RPO11_METM6
ID RPO11_METM6 Reviewed; 96 AA.
AC A9A836;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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};
GN OrderedLocusNames=MmarC6_0692;
OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=444158;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C6 / ATCC BAA-1332;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C6.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX01509.1; -; Genomic_DNA.
DR RefSeq; WP_012193548.1; NC_009975.1.
DR AlphaFoldDB; A9A836; -.
DR SMR; A9A836; -.
DR STRING; 444158.MmarC6_0692; -.
DR EnsemblBacteria; ABX01509; ABX01509; MmarC6_0692.
DR GeneID; 5739044; -.
DR KEGG; mmx:MmarC6_0692; -.
DR eggNOG; arCOG04111; Archaea.
DR HOGENOM; CLU_090381_5_0_2; -.
DR OMA; SNPTIML; -.
DR OrthoDB; 129321at2157; -.
DR PhylomeDB; A9A836; -.
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 Transcription; Transferase.
FT CHAIN 1..96
FT /note="DNA-directed RNA polymerase subunit Rpo11"
FT /id="PRO_1000114193"
SQ SEQUENCE 96 AA; 10854 MW; AA5E674B338A750B CRC64;
MNYVNILEKS KNFIELELVN DDHSLSNLIK EVLLSKKGVI LASYGVEHPV LDPDTGRYIS
NPRIMLKTDA KTDAEKVLKE ALKDIVDLCN KTLKEL
