ID A0A3N6FFW1_9ACTN Unreviewed; 340 AA. AC A0A3N6FFW1; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 10-APR-2019, entry version 2. DE RecName: Full=DNA-directed RNA polymerase subunit alpha {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|HAMAP-Rule:MF_00059}; DE AltName: Full=RNA polymerase subunit alpha {ECO:0000256|HAMAP-Rule:MF_00059}; DE AltName: Full=Transcriptase subunit alpha {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 RT of 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 CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {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, CC ChEBI:CHEBI:83400; EC=2.7.7.6; Evidence={ECO:0000256|HAMAP- CC 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 CC associated with the core the holoenzyme is formed, which can CC initiate transcription. {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- DOMAIN: The N-terminal domain is essential for RNAP assembly and CC basal transcription, whereas the C-terminal domain is involved in CC interaction with transcriptional regulators and with upstream CC promoter elements. {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family. CC {ECO:0000256|HAMAP-Rule:MF_00059}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 Proteomes; UP000279576; Unassembled WGS sequence. 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 PANTHER; PTHR32108; PTHR32108; 1. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF03118; RNA_pol_A_CTD; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR ProDom; PD001179; RNAP_asu_C; 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 Complete proteome {ECO:0000313|Proteomes:UP000279576}; KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059, KW ECO:0000313|EMBL:RPK70897.1}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059, KW ECO:0000313|EMBL:RPK70897.1}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_00059}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00059, KW ECO:0000313|EMBL:RPK70897.1}. FT DOMAIN 18 225 RPOLD. {ECO:0000259|SMART:SM00662}. FT REGION 1 229 Alpha N-terminal domain (alpha-NTD). FT {ECO:0000256|HAMAP-Rule:MF_00059}. FT REGION 232 340 Alpha C-terminal domain (alpha-CTD). FT {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 //