ID D3E471_METRM Unreviewed; 189 AA.
AC D3E471;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo7 {ECO:0000256|HAMAP-Rule:MF_00865};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00865};
DE AltName: Full=DNA-directed RNA polymerase subunit E {ECO:0000256|HAMAP-Rule:MF_00865};
GN Name=rpoE1 {ECO:0000313|EMBL:ADC47332.1};
GN Synonyms=rpo7 {ECO:0000256|HAMAP-Rule:MF_00865}, rpoE
GN {ECO:0000256|HAMAP-Rule:MF_00865};
GN OrderedLocusNames=mru_1482 {ECO:0000313|EMBL:ADC47332.1};
OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS OCM 146 / M1) (Methanobacterium ruminantium).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=634498 {ECO:0000313|EMBL:ADC47332.1, ECO:0000313|Proteomes:UP000008680};
RN [1] {ECO:0000313|EMBL:ADC47332.1, ECO:0000313|Proteomes:UP000008680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1
RC {ECO:0000313|Proteomes:UP000008680};
RX PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA Janssen P.H., Dey D., Attwood G.T.;
RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT reveals new possibilities for controlling ruminant methane emissions.";
RL PLoS ONE 5:E8926-E8926(2010).
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_00865}.
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_00865};
CC -!- SUBUNIT: Part of the RNA polymerase complex. Forms a stalk with Rpo4
CC that extends from the main structure. {ECO:0000256|HAMAP-
CC Rule:MF_00865}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00865}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- DOMAIN: Forms 2 domains with an elongated structure; Rpo4 packs into
CC the hinge region between the 2 domains. {ECO:0000256|HAMAP-
CC Rule:MF_00865}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit
CC family. {ECO:0000256|ARBA:ARBA00009307, ECO:0000256|HAMAP-
CC Rule:MF_00865}.
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DR EMBL; CP001719; ADC47332.1; -; Genomic_DNA.
DR AlphaFoldDB; D3E471; -.
DR STRING; 634498.mru_1482; -.
DR KEGG; mru:mru_1482; -.
DR PATRIC; fig|634498.28.peg.1486; -.
DR eggNOG; arCOG00675; Archaea.
DR HOGENOM; CLU_117966_0_0_2; -.
DR OMA; MRQPGLG; -.
DR OrthoDB; 7927at2157; -.
DR Proteomes; UP000008680; 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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006352; P:DNA-templated transcription initiation; IEA:InterPro.
DR CDD; cd04331; RNAP_E_N; 1.
DR CDD; cd04460; S1_RpoE; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.30.1490.120; RNA polymerase Rpb7-like, N-terminal domain; 1.
DR HAMAP; MF_00865; RNApol_arch_Rpo7; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR036898; RNA_pol_Rpb7-like_N_sf.
DR InterPro; IPR004519; RNAP_E/RPC8.
DR InterPro; IPR046399; RNApol_Rpo7.
DR InterPro; IPR045113; Rpb7-like.
DR InterPro; IPR005576; Rpb7-like_N.
DR InterPro; IPR003029; S1_domain.
DR NCBIfam; TIGR00448; rpoE; 1.
DR PANTHER; PTHR12709:SF4; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB7; 1.
DR PANTHER; PTHR12709; DNA-DIRECTED RNA POLYMERASE II, III; 1.
DR Pfam; PF00575; S1; 1.
DR Pfam; PF03876; SHS2_Rpb7-N; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF88798; N-terminal, heterodimerisation domain of RBP7 (RpoE); 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50126; S1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00865};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00865};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00865,
KW ECO:0000313|EMBL:ADC47332.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008680};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00865};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00865, ECO:0000313|EMBL:ADC47332.1}.
FT DOMAIN 79..163
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 189 AA; 21003 MW; 99162520E42A7F06 CRC64;
MTTIEGTVRI PPHRFGEPLE DVAIETLNES YNGQLDKNLG LIVGVTSIEE MGEGVLIMGD
GAAYHNVIFN AIFFKPEQQE VVEGEVIDIA EFGAFVRIGP MDGLVHVSQV TDDYINYDPR
NASLIAKESK KILTEGDRVR ARIVTLSLKG KTVQESKIGL TMRQPNLGKF EWIEKEKAKA
LEKKMAKVE
//