ID Q1QX63_CHRSD Unreviewed; 1175 AA. AC Q1QX63; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 26-NOV-2014, entry version 52. 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 OS 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|Proteomes:UP000000239} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 3043 / ATCC BAA-138 / NCIMB 13768 RC {ECO:0000313|Proteomes:UP000000239}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., RA O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., RA Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., RA Canovas D., Richardson P.; RT "Complete sequence of Chromohalobacter salexigens DSM 3043."; RL Submitted (MAR-2006) 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: Endonucleolytic cleavage of single-stranded CC RNA in A- and U-rich regions. {ECO:0000256|HAMAP-Rule:MF_00970}. CC -!- COFACTOR: CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP- CC Rule:MF_00970}; CC -!- COFACTOR: 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 -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000256|HAMAP- CC 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 RefSeq; YP_573644.1; NC_007963.1. DR ProteinModelPortal; Q1QX63; -. DR SMR; Q1QX63; 1-486. DR STRING; 290398.Csal_1592; -. DR EnsemblBacteria; ABE58945; ABE58945; Csal_1592. DR GeneID; 4027554; -. DR KEGG; csa:Csal_1592; -. DR PATRIC; 21446980; VBIChrSal113723_1602. DR eggNOG; COG1530; -. DR HOGENOM; HOG000258027; -. DR KO; K08300; -. DR OMA; LVLTEMH; -. DR OrthoDB; EOG6PCPTH; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0004521; F:endoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008995; F:ribonuclease E activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006402; P:mRNA catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00970; RNase_E; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR003029; Rbsml_prot_S1_RNA-bd_dom. 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 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:UP000000239}; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000000239}; 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:0000256|HAMAP-Rule: FT MF_00970}. FT REGION 401 404 Required for zinc-mediated FT homotetramerization and catalytic FT activity. {ECO:0000256|HAMAP-Rule: FT MF_00970}. 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 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 //