(data stored in SCRATCH zone)

SWISSPROT: C8W413_DESAS

ID   C8W413_DESAS            Unreviewed;       315 AA.
AC   C8W413;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=Dtox_0314 {ECO:0000313|EMBL:ACV61267.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61267.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61267.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV61267.1; -; Genomic_DNA.
DR   RefSeq; WP_015755988.1; NC_013216.1.
DR   STRING; 485916.Dtox_0314; -.
DR   EnsemblBacteria; ACV61267; ACV61267; Dtox_0314.
DR   KEGG; dae:Dtox_0314; -.
DR   eggNOG; ENOG4105CTF; Bacteria.
DR   eggNOG; COG0202; LUCA.
DR   HOGENOM; HOG000218480; -.
DR   KO; K03040; -.
DR   OMA; LMKFRNF; -.
DR   OrthoDB; 662686at2; -.
DR   BioCyc; DACE485916:G1GFV-329-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8W413.
DR   SWISS-2DPAGE; C8W413.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00059,
KW   ECO:0000313|EMBL:ACV61267.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   DOMAIN       19    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      245    315       Alpha C-terminal domain (alpha-CTD).
FT                                {ECO:0000256|HAMAP-Rule:MF_00059}.
FT   COILED      271    291       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   315 AA;  35457 MW;  3C9280AD1756CB51 CRC64;
     MQIEKPRIEC VETNEDNTYG KFIVEPLERG YGITLGNSLR RILLSSLPGV AVTSVKIDGV
     LHEFSTVPGV REDVTDIILN LKSLRLKMHG EADEKILRIE AQGEGEVRAG DIVPDSDVEI
     LNPDMYIATL AANGRLSMDI TIARGRGYFS AERNKKGEPI IGVIPIDSIF TPVYKVNYSV
     ENTRVGQRTD YDKLSIEIWT DGSIHPDEAA SLAAKIMSEH LQLFIGLTEE TKDVEIMVEK
     EEEKKDKIME MTIEELDLSV RSYNCLKRAC INTVEELIQR NEEDMMKVRN LGKKSLEEVI
     QKLNELGVSL KESEE
//

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