RPO4_METJA
ID RPO4_METJA Reviewed; 115 AA.
AC Q60351;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo4 {ECO:0000255|HAMAP-Rule:MF_00864};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00864};
DE AltName: Full=DNA-directed RNA polymerase subunit F {ECO:0000255|HAMAP-Rule:MF_00864, ECO:0000303|PubMed:11058130};
DE Short=mjF {ECO:0000303|PubMed:11058130};
GN Name=rpo4 {ECO:0000255|HAMAP-Rule:MF_00864};
GN Synonyms=rpoF {ECO:0000255|HAMAP-Rule:MF_00864}; OrderedLocusNames=MJ0039;
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 RPO7, 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).
RN [3] {ECO:0007744|PDB:1GO3}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 9-115, AND SUBUNIT.
RX PubMed=11741548; DOI=10.1016/s1097-2765(01)00379-3;
RA Todone F., Brick P., Werner F., Weinzierl R.O., Onesti S.;
RT "Structure of an archaeal homolog of the eukaryotic RNA polymerase II
RT RPB4/RPB7 complex.";
RL Mol. Cell 8:1137-1143(2001).
CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC transcription of DNA into RNA using the four ribonucleoside
CC triphosphates as substrates. This subunit is less well bound than the
CC others. {ECO:0000255|HAMAP-Rule:MF_00864}.
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_00864};
CC -!- SUBUNIT: Part of the RNA polymerase complex. Forms a stalk with Rpo7
CC that extends from the main structure. {ECO:0000255|HAMAP-Rule:MF_00864,
CC ECO:0000269|PubMed:11741548, ECO:0000305|PubMed:11058130}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00864}.
CC -!- SIMILARITY: Belongs to the eukaryotic RPB4 RNA polymerase subunit
CC family. {ECO:0000255|HAMAP-Rule:MF_00864, ECO:0000305|PubMed:11741548}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305|PubMed:11741548}.
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DR EMBL; L77117; AAB98020.1; -; Genomic_DNA.
DR PIR; G64304; G64304.
DR PDB; 1GO3; X-ray; 1.75 A; F/N=9-115.
DR PDBsum; 1GO3; -.
DR AlphaFoldDB; Q60351; -.
DR SMR; Q60351; -.
DR IntAct; Q60351; 1.
DR STRING; 243232.MJ_0039; -.
DR EnsemblBacteria; AAB98020; AAB98020; MJ_0039.
DR KEGG; mja:MJ_0039; -.
DR eggNOG; arCOG01016; Archaea.
DR HOGENOM; CLU_165892_1_0_2; -.
DR InParanoid; Q60351; -.
DR OMA; VDIMPED; -.
DR PhylomeDB; Q60351; -.
DR EvolutionaryTrace; Q60351; -.
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:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR Gene3D; 1.10.150.80; -; 1.
DR HAMAP; MF_00864; RNApol_arch_Rpo4; 1.
DR InterPro; IPR010997; HRDC-like_sf.
DR InterPro; IPR044876; HRDC_dom_sf.
DR InterPro; IPR005574; Rpb4/RPC9.
DR InterPro; IPR010924; Rpo4.
DR PANTHER; PTHR39646; PTHR39646; 1.
DR Pfam; PF03874; RNA_pol_Rpb4; 1.
DR PIRSF; PIRSF005053; RNA_pol_F_arch; 1.
DR SUPFAM; SSF47819; SSF47819; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..115
FT /note="DNA-directed RNA polymerase subunit Rpo4"
FT /id="PRO_0000106663"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 22..35
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 40..52
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 57..69
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:1GO3"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:1GO3"
SQ SEQUENCE 115 AA; 13389 MW; 898CE40770B73730 CRC64;
MYQAKRERMI GKKILGERYV TVSEAAEIMY NRAQIGELSY EQGCALDYLQ KFAKLDKEEA
KKLVEELISL GIDEKTAVKI ADILPEDLDD LRAIYYKREL PENAEEILEI VRKYI
