ID A0A221SCQ3_ANEPI Unreviewed; 695 AA. AC A0A221SCQ3; DT 25-OCT-2017, integrated into UniProtKB/TrEMBL. DT 25-OCT-2017, sequence version 1. DT 14-DEC-2022, entry version 19. DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01323}; DE AltName: Full=PEP {ECO:0000256|HAMAP-Rule:MF_01323}; DE AltName: Full=Plastid-encoded RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; DE Short=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01323}; GN Name=rpoC1 {ECO:0000256|HAMAP-Rule:MF_01323, GN ECO:0000313|EMBL:ASN73783.1}; OS Aneura pinguis (Greasewort) (Riccardia pinguis). OG Plastid; Chloroplast {ECO:0000313|EMBL:ASN73783.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta; OC Jungermanniopsida; Metzgeriidae; Metzgeriales; Aneuraceae; Aneura. OX NCBI_TaxID=39026 {ECO:0000313|EMBL:ASN73783.1}; RN [1] {ECO:0000313|EMBL:ASN73783.1} RP NUCLEOTIDE SEQUENCE. RA Sawicki J.; RT "The extraordinary variation of the organellar genomes of the Aneura RT pinguis revealed advanced cryptic speciation of the early land plants."; RL Submitted (MAR-2017) 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_01323, ECO:0000256|RuleBase:RU004279}. 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_01323, ECO:0000256|RuleBase:RU004279}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01323}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01323}; CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01323}; 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_01323}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000256|HAMAP- CC Rule:MF_01323}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC1 CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01323}. 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; KY702720; ASN73783.1; -; Genomic_DNA. DR AlphaFoldDB; A0A221SCQ3; -. 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:0000287; F:magnesium ion binding; 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 Gene3D; 1.10.274.100; -; 1. DR Gene3D; 4.10.860.120; -; 1. DR HAMAP; MF_01323; RNApol_bact_RpoC1; 1. DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime. DR InterPro; IPR000722; RNA_pol_asu. DR InterPro; IPR006592; RNA_pol_N. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf. DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain. DR InterPro; IPR034678; RNApol_RpoC1. DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 2. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR SMART; SM00663; RPOLA_N; 1. PE 3: Inferred from homology; KW Chloroplast {ECO:0000313|EMBL:ASN73783.1}; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01323}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01323}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01323}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01323}; Plastid {ECO:0000313|EMBL:ASN73783.1}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01323}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01323}; Zinc {ECO:0000256|HAMAP-Rule:MF_01323}. FT DOMAIN 262..543 FT /note="RPOLA_N" FT /evidence="ECO:0000259|SMART:SM00663" FT BINDING 69 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 87 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 90 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 489 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 491 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" FT BINDING 493 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01323" SQ SEQUENCE 695 AA; 80459 MW; 7FD206EE58DC794D CRC64; MIHRIKYQRL RIELASPEQI RNWAERKLPD GEIVGRVTKP YTLHYKTHKP EKDGLFCERI FGPVKSGVCI CGRYKGIAGG KETTKFCEHC GVDLTKSRIR RYRMGYIELA CPVTHVWYLK RLPSCIANLL DKPLKELESL VHCDLFTARP INEKPTLLKL HGLFKYEDQS WRDVFPRFFS CGGFEIFHDR EIATGGDAIK KQLIDLDLQG VMSHAHSEWK ELTKQESTGT DWGDRKIQRN KDLLVRRMKL SKYFVQTNIK PEWMVLSLLP VLPPELRPMI ELGEGELITS DLNELYRRVI YRNNTLLDFL ARSDSTPGGL IVCQKRLVQE AVDALIDNGI RGQPMRDNHN RPYKSFSDLI EGKEGRFREN LLGKRVDYSG RSVIVVGPSL PLHRCGLPRE MAMELFQAFV IRGLIGRNLA LNLRAAKTMI RGNKPIIWKI LQEVMEEHPI LLNRAPTLHR LGIQAFQPVL VHGRAIHLHP LVRSGFNADF DGDQMAVHVP LSLEAQVEAR LLMLSRRNLL SPATGEPLCI PSQDMLLGLY ALTMENRQGI YGNKYSLDNN KETYLKNLSF PKISYFHGYE DVYKAHRQRE IHSHSILWLR WQTNFRMITS MTREEPIEIQ YETSGISYRI YDHYQLEINA QRGIISIYIC TTVGRVLFNQ RIDEAIQGTC QASSRRNMVY MEERFLISLI RKFES //