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Database: UniProt
Entry: M1XL16_NATM8
LinkDB: M1XL16_NATM8
Original site: M1XL16_NATM8 
ID   M1XL16_NATM8            Unreviewed;       247 AA.
AC   M1XL16;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
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=rpoD {ECO:0000256|HAMAP-Rule:MF_00320,
GN   ECO:0000313|EMBL:CCQ36905.1};
GN   Synonyms=rpo3 {ECO:0000256|HAMAP-Rule:MF_00320};
GN   OrderedLocusNames=Nmlp_2752 {ECO:0000313|EMBL:CCQ36905.1};
OS   Natronomonas moolapensis (strain DSM 18674 / CECT 7526 / JCM 14361 /
OS   8.8.11).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Natronomonas.
OX   NCBI_TaxID=268739 {ECO:0000313|EMBL:CCQ36905.1, ECO:0000313|Proteomes:UP000011867};
RN   [1] {ECO:0000313|EMBL:CCQ36905.1, ECO:0000313|Proteomes:UP000011867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18674 / JCM 14361 / 8.8.11
RC   {ECO:0000313|Proteomes:UP000011867};
RX   PubMed=23516216; DOI=10.1128/genomeA.00095-13;
RA   Dyall-Smith M.L., Pfeiffer F., Oberwinkler T., Klee K., Rampp M., Palm P.,
RA   Gross K., Schuster S.C., Oesterhelt D.;
RT   "Genome of the haloarchaeon Natronomonas moolapensis, a neutrophilic member
RT   of a previously haloalkaliphilic genus.";
RL   Genome Announc. 1:e0009513-e0009513(2013).
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}.
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DR   EMBL; HF582854; CCQ36905.1; -; Genomic_DNA.
DR   RefSeq; WP_015409671.1; NC_020388.1.
DR   AlphaFoldDB; M1XL16; -.
DR   STRING; 268739.Nmlp_2752; -.
DR   GeneID; 14652198; -.
DR   KEGG; nmo:Nmlp_2752; -.
DR   eggNOG; arCOG04241; Archaea.
DR   HOGENOM; CLU_038421_3_1_2; -.
DR   OrthoDB; 84933at2157; -.
DR   Proteomes; UP000011867; 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: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:CCQ36905.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011867};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00320};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00320, ECO:0000313|EMBL:CCQ36905.1}.
FT   DOMAIN          16..244
FT                   /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT                   /evidence="ECO:0000259|SMART:SM00662"
SQ   SEQUENCE   247 AA;  27143 MW;  CD32269A7FC58FC7 CRC64;
     MSGQYDVTFI ERDERSARFL VRGISPAFAN GIRRAMVADV PTLSVDTVRV IENSSVMFDE
     QIALRLGLIP LTTPDDYEPE ETVTLAIDVE GPATAYSGDL VSSDGQVQPA EENVPIIDLK
     EGQRLELEAD AELGYGKDHA KHQGGVAVGY RHLQRVALGD DRDEFAEDDP EIIRGVIEDD
     GELVETASFD NDLSDRYPDR EVSVEDVPNA FVFDVETDGS MTVDELVLKA VESLRTRADE
     LEAAVQL
//
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