ID A0A0D6NNR0_9PROT Unreviewed; 954 AA.
AC A0A0D6NNR0; A0A6N3SWX8;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 08-OCT-2025, entry version 38.
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=Abor_037_002 {ECO:0000313|EMBL:GAN67056.1};
OS Acetobacter orientalis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Acetobacterales; Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=146474 {ECO:0000313|EMBL:GAN67056.1, ECO:0000313|Proteomes:UP000032670};
RN [1] {ECO:0000313|EMBL:GAN67056.1, ECO:0000313|Proteomes:UP000032670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=21F-2 {ECO:0000313|EMBL:GAN67056.1,
RC ECO:0000313|Proteomes:UP000032670};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acetobacter orientalis 21F-2.";
RL Submitted (NOV-2012) 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: Homotetramer formed by a dimer of dimers. {ECO:0000256|HAMAP-
CC 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:GAN67056.1}.
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DR EMBL; BAMX01000037; GAN67056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6NNR0; -.
DR STRING; 1231341.Abor_037_002; -.
DR Proteomes; UP000032670; 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:UniProtKB-EC.
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 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 SUPFAM; SSF50249; Nucleic acid-binding proteins; 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|ARBA:ARBA00022490, 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|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};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|HAMAP-Rule:MF_00970};
KW Reference proteome {ECO:0000313|Proteomes:UP000032670};
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 206..477
FT /note="RNA-binding protein AU-1/Ribonuclease E/G"
FT /evidence="ECO:0000259|Pfam:PF10150"
FT DOMAIN 489..573
FT /note="RNase E/G thioredoxin-like"
FT /evidence="ECO:0000259|Pfam:PF20833"
FT REGION 112..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..493
FT /note="Required for zinc-mediated homotetramerization and
FT catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT REGION 605..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..954
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..134
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..625
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..698
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..711
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..812
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..929
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..954
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 432
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 490
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 493
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 954 AA; 106657 MW; EB47B060262CA54E CRC64;
MLIDATHAEE TRVVVMDGNR LEDYDVEAAA KKQLKGNIYL ARVIRVEPSL QAAFVEYGGN
RHGFLAFSEI HPDYYQIPVA DREKLLALQA EEEALIDADE DNEDTDAQDL NAEADDEDAE
QSDEQETAEA EADGSENRRA PRRNGGPDYV GGETDTGEEA LIQKRIARFL RNYRIQEVIR
RRQVLLVQVV KEERGNKGAA LTTYVSLAGR YCVLMPNALR GGGVSRKITS VADRRRLRDI
ISDLNLPRGM AMIVRTAGAQ RPGPEITRDC EYLLHLWDDI RELTLQSVAP ALIYEEASLV
KRAIRDVYTR EISEILVDGE SGWKAARDFM RLLMPQHAEK VRLWNKENQP LFTHYHVEGH
LDAMFSPVVS LRSGGYLVIN QTEALVAIDV NSGKSTNQRN IEETAFRTNQ EAADEVARQL
RLRDLAGLIV IDFIDMESRR HNVMIERRLK EALRHDRARI QMGGISHFGL LEMSRQRLRP
SVAEAVFAPC PHCQGTGMVR GIESSALHVL RSVEEEGARR RASAITVHVA PEIAFYILNN
KRTWLAEIEK RHYMEVLFAP DSSLPAPEVR IERLQPARVQ RAPAPIQPPL ENVAIEHTPV
EAPAELDEVE EPRQTATPEN ATAATPDEDE PRRRRRRRRR GGNGNRDERT PQAEQHEQNT
HANAPESEAD EQPETYTVEE ANGENLAPGR RRTRHSRVQR QPQQEVQVQV PIAQGPAPRQ
EQRRPSQVWQ GPTPANPFGG SIDIFDLIEN STMQAEEARK AAPVAQPAKG EAAVVAPTPA
PVAAPVQPAK VEAEPEEAEA QPARRRAPRR RRKTEETSTE SNDLLADTAP VAVSPAAEAD
SVQDEDEAPK PRRRRAPRKT AEADAAPEAS TEEKPRATRG RPRRKAEGTD EAADAAEAEK
PAPRRRRAAT KAEPAKTEAA AEPDAQAADP SIVQPIVIDD EQPAPRRRTG WWRR
//
