ID A0A4U0YHS4_9GAMM Unreviewed; 1100 AA. AC A0A4U0YHS4; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 03-MAY-2023, entry version 15. 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=FA869_10480 {ECO:0000313|EMBL:TKA91520.1}; OS Halopseudomonas bauzanensis. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Halopseudomonas. OX NCBI_TaxID=653930 {ECO:0000313|EMBL:TKA91520.1, ECO:0000313|Proteomes:UP000305198}; RN [1] {ECO:0000313|EMBL:TKA91520.1, ECO:0000313|Proteomes:UP000305198} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SBBB {ECO:0000313|EMBL:TKA91520.1, RC ECO:0000313|Proteomes:UP000305198}; RA Bhattacharya S., Roy C., Mondal N., Sarkar J., Mandal S., Rameez M.J., RA Ghosh W.; RT "Crypto-aerobic microbial life in anoxic (sulfidic) marine sediments."; RL Submitted (APR-2019) 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 -!- 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:TKA91520.1}. 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; SWAV01000003; TKA91520.1; -; Genomic_DNA. DR AlphaFoldDB; A0A4U0YHS4; -. DR Proteomes; UP000305198; 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 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; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. 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; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}; KW Endonuclease {ECO:0000256|HAMAP-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|HAMAP-Rule:MF_00970}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00970}; Nuclease {ECO:0000256|HAMAP-Rule:MF_00970}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00970}; rRNA processing {ECO:0000256|HAMAP-Rule:MF_00970}; KW rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00970}; KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_00970}; KW 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 577..794 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 868..898 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 967..1100 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 597..649 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 677..693 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 697..719 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 758..781 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 868..889 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 977..999 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 1100 AA; 119439 MW; 73A7708DB778BFD5 CRC64; MKRMLINATQ PEELRVALVD GQKLYDLDIE SGAREQKKSN IYKGRITRVE PSLEAAFVDF GSERHGFLPL KEISREYFTK QPEGRVNIKE VLKEGQEVIV QVDKEERGNK GAALTTFISL AGRYLVLMPN NPRAGGISRR IEGEERNELR EALNSLNVPA DMGMIVRTAG LGRSAEELQW DLDYLLQLWE AIKSASSERS GTFLIYQESN VIIRAIRDYL RQDIGEVLID SETVKEEALN FISQVMPQYA SKVKLYEDSV PLFNRFQIES QIETAFEREV KLPSGGSIVI DHTEALVSID INSARATKGG DIEETALQTN LEAAEEIARQ LRLRDIGGLI VIDFIDMTPA KNQRAVEERV RESLEADRAR VQVGRISRFG LLEMSRQRLR PSLGETSGIV CPRCNGRGTI RDVESLSLSV LRLIEEEALK DRTAEVRAHV PVSIATFLLN EKRDVLAKTE ARTKVRLLVL PNPHMDTPHF EVQRLRDDQE AVLNGESSYS MTTEAEPEEP VQVSQTRAIV RQEAAVKTLA HSRPAPTAAP APAPAPVAAA NKAIQESQPG LIKSLIKSLV GMFAQDNRQE EEAEQQATSQ ANRKPAADGR GNERRSNRNR RPRPERDNRG GARGNRGGET AAERTDKPQR SERKSSDVVA DTDAATPSAS KPAEGTTGRR RRRSPTAAAT AESSEQRATA TEQAPARQDR RPQRQAEQAT VKDEELPVEQ NAEQTDSENT AEGERPKRRS RNSQRRRNNR RSRSAQDDQS GDNAASANQT SEATDDSNAS KPVTAEHGDA AATDVKVPAA AAVAVTEAVA ASEGHEPAEM INEPAVEAAL PEATTEALAE VKQPVEAGLT QAVSDIEQSI ENAVEAFNQS QRDDSAPAQA ETEVTQAEPS ATADAAEPAV VVAEEQPAAV IEPVAETAAA VEPEAPVAQA PEAEPAPVVT EEAAPALAQV EVQEPAPVAQ EPVEQAIPAL TESGRAFNDP REIRKRRMEA KRLAEQAEAQ AKAEAEAPAP AVEADAEPTA AAEPVSEAMA EAQEVIEHIP EAQVADQAEA ATDAQSAEPA AEAALPSPAE GEVPEHPATS APVQQDATEE DDNRPETPKG //