ID   A0A0N8QMB1_9PSED        Unreviewed;      1114 AA.
AC   A0A0N8QMB1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   07-APR-2021, entry version 21.
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; Proteobacteria; 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   -!- 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}.
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DR   EMBL; RBRC01000355; RMQ28120.1; -; Genomic_DNA.
DR   EnsemblBacteria; RMQ28120; RMQ28120; ALQ06_00675.
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: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: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   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|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|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|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   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   COILED          314..334
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        592..694
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..738
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..765
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..820
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..867
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1066
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1095
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1114
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   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
//