ID V4XMT4_9ARCH Unreviewed; 192 AA.
AC V4XMT4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=A07HN63_00505 {ECO:0000313|EMBL:ESS09699.1};
OS uncultured archaeon A07HN63.
OC Archaea; environmental samples.
OX NCBI_TaxID=1412873 {ECO:0000313|EMBL:ESS09699.1, ECO:0000313|Proteomes:UP000030667};
RN [1] {ECO:0000313|Proteomes:UP000030667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24335829;
RA Podell S., Emerson J.B., Jones C.M., Ugalde J.A., Welch S.,
RA Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "Seasonal fluctuations in ionic concentrations drive microbial succession
RT in a hypersaline lake community.";
RL ISME J. 0:0-0(2013).
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}.
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; KI543197; ESS09699.1; -; Genomic_DNA.
DR AlphaFoldDB; V4XMT4; -.
DR STRING; 1412873.A07HN63_00505; -.
DR PATRIC; fig|1412873.3.peg.549; -.
DR Proteomes; UP000030667; 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 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 Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00865}; Transferase {ECO:0000256|HAMAP-Rule:MF_00865}.
FT DOMAIN 82..166
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
FT REGION 153..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 192 AA; 21356 MW; D7F3321817104587 CRC64;
MYKRVRLTDT VEVPPEKLAD VSHERVKRLL QDKLEGRMDE DVGSVVSVIE VHDIGEGTVL
PNRPGVYYEA EFDALTFDPS MQEVTDGTVV EVVEFGAFVG IGPVDGLLHV SQISDEYLAH
DEENQQLAST ESDESLAVDD AVRTRIVTKS IDERNPRDSK IGLTAKQPGL GKHEWLERAR
KRREQDATAE GA
//
