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Database: UniProt
Entry: A0A0L0LZT8_9BURK
LinkDB: A0A0L0LZT8_9BURK
Original site: A0A0L0LZT8_9BURK 
ID   A0A0L0LZT8_9BURK        Unreviewed;      1047 AA.
AC   A0A0L0LZT8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUN-2019, entry version 18.
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=BPUN_2211 {ECO:0000313|EMBL:KND55583.1};
OS   Candidatus Paraburkholderia kirkii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=198822 {ECO:0000313|EMBL:KND55583.1, ECO:0000313|Proteomes:UP000053677};
RN   [1] {ECO:0000313|Proteomes:UP000053677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot2 {ECO:0000313|Proteomes:UP000053677};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-2015) 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: Homotetramer formed by a dimer of dimers.
CC       {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:KND55583.1}.
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DR   EMBL; LFKV01000015; KND55583.1; -; Genomic_DNA.
DR   EnsemblBacteria; KND55583; KND55583; BPUN_2211.
DR   PATRIC; fig|198822.17.peg.2290; -.
DR   BioCyc; GCF_001189345:G1EM4-1732-MONOMER; -.
DR   Proteomes; UP000053677; 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; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053677};
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   ECO:0000313|EMBL:KND55583.1};
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:UP000053677};
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    118       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   REGION      404    407       Required for zinc-mediated
FT                                homotetramerization and catalytic
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_00970}.
FT   REGION      513    548       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   REGION      571    870       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   REGION      918    943       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   REGION     1005   1047       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   COILED      350    370       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    514    530       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   COMPBIAS    585    606       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   COMPBIAS    627    694       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   COMPBIAS    706    730       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   COMPBIAS   1005   1028       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   COMPBIAS   1032   1047       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0L0LZT8}.
FT   METAL       303    303       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       346    346       Magnesium; catalytic. {ECO:0000256|HAMAP-
FT                                Rule:MF_00970}.
FT   METAL       404    404       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
FT   METAL       407    407       Zinc; shared with dimeric partner.
FT                                {ECO:0000256|HAMAP-Rule:MF_00970}.
SQ   SEQUENCE   1047 AA;  114424 MW;  A066B129ED932222 CRC64;
     MKRMLFNATQ QEELRVAIVD GQKLINIDIE TAGREQRKGN IYKGVVTRIE PSLEACFVNY
     GEDRHGFLPF KEVARQYFRD GVEMRSARIQ DALREGQELI VQVEKEERGN KGAALTTFIS
     LAGRYLVLMP NNPRGGGVSR RIESDERQEL RETMAQLELP EGMSIIARTA GIGRSAEELQ
     WDLNYLMQLW RAIEAASQSG VAGQPMLIYL ESSLVIRAIR DYFQPDIGEI LIDTTEIHDQ
     ARAFMDIVMP DNLSKVKRYH DDVPLFSRFQ IEHQIETAYS RTVPLPSGGG IVIDHTEALV
     AIDVNSARAT KGADIEETAT RTNLEAADEV ARQLRLRDLG GLIVIDFIDM ESAKSQREVE
     QRLKDALKHD RARVQMGKIS RFGLMELSRQ RLRPALSEGS HVTCPRCNGT GHIRDTESSA
     LQVLRIIQEE AMKENTAAIH CQVPVEVTAF LLNEKRSEIN KIESRFKVNV VLIPNKHLET
     PHYKLERLRH DDARLDDPRA SWKMAVEAAS ELESETGYSK RSEEVKPKQE AAVKGITPEK
     PAPVEAAPAP VPASGGLIAW IKNLFGIQPE AKPAPAPVET QPAVRPQRER SERTGGGDRN
     RNRRGAAAGR EGAAAGAATG GNGAGRQGAR REDREARGGR EGRELREVRE PREAREPREA
     REPREPREPR EARDRNAERA ARPEAGERRK PQPEAAVEAL TQGETVVSEV VETMQVGTDV
     AQQPGSDAAT ADQTAGARDS EERRRRRRGR RGGRRERDEE GMTVNHAADV AEAEGAAESV
     SAQAGVFDAE AVQEAAARRE TRPTAPQPVA EPVEPQVEKP AEVKPQEQAP AAAEEAPVAR
     TQEAEPFELK APTPEPATPD LFAKPTPALA VENPFGPSPK VVETKVADPF APVATEEAKP
     VETARPVEAA AAEAAPQAAV EAAEATEPVK TAAVAPTPEA TSVEPIEAAE TPATMAAPEP
     VAVVAEPVKS AAPAAPATST SIAVEALQPM LERAGLVWVN TDEGKLREAN DAAAREPAPV
     RVPRERKPLP PTDTTPMQQV ETSKSIH
//
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