ID A0A1F5CWF1_9ARCH Unreviewed; 76 AA.
AC A0A1F5CWF1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo6 {ECO:0000256|HAMAP-Rule:MF_00192};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00192};
DE AltName: Full=DNA-directed RNA polymerase subunit K {ECO:0000256|HAMAP-Rule:MF_00192};
GN Name=rpo6 {ECO:0000256|HAMAP-Rule:MF_00192};
GN Synonyms=rpoK {ECO:0000256|HAMAP-Rule:MF_00192};
GN ORFNames=A3K79_05035 {ECO:0000313|EMBL:OGD47173.1};
OS Candidatus Bathyarchaeota archaeon RBG_13_46_16b.
OC Archaea; Candidatus Bathyarchaeota.
OX NCBI_TaxID=1797378 {ECO:0000313|EMBL:OGD47173.1, ECO:0000313|Proteomes:UP000176481};
RN [1] {ECO:0000313|EMBL:OGD47173.1, ECO:0000313|Proteomes:UP000176481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00192};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP-
CC Rule:MF_00192}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00192}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo6/eukaryotic RPB6 RNA polymerase
CC subunit family. {ECO:0000256|HAMAP-Rule:MF_00192}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGD47173.1}.
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DR EMBL; MEZE01000030; OGD47173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5CWF1; -.
DR Proteomes; UP000176481; Unassembled WGS sequence.
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:DNA-templated transcription; 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 PANTHER; PTHR47227; DNA-DIRECTED RNA POLYMERASE SUBUNIT K; 1.
DR PANTHER; PTHR47227:SF5; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC2; 1.
DR Pfam; PF01192; RNA_pol_Rpb6; 1.
DR PIRSF; PIRSF000778; RpoK/RPB6; 1.
DR SMART; SM01409; RNA_pol_Rpb6; 1.
DR SUPFAM; SSF63562; RPB6/omega subunit-like; 1.
DR PROSITE; PS01111; RNA_POL_K_14KD; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00192};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00192};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00192};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00192}; Transferase {ECO:0000256|HAMAP-Rule:MF_00192}.
SQ SEQUENCE 76 AA; 8226 MW; 791EBC5B35B9032C CRC64;
MGPPKITRFE KARVVGARAL QISMGAPILV ELSEGSSSPI DIALKELGTG MLPMTIRRTL
PDGSFQDIPL KWLIAH
//
