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Database: UniProt
Entry: D2TTR9_CITRI
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ID   D2TTR9_CITRI            Unreviewed;      1076 AA.
AC   D2TTR9;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   11-JUN-2014, entry version 24.
DE   RecName: Full=Ribonuclease E;
DE            Short=RNase E;
DE            EC=3.1.26.12;
GN   Name=rne; OrderedLocusNames=ROD_11461;
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype
OS   4280).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168;
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M.,
RA   Schroeder G.N., Quail M.A., Lennard N., Corton C., Barron A.,
RA   Clark L., Toribio A.L., Parkhill J., Dougan G., Frankel G.,
RA   Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent
RT   evolution with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
CC   -!- FUNCTION: Endoribonuclease that plays a central role in RNA
CC       processing and decay. Required for the maturation of 5S and 16S
CC       rRNAs and the majority of tRNAs. Also involved in the degradation
CC       of most mRNAs (By similarity).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of single-stranded
CC       RNA in A- and U-rich regions.
CC   -!- COFACTOR: Binds 1 Mg(2+) ion per subunit (By similarity).
CC   -!- COFACTOR: Binds 2 Zn(2+) ions per homotetramer (By similarity).
CC   -!- SUBUNIT: Component of the RNA degradosome, which is a multiprotein
CC       complex involved in RNA processing and mRNA degradation. Within
CC       the RNA degradosome, Rnase E assembles into a homotetramer formed
CC       by a dimer of dimers (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Cell inner membrane; Peripheral
CC       membrane protein; Cytoplasmic side (By similarity).
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC   -!- SIMILARITY: Contains 1 S1 motif domain.
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DR   EMBL; FN543502; CBG87913.1; -; Genomic_DNA.
DR   RefSeq; YP_003364739.1; NC_013716.1.
DR   EnsemblBacteria; CBG87913; CBG87913; ROD_11461.
DR   GeneID; 8710616; -.
DR   KEGG; cro:ROD_11461; -.
DR   PATRIC; 32026184; VBICitRod33214_1122.
DR   HOGENOM; HOG000258027; -.
DR   KO; K08300; -.
DR   OMA; ENTKEVH; -.
DR   BioCyc; CROD637910:GJIG-1161-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00970; RNase_E; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR021968; PNPase_C.
DR   InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR022967; RNA-binding_domain_S1.
DR   InterPro; IPR028878; RNase_E.
DR   InterPro; IPR004659; RNase_E/G.
DR   Pfam; PF12111; PNPase_C; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00757; RNaseEG; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm;
KW   Endonuclease; Hydrolase; Magnesium; Membrane; Metal-binding; Nuclease;
KW   RNA-binding; rRNA processing; tRNA processing; Zinc.
FT   DOMAIN       39    119       S1 motif (By similarity).
FT   REGION      404    407       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity (By similarity).
FT   METAL       303    303       Magnesium; catalytic (By
FT                                similarity){EA3}.
FT   METAL       346    346       Magnesium; catalytic (By
FT                                similarity){EA3}.
FT   METAL       404    404       Zinc; shared with dimeric partner (By
FT                                similarity){EA3}.
FT   METAL       407    407       Zinc; shared with dimeric partner (By
FT                                similarity){EA3}.
SQ   SEQUENCE   1076 AA;  119537 MW;  58CE38146C3887BC CRC64;
     MKRMLINATQ QEELRVALVD GQRLYDLDIE SPGHEQKKAN IYKGKITRIE PSLEAAFVDY
     GAERHGFLPL KEIAREYFPA SYNAHGRPNI KDVLREGQEV IVQIDKEERG NKGAALTTFI
     SLAGSYLVLM PNNPRAGGIS RRIEGDDRTE LKEALASLEL PEGMGLIVRT AGVGKSAEAL
     QWDLSFRLKH WEAIQKAAES RPAPFLIHQE SNVIVRAFRD YLRQDIGEIL IDNPKVMEMA
     RQHIAALGRP DFSSKIKLYT GEIPLFSHYQ IESQIESAFQ REVRLPSGGS IVIDSTEALT
     AIDINSARAT RGGDIEETAF NTNLEAADEI ARQLRLRDLG GLIVIDFIDM TPVRHQRAVE
     NRLREAVRQD RARIQISHIS RFGLLEMSRQ RLSPSLGESS HHVCPRCSGT GTVRDNESLS
     LSILRLIEEE ALKENTQEVH AIVPVPIASY LLNEKRTAVN AIETRQNGVR CVIVPNDQME
     TPHYSVLRVR KGEETPTLSY MLPKLHEEAM ALPSEEEYAE RKRPEQPALA TFAMPDVPPA
     PEPAEPVVKA AAPKAAAAPA APAEPGLLSR LFGALKSLFS GGEEAKPAEQ PAPKAAEKPE
     RQQDRRKRQN NRRDRNDRNE RSERRDSRDN RSERAESGES RDENRRNRRQ AQQSADRDNR
     QQTAEVAEKA KSGDEQQPQP RRERNRRRSE EKRQAQQEVK ALSIDEQQTQ DTEQEERVRP
     AQPRRKQRQL AQKVRYTDNA ADSEVVVAQV SEEKVATPVA EESAPVQSTE LAKVPLPVVA
     EAPQEQEESS EARDSAGMPR RSRRSPRHLR VSGQRRRRYR DERYPLQSPM PLTVACASPE
     MASGKVWIRY PVARPQDAEQ REQEIEQVQA QPVAAEPQAV VAAVEVAETV VETVAQQAPV
     QPEETIETTH PEVIAAPVDE QPQVIAEADV PVAEEVAAEA QPVVAAEESA PVAEETAEVV
     TVEPEVAVEP VAVEPEVVAE PVKEQDVVEE VVAPAPVAAP VETVKVEKPV AVTPLAEHSH
     ATAPMTRAPA PEYVPEAPRH SEWQRPAFVF EGKGAAGGHS ATHHASAAPT RPQPVE
//
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