(data stored in ACNUC7421 zone)

SWISSPROT: RPOA_RUEPO

ID   RPOA_RUEPO              Reviewed;         338 AA.
AC   Q5LW32;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
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=rpoA {ECO:0000255|HAMAP-Rule:MF_00059};
GN   OrderedLocusNames=SPO0511;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C.,
RA   Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A.,
RA   Rahe E., Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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; CP000031; AAV93828.1; -; Genomic_DNA.
DR   RefSeq; WP_011046270.1; NC_003911.12.
DR   SMR; Q5LW32; -.
DR   STRING; 246200.SPO0511; -.
DR   EnsemblBacteria; AAV93828; AAV93828; SPO0511.
DR   KEGG; sil:SPO0511; -.
DR   eggNOG; ENOG4105CTF; Bacteria.
DR   eggNOG; COG0202; LUCA.
DR   HOGENOM; HOG000218481; -.
DR   KO; K03040; -.
DR   OMA; LMKFRNF; -.
DR   OrthoDB; 662686at2; -.
DR   BioCyc; RPOM246200:G1G48-518-MONOMER; -.
DR   Proteomes; UP000001023; 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; Q5LW32.
DR   SWISS-2DPAGE; Q5LW32.
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_0000175378.
FT   REGION        1    234       Alpha N-terminal domain (alpha-NTD).
FT                                {ECO:0000255|HAMAP-Rule:MF_00059}.
FT   REGION      250    338       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000255|HAMAP-Rule:MF_00059}.
SQ   SEQUENCE   338 AA;  37147 MW;  D521962A820C05EE CRC64;
     MIHKNWAELI KPTQLEVKPG NDPARQATVI AEPLERGFGL TLGNALRRIL MSSLQGAAIS
     SVQIDNVLHE FSSVAGVRED VTDIILNLKQ VSLRMDVEGP KRLSVNAKGP AVVTAGDISE
     SAGIEVLNRD HVICHLDDGA DLFMELTVNT GKGYVSADKN RPEDAPIGLI PIDAIYSPVK
     KVAYDVQPTR EGQVLDYDKL TMKIETDGSI TPDDAVAFAA RILQDQLSIF VNFDEPESAG
     RQDDDDGLEF NPLLLKKVDE LELSVRSANC LKNDNIVYIG DLIQKTEAEM LRTPNFGRKS
     LNEIKEVLSG MGLHLGMDVE DWPPDNIEDL AKKFEDAF
//

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