ID A0A366AP74_9VIBR Unreviewed; 1052 AA. AC A0A366AP74; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 31-JUL-2019, entry version 6. 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=DLR71_03550 {ECO:0000313|EMBL:RBM65075.1}; OS Vibrio sp. 2017V-1105. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=2204203 {ECO:0000313|EMBL:RBM65075.1, ECO:0000313|Proteomes:UP000252343}; RN [1] {ECO:0000313|EMBL:RBM65075.1, ECO:0000313|Proteomes:UP000252343} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2017V-1105 {ECO:0000313|EMBL:RBM65075.1, RC ECO:0000313|Proteomes:UP000252343}; RA Islam M.T., Liang K., Im M.S., Winkjer J., Busby S., Batra D., RA Rowe L., Tarr C.L., Boucher Y.; RT "Draft genome sequences of nine Vibrio sp. clinical isolates from RT across the United States representing the closest known relative of RT Vibrio cholerae."; RL Submitted (JUN-2018) 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: 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: 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:RBM65075.1}. 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; QKKT01000003; RBM65075.1; -; Genomic_DNA. DR Proteomes; UP000252343; Unassembled WGS sequence. 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:UP000252343}; 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 39 119 S1 motif. {ECO:0000259|PROSITE:PS50126}. FT REGION 403 406 Required for zinc-mediated FT homotetramerization and catalytic FT activity. {ECO:0000256|HAMAP-Rule: FT MF_00970}. FT REGION 536 557 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 584 821 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 1029 1052 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 594 685 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 700 715 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 782 804 Basic. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 1034 1052 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT METAL 302 302 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00970}. FT METAL 345 345 Magnesium; catalytic. {ECO:0000256|HAMAP- FT Rule:MF_00970}. FT METAL 403 403 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00970}. FT METAL 406 406 Zinc; shared with dimeric partner. FT {ECO:0000256|HAMAP-Rule:MF_00970}. SQ SEQUENCE 1052 AA; 117526 MW; 1195AC75400546F1 CRC64; MKRMLINATQ KEELRVALVD GQRLFDLDIE SPGHESKKAN IYKGRITRIE PSLEAAFVDY GAERHGFLPL KEIAREYFPD GYSYQGRPNI KDVLNEGQEV IVQIEKEERG SKGAALTTFI SLAGSYLVLM PNNPRAGGIS RRIEGDERTE LKSALSSLEL PQGMGLIVRT AGVGKSAEEL EWDLNVLLKH WSAIKQASDS NPAPFLIHQE SNVIVRAIRD YLRRDIGEIL IDSNSIYERA LEHIRLVRPD FVNRVKKYEG EVPLFSHFQI ESQIESAFQR EVRLPSGGSI VIDPTEALTS IDINSARATK GGDIEETALN TNLEAADEIA RQLRLRDLGG LVVIDFIDMT PVRHQREVEN RLREAVRVDR ARVQIGRISR FGLLEMSRQR LSPSLAEASH HICPRCKGTG VIRDNESLAL SVLRLIEEEA LKDNTSQVLA VVPVSIASYL LNEKRRSINH IEKAQQVRIT IVPNSDMETP HFEVIRVREG EEQDVLSYLI PKKLEAMKEA EGKEVVDVEL KPKRIEEPVL KGFAAPAEAV PAPTPKPKAE PQPVAEVQQP AQPGFFSRVF KAIASLFSAT PEAAKVEAPV TQNSEQDKPR RERNERNNDR RRNPRDKNRR RGNEENNERN DKETSNNNRK PQERKPKQER GERNERNDRN ERPETERPER QDRRNKRDES KTAKLLEQGR QLAAEAQQEV KAVEPKEEKA AVVKERRQRR KLSKQIRVKD QLAAEELDNL STAPVDNAFD APAPVNLPVT DDFSDSAQED NEQDDQKQRR NRRSPRHLRA SGQRRRRGRD RRPNPFRLRK GGVASPEMAM GKVMPRYDLA PRPQSRHETA EGAQHVTHVT PTAATAVVES EKVAAPRVLG GVAFPEMAMG KVIVCRETAA VQPEPVVQEP VITDVIAETL IAPVEPVVVE AAVIEAPVIE ESATETAALE TVVAKVAEVE EPAKISDEVV AQTTVEVIAD KMAEPIKVVK PVTVSATSLT AKAVIQQPYA SSPMTKAPGS DDIREVQVNA APLRAERYQA RGAGSQVARN QASAGMSKPQ SF //