(data stored in ACNUC7421 zone)

SWISSPROT: RPOA2_STRAW

ID   RPOA2_STRAW             Reviewed;         338 AA.
AC   Q82QR5;
DT   02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   08-MAY-2019, entry version 105.
DE   RecName: Full=DNA-directed RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            Short=RNAP subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00059};
DE   AltName: Full=RNA polymerase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
DE   AltName: Full=Transcriptase subunit alpha {ECO:0000255|HAMAP-Rule:MF_00059};
GN   Name=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00059};
GN   OrderedLocusNames=SAV_440;
OS   Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 /
OS   NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=227882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=11572948; DOI=10.1073/pnas.211433198;
RA   Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C.,
RA   Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T.,
RA   Kikuchi H., Shiba T., Sakaki Y., Hattori M.;
RT   "Genome sequence of an industrial microorganism Streptomyces
RT   avermitilis: deducing the ability of producing secondary
RT   metabolites.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 /
RC   NRRL 8165 / MA-4680;
RX   PubMed=12692562; DOI=10.1038/nbt820;
RA   Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T.,
RA   Sakaki Y., Hattori M., Omura S.;
RT   "Complete genome sequence and comparative analysis of the industrial
RT   microorganism Streptomyces avermitilis.";
RL   Nat. Biotechnol. 21:526-531(2003).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
CC       of DNA into RNA using the four ribonucleoside triphosphates as
CC       substrates. {ECO:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00059}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase alpha chain family.
CC       {ECO:0000255|HAMAP-Rule:MF_00059}.
DR   EMBL; BA000030; BAC68150.1; -; Genomic_DNA.
DR   RefSeq; WP_010981878.1; NZ_BAVY01000048.1.
DR   SMR; Q82QR5; -.
DR   STRING; 227882.SAV_440; -.
DR   EnsemblBacteria; BAC68150; BAC68150; SAVERM_440.
DR   KEGG; sma:SAVERM_440; -.
DR   eggNOG; ENOG4105CTF; Bacteria.
DR   eggNOG; COG0202; LUCA.
DR   HOGENOM; HOG000218480; -.
DR   KO; K03040; -.
DR   OMA; WGVTIGN; -.
DR   OrthoDB; 662686at2; -.
DR   BioCyc; SAVE227882:G1G23-496-MONOMER; -.
DR   Proteomes; UP000000428; Chromosome.
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   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;
DR   PRODOM; Q82QR5.
DR   SWISS-2DPAGE; Q82QR5.
KW   Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transcription;
KW   Transferase.
FT   CHAIN         1    338       DNA-directed RNA polymerase subunit
FT                                alpha.
FT                                /FTId=PRO_0000175391.
FT   REGION        1    226       Alpha N-terminal domain (alpha-NTD).
FT                                {ECO:0000255|HAMAP-Rule:MF_00059}.
FT   REGION      243    338       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000255|HAMAP-Rule:MF_00059}.
SQ   SEQUENCE   338 AA;  36501 MW;  E675171EF008FD9F CRC64;
     MLIAQRPSLT EEVVDEFRSR FVIEPLEPGF GYTLGNSLRR TLLSSIPGAA VTSIRVDGVL
     HEFTTVPGVK EDVTDLILNI KQLVVSSEHD EPVVMYLRKQ GPGLVTAADI APPAGVEVHN
     PDLVLATLNG KGKLEMELTV ERGRGYVSAV QNKQVGQEIG RIPVDSIYSP VLKVTYKVEA
     TRVEQRTDFD KLIVDVETKQ AMRPRDAMAS AGKTLVELFG LARELNIDAE GIDMGPSPVD
     AALAADLVMP IEELELTVRS YNCLKREGVH SVGELVARSE ADLLDIRNFG AKSIDEVKAK
     LAGMGLGLKD SPPGFDPTAA ALGADDDADA GFLETEHY
//

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