(data stored in SCRATCH zone)

SWISSPROT: A0A0F6BHU2_GEOS0

ID   A0A0F6BHU2_GEOS0        Unreviewed;       314 AA.
AC   A0A0F6BHU2;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   08-MAY-2019, entry version 23.
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   OrderedLocusNames=GY4MC1_0137 {ECO:0000313|EMBL:ADP72993.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72993.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72993.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72993.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) 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}.
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DR   EMBL; CP002293; ADP72993.1; -; Genomic_DNA.
DR   RefSeq; WP_003247622.1; NC_014650.1.
DR   EnsemblBacteria; ADP72993; ADP72993; GY4MC1_0137.
DR   GeneID; 29237227; -.
DR   KEGG; gmc:GY4MC1_0137; -.
DR   KO; K03040; -.
DR   OMA; LMKFRNF; -.
DR   OrthoDB; 662686at2; -.
DR   BioCyc; GSP581103:G1GOQ-164-MONOMER; -.
DR   Proteomes; UP000002034; 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; A0A0F6BHU2.
DR   SWISS-2DPAGE; A0A0F6BHU2.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059,
KW   ECO:0000313|EMBL:ADP72993.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   DOMAIN       20    227       RPOLD. {ECO:0000259|SMART:SM00662}.
FT   REGION        1    228       Alpha N-terminal domain (alpha-NTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   REGION      247    314       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   COILED      224    251       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   314 AA;  34835 MW;  9A88902AE1E9D423 CRC64;
     MIEIEKPRIE TVEISEDAKY GKFVVEPLER GYGTTLGNSL RRILLSSLPG AAVTSVQIDG
     VLHEFSTIDG VVEDVTAIIL NIKKLALKIY SDEEKTLEID AQGEGVVTAA DITHDSDVEI
     LNPDLHIATL AEGGRLRMRM TAKRGRGYVP AEANKREDQP IGVIPIDSIY TPVSRVAYQV
     ENTRVGQVTD YDKLTIDVWT DGSIGPKEAI ALGAKILTEH LNIFVSLTDE AQNAEIMVEK
     EEDQKEKVLE MTIEELDLSV RSYNCLKRAG INTVQELTQK TEEDMMKVRN LGRKSLEEVK
     AKLAELGLSL RKDD
//

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