ID A0A0N8QMB1_9PSED Unreviewed; 1114 AA. AC A0A0N8QMB1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 18-JAN-2017, entry version 7. 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 ORFNames=ALO86_03833 {ECO:0000313|EMBL:KPW44294.1}; OS Pseudomonas syringae pv. berberidis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=251704 {ECO:0000313|EMBL:KPW44294.1, ECO:0000313|Proteomes:UP000050565}; RN [1] {ECO:0000313|EMBL:KPW44294.1, ECO:0000313|Proteomes:UP000050565} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICMP4116 {ECO:0000313|EMBL:KPW44294.1, RC ECO:0000313|Proteomes:UP000050565}; RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.; RT "Genome announcement of multiple Pseudomonas syringae strains."; RL Submitted (SEP-2015) 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. {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of single-stranded CC RNA in A- and U-rich regions. {ECO:0000256|HAMAP-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: 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. {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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:KPW44294.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; LJPU01000327; KPW44294.1; -; Genomic_DNA. DR EnsemblBacteria; KPW44294; KPW44294; ALO86_03833. DR Proteomes; UP000050565; Unassembled WGS sequence. 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 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:UP000050565}; 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 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 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 39 117 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT REGION 401 404 Required for zinc-mediated FT homotetramerization and catalytic FT activity. {ECO:0000256|HAMAP-Rule: FT MF_00970}. FT METAL 300 300 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00970}. FT METAL 343 343 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00970}. FT METAL 401 401 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00970}. FT METAL 404 404 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00970}. SQ SEQUENCE 1114 AA; 122335 MW; 26A29969AFF42869 CRC64; MKRMLINATQ PEELRVALVD GQRLYDLDIE SGAREQKKAN IYKGRITRIE PSLEAAFVDF GSERHGFLPL KEISREYFKK APEGRVNIKD VLSEGQEVIV QVEKEERGNK GAALTTFISL AGRYLVLMPN NPRAGGISRR IEGEERNELR EALNGLIAPA DMGLIVRTAG LGRSSEEMQW DLDYLLQLWT AIKEASLDRS APFLIYQESN VIIRAIRDYL RQDIGEVLID SVEAQEEALT FIRQVMPQYA SKIKLYEDSV PLFNRFQIES QIETAFQRVV ELPSGGSIVI DPTEALVSID INSARATKGS DIEETALQTN LEAAEEIARQ LRLRDIGGLI VIDFIDMTPA KNQRAVEEKV RESLEADRAR VQVGRISRFG LLEMSRQRLR PSLGESSGIV CPRCNGTGII RDVESLSLAI LRLIEEEALK DRTAEVRAQV PIPVAAFLLN EKRNSITKIE LRTRARIIIL PNDQLETPHF EVQRLRDDSP EAHNSQTSYE IAAAAAAAEV EEIAPLAAAT RTLVRQEAAV KTAPARANAP VPVEVAAPAP TPAPVAHEPS LFKGLVKSLV SLFATKEEPV VAPAVVEKPA AEQRPARNEE RRNGRQQSRG RNNRRDEERK PREERAPREE RAERAPREER APREERAPRE ERAVREPREA REESAPREER PARTSRERKP REAREDRPVR ELREPLDAVA TAAQAGPAVN LAREERPERA PREERQPRAP REERQPRAEQ AAVAVSEEEE VLLNDEQAND DNQDGNDGSE GDRPRRRSRG QRRRSNRRER QRDANGNVIE GSEENGSEEN GAEETVNDED NSATDLSAGL GFTAAAASGV ISATAEADAH QQAERANSTT QSAPAAEPVQ QAAVAHAPVV ETPAVEAPVA ETSAVETPAP QAPAAEQTAE VPAVEAPVAD DAPVAQPAPE VEVQPAAVEA PAIAAQTELF EAPHAERVVP FTPTPAPAPQ APVEAAAHEQ VPATESSELP TPVEAPAAEP AAFVKDEPAP YIAPQAAVEE QASAPAEQEP VIVETPAVPV SSTGRAPNDP REVRRRKREE EARRQQETTA ASAQAESAQP SQATEEKTDV ATTEQPAVQP HHDAEKETEP KPLV //