ID A0A1G3Z2H6_9BACT Unreviewed; 1386 AA. AC A0A1G3Z2H6; DT 18-JAN-2017, integrated into UniProtKB/TrEMBL. DT 18-JAN-2017, sequence version 1. DT 13-SEP-2023, entry version 26. DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322}; DE Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322}; DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322}; DE AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322}; DE AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322}; GN Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322}; GN ORFNames=A2007_00700 {ECO:0000313|EMBL:OHE71096.1}; OS Verrucomicrobia bacterium GWC2_42_7. OC Bacteria; Verrucomicrobiota. OX NCBI_TaxID=1802430 {ECO:0000313|EMBL:OHE71096.1, ECO:0000313|Proteomes:UP000184561}; RN [1] {ECO:0000313|EMBL:OHE71096.1, ECO:0000313|Proteomes:UP000184561} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=27774985; DOI=10.1038/ncomms13219; RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J., RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L., RA Williams K.H., Hubbard S.S., Banfield J.F.; RT "Thousands of microbial genomes shed light on interconnected biogeochemical RT processes in an aquifer system."; RL Nat. Commun. 7:13219-13219(2016). 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_01322, 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_01322, ECO:0000256|RuleBase:RU004279}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01322}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01322}; CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' CC and 1 omega subunit. When a sigma factor is associated with the core CC the holoenzyme is formed, which can initiate transcription. CC {ECO:0000256|HAMAP-Rule:MF_01322}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01322}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:OHE71096.1}. 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; MIDO01000115; OHE71096.1; -; Genomic_DNA. DR Proteomes; UP000184561; Unassembled WGS sequence. 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 CDD; cd02655; RNAP_beta'_C; 1. DR CDD; cd01609; RNAP_beta'_N; 1. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.150.390; -; 1. DR Gene3D; 1.10.1790.20; -; 1. DR Gene3D; 1.10.40.90; -; 1. DR Gene3D; 2.40.40.20; -; 1. DR Gene3D; 2.40.50.100; -; 3. DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1. DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1. DR HAMAP; MF_01322; RNApol_bact_RpoC; 1. DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime. DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact. 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; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain. DR InterPro; IPR038120; Rpb1_funnel_sf. DR NCBIfam; TIGR02386; rpoC_TIGR; 1. DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR SMART; SM00663; RPOLA_N; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_01322}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01322}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01322}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_01322}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_01322}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01322}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}. FT DOMAIN 237..516 FT /note="RNA polymerase N-terminal" FT /evidence="ECO:0000259|SMART:SM00663" FT REGION 1365..1386 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1368..1386 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 71 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT BINDING 73 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT BINDING 89 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT BINDING 462 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT BINDING 464 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT BINDING 466 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" SQ SEQUENCE 1386 AA; 152998 MW; 6F73DD8413538F50 CRC64; MSTQEVRDIL GFDQEQVFDY VGIAIAAPDV MRSWSKGEVK NPETINYRTF KPEPGGLFCQ RIFGPVRDYE CACGKYKRIK YKGVVCDRCG VEVTVSRVRR DRMGHIELAV PISHIWFLKS MPSRVGLLLD MTARDLEKVI YYENYIVIDP GKTPLEKKAL LSEQEFLQLQ EEYGDDAFFA KMGAEAIRIL LAELDLAQMV QEIEEEIHSS RSKQSKKKLA KRLKIISGFL NSGTRPEWMV LEVLPVIPPD LRPLVPLEGG RFATSDLNDL YRRVINRNNR LKNLLQLKTP DVIINNEKRM LQESVDALFD NGRHGRPVTA AGNRPLKSLS DMLKGKQGRF RQNLLGKRVD YSGRSVIVIG PELRLHQCGL PKKMALVLFE PFIIRRLKEL GFVHTVRGAR KMIENKSPEV WDILEEVTKG HPVLLNRAPT LHRLSIQAFE PQLIEGDAIR LHPLVCSAYN ADFDGDQMAV HVPLSLEAIL ESKLLMLASN NIFSPSSGKP VLTPSQDIVL GSYYLTVEPR RKPSEGERVP LLQSTREALA AEVEGMLSKH QWVDFVNPDF GRKTIFGNAA KKIIRTTVGR VIYNSIWPKS LGFVNGPVAK SKLGDMILNL YKIASTKQEA VDTLDRLKEM GFKIATKAGI SIGIGDMIIP TEKSGIVNKS RKRLEEVDSQ YQKGIITEGE RTNKVIDIWS SATDEIAKAT FACLESNEGK EGINPVFLMM DSGARGNRQQ VRQLCGARGL MAKPSGEIIE RPILSSFREG LSVLEYFVST HGTRKGLADT ALKTADAGYM TRKLCDVAMD CIISSLDDGN RDGVWKHAIY EGDDEVVKLS DRIVGRCSSE DVYSPLNPDE ILVKSGEILT PEVAEKIEDL GIDRVKIMSP LTHLKRGGLS AKAYGIDPAT NKLVEMGTAV GIIAAQSIGE PGTQLTMRTF HVGGVASQVL KNPEIRVRHN GQIKFKGLRL VQTADGASIV LNKTGSVIIM DKEDHELESY HIVAGAVLMV ADGSEIHKGD VLAMWDPHNI PILSEKGGSV GFKDMIPGVT VKRELDESTG RIATVVIEHK EDLNPTVEVK ALAGNKEGLS TGKVIATYAI PVGAQVVVHE GDEISPGALL AKTPRSASKT QDITGGLPRV AELFEARRPK DAAEMAKIDG IVSMGSTVRG KRRLIVSDTE TGQQEDHLIS HGRQIIVHVG DFVTKGQSLT EGAADPHEIL EILGPYAVQE YLISEIQKVY RLQGVVINDK HIELIVARML RKVRVTDPGD SDFFWGEQID RTAFIESNER IVEAGGQPGE GEPILLGVTK ASLETDSFIS AASFQETTRV LTEASTLGKV DKLSGFKENV IMGQLIPAGT GFHKYRRLKV VPMGNESVEP TDRSSQGKSV ELATIE //