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Database: UniProt
Entry: L0A8X7_CALLD
LinkDB: L0A8X7_CALLD
Original site: L0A8X7_CALLD 
ID   L0A8X7_CALLD            Unreviewed;       280 AA.
AC   L0A8X7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
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=Calag_0551 {ECO:0000313|EMBL:AFZ70311.1};
OS   Caldisphaera lagunensis (strain DSM 15908 / JCM 11604 / ANMR 0165 /
OS   IC-154).
OC   Archaea; Thermoproteota; Thermoprotei; Acidilobales; Caldisphaeraceae;
OC   Caldisphaera.
OX   NCBI_TaxID=1056495 {ECO:0000313|EMBL:AFZ70311.1, ECO:0000313|Proteomes:UP000010469};
RN   [1] {ECO:0000313|Proteomes:UP000010469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15908 / JCM 11604 / IC-154
RC   {ECO:0000313|Proteomes:UP000010469};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "Complete genome of Caldisphaera lagunensis DSM 15908.";
RL   Submitted (MAR-2012) 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; CP003378; AFZ70311.1; -; Genomic_DNA.
DR   RefSeq; WP_015232209.1; NC_019791.1.
DR   AlphaFoldDB; L0A8X7; -.
DR   STRING; 1056495.Calag_0551; -.
DR   GeneID; 14211811; -.
DR   KEGG; clg:Calag_0551; -.
DR   eggNOG; arCOG04241; Archaea.
DR   HOGENOM; CLU_038421_3_1_2; -.
DR   InParanoid; L0A8X7; -.
DR   OrthoDB; 84933at2157; -.
DR   Proteomes; UP000010469; 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; 3.30.70.20; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000010469};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00320}; Transferase {ECO:0000256|HAMAP-Rule:MF_00320}.
FT   DOMAIN          14..273
FT                   /note="DNA-directed RNA polymerase RpoA/D/Rpb3-type"
FT                   /evidence="ECO:0000259|SMART:SM00662"
SQ   SEQUENCE   280 AA;  31322 MW;  B2271927905E4735 CRC64;
     MEKSVDILDF NNNRITVYLE GFPIAFGNAL RRLVLSDVPT MAVDYVYFYD NDTSVYDEII
     AHRLGLLVLK SDDAIHKYGL PENCAGKSET DTNCYTQIVL EKELSNDSGS GIYVKASDLK
     FSDASIKPAY PDTPIVYLAP GQRIHLVAYA RLGRGKEHGK WSPASASVLQ YTTLVDINGE
     KATDECIECV SYYKEVANSL KARENTTIEY KTNINTSGLR YCEESSCKDI IKVRYDSSRL
     LLTVESNGSL EPQQIILEAS NSLDRRVEEL LEKIEKVSNA
//
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