ID A0A5C7EQP6_9ACTN Unreviewed; 1497 AA. AC A0A5C7EQP6; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 22-APR-2020, entry version 4. 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=E4J93_07950 {ECO:0000313|EMBL:TXF34637.1}; OS Collinsella sp. BA40. OC Bacteria; Actinobacteria; Coriobacteriia; Coriobacteriales; OC Coriobacteriaceae; Collinsella; unclassified Collinsella. OX NCBI_TaxID=2560852 {ECO:0000313|EMBL:TXF34637.1, ECO:0000313|Proteomes:UP000321063}; RN [1] {ECO:0000313|EMBL:TXF34637.1, ECO:0000313|Proteomes:UP000321063} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BA40 {ECO:0000313|EMBL:TXF34637.1, RC ECO:0000313|Proteomes:UP000321063}; RA Park J.-K.; RT "Collinsella canisensis sp. nov., a novel bacterium isolated from canine RT feces."; RL Submitted (AUG-2019) 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_01322, ECO:0000256|RuleBase:RU004279, CC ECO:0000256|SAAS:SAAS00054030}. 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|HAMAP-Rule:MF_01322, CC ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS01121830}; 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: 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:TXF34637.1}. 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; VOWY01000023; TXF34637.1; -; Genomic_DNA. DR Proteomes; UP000321063; Unassembled WGS sequence. 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:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR Gene3D; 1.10.132.30; -; 1. DR Gene3D; 1.10.274.100; -; 1. DR HAMAP; MF_01322; RNApol_bact_RpoC; 1. DR InterPro; IPR012754; 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; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR011260; RNAP_asu_C. DR InterPro; IPR038120; Rpb1_funnel_sf. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 1. 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 TIGRFAMs; TIGR02386; rpoC_TIGR; 1. PE 3: Inferred from homology; KW Coiled coil {ECO:0000256|SAM:Coils}; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_01322, KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442970, KW ECO:0000313|EMBL:TXF34637.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|SAAS:SAAS01207259}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01322, KW ECO:0000256|SAAS:SAAS01207262}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_01322, KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442967}; KW Reference proteome {ECO:0000313|Proteomes:UP000321063}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_01322, KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00442998}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01322, KW ECO:0000256|RuleBase:RU004279, ECO:0000256|SAAS:SAAS00443006}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|SAAS:SAAS01207265}. FT DOMAIN 310..589 FT /note="RPOLA_N" FT /evidence="ECO:0000259|SMART:SM00663" FT REGION 1473..1497 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 144..179 FT /evidence="ECO:0000256|SAM:Coils" FT METAL 62 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 64 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 77 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 80 FT /note="Zinc 1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 535 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 537 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 539 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 893 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 964 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 971 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" FT METAL 974 FT /note="Zinc 2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01322" SQ SEQUENCE 1497 AA; 165804 MW; 26BD31A20C5156DA CRC64; MADFEATDFD AVKISLASAD TIRSWSHGEV KKPETINYRT LKPEKDGLFC EKIFGPAKDW ECSCGKYKGI RFKGIVCERC GVEVTSAKVR RERMGHIELA APVSHIWYFK SPTSFPMSRL LDIKSKDLEK VLYFASYIIT HVDYDAREAD AEDLREELAA DLEEIDAECA RQIESLKEQG NPENFDEFSD EEPLTQEEIA AGIIDIEEEC KDEKQLRSDA FQAFMKLSER DLISDEPLFR EMKRYYSMYF SGDMGAEAVR DLLAAIDLES ESERLKAIIA DEDGQKQKRE KAVKRLEVVD AFLKGHNDPA NMILDVIPVI PPDLRPMVQL DGGRFAASDL NDLYRRVINR NNRLKRLLDL DAPAIIVNNE KRMLQEAVDA LFDNGRRGRP VSGRGGRPLK SLAEALKGKQ GRFRQNLLGK RVDYSGRSVI VTDPTLKLHQ CGLPKTMALE LFKPFVMKRL VELGKVENIK GAKRSIERGA SFVWDILEEV IDGRLVLLNR APTLHRLSIQ AFEPVLVEGK AIHLHPLVCA PFNADFDGDQ MSVHVPLSLQ AQAEARVLML SANNLRSPAS GKPVNVPSQD MIIGVYYLTQ ARDGLSGEGH VFASFDDALN AYDARTEVDL QAKVQVRVSA ADANHFEGEK SFFRVKNDRN EFVDYDVTGT KTCRFETTIG RIIFNRQCLP ADYEFINYKM VKGDVGKLVA ACCDRYPQAE VGPILDAIKY AGFHFATRAG LTISLWDALI PDEKPQILAE AQDRVDSINE YFEEGFINEM ERHTEVVNEW TAATDKVAAL MLDMFDEENP IYMMADSGAR GSKTQLRQLG GMRGLMADMS GETIDLPIKA NFREGLLPLE YFISTYGARK GLVDTASHTS DSGYLTRRLV DVAQDVIVRE EDCGTEEGCT YNLIIPGTDS INADLVGRCF SEDAVAADGT VVFKRGEYIE TTADINKLLD AGLKKVTLRA LLTCRSKYGV CQKCYGWDLS TRRPVAIGTA VGIIAAQSIG EPGTQLTMRT IHSGGVAGVD DITQGLPTVG RMFDVVGNVN EKILGREADL APFSGHLAIK PEKSEYVLTL TDSSDHSRVL EEKRVPASVR FMPGIEDGCE VRAGDQITKG FVNFRNLRKL TDIESTMHTF VENVKDVYTS QGVDLNDKHI EVIARQMLRR VQITNPGDSN YLLGQYVDRY EFADEVDRIA RRGGATPAAE PAILGTLKVA SSIDSWLSSA SFIRTAGVLT EAAIEGKVDH LLDLKSNVIV GKKIPVGTGL KPYSDAALTY RTSDGYVTVG GATAGNSKAL PEWAPEELKE LDEQLPQQLD WSGYDDYGSG DGSFTRNGRT ISAEDARLYL FDDLGVSQRW TNKFSEVGIE TVGDLVGKSE EDLLRIDGIG AKAIEELRDG LEAHNLLYIL DNTEDVADEE DLSQLLQMVF SPDGPDDILL GTSAPRHHYD SDEEMIGGAP SASGKDAGNG GIINEDMASI DELLNQLVDQ DDGDSPEDPN GHNSYEE //