ID RPO3_SACS2 Reviewed; 265 AA. AC P95989; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1997, sequence version 1. DT 27-MAR-2024, entry version 150. DE RecName: Full=DNA-directed RNA polymerase subunit Rpo3 {ECO:0000255|HAMAP-Rule:MF_00320}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00320}; DE AltName: Full=DNA-directed RNA polymerase subunit D {ECO:0000255|HAMAP-Rule:MF_00320, ECO:0000303|PubMed:18235446}; GN Name=rpo3 {ECO:0000255|HAMAP-Rule:MF_00320}; GN Synonyms=rpoD {ECO:0000255|HAMAP-Rule:MF_00320, GN ECO:0000303|PubMed:11427726}; OrderedLocusNames=SSO0071; GN ORFNames=C04_051 {ECO:0000303|PubMed:8899719}; 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 [GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=8899719; DOI=10.1111/j.1365-2958.1996.tb02666.x; RA Sensen C.W., Klenk H.-P., Singh R.K., Allard G., Chan C.C.-Y., Liu Q.Y., RA Penny S.L., Young F., Schenk M.E., Gaasterland T., Doolittle W.F., RA Ragan M.A., Charlebois R.L.; RT "Organizational characteristics and information content of an archaeal RT genome: 156 kb of sequence from Sulfolobus solfataricus P2."; RL Mol. Microbiol. 22:175-191(1996). RN [2] 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 [3] {ECO:0007744|PDB:2PA8, ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ} RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN RP COMPLEX WITH IRON-SULFUR (3FE-4S), X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) RP IN COMPLEX WITH RPO11 AND IRON-SULFUR (3FE-4S), IRON-SULFUR-BINDING, RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF CYS-183; CYS-203; CYS-206 AND RP CYS-209. 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_00320}. 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_00320}; CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00320, CC ECO:0000269|PubMed:18235446}; CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00320, CC ECO:0000269|PubMed:18235446}; CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. CC {ECO:0000269|PubMed:18235446}. CC -!- INTERACTION: CC P95989; Q980K0: rpo11; NbExp=2; IntAct=EBI-9022065, EBI-9022031; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}. CC -!- DOMAIN: The presence of the iron-sulfur cluster is required for CC assembly of the RNA polymerase complex. {ECO:0000269|PubMed:18235446}. CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00320}. CC -!- CAUTION: X-ray crystallography in this and other archaea shows this CC protein binds a 3Fe-4S cluster, although a 4Fe-4S cluster has been CC suggested to be present in this protein. {ECO:0000269|PubMed:18235446, CC 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; Y08257; CAA69531.1; -; Genomic_DNA. DR EMBL; AE006641; AAK40433.1; -; Genomic_DNA. DR PIR; S75417; S75417. DR RefSeq; WP_009988881.1; NC_002754.1. DR PDB; 2PA8; X-ray; 1.76 A; D=1-265. DR PDB; 2PMZ; X-ray; 3.40 A; D/S=1-265. DR PDB; 3HKZ; X-ray; 3.40 A; D/O=1-265. DR PDBsum; 2PA8; -. DR PDBsum; 2PMZ; -. DR PDBsum; 3HKZ; -. DR AlphaFoldDB; P95989; -. DR SMR; P95989; -. DR DIP; DIP-60646N; -. DR IntAct; P95989; 2. DR STRING; 273057.SSO0071; -. DR PaxDb; 273057-SSO0071; -. DR EnsemblBacteria; AAK40433; AAK40433; SSO0071. DR GeneID; 72911873; -. DR KEGG; sso:SSO0071; -. DR PATRIC; fig|273057.12.peg.72; -. DR eggNOG; arCOG04241; Archaea. DR HOGENOM; CLU_038421_3_1_2; -. DR InParanoid; P95989; -. DR PhylomeDB; P95989; -. DR BRENDA; 2.7.7.6; 6163. DR EvolutionaryTrace; P95989; -. 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:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR CDD; cd07030; RNAP_D; 1. DR Gene3D; 3.30.70.20; -; 1. DR Gene3D; 2.170.120.12; DNA-directed RNA polymerase, insert domain; 1. DR Gene3D; 3.30.1360.10; RNA polymerase, RBP11-like subunit; 1. DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1. DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS. DR InterPro; IPR011262; DNA-dir_RNA_pol_insert. DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. DR InterPro; IPR036603; RBP11-like. DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1. DR InterPro; IPR036643; RNApol_insert_sf. DR PANTHER; PTHR11800; DNA-DIRECTED RNA POLYMERASE; 1. DR PANTHER; PTHR11800:SF2; DNA-DIRECTED RNA POLYMERASE II SUBUNIT RPB3; 1. