RPO11_THEKO
ID RPO11_THEKO Reviewed; 94 AA.
AC Q5JE88;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, 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=TK1167;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
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; AP006878; BAD85356.1; -; Genomic_DNA.
DR RefSeq; WP_011250118.1; NC_006624.1.
DR PDB; 4QIW; X-ray; 3.50 A; L/U=1-94.
DR PDB; 4QJV; X-ray; 1.60 A; B/D=1-94.
DR PDB; 6KF3; EM; 3.90 A; L=1-94.
DR PDB; 6KF4; EM; 3.97 A; L=1-94.
DR PDB; 6KF9; EM; 3.79 A; L=1-94.
DR PDBsum; 4QIW; -.
DR PDBsum; 4QJV; -.
DR PDBsum; 6KF3; -.
DR PDBsum; 6KF4; -.
DR PDBsum; 6KF9; -.
DR AlphaFoldDB; Q5JE88; -.
DR SMR; Q5JE88; -.
DR STRING; 69014.TK1167; -.
DR EnsemblBacteria; BAD85356; BAD85356; TK1167.
DR GeneID; 3233683; -.
DR KEGG; tko:TK1167; -.
DR PATRIC; fig|69014.16.peg.1142; -.
DR eggNOG; arCOG04111; Archaea.
DR HOGENOM; CLU_090381_5_0_2; -.
DR InParanoid; Q5JE88; -.
DR OMA; PITMARK; -.
DR OrthoDB; 129321at2157; -.
DR PhylomeDB; Q5JE88; -.
DR Proteomes; UP000000536; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..94
FT /note="DNA-directed RNA polymerase subunit Rpo11"
FT /id="PRO_0000149337"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 22..32
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:4QIW"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:4QJV"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:4QJV"
FT HELIX 67..93
FT /evidence="ECO:0007829|PDB:4QJV"
SQ SEQUENCE 94 AA; 10997 MW; 1800B7569C031C32 CRC64;
MRIEVIRREE NLLEFYLEGE DHTFANLLTE TLHENEHVTF AGYTIEHPIT MARKPRFKVV
TDGKITPEKA LEEAAQKIFD RAREVLEAWK AAIE
