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Database: UniProt
Entry: A0A1V3KAM9_9PAST
LinkDB: A0A1V3KAM9_9PAST
Original site: A0A1V3KAM9_9PAST 
ID   A0A1V3KAM9_9PAST        Unreviewed;       947 AA.
AC   A0A1V3KAM9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   05-JUN-2019, entry version 7.
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=BKG89_03120 {ECO:0000313|EMBL:OOF70613.1};
OS   Rodentibacter heylii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Rodentibacter.
OX   NCBI_TaxID=1906744 {ECO:0000313|EMBL:OOF70613.1, ECO:0000313|Proteomes:UP000188820};
RN   [1] {ECO:0000313|EMBL:OOF70613.1, ECO:0000313|Proteomes:UP000188820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1998236014 {ECO:0000313|EMBL:OOF70613.1,
RC   ECO:0000313|Proteomes:UP000188820};
RA   Christensen H.;
RT   "Rodentibacter gen. nov. and new species.";
RL   Submitted (OCT-2016) 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:
CC       Reaction=Endonucleolytic cleavage of single-stranded RNA in A- and
CC         U-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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00970};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00970};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         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
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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OOF70613.1}.
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DR   EMBL; MLAA01000009; OOF70613.1; -; Genomic_DNA.
DR   Proteomes; UP000188820; 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: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; IPR021968; PNPase_C.
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; PF12111; PNPase_C; 1.
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:UP000188820};
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   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:UP000188820};
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    119       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      403    406       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   REGION      570    668       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V3KAM9}.
FT   REGION      723    760       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1V3KAM9}.
FT   COMPBIAS    591    605       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1V3KAM9}.
FT   COMPBIAS    606    620       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1V3KAM9}.
FT   COMPBIAS    621    636       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A1V3KAM9}.
FT   COMPBIAS    637    654       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A1V3KAM9}.
FT   METAL       302    302       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       345    345       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       403    403       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       406    406       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   947 AA;  107612 MW;  CBA4A09450A9C8D0 CRC64;
     MKRMLINATQ KEELRVALVD GQNLFDLDIE NPGHEQKKAN IYKGKITRVE PSLEAAFVDY
     GAERHGFLPL KEIAREYFPE DYVFQGRPNI RDILTEGQEV IVQVNKEERG NKGAALTTFV
     SLAGSYLVIM PNNPRAGGIS RRIEGDERLE LKEALSSLDV PDGVGLIVRT AGVGKSPEEL
     QWDLKVLLHH WEAIKQASQS RPAPFLIHQE SDVIVRAIRD YLRRDIGEIL IDHPKIYEKA
     KAHIKLVRPD FIHRVKLYQG EVPLFSHYQI ESQIESAFQR EVRLPSGGSI VIDVTEALTA
     IDINSARSTR GGDIEETALN TNLEAADEIA RQLRLRDLGG LIVIDFIDMT PIRHQREVEN
     RIRDAVRQDR ARIQISRISR FGLLEMSRQR LSPSLGESSH HVCPRCQGTG KIRDNESLSL
     SILRLIEEEA LKEKTKQVHT IVPVQIASYL LNEKRKTVRS IEKRHDVDII VVPNEAMETP
     HFRVLRVRDG EEVNELSYNL AKHHNLNEEA YIEDLHIRQQ DSTVTNIESA ESTAAVSLSI
     QTAAPIPTER KPEVSWLSKL IAKIKTLFSS KSSEKKTSKN SRKVRHNSSA RNNRRVQERR
     NARQKTISQE QTTTTAEETR LPNTERQRRS RRAEHQSNES TVNLNNVSQA KKEEQNESIP
     ARRPRREMSK SIRIVEEEVS SALKVEENID IRVDKKPDVK NQDKVIEERV AIDVENVESR
     VAENSELNEK AKSESRQRRT PRHLRVNNQR RRKSTETKSP MPLFAAVASP ELASGKVWID
     QTTVVSAKEP QFLSVNELLE QEAKKKNAQV VPATGIFVQS NSTELQPLND FITQPANESV
     EKKVQESLAR LDTDKPTNIM PEQPIDDVKT SEIPEFVRNY VFNGRLGTIS SVVHTKAEMT
     LAKADDKTNE PFPIVEWMDS RYYFYGKGGA GHHSAISHVY SEATKAE
//
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