ID A0A401HPV3_9EURY Unreviewed; 182 AA.
AC A0A401HPV3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 18-JUN-2025, entry version 21.
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 ORFNames=MHHB_P0455 {ECO:0000313|EMBL:GBF36225.1};
OS Methanofervidicoccus abyssi.
OC Archaea; Methanobacteriati; Methanobacteriota; Methanomada group;
OC Methanococci; Methanococcales; Methanofervidicoccus.
OX NCBI_TaxID=2082189 {ECO:0000313|EMBL:GBF36225.1, ECO:0000313|Proteomes:UP000290527};
RN [1] {ECO:0000313|EMBL:GBF36225.1, ECO:0000313|Proteomes:UP000290527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB {ECO:0000313|EMBL:GBF36225.1,
RC ECO:0000313|Proteomes:UP000290527};
RX PubMed=30843780; DOI=.1099/ijsem.0.003297;
RA Sakai S., Takaki Y., Miyazaki M., Ogawara M., Yanagawa K., Miyazaki J.,
RA Takai K.;
RT "Methanofervidicoccus abyssi gen. nov., sp. nov., a hydrogenotrophic
RT methanogen, isolated from a hydrothermal vent chimney in the Mid-Cayman
RT Spreading Center, the Caribbean Sea.";
RL Int. J. Syst. Evol. Microbiol. 69:1225-1230(2019).
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=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_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 -!- 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GBF36225.1}.
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DR EMBL; BFAX01000002; GBF36225.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401HPV3; -.
DR Proteomes; UP000290527; 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:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 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; NF006333; PRK08563.1; 1.
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:GBF36225.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000290527};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00865};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00865, ECO:0000313|EMBL:GBF36225.1}.
FT DOMAIN 79..163
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 182 AA; 20290 MW; F0327EF5F46B1B2B CRC64;
MVTISDVVRV PPTMFGNSLK ESIHNILVEK YEGILDKDIG LILSIGDIKE IGEGKVIYGD
GAAYHPVVFD ALCYIPELYE VVEGEVVDVV EFGIFVRLGP LDGLVHISQI MDDYVSYDPK
NEMMVGRDTG KIIKKGDIVR ARIIAVSLRE TKKRGSKIAL TMRQPGLGKI EWIEEEKKKK
KG
//
