GenomeNet

Database: UniProt
Entry: D3E471_METRM
LinkDB: D3E471_METRM
Original site: D3E471_METRM 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system