ID A0A101IKU9_9EURY Unreviewed; 264 AA.
AC A0A101IKU9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=XE07_0659 {ECO:0000313|EMBL:KUK97088.1};
OS Methanothrix harundinacea.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanotrichales; Methanotrichaceae; Methanothrix.
OX NCBI_TaxID=301375 {ECO:0000313|EMBL:KUK97088.1, ECO:0000313|Proteomes:UP000053961};
RN [1] {ECO:0000313|Proteomes:UP000053961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(2015).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK97088.1}.
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DR EMBL; LGHB01000005; KUK97088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101IKU9; -.
DR PATRIC; fig|301375.6.peg.1569; -.
DR Proteomes; UP000053961; Unassembled WGS sequence.
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; 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; PF12838; Fer4_7; 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.
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 Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_00320}; Transferase {ECO:0000256|HAMAP-Rule:MF_00320}.
FT DOMAIN 160..190
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 192..222
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 202
FT /ligand="[3Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:21137"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00320"
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"
SQ SEQUENCE 264 AA; 28233 MW; 9B3D6F0CDF701470 CRC64;
MELIELREDR ARFLLKGVKP AFANAIRRAC LSEVPSLAID EISIYDNTSV LFDEQLSLRL
GLVPIKADDL SLFSVPEECE CGGAGCPACQ VGMTLTAEGP CTVHSGDIRF ADPGEKVAFE
KIPIAILGEG EKLMLEGIVT LNRGTLHAKW QSGTHCGYKN LPDIQIADHC EGCGKCVEVC
PRKILVIGEA GGKLEVTDPT NCSLCKLCVN ECDVGAIKVV PIEDVFVMKI DTAGSMTAKD
LVAGAAAEVK RRASQLSEQL SELA
//
