ID Q1QX63_CHRSD Unreviewed; 1175 AA. AC Q1QX63; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 11-DEC-2019, entry version 92. 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 OrderedLocusNames=Csal_1592 {ECO:0000313|EMBL:ABE58945.1}; OS Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768). OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Chromohalobacter. OX NCBI_TaxID=290398 {ECO:0000313|EMBL:ABE58945.1, ECO:0000313|Proteomes:UP000000239}; RN [1] {ECO:0000313|EMBL:ABE58945.1, ECO:0000313|Proteomes:UP000000239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768 RC {ECO:0000313|Proteomes:UP000000239}; RX PubMed=22675587; DOI=10.4056/sigs.2285059; RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C., RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D., RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T., RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C., RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.; RT "Complete genome sequence of the halophilic and highly halotolerant RT Chromohalobacter salexigens type strain (1H11(T))."; RL Stand. Genomic Sci. 5:379-388(2011). 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 --------------------------------------------------------------------------- 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; CP000285; ABE58945.1; -; Genomic_DNA. DR STRING; 290398.Csal_1592; -. DR EnsemblBacteria; ABE58945; ABE58945; Csal_1592. DR KEGG; csa:Csal_1592; -. DR eggNOG; ENOG4107QQB; Bacteria. DR eggNOG; COG1530; LUCA. DR HOGENOM; HOG000258027; -. DR KO; K08300; -. DR OMA; RRTGWWK; -. DR OrthoDB; 1209444at2; -. DR BioCyc; CSAL290398:G1GJB-1639-MONOMER; -. DR Proteomes; UP000000239; Chromosome. 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00970}; KW Endonuclease {ECO:0000256|HAMAP-Rule:MF_00970}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00970, ECO:0000313|EMBL:ABE58945.1}; 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 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 487..565 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 579..1175 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 496..511 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 582..627 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 628..675 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 676..694 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 695..747 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 753..774 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 804..841 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 985..1013 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1024..1145 FT /note="Polar" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1150..1175 FT /note="Polyampholyte" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT METAL 300 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT METAL 343 FT /note="Magnesium; catalytic" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT METAL 401 FT /note="Zinc; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" FT METAL 404 FT /note="Zinc; shared with dimeric partner" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970" SQ SEQUENCE 1175 AA; 126086 MW; 1A1276DB1A134AE5 CRC64; MKRMLINATQ PEELRVALVD GQRLYDLDIE SGAREQKKAN IYRGRITRIE PSLEAAFVDF GAERHGFLPL KEISREYFTK EPSGRPNIKE VLKEGQEVIV QVDKEERGNK GAALTTFISL AGRFLVLMPN NPRAGGISRR IEGDDRAQLK DAMGQLTVPD KMGVIVRTAG IGRSPEELQW DMDYLVQVWE AITEEAGKRS APFLIYRESN VIIRAMRDYL RHDIGEVLID SPEVHEEALH FIRQVMPSYQ NKIKLYADDV PLFSRFQIES QIETAYQREV KLPSGGAVVI DHTEALVSID INSARATRGS DIEETALQTN LEAADEIARQ LRLRDIGGLV VIDFIDMTPA KNQREVENRV RDALKLDRAR VQIGRISRFG LMEMSRQRLR PSLGETSGVV CPRCNGQGTI RDVRSISLSI MRLIEEEAMK ERSSQIRAIL PVPVATYLLN EKRSVLNDIE QRQGVQVVLL PNPDMDTPHY DVQRLRDDQV SEEDGQRSSF ELPTTTELTQ EPDPALDKPM QRAEAAVKSV AHNAPAPTSL QHDTAPPATP TPAPAADAPA STPAESGLFS RLVKGLGKLL NGEDSTSPSK QSNDQAQQSG ASKTTSEARR QRQGSDQSST SRSDGDTGSK QRQNDDSRRD AGSGNGRGGN RRRRNGEESQ DRQASRSDNR DGNRSSRSSR GNGGNGGRNE NARGSGGSDK GRQDTRSDSR NDARNDSRSD SRNDGRNATK GGNKPREENK DAKAGKPKAE TPSQSAPDKQ ATSDKQTTPS QDDAPKSDGK PKRTRNNPRQ RSRKHAVNPN AVAEQEKLQA QQEAEGATST GDNTQPQATA AQASPEAEPT STAPSDAPAA AAAPTDEDES SQAAAAKSSQ DAKSRNAKSK RSRNASKPAR TASETADAAP QGKTSADAPE TAAEAPSQPR EAAAAAQPAD SATSEAPATA NADTRASAPA PSADDASALS EPKAPRDATP SAEAPADETS ASDAPRGEVS DSQPASSAAA DEATSTGRDT VEQEAATPVT KDEAATAPAT SSADADVDTR QDAASSTATP QDDTLATPAS QAEQKASTDA PAPQAEPTTP AAAAASSSDE QAPAEVSESQ PQAEPKAPSD ASATSSEEKA STETPAPQPE QTASTEASEP QQATASAPRR RRRAHNDPRE QRRLQENLFR GDDNA //