ID   A0A0N8QMB1_9PSED        Unreviewed;      1114 AA.
AC   A0A0N8QMB1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-SEP-2023, entry version 29.
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; Pseudomonadota; 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   AlphaFoldDB; A0A0N8QMB1; -.
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: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   NCBIfam; TIGR00757; RNaseEG; 1.
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   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          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   COMPBIAS        592..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..738
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        749..765
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        806..820
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..867
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1048..1066
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1067..1095
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1099..1114
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   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
//