT /evidence="ECO:0000259|Pfam:PF04998" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 290 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 297 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" FT BINDING 300 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01324" SQ SEQUENCE 1385 AA; 157388 MW; 3F1C4F49E29B0DF2 CRC64; MAEWADLFFY NKAIDGSAMK RLISRLIDHF GMAYTSHTLD QVKTLGFQQA TATSISLGID DLLTVPSKGW LVQDAEQQSF ILEKHHHYGN VHTVEKLRQS IEIWYATSEY LRQEMHPNFR MTDPSNSVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVVRRTDC GTTRGISVSP RNGMTERIWV QTLIGRVLAY NIYMGPRCIA AQNKDIGVGL VTRFITFRTQ PIYIRTPFLC RSISWICRLC YGQSPTHGDL VELGEAVGII AGQSIGEPGT QLTLRTFHTG GVFTGGTAEH VRAPFKGKIK FNEDLVHPTR TRHGHPAFLC YIDLYVTIES HDILHNVNIP PKSFLLVQND QYVESEQVIA EIRAGTSTFN FNKVKEKVRK HIYSDSEGEM HWSTDVYHAP EYKYGNVHLL PKTSHLWILS GALCRSSIVP FSLHKDQDQM NVHSVERRSI SDLSVTNDQV RHKLFSSNPY GKKGGVLDYS GPDRIISNGH WNFIYPPILH ENSDLLAKRR RNRFIIPFQS DQEREKELMP RSGISIEIPI NGVLPRNSIL AYFDDPLYRR SSSGITKYGT IGVGSIVKKE DLIEYRRAKE FRPKYQMKVD RFFFIPEEVH ILPGSSPIMV RNNSIIGVDT RIALNTRSQV GGLVRVERKK KRIELKIFSG DIYFPGATDK ISRHCGILIP PGTGKKNSKE SKKWKNWIYV QRITPTKKKY FVSVRPVVTY EIADGINLAT LFPQDPLQER DNVQLRIVNY ILYGNGKPIR GIYHTSLQLV RTCLVLNWNQ DRDGSIEEVH ASFVEVRAND LIRDFIRIDL VKSSIFYIGK RNDMASSGLI ANNGSDRTNI NPFYFKARIQ SFTQHQGTIR TLLNRNKECP SFLILLSSDC SRIGLFNGSK SHKELIKLIK EDPAIPIRNS LGPLGVVPKI TNFYSFYYFY LITHNQILLK KYFLLDNFKH TFQGLKYYLM DENGRIYNPD SCSNIIFNPF DLNWCFLPHD YCEETSTIIS LGQFICENVC ISKCGPHIKS SQVLIVHVDS LVIRSAKPHL ATPGATVHGH CGEILYEGDT LVTFIYEKSR SGDITQGLPK VEQVLEARSI DSISMNLEKR VEGWNERITR ILGIPWGFLI GAELTIAQSR ISLVNKIQKV YRSQGVQIHN RHIEIIVRQI TSKVLVSEDG MSNVFSPGEL IGLLRAERTG RALEEAICYR AILLGITRAS LNTQSFISEA SFQETARVLA KAALRGRIDW LKGLKENVVL GGMMPVGTGF KGLVHRSRQH SNIPLEIKKK NLFEEEMRDL LFHHRELFGS CIPNNFPDTS ERSFTGFNDR FILFF //