ID A0A1I6LPX5_9EURY Unreviewed; 118 AA.
AC A0A1I6LPX5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN05216559_2857 {ECO:0000313|EMBL:SFS05449.1};
OS Halomicrobium zhouii.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Halomicrobium.
OX NCBI_TaxID=767519 {ECO:0000313|EMBL:SFS05449.1, ECO:0000313|Proteomes:UP000199062};
RN [1] {ECO:0000313|EMBL:SFS05449.1, ECO:0000313|Proteomes:UP000199062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10457 {ECO:0000313|EMBL:SFS05449.1,
RC ECO:0000313|Proteomes:UP000199062};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOZK01000003; SFS05449.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6LPX5; -.
DR STRING; 767519.SAMN05216559_2857; -.
DR OrthoDB; 25158at2157; -.
DR Proteomes; UP000199062; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00864};
KW DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00864,
KW ECO:0000313|EMBL:SFS05449.1};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00864};
KW Reference proteome {ECO:0000313|Proteomes:UP000199062};
KW Transcription {ECO:0000256|HAMAP-Rule:MF_00864};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00864}.
SQ SEQUENCE 118 AA; 13943 MW; 2FE61B3288AB3626 CRC64;
MTIFKKKLDE EYLTLAETKE ILEDIEADRA VDEEREMRYE LARAIEHVNR FAELDVEEAD
EFVDQLRELE KVDEATAYKI ANLRPLDRDE LRAVFAQERY SLSGDELDEI LNVVKQYA
//
