ID A0A4U0YHS4_9PSED Unreviewed; 1100 AA. AC A0A4U0YHS4; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 16-OCT-2019, entry version 3. 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 Pseudomonas bauzanensis. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=653930 {ECO:0000313|EMBL:TKA91520.1}; RN [1] {ECO:0000313|EMBL:TKA91520.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SBBB {ECO:0000313|EMBL:TKA91520.1}; 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 RT sediments."; RL Submitted (APR-2019) 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: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 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: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 Coiled coil {ECO:0000256|SAM:Coils}; 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:TKA91520.1}; 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 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 REGION 577 794 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 868 898 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT REGION 967 1100 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COILED 314 334 {ECO:0000256|SAM:Coils}. FT COMPBIAS 597 649 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 677 693 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 697 719 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 758 781 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 868 889 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT COMPBIAS 977 999 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. 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 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 //