ID A0A3N6FFW1_9ACTN Unreviewed; 340 AA. AC A0A3N6FFW1; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 02-JUN-2021, entry version 9. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00015972, ECO:0000256|HAMAP-Rule:MF_00059}; DE Short=RNAP subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000256|ARBA:ARBA00016404, ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {ECO:0000256|ARBA:ARBA00021853, ECO:0000256|HAMAP-Rule:MF_00059}; GN Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059, GN ECO:0000313|EMBL:RPK70897.1}; GN ORFNames=EES44_04385 {ECO:0000313|EMBL:RPK70897.1}; OS Streptomyces sp. ADI96-15. OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae; OC Streptomyces. OX NCBI_TaxID=1522761 {ECO:0000313|EMBL:RPK70897.1, ECO:0000313|Proteomes:UP000279576}; RN [1] {ECO:0000313|EMBL:RPK70897.1, ECO:0000313|Proteomes:UP000279576} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ADI96-15 {ECO:0000313|EMBL:RPK70897.1, RC ECO:0000313|Proteomes:UP000279576}; RA Guerrero-Garzon J.F., Zehl M., Urban E., Schneider O., Ruckert C., RA Busche T., Kalinowski J., Zotchev S.B.; RT "Streptomyces spp. from the marine sponge Antho dichothoma: analyses of RT secondary metabolite biosynthesis gene clusters and some of their RT products."; RL Submitted (NOV-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_00059}. 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_00059}; CC -!- SUBUNIT: Homodimer. The RNAP catalytic core consists of 2 alpha, 1 CC beta, 1 beta' and 1 omega subunit. When a sigma factor is associated CC with the core the holoenzyme is formed, which can initiate CC transcription. {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and basal CC transcription, whereas the C-terminal domain is involved in interaction CC with transcriptional regulators and with upstream promoter elements. CC {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000256|ARBA:ARBA00007123, ECO:0000256|HAMAP-Rule:MF_00059}. 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:RPK70897.1}. 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; RPGX01000115; RPK70897.1; -; Genomic_DNA. DR RefSeq; WP_003948616.1; NZ_ML123107.1. DR EnsemblBacteria; RPK70897; RPK70897; EES44_04385. DR GeneID; 15147580; -. DR Proteomes; UP000279576; 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:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule. DR Gene3D; 2.170.120.12; -; 1. DR Gene3D; 3.30.1360.10; -; 1. DR HAMAP; MF_00059; RNApol_bact_RpoA; 1. DR InterPro; IPR011262; DNA-dir_RNA_pol_insert. DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. DR InterPro; IPR011773; DNA-dir_RpoA. DR InterPro; IPR036603; RBP11-like. DR InterPro; IPR011260; RNAP_asu_C. DR InterPro; IPR036643; RNApol_insert_sf. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF55257; SSF55257; 1. DR SUPFAM; SSF56553; SSF56553; 1. DR TIGRFAMs; TIGR02027; rpoA; 1. PE 3: Inferred from homology; KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478, KW ECO:0000256|HAMAP-Rule:MF_00059}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP- KW Rule:MF_00059}; KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP- KW Rule:MF_00059}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00059}. FT DOMAIN 18..225 FT /note="RPOLD" FT /evidence="ECO:0000259|SMART:SM00662" FT REGION 1..229 FT /note="Alpha N-terminal domain (alpha-NTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" FT REGION 238..340 FT /note="Alpha C-terminal domain (alpha-CTD)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059" SQ SEQUENCE 340 AA; 36684 MW; FBE7F028C96C7FB3 CRC64; MLIAQRPSLT EEVVDEFRSR FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRIDGVL HEFTTVPGVK EDVTDLILNI KQLVVSSEHD EPVVMYLRKQ GPGLVTAADI APPAGVEVHN PDLVLATLNA KGKLEMELTV ERGRGYVSAV QNKQAGQEIG RVPVDSIYSP VLKVTYKVEA TRVEQRTDFD KLIVDVETKQ AMRPRDAMAS AGKTLVELFG LARELNVDAE GIDMGPSPTD AALAADLALP IEELELTVRS YNCLKREGIH SVGELVARSE ADLLDIRNFG AKSIDEVKAK LAGMSLALKD SPPGFDPTAA ADAFGADDDA DAGFVETEQY //