ID A0A060QGA6_9PROT Unreviewed; 979 AA.
AC A0A060QGA6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=ASAP_1945 {ECO:0000313|EMBL:CDG39990.1};
OS Asaia bogorensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Asaia.
OX NCBI_TaxID=91915 {ECO:0000313|EMBL:CDG39990.1, ECO:0000313|Proteomes:UP000027583};
RN [1] {ECO:0000313|EMBL:CDG39990.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39990.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24682158; DOI=10.1093/gbe/evu062;
RA Chouaia B., Gaiarsa S., Crotti E., Comandatore F., Degli Esposti M.,
RA Ricci I., Alma A., Favia G., Bandi C., Daffonchio D.;
RT "Acetic acid bacteria genomes reveal functional traits for adaptation to
RT life in insect guts.";
RL Genome Biol. Evol. 6:912-920(2014).
RN [2] {ECO:0000313|EMBL:CDG39990.1, ECO:0000313|Proteomes:UP000027583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SF2.1 {ECO:0000313|EMBL:CDG39990.1,
RC ECO:0000313|Proteomes:UP000027583};
RX PubMed=24804722; DOI=10.1371/journal.pone.0096566;
RA Degli Esposti M., Chouaia B., Comandatore F., Crotti E., Sassera D.,
RA Lievens P.M., Daffonchio D., Bandi C.;
RT "Evolution of mitochondria reconstructed from the energy metabolism of
RT living bacteria.";
RL PLoS ONE 9:e96566-e96566(2014).
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}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
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:CDG39990.1}.
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DR EMBL; CBLX010000013; CDG39990.1; -; Genomic_DNA.
DR RefSeq; WP_023978679.1; NZ_CBLX010000013.1.
DR AlphaFoldDB; A0A060QGA6; -.
DR eggNOG; COG1530; Bacteria.
DR Proteomes; UP000027583; 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:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; IPR000637; HMGI/Y_DNA-bd_CS.
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 SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS00354; HMGI_Y; 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 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 38..188
FT /note="S1 motif"
FT /evidence="ECO:0000259|SMART:SM00316"
FT REGION 97..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..477
FT /note="Required for zinc-mediated homotetramerization and
FT catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT REGION 557..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..739
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 373
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 416
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT BINDING 474
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 477
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 979 AA; 108425 MW; 4AD69E547813FE12 CRC64;
MNKRMLIDTT HAEETRVVVM DGDRLEDYDI ETSSKKQIKG NIYLAKVIRV EPSLQAAFVD
YGGNRHGFLA FSEIHPDYFQ IPVADREKLL ALQDEDLRAD ERVETENEGA ETTADAEQAE
PAEQPDFEAR PETVGGEHDT GDEGAAARRT ARFLRNYKIQ EVIRRRQILL VQVVKEERGN
KGAALTTYVS LAGRYCVLMP NALRGGGVSR KITSDSDRKR LRDVIAELDL PRGMAMIVRT
AGAQRPGPEI TRDCEYLLQL WDDIRNHTLS SVAPTLIYEE ANLIKRAIRD LFSKDIEEII
IDGEPAWKNA REFMRLLMPH NANKVKLWRD QSQSLFGRYH VEGHLDAIFS PTAQLKSGGY
LVINQTEALV SIDVNSGRST GQRNIEDTAV RTNLEAAEEV ARQLRLRDLA GLVVIDFIDM
ESRKHNAMVE KRLKDALRSD RARIQIGQIS HFGLLEMSRQ RLRPSISEAV LVPCPHCQGT
GHVRGIESAA LHVLRALDEE GLKQKAAEIS VHITSGIALY ILNNKRDWLG EIEQRHRMRV
SFQPDDSLTP ADLRIERLRP QVPAEQRAAQ PERHEPEATP VAPASIVVEE ESDLDAVSAE
ESRDEAPREE NGREDGGRRR RRRRRRNGRR SDESRDMPQA AGADVSDEAE DEEGTAPEQD
VAASRDDQAT GDSEALIVPG RRRMRTRRVS REERGQAEAP RETRAQEPRK AETRDNADRN
GERNGAKRGN EDRRRNQPEN RWNGPTPADP FGGASFDIFD MIEQAESRLG APSARNEEPK
LTLADSATDN GGESVRAEIP ASTTNLPAEA PAETAASRVR EGDEAGARKG RGRPRRRPVA
AEQAEPAPTA PVESDSASVA EPVAVAEADQ DKPAARRRGR PRKAPAAAAL PEGDAIDAEP
AAATADAPKP RRGRTPRKAA ASDVETDSAV KAEEQAAKAP AKTSARRGKA KADDAAPVVQ
PINVDEVAPA KPRTGWWKR
//
