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Database: UniProt
Entry: V4JXC5_9CREN
LinkDB: V4JXC5_9CREN
Original site: V4JXC5_9CREN 
ID   V4JXC5_9CREN            Unreviewed;       186 AA.
AC   V4JXC5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
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=CISAcid_03310 {ECO:0000313|EMBL:ESQ21962.1};
OS   uncultured Acidilobus sp. CIS.
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Acidilobaceae;
OC   Acidilobus; environmental samples.
OX   NCBI_TaxID=1410574 {ECO:0000313|EMBL:ESQ21962.1, ECO:0000313|Proteomes:UP000017934};
RN   [1] {ECO:0000313|EMBL:ESQ21962.1, ECO:0000313|Proteomes:UP000017934}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Jay Z.J., Rusch D.B., Tringe S.G., Bailey C., Jennings R.M., Inskeep W.P.;
RT   "Predominant Acidilobus-like populations from geothermal environments of
RT   Yellowstone National Park exhibit similar metabolic potential in different
RT   hypoxic microbial communities.";
RL   Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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   -!- 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:ESQ21962.1}.
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DR   EMBL; AYMB01000001; ESQ21962.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4JXC5; -.
DR   STRING; 1410574.CISAcid_03310; -.
DR   PATRIC; fig|1410574.3.peg.318; -.
DR   Proteomes; UP000017934; 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; 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:ESQ21962.1};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00865};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00865, ECO:0000313|EMBL:ESQ21962.1}.
FT   DOMAIN          83..167
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   186 AA;  21060 MW;  0DA53CC948CA06B9 CRC64;
     MYAEYTVYEW VGVRPDLAFT GDLNKAVLDS LREELEGQVD ETLGIIISVI DAEVQGDGVL
     LPNDPQIYFP VRYRVLTYEP VLQEVSMGIV RDAREFGVFV SLGPTDGFVH RSQLMDEDVD
     YVEENRSFKG RETGRTISIG DVVRVRVTQV SKASKRLAVI RIGLTMRQPY LGKEEWQRKE
     ARGEGS
//
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