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Database: UniProt/TrEMBL
Entry: Q8YGV0_BRUME
LinkDB: Q8YGV0_BRUME
Original site: Q8YGV0_BRUME 
ID   Q8YGV0_BRUME            Unreviewed;       891 AA.
AC   Q8YGV0; D0B2X3;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   09-JUL-2014, entry version 80.
DE   RecName: Full=Ribonuclease E;
DE            Short=RNase E;
DE            EC=3.1.26.12;
GN   Name=rne; OrderedLocusNames=BMEI1057; ORFNames=BAWG_1153;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=16M;
RA   Letesson J.-J.;
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M, and 16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA   Haselkorn R., Kyrpides N., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen
RT   Brucella melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=16M;
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E.,
RA   Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Walk T., White J., Yandava C., Whatmore A.M.,
RA   Perrett L.L., O'Callaghan D., Nusbaum C., Galagan J., Birren B.;
RT   "The Genome Sequence of Brucella melitensis bv. 1 str. 16M.";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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: Homotetramer formed 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; AE008917; AAL52238.1; -; Genomic_DNA.
DR   EMBL; GG703778; EEW89045.1; -; Genomic_DNA.
DR   PIR; AC3384; AC3384.
DR   RefSeq; NP_539974.1; NC_003317.1.
DR   STRING; 224914.BMEI1057; -.
DR   EnsemblBacteria; AAL52238; AAL52238; BMEI1057.
DR   EnsemblBacteria; EEW89045; EEW89045; BAWG_1153.
DR   GeneID; 1196768; -.
DR   KEGG; bme:BMEI1057; -.
DR   PATRIC; 17797932; VBIBruMel146950_0781.
DR   eggNOG; COG1530; -.
DR   HOGENOM; HOG000258026; -.
DR   KO; K08300; -.
DR   OMA; MLQPQVT; -.
DR   OrthoDB; EOG6PCPTH; -.
DR   BioCyc; BMEL224914:GCJ0-1091-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:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; -; 2.
DR   HAMAP; MF_00970; RNase_E; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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   InterPro; IPR001878; Znf_CCHC.
DR   Pfam; PF10150; RNase_E_G; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00316; S1; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF50249; SSF50249; 2.
DR   TIGRFAMs; TIGR00757; RNaseEG; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Cytoplasm;
KW   Endonuclease; Hydrolase; Magnesium; Membrane; Metal-binding;
KW   Metalloprotease; Nuclease; Protease; RNA-binding; rRNA processing;
KW   tRNA processing; Zinc.
FT   REGION      532    535       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity (By similarity).
FT   METAL       431    431       Magnesium; catalytic (By
FT                                similarity){EA4}.
FT   METAL       474    474       Magnesium; catalytic (By
FT                                similarity){EA4}.
FT   METAL       532    532       Zinc; shared with dimeric partner (By
FT                                similarity){EA4}.
FT   METAL       535    535       Zinc; shared with dimeric partner (By
FT                                similarity){EA4}.
SQ   SEQUENCE   891 AA;  100323 MW;  B76EEDDFC870C0CC CRC64;
     MSNKMLIDAS HPEETRVIVT RGNKIEEFDF ESEHKKQLKG NIYLARVTRV EPSLQAAFVE
     YGGNRHGFLA FSEIHPDYYQ IPVADRLALL EAEAKAARAE DDEDEPRAKS DRSERNDRAR
     RNRRRGGRRD GQNGEAQANG ADKDLPAAEP VGPGFADYVA GTPAAALTQK GDIISEALDN
     GDDDDVENEE DMVESVGSED ALEELPTHTR THRRQYNIQE VIKRRQILLV QVVKEERGNK
     GAALTTYLSL AGRYSVLMPN TARGGGISRK ITNPQDRKRL KEIVKELEVP QGMGVILRTA
     GANRTKAEVK RDYEYLMRLW ENVRTLTLQS TAPALVYEEG SLIKRSIRDI YNKDITEILV
     SGENGYREAK DFMRMLMPSH AKVVQPYRDH IPIFTRNGVE AQLDRMLVPQ VTLKSGGYLI
     INQTEALVAI DVNSGRSTRE HSIEDTALQT NLEAAEEVAR QLRLRDLAGL IVVDFIDMEE
     KRNNRAVEKK MKECLKDDRA RIQVGRISHF GLLEMSRQRI RASVLESTMQ VCPHCGGTGH
     IRSDSSMALH IIRGIEDYLL RHSGFDIHVR TPAASALYVL NHKRQILADL EGRFGVEISI
     DADESVGNQH FVIDKGAPST RPVTPSAVQP MVYEDDIEDP EIPVEEDETE EEARTDVQAG
     EERSEENDRK RRRRRRRRGG RERDGRDLSA QEEAVSEEAS EEDNETDQAN EAVSSASMSE
     EDRRKKRRRG RRGGRKNRRE DDNRARRIPD PEFVGYTPVL PVKAEESIGE VVETVETVEA
     PVVEAAPEEK PEKPARKTRT RKKAVDEAPA DEAAAPAEEV VPEKPKRRTR KAAAKPVVEA
     EDVAEVKETV AAETQVETIA EPKSTEPVVT SSESEDRKPK RSGWWQKKGF F
//
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