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Entry: A0A0A7V0K7_9ARCH
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Original site: A0A0A7V0K7_9ARCH 
ID   A0A0A7V0K7_9ARCH        Unreviewed;       200 AA.
AC   A0A0A7V0K7;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
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=rpoA {ECO:0000313|EMBL:AJA92418.1};
GN   Synonyms=rpo3 {ECO:0000256|HAMAP-Rule:MF_00320}, rpoD
GN   {ECO:0000256|HAMAP-Rule:MF_00320};
GN   ORFNames=A7X95_07070 {ECO:0000313|EMBL:PTL87619.1}, T478_0402
GN   {ECO:0000313|EMBL:AJA92418.1};
OS   Candidatus Nitrosopelagicus brevis.
OC   Archaea; Nitrososphaerota.
OX   NCBI_TaxID=1410606 {ECO:0000313|EMBL:AJA92418.1, ECO:0000313|Proteomes:UP000030944};
RN   [1] {ECO:0000313|EMBL:AJA92418.1, ECO:0000313|Proteomes:UP000030944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CN25 {ECO:0000313|EMBL:AJA92418.1}, and V2
RC   {ECO:0000313|Proteomes:UP000030944};
RX   PubMed=25587132; DOI=10.1073/pnas.1416223112;
RA   Santoro A.E., Dupont C.L., Richter R.A., Craig M.T., Carini P.,
RA   McIlvin M.R., Yang Y., Orsi W.D., Moran D.M., Saito M.A.;
RT   "Genomic and proteomic characterization of "Candidatus Nitrosopelagicus
RT   brevis": An ammonia-oxidizing archaeon from the open ocean.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:1173-1178(2015).
RN   [2] {ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|Proteomes:UP000241022};
RA   Dupont C., Santoro A.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:PTL87619.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL87619.1};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:PTL87619.1, ECO:0000313|Proteomes:UP000241022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U25 {ECO:0000313|EMBL:PTL87619.1,
RC   ECO:0000313|Proteomes:UP000241022};
RA   Carini P.;
RT   "Transcriptomics of ammonia oxidizing archaea.";
RL   Submitted (APR-2018) 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   -!- 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; CP007026; AJA92418.1; -; Genomic_DNA.
DR   EMBL; LXWN01000002; PTL87619.1; -; Genomic_DNA.
DR   RefSeq; WP_048104766.1; NZ_LXWN01000002.1.
DR   STRING; 1410606.T478_0402; -.
DR   GeneID; 24816299; -.
DR   KEGG; nbv:T478_0402; -.
DR   HOGENOM; CLU_038421_3_2_2; -.
DR   OrthoDB; 84933at2157; -.
DR   Proteomes; UP000030944; Chromosome.
DR   Proteomes; UP000241022; 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; 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; 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.
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:AJA92418.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030944};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00320};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00320, ECO:0000313|EMBL:AJA92418.1}.
FT   DOMAIN          12..195
FT                   /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT                   /evidence="ECO:0000259|SMART:SM00662"
SQ   SEQUENCE   200 AA;  21738 MW;  F3AD15E97742FD0D CRC64;
     MSLEIINENE EKVSVKIKGV PLQYANALRR ICLNGVPIYA VESVDMLENS SVLADEGVAH
     RVGLIPLKTD LESSKADNEN DKIMLTLDSG ISDETRTILS GDLKSQDSNV VPTSDDIPIV
     TLAPGQSIKF EAHARLGKGT EHAKWNSANI VTLTESDKDD ERILTVESTG ALNPKHIILS
     SVEQLASKLS EFKTTISEIK
//
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