ID A0A0P7GCK9_9EURY Unreviewed; 118 AA.
AC A0A0P7GCK9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo4 {ECO:0000256|HAMAP-Rule:MF_00864};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00864};
DE AltName: Full=DNA-directed RNA polymerase subunit F {ECO:0000256|HAMAP-Rule:MF_00864};
GN Name=rpo4 {ECO:0000256|HAMAP-Rule:MF_00864};
GN Synonyms=rpoF {ECO:0000256|HAMAP-Rule:MF_00864};
GN ORFNames=SY89_02466 {ECO:0000313|EMBL:KPN31717.1};
OS Halolamina pelagica.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae.
OX NCBI_TaxID=699431 {ECO:0000313|EMBL:KPN31717.1, ECO:0000313|Proteomes:UP000050535};
RN [1] {ECO:0000313|Proteomes:UP000050535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDK2 {ECO:0000313|Proteomes:UP000050535};
RA Hoang H.T., Killian M.L., Madson D.M., Arruda P.H.E., Sun D.,
RA Schwartz K.J., Yoon K.;
RL Submitted (NOV-2013) 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. This subunit is less well bound than the
CC others. {ECO:0000256|HAMAP-Rule:MF_00864}.
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_00864};
CC -!- SUBUNIT: Part of the RNA polymerase complex. Forms a stalk with Rpo7
CC that extends from the main structure. {ECO:0000256|HAMAP-
CC Rule:MF_00864}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00864}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC family. {ECO:0000256|HAMAP-Rule:MF_00864}.
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:KPN31717.1}.
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DR EMBL; LGUC01000001; KPN31717.1; -; Genomic_DNA.
DR RefSeq; WP_054584216.1; NZ_LGUC01000001.1.
DR AlphaFoldDB; A0A0P7GCK9; -.
DR STRING; 699431.SY89_02466; -.
DR PATRIC; fig|699431.3.peg.2533; -.
DR OrthoDB; 25158at2157; -.
DR Proteomes; UP000050535; 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:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR Gene3D; 6.10.140.10; -; 1.
DR Gene3D; 1.10.150.80; HRDC domain; 1.
DR HAMAP; MF_00864; RNApol_arch_Rpo4; 1.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR005574; Rpb4/RPC9.
DR InterPro; IPR010924; Rpo4.
DR PANTHER; PTHR39646:SF1; DNA-DIRECTED RNA POLYMERASE SUBUNIT RPO4; 1.
DR PANTHER; PTHR39646; RNA POLYMERASE RPB4; 1.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR PIRSF; PIRSF005053; RNA_pol_F_arch; 1.
DR SUPFAM; SSF47819; HRDC-like; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00864};
KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00864,
KW ECO:0000313|EMBL:KPN31717.1};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00864};
KW Reference proteome {ECO:0000313|Proteomes:UP000050535};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_00864};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00864}.
FT COILED 5..35
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 118 AA; 13823 MW; 91D71A65893271C3 CRC64;
MTIFKEKLDE EYLTAAEVKE ELQDVEEQRA AEDDRELRYE LARAIEHVNR FALLDAEESR
ELVERLKELD KVDNPTAHKI ADLLPRDRDE LRTVYAQERY SLSGDELDAI LDIVAEYA
//
