ID   RPO3_METMA              Reviewed;         266 AA.
AC   Q8PV16;
DT   10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   10-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 137.
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}; OrderedLocusNames=MM_2158;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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}.
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DR   EMBL; AE008384; AAM31854.1; -; Genomic_DNA.
DR   RefSeq; WP_011034089.1; NC_003901.1.
DR   AlphaFoldDB; Q8PV16; -.
DR   SMR; Q8PV16; -.
DR   STRING; 192952.MM_2158; -.
DR   EnsemblBacteria; AAM31854; AAM31854; MM_2158.
DR   GeneID; 44088201; -.
DR   KEGG; mma:MM_2158; -.
DR   PATRIC; fig|192952.21.peg.2475; -.
DR   eggNOG; arCOG04241; Archaea.
DR   HOGENOM; CLU_038421_3_1_2; -.
DR   OMA; ECLRHPE; -.
DR   Proteomes; UP000000595; 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; IPR017896; 4Fe4S_Fe-S-bd.
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; PS00198; 4FE4S_FER_1; 1.
DR   PROSITE; PS51379; 4FE4S_FER_2; 2.
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; Reference proteome; Transcription;
KW   Transferase.
FT   CHAIN           1..266
FT                   /note="DNA-directed RNA polymerase subunit Rpo3"
FT                   /id="PRO_0000132756"
FT   BINDING         205
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT   BINDING         208
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
FT   BINDING         211
FT                   /ligand="[3Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21137"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00320"
SQ   SEQUENCE   266 AA;  28896 MW;  CE9A899955EA47EF CRC64;
     MTMEVDILEL SDRSAKFVLS RVSMAFANGV RRAMIADVPT LAIEYVNLYD NTSVLYDEQL
     ALRLSLIPLV TDIETYMPQA ECEVCGGEGC PACEVSLTLS AEGPGTVYSR DLISSDPKIQ
     PADPNIPIVE LKKGQKLVLE AIAHMGYGRD SVKWQAGVAC GYKNVPVITI ENCDACGHCA
     AECPKGIIRV EEAGARIAED DLIKCSLCRL CEQVCDINAI KVDFYENAFV FTMESDGSYT
     AKDLTINAAN VIKGKAEELL AILDQL