RPO6_PYRFU
ID RPO6_PYRFU Reviewed; 57 AA.
AC Q8U0E8;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo6 {ECO:0000255|HAMAP-Rule:MF_00192};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00192};
DE AltName: Full=DNA-directed RNA polymerase subunit K {ECO:0000255|HAMAP-Rule:MF_00192};
GN Name=rpo6 {ECO:0000255|HAMAP-Rule:MF_00192};
GN Synonyms=rpoK {ECO:0000255|HAMAP-Rule:MF_00192}; OrderedLocusNames=PF1642;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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_00192}.
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_00192};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00192}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00192}.
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DR EMBL; AE009950; AAL81766.1; -; Genomic_DNA.
DR RefSeq; WP_011012789.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U0E8; -.
DR SMR; Q8U0E8; -.
DR IntAct; Q8U0E8; 1.
DR MINT; Q8U0E8; -.
DR STRING; 186497.PF1642; -.
DR PRIDE; Q8U0E8; -.
DR EnsemblBacteria; AAL81766; AAL81766; PF1642.
DR GeneID; 41713467; -.
DR KEGG; pfu:PF1642; -.
DR PATRIC; fig|186497.12.peg.1708; -.
DR eggNOG; arCOG01268; Archaea.
DR HOGENOM; CLU_112527_5_0_2; -.
DR OMA; HNRYEKA; -.
DR OrthoDB; 126193at2157; -.
DR PhylomeDB; Q8U0E8; -.
DR Proteomes; UP000001013; 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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.940.10; -; 1.
DR HAMAP; MF_00192; RNApol_arch_Rpo6; 1.
DR InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS.
DR InterPro; IPR006110; Pol_omega/Rpo6/RPB6.
DR InterPro; IPR036161; RPB6/omega-like_sf.
DR InterPro; IPR006111; Rpo6/Rpb6.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR SUPFAM; SSF63562; SSF63562; 1.
DR PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..57
FT /note="DNA-directed RNA polymerase subunit Rpo6"
FT /id="PRO_0000133819"
SQ SEQUENCE 57 AA; 6237 MW; E5F00E89304F9709 CRC64;
MFKYTRFEKA RIIGARALQI SMGAPVLIDV PPGITPLEAA ILEFEKGVIP ITVIRPS