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF56553; Insert subdomain of RNA polymerase alpha subunit; 1. DR SUPFAM; SSF55257; RBP11-like subunits of RNA polymerase; 1. DR PROSITE; PS00446; RNA_POL_D_30KD; 1. PE 1: Evidence at protein level; KW 3D-structure; 3Fe-4S; Cytoplasm; DNA-directed RNA polymerase; Iron; KW Iron-sulfur; Metal-binding; Nucleotidyltransferase; Reference proteome; KW Transcription; Transferase. FT CHAIN 1..265 FT /note="DNA-directed RNA polymerase subunit Rpo3" FT /id="PRO_0000132765" FT BINDING 183 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000305|PubMed:18235446" FT BINDING 203 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320, FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PA8, FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ" FT BINDING 206 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320, FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PA8, FT ECO:0007744|PDB:3HKZ" FT BINDING 209 FT /ligand="[3Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:21137" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00320, FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PA8, FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ" FT MUTAGEN 183 FT /note="C->S: Abolishes iron-sulfur-binding, causing FT aggregation of Rpo3 and preventing the functional FT Rpo3-Rpo11 subcomplex from being formed; when associated FT with S-203; S-206 and S-209." FT /evidence="ECO:0000269|PubMed:18235446" FT MUTAGEN 203 FT /note="C->S: Abolishes iron-sulfur-binding, causing FT aggregation of Rpo3 and preventing the functional FT Rpo3-Rpo11 subcomplex from being formed; when associated FT with S-183; S-206 and S-209." FT /evidence="ECO:0000269|PubMed:18235446" FT MUTAGEN 206 FT /note="C->S: Abolishes iron-sulfur-binding, causing FT aggregation of Rpo3 and preventing the functional FT Rpo3-Rpo11 subcomplex from being formed; when associated FT with S-183; S-203 and S-209." FT /evidence="ECO:0000269|PubMed:18235446" FT MUTAGEN 209 FT /note="C->S: Abolishes iron-sulfur-binding, causing FT aggregation of Rpo3 and preventing the functional FT Rpo3-Rpo11 subcomplex from being formed; when associated FT with S-183; S-203 and S-206." FT /evidence="ECO:0000269|PubMed:18235446" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 10..20 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 22..34 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 38..49 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 55..62 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 72..75 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 79..81 FT /evidence="ECO:0007829|PDB:2PA8" FT TURN 90..92 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 93..101 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 103..105 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 111..113 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 115..118 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 129..133 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 138..148 FT /evidence="ECO:0007829|PDB:2PA8" FT TURN 150..152 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 154..156 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 159..172 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 179..182 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 188..191 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 200..202 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 208..213 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 216..232 FT /evidence="ECO:0007829|PDB:2PA8" FT STRAND 234..236 FT /evidence="ECO:0007829|PDB:2PA8" FT HELIX 238..263 FT /evidence="ECO:0007829|PDB:2PA8" SQ SEQUENCE 265 AA; 30294 MW; C5B9B863A78250AA CRC64; MSINLLHKDD TRIDLVFEGY PLEFVNAIRR ASMLYVPIMA VDDVYFIENN SPLYDEILAH RLALIPFMSE EALDTYRWPE ECIECTENCE KCYTKIYIEA EAPNEPRMIY SKDIKSEDPS VVPISGDIPI VLLGTNQKIS LEARLRLGYG KEHAKFIPVS LSVVRYYPKV EILANCEKAV NVCPEGVFEL KDGKLSVKNE LSCTLCEECL RYCNGSIRIS FVEDKYILEI ESVGSLKPER ILLEAGKSII RKIEELEKKL VEVVK //