ID A0A1M5K0E4_9EURY Unreviewed; 76 AA.
AC A0A1M5K0E4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 33.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo5 {ECO:0000256|HAMAP-Rule:MF_00025};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00025};
DE AltName: Full=DNA-directed RNA polymerase subunit H {ECO:0000256|HAMAP-Rule:MF_00025};
GN Name=rpo5 {ECO:0000256|HAMAP-Rule:MF_00025};
GN Synonyms=rpoH {ECO:0000256|HAMAP-Rule:MF_00025};
GN ORFNames=SAMN05443636_0325 {ECO:0000313|EMBL:SHG46010.1};
OS Halobaculum gomorrense.
OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group;
OC Halobacteria; Halobacteriales; Haloferacaceae; Halobaculum.
OX NCBI_TaxID=43928 {ECO:0000313|EMBL:SHG46010.1, ECO:0000313|Proteomes:UP000184357};
RN [1] {ECO:0000313|EMBL:SHG46010.1, ECO:0000313|Proteomes:UP000184357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9297 {ECO:0000313|EMBL:SHG46010.1,
RC ECO:0000313|Proteomes:UP000184357};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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. {ECO:0000256|HAMAP-Rule:MF_00025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) +
CC diphosphate; 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_00025};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP-
CC Rule:MF_00025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00025}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase
CC subunit family. {ECO:0000256|HAMAP-Rule:MF_00025}.
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DR EMBL; FQWV01000001; SHG46010.1; -; Genomic_DNA.
DR RefSeq; WP_073306659.1; NZ_FQWV01000001.1.
DR AlphaFoldDB; A0A1M5K0E4; -.
DR STRING; 43928.SAMN05443636_0325; -.
DR OrthoDB; 30537at2157; -.
DR Proteomes; UP000184357; 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:InterPro.
DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:TreeGrafter.
DR GO; GO:0006362; P:transcription elongation by RNA polymerase I; IEA:TreeGrafter.
DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IEA:TreeGrafter.
DR Gene3D; 3.90.940.20; RPB5-like RNA polymerase subunit; 1.
DR HAMAP; MF_00025; RNApol_Rpo5_RPB5; 1.
DR InterPro; IPR014381; Arch_Rpo5/euc_Rpb5.
DR InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR InterPro; IPR035913; RPB5-like_sf.
DR NCBIfam; NF007129; PRK09570.1; 1.
DR PANTHER; PTHR10535; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1; 1.
DR PANTHER; PTHR10535:SF0; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1; 1.
DR Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR SUPFAM; SSF55287; RPB5-like RNA polymerase subunit; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00025};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00025};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00025};
KW Reference proteome {ECO:0000313|Proteomes:UP000184357};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00025}; Transferase {ECO:0000256|HAMAP-Rule:MF_00025}.
FT DOMAIN 2..74
FT /note="RNA polymerase subunit H/Rpb5 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01191"
SQ SEQUENCE 76 AA; 8675 MW; FA453F73764D4182 CRC64;
MVNVSEHELV PDHTLLEDAD EIEEVLDEYN VKRTDLPKIK RTDPAVPDEA EAGDVIRIER
DSRTTDTAVV YRLVVE
//
