RNE_NOSS1
ID RNE_NOSS1 Reviewed; 687 AA.
AC Q8YP69;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ribonuclease E {ECO:0000303|PubMed:24563514};
DE Short=AnaRne {ECO:0000303|PubMed:24563514};
DE Short=RNase E;
DE EC=3.1.26.12;
GN Name=rne {ECO:0000303|PubMed:24563514}; OrderedLocusNames=alr4331;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
RN [2]
RP FUNCTION AS AN ENDONUCLEASE, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP 670-ARG--ALA-678.
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=24563514; DOI=10.1261/rna.043513.113;
RA Zhang J.Y., Deng X.M., Li F.P., Wang L., Huang Q.Y., Zhang C.C., Chen W.L.;
RT "RNase E forms a complex with polynucleotide phosphorylase in cyanobacteria
RT via a cyanobacterial-specific nonapeptide in the noncatalytic region.";
RL RNA 20:568-579(2014).
CC -!- FUNCTION: Endoribonuclease that plays a central role in rRNA and tRNA
CC processing and mRNA decay. Has been shown to act on 9S rRNA (the
CC precursor of 5S rRNA). {ECO:0000269|PubMed:24563514}.
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:0000250|UniProtKB:P72656};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P21513};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P21513};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P21513};
CC Note=Binds 2 Zn(2+) ions per homotetramer. Zinc ions are bound between
CC subunits. {ECO:0000250|UniProtKB:P21513};
CC -!- SUBUNIT: May form homodimers or higher order multimers. Interacts with
CC polynucleotide phosphorylase (PNPase, pnp) via the C4 Arg-rich motif
CC (residues 670-678) (PubMed:24563514). A homotetramer formed by a dimer
CC of dimers (By similarity). {ECO:0000250|UniProtKB:P21513,
CC ECO:0000269|PubMed:24563514}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P72656}.
CC -!- SIMILARITY: Belongs to the RNase E/G family. {ECO:0000305}.
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DR EMBL; BA000019; BAB76030.1; -; Genomic_DNA.
DR PIR; AD2347; AD2347.
DR RefSeq; WP_010998469.1; NZ_RSCN01000027.1.
DR AlphaFoldDB; Q8YP69; -.
DR SMR; Q8YP69; -.
DR STRING; 103690.17133467; -.
DR EnsemblBacteria; BAB76030; BAB76030; BAB76030.
DR KEGG; ana:alr4331; -.
DR eggNOG; COG1530; Bacteria.
DR OMA; ILQPYGQ; -.
DR OrthoDB; 1209444at2; -.
DR Proteomes; UP000002483; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR InterPro; IPR004659; RNase_E/G.
DR InterPro; IPR022967; S1_dom.
DR InterPro; IPR003029; S1_domain.
DR PANTHER; PTHR30001; PTHR30001; 1.
DR Pfam; PF10150; RNase_E_G; 1.
DR SMART; SM00316; S1; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR TIGRFAMs; TIGR00757; RNaseEG; 1.
DR PROSITE; PS50126; S1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Reference proteome; RNA-binding; rRNA processing; rRNA-binding;
KW tRNA processing; tRNA-binding; Zinc.
FT CHAIN 1..687
FT /note="Ribonuclease E"
FT /id="PRO_0000450522"
FT DOMAIN 35..117
FT /note="S1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
FT REGION 650..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 670..678
FT /note="C4 Arg-rich motif, necessary and sufficient to
FT confer PNPase binding on another protein"
FT /evidence="ECO:0000269|PubMed:24563514"
FT COMPBIAS 665..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 339
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT BINDING 400
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P21513"
FT MUTAGEN 670..678
FT /note="Missing: No longer interacts with PNPase."
FT /evidence="ECO:0000269|PubMed:24563514"
SQ SEQUENCE 687 AA; 76169 MW; 564187883AD71B1F CRC64;
MPKQIIIAEQ HQIAAVFSED QIQELVVATG HHQIGDIYLG VVENVLPGID AAFVNIGDPE
RNGFIHVTDL GPLRLKRTAA AITELLAPQQ KVLVQVMKEP TGTKGPRLTG NITLPGRYVV
LMPYGRGVNL SRRIKSESER NRLRALAILI KPAGMGLLVR TEAEGKPEEA IIEDLEVLQK
QWEAIQQEAQ STRAPALLNR DDDFIQRVLR DMYGADVNRI VVDSSTGLKR VKQYLQNWSG
GQTPQGLLID HHRDRSPILE YFRINAAIRE ALKPRVDLPS GGYIIIEPTE ALTVIDVNSG
SFTRSATARE TVLWTNCEAA TEIARQLRLR NIAGVIVVDF IDMESRRDQL QVLEHFNKAL
RADKARPQIA QLTELGLVEL TRKRQGQNIY ELFGDTCPAC GGLGHTVRLP GETENRLPTP
AAEVPERFVS LPTREPRLPT ARTTEPRETY DGFGEAFEND SDLGALNLIN HPSYQELNDN
NKRRARTRRS RIGINGTNGK DEQRITANPL AFISESDLDL DGDVELSAPP ELPTPNLGKS
GWIERAERTK VIKTEPVKPV VEPPEIRTVE MTPEEQDIFA LMGISPLIKL EQEVKNPKSV
IINIVQPGQT PTIPTEITPE PVAKVTPSVE VNTPKVKLES KSVSVAATEP IKLTETMEES
EVNAASTANR RRRRRSSASD SDTGEDS
