ID   RNE_PORPU               Reviewed;         511 AA.
AC   P51211;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Ribonuclease E/G-like protein;
DE            Short=RNase E/G-like protein;
DE            EC=3.1.26.-;
GN   Name=rne;
OS   Porphyra purpurea (Red seaweed) (Ulva purpurea).
OG   Plastid; Chloroplast.
OC   Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra.
OX   NCBI_TaxID=2787;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Avonport;
RA   Reith M.E., Munholland J.;
RT   "Complete nucleotide sequence of the Porphyra purpurea chloroplast
RT   genome.";
RL   Plant Mol. Biol. Rep. 13:333-335(1995).
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; U38804; AAC08097.1; -; Genomic_DNA.
DR   PIR; S73132; S73132.
DR   RefSeq; NP_053821.1; NC_000925.1.
DR   AlphaFoldDB; P51211; -.
DR   SMR; P51211; -.
DR   GeneID; 809835; -.
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   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   3: Inferred from homology;
KW   Chloroplast; Endonuclease; Hydrolase; Magnesium; Metal-binding;
KW   mRNA processing; Nuclease; Plastid; RNA-binding.
FT   CHAIN           1..511
FT                   /note="Ribonuclease E/G-like protein"
FT                   /id="PRO_0000097377"
FT   DOMAIN          35..117
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00180"
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"
SQ   SEQUENCE   511 AA;  58795 MW;  599B4AEBFFA76F9F CRC64;
     MTNTIVISCL HNIAAILYCG QIQKLVVANA HYQVSDIYLG TVDKIFSGIN AAFVDLGKNE
     YSGFIHISDT GPLKKKYYIN NITNILTIRQ KILVQIIKEP TLNKGPRLTA NITLSGRYIV
     LMPFSQAICI SRKIYDEDER HYLKALAILI KPPTMGLLFR PSAIGIDEEI ILSELTNLKE
     QWYFIQKSAI NNCAPVLLYK DEDIVKKVIR DFYDNNTKNI VIDSNLGLKQ LNYYINTWQC
     NFSSTIPSLQ LYSSNKCILD TFRINQAISR ALIPKVDLIL GGYMFIETLE AFTIIDVNSG
     SFNNSTSARE TVLKTNCSAA TEIAYQLKIR NIAGVIIIDF IDMESQRDQL QLLEHFDKEL
     SLDDAKPQIV QLSELGLVEL TRRRKGKSLY ELVSNDSNYF HFFIQLEQLD SIKPSSYKSK
     RLSSSVKSWL FSEIDMINRV FFKKSNLYRL SNFYYARNLY IIYSDFTVNK NIQLAARYKL
     MYSLQNIQIL PSTWYFNFLD IHTNNITNYL S