ID A0A0K2LX27_9NOST Unreviewed; 314 AA.
AC A0A0K2LX27;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:ARBA00033070, ECO:0000256|HAMAP-Rule:MF_00059};
DE AltName: Full=Transcriptase subunit alpha {ECO:0000256|ARBA:ARBA00032524, ECO:0000256|HAMAP-Rule:MF_00059};
GN Name=rpoA {ECO:0000256|HAMAP-Rule:MF_00059};
GN ORFNames=AA650_06700 {ECO:0000313|EMBL:ALB40196.1};
OS Anabaena sp. WA102.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Anabaena.
OX NCBI_TaxID=1647413 {ECO:0000313|EMBL:ALB40196.1, ECO:0000313|Proteomes:UP000056652};
RN [1] {ECO:0000313|EMBL:ALB40196.1, ECO:0000313|Proteomes:UP000056652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WA102 {ECO:0000313|EMBL:ALB40196.1,
RC ECO:0000313|Proteomes:UP000056652};
RA Brown N.M.;
RT "The finished genome of an anatoxin-a-producing Anabaena isolate reveals
RT extensive genome rearrangement.";
RL Submitted (MAY-2015) 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: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_00059};
CC -!- SUBUNIT: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is 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 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 ---------------------------------------------------------------------------
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; CP011456; ALB40196.1; -; Genomic_DNA.
DR RefSeq; WP_027402086.1; NZ_CP011456.1.
DR AlphaFoldDB; A0A0K2LX27; -.
DR STRING; 1647413.AA650_06700; -.
DR GeneID; 79794806; -.
DR KEGG; awa:AA650_06700; -.
DR PATRIC; fig|1647413.5.peg.1586; -.
DR OrthoDB; 9805706at2; -.
DR Proteomes; UP000056652; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd06928; RNAP_alpha_NTD; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1.
DR Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 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 NCBIfam; TIGR02027; rpoA; 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 SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF47789; C-terminal domain of RNA polymerase alpha subunit; 1.
DR SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1.
DR SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 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 20..226
FT /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
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 241..314
FT /note="Alpha C-terminal domain (alpha-CTD)"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00059"
SQ SEQUENCE 314 AA; 34912 MW; 83F956285ED92A3F CRC64;
MAQFQIECVE SNAEESRSYY SKFVLEPLDR GQGTTVGNAL RRVLLSNLEG TSVTAVRIAG
VSHEFATVPG VREDVLEMLM RMKDVILKSY SSQPQIGRLL VNGPATVTVA HFDLPSEVEV
IDPTQYIATI AEGGKLEMEF RIERGKGYRT VERGREEATS LDFLQIDSVF MPVRKVNYSV
EETRDDGFLK DRLLLEVWTN GSISPQEALS SAAGILVDLF NPLKDISLEP TDTGSDIPDD
PTAQIPIEEL QLSVRAYNCL KRAQVNSVAD LLDYTQEDLL EIKNFGQKSA EEVVEALQRR
LGITLPQERS SKPS
//