ID   RNE_NEPOL               Reviewed;         375 AA.
AC   Q9TL10;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Ribonuclease E/G-like protein;
DE            Short=RNase E/G-like protein;
DE            EC=3.1.26.-;
GN   Name=rne;
OS   Nephroselmis olivacea (Green alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Chlorophyta; Nephroselmidophyceae;
OC   Nephroselmidales; Nephroselmidaceae; Nephroselmis.
OX   NCBI_TaxID=31312;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-484 / S-N-5-8;
RX   PubMed=10468594; DOI=10.1073/pnas.96.18.10248;
RA   Turmel M., Otis C., Lemieux C.;
RT   "The complete chloroplast DNA sequence of the green alga Nephroselmis
RT   olivacea: insights into the architecture of ancestral chloroplast
RT   genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:10248-10253(1999).
CC   -!- FUNCTION: Involved in intercistronic processing of primary transcripts
CC       from chloroplast operons. The endonucleolytic activity of the enzyme
CC       depends on the number of phosphates at the 5' end, is inhibited by
CC       structured RNA, and preferentially cleaves A/U-rich sequences.
CC       {ECO:0000250|UniProtKB:F4IV66}.
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   -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC       {ECO:0000250|UniProtKB:F4IV66}.
CC   -!- SIMILARITY: Belongs to the RNase E/G family. {ECO:0000305}.
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DR   EMBL; AF137379; AAD54806.1; -; Genomic_DNA.
DR   RefSeq; NP_050835.1; NC_000927.1.
DR   AlphaFoldDB; Q9TL10; -.
DR   SMR; Q9TL10; -.
DR   PRIDE; Q9TL10; -.
DR   GeneID; 801930; -.
DR   GO; GO:0009570; C:chloroplast stroma; 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:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   InterPro; IPR019307; RNA-bd_AU-1/RNase_E/G.
DR   InterPro; IPR004659; RNase_E/G.
DR   PANTHER; PTHR30001; PTHR30001; 1.
DR   Pfam; PF10150; RNase_E_G; 1.
PE   3: Inferred from homology;
KW   Chloroplast; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   mRNA processing; Nuclease; Plastid; RNA-binding.
FT   CHAIN           1..375
FT                   /note="Ribonuclease E/G-like protein"
FT                   /id="PRO_0000097376"
FT   BINDING         286
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
FT   BINDING         325
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
SQ   SEQUENCE   375 AA;  42619 MW;  7088BAC0478A8201 CRC64;
     MLVVGNRIVD VSRHTSIGTI VIATVDKLAP GLGIAFVSWT HGQGKGGLPS TKKHYGILPL
     RSWRGRGPLD FATTHELTGE NLILQHGDFV LVQIVQDGNH AKVHLVSGHI ALTTSRLVVW
     PGLSSKDWIF SHQIGQKINN YLHVRKLVSY MRRDQILCTG PQRWMKEQYA LEHQWENFVL
     EFIEQPTGIS YLTSMTEKFV SPVCAEWFQH PLSVWIIGCN LQIRESMTKW MITHVPHKSR
     HIEITTLDAW KNWYNLHRAA IVQPQIPLRS GGTMIIEFTE IGWSFDINSG IGLEIGSKTC
     ANEEAIYAIA QQILLRSMHG FILIDFIGDI DLEKLRVNLI QFTSLLEQDS YHIRIISISA
     DGLVCVIRHR RSKLI