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Database: UniProt
Entry: A6SXN9_JANMA
LinkDB: A6SXN9_JANMA
Original site: A6SXN9_JANMA 
ID   A6SXN9_JANMA            Unreviewed;       974 AA.
AC   A6SXN9;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   05-JUN-2019, entry version 63.
DE   RecName: Full=Ribonuclease E {ECO:0000256|HAMAP-Rule:MF_00970};
DE            Short=RNase E {ECO:0000256|HAMAP-Rule:MF_00970};
DE            EC=3.1.26.12 {ECO:0000256|HAMAP-Rule:MF_00970};
GN   Name=rne {ECO:0000256|HAMAP-Rule:MF_00970,
GN   ECO:0000313|EMBL:ABR88437.1};
GN   OrderedLocusNames=mma_1346 {ECO:0000313|EMBL:ABR88437.1};
OS   Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=375286 {ECO:0000313|EMBL:ABR88437.1, ECO:0000313|Proteomes:UP000006388};
RN   [1] {ECO:0000313|EMBL:ABR88437.1, ECO:0000313|Proteomes:UP000006388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marseille {ECO:0000313|EMBL:ABR88437.1,
RC   ECO:0000313|Proteomes:UP000006388};
RX   PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA   Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M.,
RA   Raoult D., Drancourt M.;
RT   "Genome analysis of Minibacterium massiliensis highlights the
RT   convergent evolution of water-living bacteria.";
RL   PLoS Genet. 3:1454-1463(2007).
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. {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and
CC         U-rich regions.; EC=3.1.26.12; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC       Note=Binds 2 Zn(2+) ions per homotetramer. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- SUBUNIT: Homotetramer formed by a dimer of dimers.
CC       {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}.
CC       Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic
CC       side {ECO:0000256|HAMAP-Rule:MF_00970}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. RNase E subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00970}.
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DR   EMBL; CP000269; ABR88437.1; -; Genomic_DNA.
DR   RefSeq; WP_012079203.1; NC_009659.1.
DR   STRING; 375286.mma_1346; -.
DR   EnsemblBacteria; ABR88437; ABR88437; mma_1346.
DR   KEGG; mms:mma_1346; -.
DR   eggNOG; ENOG4107QQB; Bacteria.
DR   eggNOG; COG1530; LUCA.
DR   HOGENOM; HOG000258027; -.
DR   KO; K08300; -.
DR   OMA; DHLETPH; -.
DR   OrthoDB; 1209444at2; -.
DR   BioCyc; JSP375286:MMA_RS07000-MONOMER; -.
DR   Proteomes; UP000006388; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00970; RNase_E; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR028878; RNase_E.
DR   InterPro; IPR004659; RNase_E/G.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
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 {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006388};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00970,
KW   ECO:0000313|EMBL:ABR88437.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006388};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00970};
KW   rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   DOMAIN       39    124       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      402    405       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   REGION      505    527       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A6SXN9}.
FT   REGION      574    681       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A6SXN9}.
FT   REGION      712    785       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A6SXN9}.
FT   REGION      947    974       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A6SXN9}.
FT   COMPBIAS    508    525       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A6SXN9}.
FT   COMPBIAS    584    623       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A6SXN9}.
FT   COMPBIAS    638    678       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A6SXN9}.
FT   COMPBIAS    755    773       Polar. {ECO:0000256|MobiDB-lite:A6SXN9}.
FT   METAL       301    301       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       344    344       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       402    402       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       405    405       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   974 AA;  106266 MW;  2234B220796A8E10 CRC64;
     MKRMLFNATQ QEELRVAIVN GQKLIDIDIE TTGREQRKSN IYKGVITRIE PSLEACFVSY
     GEDRHGFLPF KEVARTYFKE GVDVRNASIK DALREGQEIM VQVEKEERGN KGAALTSFIS
     LAGRYLVLMP NNPRGGGVSR RVEGEDRQEL RETMDKLDLP QGMSVIARTA GIGRNVDELQ
     WDLNYLMQLW RAIEGAGQSG GGAFLIYQES SLVIRAIRDY FQPDIGEILI DTDEIYEQAQ
     QFMSHVMPDM VHRVKRYRDD VPLFSRFQIE HQIETAYSRT VPLPSGGAIV IDHTEALVSV
     DVNSARATRG SDIETTAFHT NCEAAEEVAR QLRLRDLGGL IVIDFIDMEN AKNQREVETR
     LKDALHYDRA RVQMGKISRF GLMELSRQRL RPSLSEGSHV TCPRCNGTGH IRDTESSALQ
     VLRIIQEEAM KENSASIHVQ APVDVAAFLL NEKRGEILKI ETRHRVSVIL IPNKHLETPH
     YKLERIKHDD PRLEETQASY AMTEEADTDI SYGKRQKEEG KPRQEAMVKG ITPDQPAPIV
     ERKPVEAAKA APVEAKGFFQ KLFAFLGGGA EQPKAAAAQP AAEDKQQRSR ERGERNANGG
     RNQRNRSRGG RGRDREERDE TAKPAQAPAA AEAQARPPRP PREPREPREP REGNAEGQGR
     RERTPRPPRE ERKEVVAEDP ALLQGAAIAA SVAPARNAVP AGEAGEAIVV LDANGIPVPA
     AEGEEQPRRR RRRGGRNRNR RDRDNAEAGT ENEGNEDGVN ATQEQQDDGE QNAAAPQVQP
     REVAPAAVNE AVATEAPVSA LTAAIAAPLV PQEVAREEVA VPAVVFTHEP VAQVVEAAPA
     PVIAAAPVAE AAVAEPAAVV EVAAVEVAAV VVEAAPAPVV AAPVQEAPAA VPAAAPTPAP
     APAPAAPVAA APASDNLTAV LQAAGLVLAS TNPEKLRAAQ EEAAKYVAPA RVPRERKPLP
     PQSTEPLVQM ETKR
//
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