ID A2SR75_METLZ Unreviewed; 190 AA.
AC A2SR75;
DT 06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 83.
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=rpo7 {ECO:0000256|HAMAP-Rule:MF_00865};
GN Synonyms=rpoE {ECO:0000256|HAMAP-Rule:MF_00865};
GN OrderedLocusNames=Mlab_0658 {ECO:0000313|EMBL:ABN06831.1};
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358 {ECO:0000313|EMBL:ABN06831.1, ECO:0000313|Proteomes:UP000000365};
RN [1] {ECO:0000313|EMBL:ABN06831.1, ECO:0000313|Proteomes:UP000000365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z {ECO:0000313|Proteomes:UP000000365};
RX PubMed=21304657; DOI=10.4056.sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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|HAMAP-Rule:MF_00865}.
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DR EMBL; CP000559; ABN06831.1; -; Genomic_DNA.
DR RefSeq; WP_011833032.1; NC_008942.1.
DR AlphaFoldDB; A2SR75; -.
DR STRING; 410358.Mlab_0658; -.
DR GeneID; 4795135; -.
DR KEGG; mla:Mlab_0658; -.
DR eggNOG; arCOG00675; Archaea.
DR HOGENOM; CLU_117966_0_0_2; -.
DR OrthoDB; 7927at2157; -.
DR Proteomes; UP000000365; 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; DNA-DIRECTED RNA POLYMERASE II, III; 1.
DR PANTHER; PTHR12709:SF1; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC8; 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:ABN06831.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000365};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00865};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00865, ECO:0000313|EMBL:ABN06831.1}.
FT DOMAIN 82..166
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 190 AA; 21242 MW; 6F2629A3A3E28D59 CRC64;
MYYKLKLNDK VRVPPERMGE DLNTVILDVL QEQFEGSVDK EMGIFIAVTG VNRVGDGEII
YSDGGAYYDV DFEAVVLRLS LQEIIEGVVV ETTSFGAFVS LGPIDAMLHM SQISDEYIDY
DEKNSRLVCK DSGRTIGVGD TLRARVVALS LNERDPRESK IGLTMRQPGL GTLAWIEEDM
NKEKAEKELK
//
