ID Q46GD0_METBF Unreviewed; 266 AA.
AC Q46GD0;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 126.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo3 {ECO:0000256|HAMAP-Rule:MF_00320};
DE EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_00320};
DE AltName: Full=DNA-directed RNA polymerase subunit D {ECO:0000256|HAMAP-Rule:MF_00320};
GN Name=rpo3 {ECO:0000256|HAMAP-Rule:MF_00320};
GN Synonyms=rpoD {ECO:0000256|HAMAP-Rule:MF_00320};
GN OrderedLocusNames=Mbar_A0075 {ECO:0000313|EMBL:AAZ69062.1};
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797 {ECO:0000313|EMBL:AAZ69062.1};
RN [1] {ECO:0000313|EMBL:AAZ69062.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fusaro {ECO:0000313|EMBL:AAZ69062.1};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Goodwin L.A., Saunders E.H., Schmutz J.,
RA Larimer F., Land M., Anderson I., Richardson P.;
RT "Complete sequence of chromosome 1 of Methanosarcina barkeri str. fusaro.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00320};
CC -!- COFACTOR:
CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00320};
CC Note=Binds 1 [3Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00320};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000256|HAMAP-
CC Rule:MF_00320}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00320}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000256|ARBA:ARBA00025804, ECO:0000256|HAMAP-
CC Rule:MF_00320}.
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DR EMBL; CP000099; AAZ69062.1; -; Genomic_DNA.
DR AlphaFoldDB; Q46GD0; -.
DR STRING; 269797.Mbar_A0075; -.
DR PaxDb; 269797-Mbar_A0075; -.
DR KEGG; mba:Mbar_A0075; -.
DR eggNOG; arCOG04241; Archaea.
DR HOGENOM; CLU_038421_3_1_2; -.
DR OrthoDB; 84933at2157; -.
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:0016491; F:oxidoreductase activity; IEA:UniProt.
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; 3.30.70.3110; -; 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; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
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; 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 {ECO:0000256|HAMAP-Rule:MF_00320};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00320};
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_00320}; Iron {ECO:0000256|HAMAP-Rule:MF_00320};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00320};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00320};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00320,
KW ECO:0000313|EMBL:AAZ69062.1};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00320};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00320, ECO:0000313|EMBL:AAZ69062.1}.
FT DOMAIN 164..193
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 196..225
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 205
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00320"
FT BINDING 208
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00320"
FT BINDING 211
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00320"
SQ SEQUENCE 266 AA; 28803 MW; E26E04E2106CACBF CRC64;
MTMEVDILEL SDRSAKFVLS KVSTSFANGI RRAMIADVPT LAIEYVNLYE NTSVLYDEQL
ALRLSLIPLV TDVETYVPQA ECDVCGGEGC PACEVSLTLS AEGPCTVYSR DLISSDPKIQ
PADPNIPIVE LKKGQKLVLE ALAHMGYGRD SVKWQAGVAC GYKNVPVITI ENCDACGHCA
AECPKGIIRF EESGAKVSSE DVLKCSLCKL CEQVCDIHAI KIGFDENAFV FTMESDGSYT
AKDLALNASN VIKGKAEELL SILDQF
//
