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Entry: L9WFA8_9EURY
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Original site: L9WFA8_9EURY 
ID   L9WFA8_9EURY            Unreviewed;       249 AA.
AC   L9WFA8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 43.
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=C495_01910 {ECO:0000313|EMBL:ELY48190.1};
OS   Natronorubrum sulfidifaciens JCM 14089.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC   Natrialbaceae; Natronorubrum.
OX   NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY48190.1, ECO:0000313|Proteomes:UP000011661};
RN   [1] {ECO:0000313|EMBL:ELY48190.1, ECO:0000313|Proteomes:UP000011661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY48190.1,
RC   ECO:0000313|Proteomes:UP000011661};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
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   -!- 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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-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:ELY48190.1}.
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DR   EMBL; AOHX01000025; ELY48190.1; -; Genomic_DNA.
DR   RefSeq; WP_008159495.1; NZ_AOHX01000025.1.
DR   AlphaFoldDB; L9WFA8; -.
DR   STRING; 1230460.C495_01910; -.
DR   PATRIC; fig|1230460.4.peg.382; -.
DR   eggNOG; arCOG04241; Archaea.
DR   OrthoDB; 84933at2157; -.
DR   Proteomes; UP000011661; 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: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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
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; 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   3: Inferred from homology;
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};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00320,
KW   ECO:0000313|EMBL:ELY48190.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011661};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00320};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00320, ECO:0000313|EMBL:ELY48190.1}.
FT   DOMAIN          16..246
FT                   /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT                   /evidence="ECO:0000259|SMART:SM00662"
SQ   SEQUENCE   249 AA;  27590 MW;  ADE0A387417F4A84 CRC64;
     MTEDYDVEFV EHEDRYARFL VRGVTPAFAN GLRRAMLADV PTLAIDTVRF IENSSVMFDE
     QLALRLGLVP LTTPPEAEFA EGDTVTLSID VEGPATAYSG DLVSSDDLVQ PADENVPIID
     LKDDQRLEAE ADAVFNRGKN HAKHQGAVSA GYRHLQRVEV VDDLPEFEEQ ESRIIRGVIE
     ADGELIQTSE FDHDLSNRYP GKQVEIEDVP NAFVFNIETD GSFPVDELVT RAADSIEARA
     AELEDAVQL
//
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