ID   A0A366AP74_9VIBR        Unreviewed;      1052 AA.
AC   A0A366AP74;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   02-DEC-2020, entry version 10.
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=DLR71_03550 {ECO:0000313|EMBL:RBM65075.1};
OS   Vibrio sp. 2017V-1105.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=2204203 {ECO:0000313|EMBL:RBM65075.1, ECO:0000313|Proteomes:UP000252343};
RN   [1] {ECO:0000313|EMBL:RBM65075.1, ECO:0000313|Proteomes:UP000252343}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2017V-1105 {ECO:0000313|EMBL:RBM65075.1,
RC   ECO:0000313|Proteomes:UP000252343};
RA   Islam M.T., Liang K., Im M.S., Winkjer J., Busby S., Batra D., Rowe L.,
RA   Tarr C.L., Boucher Y.;
RT   "Draft genome sequences of nine Vibrio sp. clinical isolates from across
RT   the United States representing the closest known relative of Vibrio
RT   cholerae.";
RL   Submitted (JUN-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:RBM65075.1}.
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; QKKT01000003; RBM65075.1; -; Genomic_DNA.
DR   Proteomes; UP000252343; 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   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|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   DOMAIN          39..119
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          403..406
FT                   /note="Required for zinc-mediated homotetramerization and
FT                   catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT   REGION          536..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          584..821
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1029..1052
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..685
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        700..715
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..804
FT                   /note="Basic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1034..1052
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   METAL           302
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT   METAL           345
FT                   /note="Magnesium; catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT   METAL           403
FT                   /note="Zinc; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT   METAL           406
FT                   /note="Zinc; shared with dimeric partner"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
SQ   SEQUENCE   1052 AA;  117526 MW;  1195AC75400546F1 CRC64;
     MKRMLINATQ KEELRVALVD GQRLFDLDIE SPGHESKKAN IYKGRITRIE PSLEAAFVDY
     GAERHGFLPL KEIAREYFPD GYSYQGRPNI KDVLNEGQEV IVQIEKEERG SKGAALTTFI
     SLAGSYLVLM PNNPRAGGIS RRIEGDERTE LKSALSSLEL PQGMGLIVRT AGVGKSAEEL
     EWDLNVLLKH WSAIKQASDS NPAPFLIHQE SNVIVRAIRD YLRRDIGEIL IDSNSIYERA
     LEHIRLVRPD FVNRVKKYEG EVPLFSHFQI ESQIESAFQR EVRLPSGGSI VIDPTEALTS
     IDINSARATK GGDIEETALN TNLEAADEIA RQLRLRDLGG LVVIDFIDMT PVRHQREVEN
     RLREAVRVDR ARVQIGRISR FGLLEMSRQR LSPSLAEASH HICPRCKGTG VIRDNESLAL
     SVLRLIEEEA LKDNTSQVLA VVPVSIASYL LNEKRRSINH IEKAQQVRIT IVPNSDMETP
     HFEVIRVREG EEQDVLSYLI PKKLEAMKEA EGKEVVDVEL KPKRIEEPVL KGFAAPAEAV
     PAPTPKPKAE PQPVAEVQQP AQPGFFSRVF KAIASLFSAT PEAAKVEAPV TQNSEQDKPR
     RERNERNNDR RRNPRDKNRR RGNEENNERN DKETSNNNRK PQERKPKQER GERNERNDRN
     ERPETERPER QDRRNKRDES KTAKLLEQGR QLAAEAQQEV KAVEPKEEKA AVVKERRQRR
     KLSKQIRVKD QLAAEELDNL STAPVDNAFD APAPVNLPVT DDFSDSAQED NEQDDQKQRR
     NRRSPRHLRA SGQRRRRGRD RRPNPFRLRK GGVASPEMAM GKVMPRYDLA PRPQSRHETA
     EGAQHVTHVT PTAATAVVES EKVAAPRVLG GVAFPEMAMG KVIVCRETAA VQPEPVVQEP
     VITDVIAETL IAPVEPVVVE AAVIEAPVIE ESATETAALE TVVAKVAEVE EPAKISDEVV
     AQTTVEVIAD KMAEPIKVVK PVTVSATSLT AKAVIQQPYA SSPMTKAPGS DDIREVQVNA
     APLRAERYQA RGAGSQVARN QASAGMSKPQ SF
//