ID   RPO3_METJA              Reviewed;         191 AA.
AC   Q57648;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
DE            EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00320};
DE   AltName: Full=DNA-directed RNA polymerase subunit D {ECO:0000255|HAMAP-Rule:MF_00320};
DE            Short=mjD {ECO:0000303|PubMed:11058130};
GN   Name=rpo3 {ECO:0000255|HAMAP-Rule:MF_00320};
GN   Synonyms=rpoD {ECO:0000255|HAMAP-Rule:MF_00320}; OrderedLocusNames=MJ0192;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   INTERACTION WITH RPO12, AND SUBUNIT.
RX   PubMed=11058130; DOI=10.1093/nar/28.21.4299;
RA   Werner F., Eloranta J.J., Weinzierl R.O.;
RT   "Archaeal RNA polymerase subunits F and P are bona fide homologs of
RT   eukaryotic RPB4 and RPB12.";
RL   Nucleic Acids Res. 28:4299-4305(2000).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00320};
CC   -!- SUBUNIT: Part of the RNA polymerase complex (By similarity). Interacts
CC       with Rpo12. Forms an Rpo3-Rpo10-Rpo11-Rpo12 complex upon coexpression
CC       (PubMed:11058130). {ECO:0000255|HAMAP-Rule:MF_00320,
CC       ECO:0000269|PubMed:11058130}.
CC   -!- INTERACTION:
CC       Q57648; Q57832: rpo11; NbExp=3; IntAct=EBI-2567023, EBI-2567038;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}.
CC   -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC       subunit family. {ECO:0000255|HAMAP-Rule:MF_00320}.
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DR   EMBL; L77117; AAB98172.1; -; Genomic_DNA.
DR   PIR; A64324; A64324.
DR   RefSeq; WP_010869687.1; NC_000909.1.
DR   AlphaFoldDB; Q57648; -.
DR   SMR; Q57648; -.
DR   IntAct; Q57648; 3.
DR   STRING; 243232.MJ_0192; -.
DR   EnsemblBacteria; AAB98172; AAB98172; MJ_0192.
DR   GeneID; 1451040; -.
DR   KEGG; mja:MJ_0192; -.
DR   eggNOG; arCOG04241; Archaea.
DR   HOGENOM; CLU_038421_3_1_2; -.
DR   InParanoid; Q57648; -.
DR   OMA; AKWQPCN; -.
DR   OrthoDB; 72726at2157; -.
DR   PhylomeDB; Q57648; -.
DR   Proteomes; UP000000805; 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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.170.120.12; -; 1.
DR   Gene3D; 3.30.1360.10; -; 2.
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   Pfam; PF01000; RNA_pol_A_bac; 1.
DR   Pfam; PF01193; RNA_pol_L; 1.
DR   SMART; SM00662; RPOLD; 1.
DR   SUPFAM; SSF55257; SSF55257; 1.
DR   SUPFAM; SSF56553; SSF56553; 1.
DR   PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW   Reference proteome; Transcription; Transferase.
FT   CHAIN           1..191
FT                   /note="DNA-directed RNA polymerase subunit Rpo3"
FT                   /id="PRO_0000132754"
SQ   SEQUENCE   191 AA;  21699 MW;  3F5B96CA0D242A96 CRC64;
     MITIKEKRKT RIGEEFIFSL KAPISFSNAI RRIMISEVPT FAIEDVYIYE NSSSMDDEIL
     AHRLGLIPIK GKPLLENEVI TFTLEKEGPC TVYSSDLKSE NGEVAFKNIP IVKLGKGQRI
     QIECEAIPGI GKVHAKWQPC NAVYKQIADD EVEFFVETFG QMEAEEILEE AVKILKNKAE
     SFLQQLEMIE Q