ID G4RNX1_THETK Unreviewed; 189 AA.
AC G4RNX1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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:CCC81265.1};
GN Synonyms=rpo7 {ECO:0000256|HAMAP-Rule:MF_00865}, rpoE
GN {ECO:0000256|HAMAP-Rule:MF_00865};
GN OrderedLocusNames=TTX_0605 {ECO:0000313|EMBL:CCC81265.1};
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679 {ECO:0000313|EMBL:CCC81265.1, ECO:0000313|Proteomes:UP000002654};
RN [1] {ECO:0000313|EMBL:CCC81265.1, ECO:0000313|Proteomes:UP000002654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000313|Proteomes:UP000002654};
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
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; FN869859; CCC81265.1; -; Genomic_DNA.
DR RefSeq; WP_014126522.1; NC_016070.1.
DR AlphaFoldDB; G4RNX1; -.
DR STRING; 768679.TTX_0605; -.
DR PaxDb; 768679-TTX_0605; -.
DR GeneID; 11263601; -.
DR KEGG; ttn:TTX_0605; -.
DR PATRIC; fig|768679.9.peg.617; -.
DR eggNOG; arCOG00675; Archaea.
DR HOGENOM; CLU_117966_0_0_2; -.
DR OrthoDB; 7927at2157; -.
DR Proteomes; UP000002654; 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:CCC81265.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002654};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00865};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00865, ECO:0000313|EMBL:CCC81265.1}.
FT DOMAIN 83..165
FT /note="S1 motif"
FT /evidence="ECO:0000259|PROSITE:PS50126"
SQ SEQUENCE 189 AA; 21100 MW; D627696D07ACD29F CRC64;
MPFRLVEAED YIRVPPSDFN KPLEDVALGQ LRSKYEGKSF RDLGYVVAVL DAKVNREGVI
IFGDGATYHK AIFHILTFMP LDGEVVHGIV ESAREVGVMV RIGPVLGFIN KIHLMDEPNV
LFDASTKSFI GERTKKKLSI GDVVRARITG ISYVAQKEGV DLALRITMTM RMPGLGKLEW
LKEKKGKKP
//
