ID   RPO3_SULIN              Reviewed;         265 AA.
AC   C3NMQ0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 61.
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};
GN   Name=rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
GN   Synonyms=rpoD {ECO:0000255|HAMAP-Rule:MF_00320};
GN   OrderedLocusNames=YN1551_0745;
OS   Sulfolobus islandicus (strain Y.N.15.51 / Yellowstone #2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=419942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y.N.15.51 / Yellowstone #2;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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       Note=Binds 1 [3Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00320};
CC   -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC       Rule:MF_00320}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}.
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 other archaea shows this protein
CC       binds a 3Fe-4S cluster, although a 4Fe-4S cluster has been suggested to
CC       be present in this protein. {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; CP001404; ACP47870.1; -; Genomic_DNA.
DR   RefSeq; WP_012714155.1; NC_012623.1.
DR   AlphaFoldDB; C3NMQ0; -.
DR   SMR; C3NMQ0; -.
DR   EnsemblBacteria; ACP47870; ACP47870; YN1551_0745.
DR   GeneID; 7811732; -.
DR   KEGG; sin:YN1551_0745; -.
DR   HOGENOM; CLU_038421_3_1_2; -.
DR   OMA; ECLRHPE; -.
DR   Proteomes; UP000006818; 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: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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 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   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
DR   PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE   3: Inferred from homology;
KW   3Fe-4S; Cytoplasm; DNA-directed RNA polymerase; Iron; Iron-sulfur;
KW   Metal-binding; Nucleotidyltransferase; Transcription; Transferase.
FT   CHAIN           1..265
FT                   /note="DNA-directed RNA polymerase subunit Rpo3"
FT                   /id="PRO_1000205118"
FT   BINDING         203
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT   BINDING         206
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT   BINDING         209
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
SQ   SEQUENCE   265 AA;  30214 MW;  5E6CAED3635BFE7E CRC64;
     MSINLLHKDD KRIDLVFEGY PLEFVNAIRR ATMLYVPVMS IDDVYFIENN SPLYDEILAH
     RLALIPFTSE EALDTYRWPE ECIECTENCE KCYTKIYIEA EALNEPKMLY SKDIKSEDPS
     IVPISGDIPI VLLGANQKIS LEARLRLGYG KEHAKFIPVS LAIVRYYPKV EILGNCEKAA
     TVCPEGVFEL KDGKLSVKNE LACTLCEECL RYCNGLIRIS SIEDKYILEL ESVGSLKPER
     ILLEAGKSII RKIEELEKKL VEVIK