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Database: UniProt/TrEMBL
Entry: C6WYW9_METML
LinkDB: C6WYW9_METML
Original site: C6WYW9_METML 
ID   C6WYW9_METML            Unreviewed;        70 AA.
AC   C6WYW9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   19-FEB-2014, entry version 30.
DE   RecName: Full=DNA-directed RNA polymerase subunit omega;
DE            Short=RNAP omega subunit;
DE            EC=2.7.7.6;
DE   AltName: Full=RNA polymerase omega subunit;
DE   AltName: Full=Transcriptase subunit omega;
GN   Name=rpoZ; OrderedLocusNames=Mmol_0184;
OS   Methylotenera mobilis (strain JLW8 / ATCC BAA-1282 / DSM 17540).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Methylophilales;
OC   Methylophilaceae; Methylotenera.
OX   NCBI_TaxID=583345;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLW8 / ATCC BAA-1282 / DSM 17540;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., LaButti K.M., Clum A., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Kayluzhnaya M.,
RA   Chistoserdova L.;
RT   "Complete sequence of Methylotenera mobilis JLW8.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes RNA polymerase assembly. Latches the N- and C-
CC       terminal regions of the beta' subunit thereby facilitating its
CC       interaction with the beta and alpha subunits (By similarity).
CC   -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
CC       + RNA(n+1).
CC   -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1
CC       beta' and 1 omega subunit. When a sigma factor is associated with
CC       the core the holoenzyme is formed, which can initiate
CC       transcription (By similarity).
CC   -!- SIMILARITY: Belongs to the RNA polymerase subunit omega family.
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DR   EMBL; CP001672; ACT47094.1; -; Genomic_DNA.
DR   RefSeq; YP_003047621.1; NC_012968.1.
DR   STRING; 583345.Mmol_0184; -.
DR   EnsemblBacteria; ACT47094; ACT47094; Mmol_0184.
DR   GeneID; 8171597; -.
DR   KEGG; mmb:Mmol_0184; -.
DR   PATRIC; 22610493; VBIMetMob89187_0186.
DR   eggNOG; COG1758; -.
DR   HOGENOM; HOG000245721; -.
DR   KO; K03060; -.
DR   OMA; PNRFQLT; -.
DR   OrthoDB; EOG6Q5NV5; -.
DR   ProtClustDB; PRK00392; -.
DR   BioCyc; MMOB583345:GHCF-185-MONOMER; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.90.940.10; -; 1.
DR   HAMAP; MF_00366; RNApol_bact_RpoZ; 1.
DR   InterPro; IPR003716; DNA-dir_RNA_pol_omega.
DR   InterPro; IPR006110; Pol_omega/K/RPB6.
DR   InterPro; IPR012293; RNAP_RPB6_omega.
DR   Pfam; PF01192; RNA_pol_Rpb6; 1.
DR   SUPFAM; SSF63562; SSF63562; 1.
DR   TIGRFAMs; TIGR00690; rpoZ; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA-directed RNA polymerase;
KW   Nucleotidyltransferase; Transcription; Transferase.
SQ   SEQUENCE   70 AA;  7711 MW;  707ED83C4ED76F03 CRC64;
     MARITVDDCL EKIPNRFQLT LVAAYRARQL HNGAEPQVNV QNTRDKSTVV ALREIAAGKV
     GVEILARGHS
//
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