ID H3NTU5_9GAMM Unreviewed; 902 AA.
AC H3NTU5;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=OMB55_00010540 {ECO:0000313|EMBL:EHQ57327.1};
OS gamma proteobacterium HIMB55.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX NCBI_TaxID=745014 {ECO:0000313|EMBL:EHQ57327.1, ECO:0000313|Proteomes:UP000003408};
RN [1] {ECO:0000313|EMBL:EHQ57327.1, ECO:0000313|Proteomes:UP000003408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB55 {ECO:0000313|EMBL:EHQ57327.1,
RC ECO:0000313|Proteomes:UP000003408};
RX PubMed=22493201; DOI=10.1128/JB.00171-12;
RA Huggett M.J., Rappe M.S.;
RT "Genome Sequence of Strain HIMB55, a Novel Marine Gammaproteobacterium of
RT the OM60/NOR5 Clade.";
RL J. Bacteriol. 194:2393-2394(2012).
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 -!- SIMILARITY: Belongs to the RNase E/G family. RNase G subfamily.
CC {ECO:0000256|ARBA:ARBA00005663}.
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:EHQ57327.1}.
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DR EMBL; AGIF02000001; EHQ57327.1; -; Genomic_DNA.
DR AlphaFoldDB; H3NTU5; -.
DR STRING; 745014.OMB55_00010540; -.
DR PATRIC; fig|745014.4.peg.1069; -.
DR eggNOG; COG1530; Bacteria.
DR OrthoDB; 9804278at2; -.
DR Proteomes; UP000003408; 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; IPR048583; RNase_E_G_thioredoxin-like.
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; PF20833; RNase_E_G_Thio; 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|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW Rule:MF_00970};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00970}; 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|ARBA:ARBA00023136, 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 Reference proteome {ECO:0000313|Proteomes:UP000003408};
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 527..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..696
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 345
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 403
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 406
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 902 AA; 98520 MW; 298A3B59BACE36F6 CRC64;
MKKMLINATE REEVRVALVD GQRLYDLDIE NRARLQTKAN VYKAKVTRVE PSLEAAFVDF
GAERHGFLPL KEIAHQYYRS AAPSDGKMRI KDAIKEGTEV IVQVDKEERG TKGAALTTYI
SLPGRYMVLM PNNPKAGGIS RRIEGDDRSE LRDALNQLEI PNGMGVIIRT AGVGRSAEEL
QWDLDYLLKL WAAISEAADE NPPQTLLYQE SDVIIRAIRD YLKDDIDQVL IDEAHAHRQA
LDFVSMVMPK YQNRIKAYDD SLPLFNRFQV EGQIETAFQR EVRLPSGGSI VIDPTEALVS
IDINSARATK GSDIEQTALQ TNLEAADEIA RQLRLRDMGG LVVIDFIDMN ASKNQRAVEN
RMRDALEIDR ARVQLGRISR FGLLEMSRQR LRPSLGETSG MVCPRCTGQG TIRDTKSLAL
AILRLIQEEA SKERTGEVRV IVPVDVSAFL LNEKRSAVGE IEQETKVRVV IIPNPNMQTP
HFEVIRLRDD EVDDDQRESF EIDLSAFEAE AATNDEEKAA PAPQALVRGV TPDAPPPAAS
PAPEKVEQAP AVAETESTSK PGLFPRLWAA LFAPMPKAEE VEEKDSKDEK KSEARSGNKA
KRRNNRQRKR PAKQTDADAN VETKTSADTP SVADNENGES GAEGEPKKRR RRGRRGGRRR
SAGEAGSDNT VAITADTDGD LEESSNEVDA DSTDETSAGE NAEPRHRPAD KRTEGRRRRR
RGPKTDGAVT EQTASETSSD GAAAAISAET LEAAAGNDTA GSKDGSAEIF ATVQSASVTE
VSEDAKPMEP GTATVASKSS DIDSSSDKSE PVLAASQTPS GALDLSGITE DGRAINDPRV
DAKPITEIRV ETAKRALFSS EAFPDAMKIA NNPERAANDP RGPRAVEAAE GTDSEENNAQ
EA
//
