ID RPO1C_SACS2 Reviewed; 392 AA. AC P58192; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=DNA-directed RNA polymerase subunit Rpo1C {ECO:0000255|HAMAP-Rule:MF_00411}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00411}; DE AltName: Full=DNA-directed RNA polymerase subunit A'' {ECO:0000255|HAMAP-Rule:MF_00411}; GN Name=rpo1C {ECO:0000255|HAMAP-Rule:MF_00411}; GN Synonyms=rpoA2 {ECO:0000255|HAMAP-Rule:MF_00411}; GN OrderedLocusNames=SSO0223; 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 (3.4 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX, RP FUNCTION, AND SUBUNIT. 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. Forms part of the jaw domain. CC {ECO:0000255|HAMAP-Rule:MF_00411, ECO:0000269|PubMed:18235446}. 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_00411}; CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. CC {ECO:0000269|PubMed:18235446}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00411}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000255|HAMAP-Rule:MF_00411}. CC -!- SEQUENCE CAUTION: CC Sequence=AAK40565.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AAK40565.1; ALT_INIT; Genomic_DNA. DR PIR; F90163; F90163. DR RefSeq; WP_009990475.1; NC_002754.1. DR PDB; 2PMZ; X-ray; 3.40 A; C/G=1-392. DR PDB; 3HKZ; X-ray; 3.40 A; C/M=1-392. DR PDBsum; 2PMZ; -. DR PDBsum; 3HKZ; -. DR AlphaFoldDB; P58192; -. DR SMR; P58192; -. DR DIP; DIP-60639N; -. DR IntAct; P58192; 1. DR STRING; 273057.SSO0223; -. DR PaxDb; 273057-SSO0223; -. DR EnsemblBacteria; AAK40565; AAK40565; SSO0223. DR GeneID; 72912029; -. DR KEGG; sso:SSO0223; -. DR PATRIC; fig|273057.12.peg.220; -. DR eggNOG; arCOG04256; Archaea. DR HOGENOM; CLU_037097_1_0_2; -. DR InParanoid; P58192; -. DR PhylomeDB; P58192; -. DR BRENDA; 2.7.7.6; 6163. DR EvolutionaryTrace; P58192; -. 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:UniProtKB-UniRule. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd06528; RNAP_A; 1. DR Gene3D; 1.10.150.390; -; 1. DR HAMAP; MF_00411; RNApol_arch_Rpo1C; 1. DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR012757; RPO1C. DR NCBIfam; TIGR02389; RNA_pol_rpoA2; 1. DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR19376:SF69; DNA-DIRECTED RNA POLYMERASE SUBUNIT RPO1C; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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..392 FT /note="DNA-directed RNA polymerase subunit Rpo1C" FT /id="PRO_0000074026" FT HELIX 11..17 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 20..23 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 29..34 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 47..56 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 57..59 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 67..74 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 75..78 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 102..109 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 118..122 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 131..139 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 146..148 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 151..155 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 157..160 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 162..165 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 169..173 FT /evidence="ECO:0007829|PDB:3HKZ" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 186..188 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:3HKZ" FT HELIX 221..224 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 228..230 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 243..245 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 247..252 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 256..260 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 261..264 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 276..281 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 283..292 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 293..297 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 307..317 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 318..322 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 328..331 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 332..336 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 338..343 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 350..356 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 365..367 FT /evidence="ECO:0007829|PDB:2PMZ" FT HELIX 368..372 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 377..379 FT /evidence="ECO:0007829|PDB:2PMZ" FT TURN 380..382 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:2PMZ" SQ SEQUENCE 392 AA; 43488 MW; 5B0E871D056CE08B CRC64; MIDEKDKPYL EEKVKQASNI LPQKIVDDLK NLILNKEIIV TRDEIDKIFD LAIKEYSEGL IAPGEAIGIV AAQSVGEPGT QMTLRTFHFA GIRELNVTLG LPRLIEIVDA KKVPSTPMMT IYLTDEYKRD RDKALEVARK LEYTKIENVV SSTSIDIASM SIILQLDNEM LKDKGVTVDD VKKAIGRLKL GDFMIEESED STLNINFANI DSIAALFKLR DKILNTKIKG IKGIKRAIVQ KKGDEYIILT DGSNLSGVLS VKGVDVAKVE TNNIREIEEV FGIEAAREII IREISKVLAE QGLDVDIRHI LLIADVMTRT GIVRQIGRHG VTGEKNSVLA RAAFEVTVKH LLDAAARGDV EEFKGVVENI IIGHPIKLGT GMVELTMRPI LR //