RPO5_METJA
ID RPO5_METJA Reviewed; 78 AA.
AC Q58443;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=DNA-directed RNA polymerase subunit Rpo5 {ECO:0000255|HAMAP-Rule:MF_00025};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00025};
DE AltName: Full=DNA-directed RNA polymerase subunit H {ECO:0000255|HAMAP-Rule:MF_00025};
GN Name=rpo5 {ECO:0000255|HAMAP-Rule:MF_00025};
GN Synonyms=rpoH {ECO:0000255|HAMAP-Rule:MF_00025}; OrderedLocusNames=MJ1039;
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 STRUCTURE BY NMR.
RX PubMed=10191143; DOI=10.1006/jmbi.1999.2638;
RA Thiru A., Hodach M., Eloranta J.J., Kostourou V., Weinzierl R.O.,
RA Matthews S.;
RT "RNA polymerase subunit H features a beta-ribbon motif within a novel fold
RT that is present in archaea and eukaryotes.";
RL J. Mol. Biol. 287:753-760(1999).
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_00025}.
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_00025};
CC -!- SUBUNIT: Part of the RNA polymerase complex. {ECO:0000255|HAMAP-
CC Rule:MF_00025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00025}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase
CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00025}.
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DR EMBL; L77117; AAB99042.1; -; Genomic_DNA.
DR PIR; F64429; F64429.
DR RefSeq; WP_010870552.1; NC_000909.1.
DR PDB; 1HMJ; NMR; -; A=1-78.
DR PDBsum; 1HMJ; -.
DR AlphaFoldDB; Q58443; -.
DR BMRB; Q58443; -.
DR SMR; Q58443; -.
DR STRING; 243232.MJ_1039; -.
DR EnsemblBacteria; AAB99042; AAB99042; MJ_1039.
DR GeneID; 1451936; -.
DR KEGG; mja:MJ_1039; -.
DR eggNOG; arCOG04258; Archaea.
DR HOGENOM; CLU_058320_4_0_2; -.
DR InParanoid; Q58443; -.
DR OMA; PKIYHDD; -.
DR OrthoDB; 123463at2157; -.
DR PhylomeDB; Q58443; -.
DR EvolutionaryTrace; Q58443; -.
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:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.940.20; -; 1.
DR HAMAP; MF_00025; RNApol_Rpo5_RPB5; 1.
DR InterPro; IPR014381; Arch_Rpo5/euc_Rpb5.
DR InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR InterPro; IPR020608; RNA_pol_subH/Rpb5_CS.
DR InterPro; IPR035913; RPB5-like_sf.
DR PANTHER; PTHR10535; PTHR10535; 1.
DR Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR SUPFAM; SSF55287; SSF55287; 1.
DR PROSITE; PS01110; RNA_POL_H_23KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..78
FT /note="DNA-directed RNA polymerase subunit Rpo5"
FT /id="PRO_0000146092"
SQ SEQUENCE 78 AA; 9001 MW; CDF2DAF342E6D41B CRC64;
MKVTDHILVP KHEIVPKEEV EEILKRYNIK IQQLPKIYED DPVIQEIGAK EGDVVRVIRK
SPTAGVSIAY RLVIKRII
