ID RPO13_SACS2 Reviewed; 104 AA. AC Q980B8; DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 27-MAR-2024, entry version 97. DE RecName: Full=DNA-directed RNA polymerase subunit Rpo13 {ECO:0000305}; DE EC=2.7.7.6 {ECO:0000250|UniProtKB:Q4JAJ6}; GN Name=rpo13 {ECO:0000305}; OrderedLocusNames=SSO0396; 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: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. Probably binds dsDNA. CC {ECO:0000250|UniProtKB:Q4JAJ6}. 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:0000250|UniProtKB:Q4JAJ6}; CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. CC {ECO:0000269|PubMed:18235446, ECO:0007744|PDB:3HKZ}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB65}. CC -!- SIMILARITY: Belongs to the archaeal Rpo13 RNA polymerase subunit CC family. {ECO:0000305}. 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; AAK40725.1; -; Genomic_DNA. DR PIR; F90183; F90183. DR RefSeq; WP_009988796.1; NC_002754.1. DR PDB; 3HKZ; X-ray; 3.40 A; Y/Z=1-104. DR PDBsum; 3HKZ; -. DR AlphaFoldDB; Q980B8; -. DR SMR; Q980B8; -. DR STRING; 273057.SSO0396; -. DR PaxDb; 273057-SSO0396; -. DR EnsemblBacteria; AAK40725; AAK40725; SSO0396. DR GeneID; 72912209; -. DR KEGG; sso:SSO0396; -. DR PATRIC; fig|273057.12.peg.392; -. DR eggNOG; arCOG05938; Archaea. DR HOGENOM; CLU_177471_0_0_2; -. DR InParanoid; Q980B8; -. DR BRENDA; 2.7.7.6; 6163. DR EvolutionaryTrace; Q980B8; -. DR Proteomes; UP000001974; 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:UniProtKB-KW. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 6.20.450.10; -; 1. DR InterPro; IPR021985; RNA_pol_Rpo13. DR Pfam; PF12136; RNA_pol_Rpo13; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA-binding; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase. FT CHAIN 1..104 FT /note="DNA-directed RNA polymerase subunit Rpo13" FT /id="PRO_0000453789" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 78..104 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..28 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..97 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT HELIX 43..53 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 60..72 FT /evidence="ECO:0007829|PDB:3HKZ" FT TURN 73..76 FT /evidence="ECO:0007829|PDB:3HKZ" SQ SEQUENCE 104 AA; 12176 MW; 298E559164C310EE CRC64; MVSGMSTDEE KEGTSDEEVN EEKEVEETSE DEFPKLSIQD IELLMRNTEI WDNLLNGKIT LEEAKKLFED NYKEYEKRDS RRKAKKAVSK KVKKTKKKEK SVEG //