ID A0A0N8QMB1_9PSED Unreviewed; 1114 AA. AC A0A0N8QMB1; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 27-NOV-2024, entry version 32. 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=ALQ06_00675 {ECO:0000313|EMBL:RMQ28120.1}; OS Pseudomonas syringae pv. berberidis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=251704 {ECO:0000313|EMBL:RMQ28120.1, ECO:0000313|Proteomes:UP000278721}; RN [1] {ECO:0000313|EMBL:RMQ28120.1, ECO:0000313|Proteomes:UP000278721} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ICMP 4065 {ECO:0000313|EMBL:RMQ28120.1, RC ECO:0000313|Proteomes:UP000278721}; RA Dillon M., Thakur S., Almeida R.N.D., Weir B.S., Guttman D.S.; RT "Recombination of ecologically and evolutionarily significant loci RT maintains genetic cohesion in the Pseudomonas syringae species complex."; RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Endoribonuclease that plays a central role in RNA processing CC and decay. Required for the maturation of 5S and 16S rRNAs and the CC majority of tRNAs. Also involved in the degradation of most mRNAs. CC {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and U- CC 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; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00970}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00970}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000256|HAMAP-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 the RNA CC degradosome, RNase E assembles into a homotetramer formed by a dimer of CC dimers. {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}. Cell CC inner membrane {ECO:0000256|HAMAP-Rule:MF_00970}; Peripheral membrane CC protein {ECO:0000256|HAMAP-Rule:MF_00970}; Cytoplasmic side CC {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 -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily. CC {ECO:0000256|ARBA:ARBA00005663}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:RMQ28120.1}. 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; RBRC01000355; RMQ28120.1; -; Genomic_DNA. DR AlphaFoldDB; A0A0N8QMB1; -. DR Proteomes; UP000278721; 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:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro. DR GO; GO:0004521; F:RNA endonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. 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 CDD; cd04453; S1_RNase_E; 1. DR FunFam; 2.40.50.140:FF:000040; Ribonuclease E; 1. DR FunFam; 3.40.1260.20:FF:000002; Ribonuclease E; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 3.40.1260.20; Ribonuclease E, catalytic domain; 1. 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; IPR048583; RNase_E_G_thioredoxin-like. DR InterPro; IPR003029; S1_domain. DR NCBIfam; TIGR00757; RNaseEG; 1. DR PANTHER; PTHR30001; RIBONUCLEASE; 1. DR PANTHER; PTHR30001:SF1; RIBONUCLEASE E_G-LIKE PROTEIN, CHLOROPLASTIC; 1. DR Pfam; PF10150; RNase_E_G; 1. DR Pfam; PF20833; RNase_E_G_Thio; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_00970}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}; KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00970}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00970}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00970}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00970}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW rRNA processing {ECO:0000256|ARBA:ARBA00022552, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|HAMAP- KW Rule:MF_00970}; KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP- KW Rule:MF_00970}; tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00970}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_00970}. FT DOMAIN 39..117 FT /note="S1 motif" FT /evidence="ECO:0000259|PROSITE:PS50126" FT REGION 401..404 FT /note="Required for zinc-mediated homotetramerization and FT catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT REGION 585..828 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 842..933 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 959..1114 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 592..694 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 712..738 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 749..765 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 806..820 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 851..867 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1048..1066 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1067..1095 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1099..1114 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 300 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT BINDING 343 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT BINDING 401 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT BINDING 404 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="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 //