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RPO11_PYRAE
ID   RPO11_PYRAE             Reviewed;          92 AA.
AC   Q8ZW46;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo11 {ECO:0000255|HAMAP-Rule:MF_00261};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00261};
DE   AltName: Full=DNA-directed RNA polymerase subunit L {ECO:0000255|HAMAP-Rule:MF_00261};
GN   Name=rpo11 {ECO:0000255|HAMAP-Rule:MF_00261};
GN   Synonyms=rpoL {ECO:0000255|HAMAP-Rule:MF_00261}; OrderedLocusNames=PAE1978;
OS   Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS   104966 / NBRC 100827 / IM2).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=178306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX   PubMed=11792869; DOI=10.1073/pnas.241636498;
RA   Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA   Miller J.H.;
RT   "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT   aerophilum.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_00261}.
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:0000255|HAMAP-Rule:MF_00261};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00261}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00261}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo11/eukaryotic RPB11/RPC19 RNA
CC       polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00261}.
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DR   EMBL; AE009441; AAL63856.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8ZW46; -.
DR   SMR; Q8ZW46; -.
DR   STRING; 178306.PAE1978; -.
DR   EnsemblBacteria; AAL63856; AAL63856; PAE1978.
DR   KEGG; pai:PAE1978; -.
DR   PATRIC; fig|178306.9.peg.1460; -.
DR   eggNOG; arCOG04111; Archaea.
DR   HOGENOM; CLU_090381_5_3_2; -.
DR   InParanoid; Q8ZW46; -.
DR   OMA; NVRFRIK; -.
DR   Proteomes; UP000002439; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
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; 3.30.1360.10; -; 1.
DR   HAMAP; MF_00261; RNApol_arch_Rpo11; 1.
DR   InterPro; IPR036603; RBP11-like.
DR   InterPro; IPR009025; RBP11-like_dimer.
DR   InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS.
DR   InterPro; IPR022905; Rpo11.
DR   Pfam; PF13656; RNA_pol_L_2; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   PROSITE; PS01154; RNA_POL_L_13KD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..92
FT                   /note="DNA-directed RNA polymerase subunit Rpo11"
FT                   /id="PRO_0000149334"
SQ   SEQUENCE   92 AA;  10678 MW;  4DDAD3D0C2AD01D4 CRC64;
     MSPVLRLEIL KLDDKYLELK AKGETYTLFS PLVEYLSNDP DVEYVQFDVD HPLQENAYFK
     LKVKRGNPLE AIQRAVNAIL SDLEELERGF FS
 
 
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