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Database: UniProt
Entry: A0A089ZPJ6_9PSED
LinkDB: A0A089ZPJ6_9PSED
Original site: A0A089ZPJ6_9PSED 
ID   A0A089ZPJ6_9PSED        Unreviewed;      1139 AA.
AC   A0A089ZPJ6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
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=LT40_00670 {ECO:0000313|EMBL:AIS15996.1};
OS   Pseudomonas rhizosphaerae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216142 {ECO:0000313|EMBL:AIS15996.1, ECO:0000313|Proteomes:UP000029499};
RN   [1] {ECO:0000313|EMBL:AIS15996.1, ECO:0000313|Proteomes:UP000029499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16299 {ECO:0000313|EMBL:AIS15996.1};
RX   PubMed=25483321; DOI=10.1016/j.jbiotec.2014.11.031;
RA   Kwak Y., Jung B.K., Shin J.H.;
RT   "Complete genome sequence of Pseudomonas rhizosphaerae IH5T (=DSM 16299T),
RT   a phosphate-solubilizing rhizobacterium for bacterial biofertilizer.";
RL   J. Biotechnol. 193:137-138(2015).
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}.
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DR   EMBL; CP009533; AIS15996.1; -; Genomic_DNA.
DR   RefSeq; WP_043185195.1; NZ_CP009533.1.
DR   AlphaFoldDB; A0A089ZPJ6; -.
DR   STRING; 216142.LT40_00670; -.
DR   KEGG; prh:LT40_00670; -.
DR   eggNOG; COG1530; Bacteria.
DR   HOGENOM; CLU_003468_0_3_6; -.
DR   Proteomes; UP000029499; Chromosome.
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:UP000029499};
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          36..114
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
FT   REGION          398..401
FT                   /note="Required for zinc-mediated homotetramerization and
FT                   catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT   REGION          584..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1053..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        592..752
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        845..872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1095..1115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         297
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT   BINDING         340
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00970"
FT   BINDING         398
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         401
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   1139 AA;  124548 MW;  F4B8C061A88D9936 CRC64;
     MLINATQPEE LRVALVDGQR LYDLDIESGA REQKKANIYK GRITRIEPSL EAAFVDFGSE
     RHGFLPLKEI SREYFKKNPE GRVNIKEVLS EGQEVIVQVE KEERGNKGAA LTTFISLAGR
     YLVLMPNNPR AGGISRRIEG EERNELREAL NGLVAPADMG LIVRTAGLGR SSEEMQWDLD
     YLLQLWTAIK EASLDRSAPF LIYQESNVII RAIRDYLRQD IGEVLIDSVE AQDEALTFIR
     QVMPQYASKI KLYEDSVPLF NRFQIESQIE TAFQRVVELP SGGSIVIDPT EALVSIDINS
     ARATKGSDIE ETALQTNLEA AEEIARQLRL RDIGGLIVID FIDMTPAKNQ RAVEDKVRES
     LEADRARVQV GRISRFGLLE MSRQRLRPSL GESSGIVCPR CSGTGIIRDV ESLSLAILRL
     IEEEALKDRT AEVRAQVPIP VAAFLLNEKR NSITKIELRT RARIVILPND HLETPHFEVQ
     RLRDDSPEAH SGQSSYEIAA AAAEVEEVQP AAATRTLVRQ EAAVKTAPTR TAAPVSAEEA
     APVAAAAPTP APAPQIAEPS LFKGLVKSLV SLFATKEAPA APVVVEKPAA TTTERPAREE
     RRNGRQQSRN RSNSRRDEER KPREDRAPRE DRSAREDAPA AREERPARAP REERQPRAPR
     EDRRPRNGGD DAPRVRELRE PLDAPTAREE RPAREERAPR EERVVREERA PREERAPREE
     RPAREERTPG EERPAREERQ PRPAREERVA QQNAAESEVG ATEEALTNDE LLQDDNPEGN
     DGDRPRRRSR GQRRRSNRRE RQRDANGDVI EGSEESNESA TEGESNGAAV AAGVAVTAVV
     AQSAISASAE AQAHEQAEQA NRSVQPAAAE STAESESLAA PEIVATAPTA EAAVDTPAAA
     PAQSDSPAEI ERPATVSAPD TWAAPVNESA APVIEQQPVV EAAKPAETTE PVQQDAAEPV
     ELTPPFDTTP TPISPPGADV EVDAPVVVDP AQVSESAFQP PVAQASEEAP SLPVEPALHQ
     ISEPAAAEPL SIEPVFVDAV VVEPALVEPV RFEPATSQPV AEPVPASEPV VVAEPEPIQE
     AEPAPAVPSN GRAPNDPREV RRRKREAEEA AKNAAFKPEA EVSSAADAQD AHDEPKPQA
//
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