ID RPO7_SACS2 Reviewed; 180 AA. AC Q980A3; DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 27-MAR-2024, entry version 118. DE RecName: Full=DNA-directed RNA polymerase subunit Rpo7 {ECO:0000255|HAMAP-Rule:MF_00865}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00865}; DE AltName: Full=DNA-directed RNA polymerase subunit E {ECO:0000255|HAMAP-Rule:MF_00865}; DE AltName: Full=DNA-directed RNA polymerase, subunit E' {ECO:0000303|PubMed:18235446}; GN Name=rpo7 {ECO:0000255|HAMAP-Rule:MF_00865}; GN Synonyms=rpoE {ECO:0000255|HAMAP-Rule:MF_00865}; OrderedLocusNames=SSO0415; OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OS (Sulfolobus solfataricus). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=273057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). RN [2] {ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ} RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, AND RP SUBUNIT. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=18235446; DOI=10.1038/nature06530; RA Hirata A., Klein B.J., Murakami K.S.; RT "The X-ray crystal structure of RNA polymerase from Archaea."; RL Nature 451:851-854(2008). CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the CC transcription of DNA into RNA using the four ribonucleoside CC triphosphates as substrates. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00865}; CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. Forms a stalk CC with Rpo4 that extends from the main structure. CC {ECO:0000269|PubMed:18235446}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP- CC Rule:MF_00865, ECO:0000269|PubMed:18235446}. CC -!- SIMILARITY: Belongs to the eukaryotic RPB7/RPC8 RNA polymerase subunit CC family. {ECO:0000255|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; AE006641; AAK40742.1; -; Genomic_DNA. DR PIR; G90185; G90185. DR RefSeq; WP_009988767.1; NC_002754.1. DR PDB; 2PMZ; X-ray; 3.40 A; E/T=1-180. DR PDB; 3HKZ; X-ray; 3.40 A; E/Q=1-180. DR PDBsum; 2PMZ; -. DR PDBsum; 3HKZ; -. DR AlphaFoldDB; Q980A3; -. DR SMR; Q980A3; -. DR DIP; DIP-60644N; -. DR IntAct; Q980A3; 1. DR STRING; 273057.SSO0415; -. DR PaxDb; 273057-SSO0415; -. DR EnsemblBacteria; AAK40742; AAK40742; SSO0415. DR GeneID; 72912226; -. DR KEGG; sso:SSO0415; -. DR PATRIC; fig|273057.12.peg.409; -. DR eggNOG; arCOG00675; Archaea. DR HOGENOM; CLU_117966_0_0_2; -. DR InParanoid; Q980A3; -. DR PhylomeDB; Q980A3; -. DR BRENDA; 2.7.7.6; 6163. DR EvolutionaryTrace; Q980A3; -. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB. 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 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase. FT CHAIN 1..180 FT /note="DNA-directed RNA polymerase subunit Rpo7" FT /id="PRO_0000453813" FT DOMAIN 82..165 FT /note="S1 motif" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00865" FT STRAND 2..13 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 22..31 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 44..48 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 65..77 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 89..92 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 94..100 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 102..110 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 111..113 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 122..125 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 130..132 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 160..163 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 166..168 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 172..175 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 176..178 FT /evidence="ECO:0007829|PDB:2PMZ" SQ SEQUENCE 180 AA; 20329 MW; 2351BE9ADA4847C7 CRC64; MYKLIKARSI VRIPPNEFGK PLNEIALNEL RQQYQEKILK DLGLVLAILN VKTSEEGILV FGDGATYHEV EFDMITYVPV VQEVVEGEVL QVDNYGIFVN LGPMDGLVHI SQITDDTLKY DNVRGIIFGE KSKKVIQKGD KVRARVISVA STVTGRLPRI ALTMRQPYLG KLEWITQTKK //