ID   RNE_GUITH               Reviewed;         429 AA.
AC   O78453;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Ribonuclease E/G-like protein;
DE            Short=RNase E/G-like protein;
DE            EC=3.1.26.-;
GN   Name=rne;
OS   Guillardia theta (Cryptophyte) (Cryptomonas phi).
OG   Plastid; Chloroplast.
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=55529;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9929392; DOI=10.1007/pl00006462;
RA   Douglas S.E., Penny S.L.;
RT   "The plastid genome of the cryptophyte alga, Guillardia theta: complete
RT   sequence and conserved synteny groups confirm its common ancestry with red
RT   algae.";
RL   J. Mol. Evol. 48:236-244(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF041468; AAC35644.1; -; Genomic_DNA.
DR   RefSeq; NP_050710.1; NC_000926.1.
DR   AlphaFoldDB; O78453; -.
DR   SMR; O78453; -.
DR   GeneID; 857011; -.
DR   HOGENOM; CLU_640066_0_0_1; -.
DR   OMA; HANHITD; -.
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   PANTHER; PTHR30001; PTHR30001; 2.
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..429
FT                   /note="Ribonuclease E/G-like protein"
FT                   /id="PRO_0000097374"
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
FT   BINDING         332
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P21513"
SQ   SEQUENCE   429 AA;  50078 MW;  5112DC1BC624023F CRC64;
     MSFNIIILKE LGFSLVFSQS KCEYIIFQKE QCGLNDIYFG FIPRQSIYPT LNAAFVTLDS
     ERNQGFIPFT LLIKKSNQQF VIPNSVFLIQ VIKEPTINKP ATLTSHIFLN SFNLNLQFSG
     IDCKYLNLYP NIKFLHICLI TLLIPSGLDI NFDHSMKDIL YLDLIGQSKI LYYSFSNLFT
     KLLRIKKMPQ FIFRNSNFFL PILNKLSLSS INDFFVSSYQ RAVYLRHFLI THYFTIKQTD
     YRILFYPTAY KSMQLYYLDM LFYRSLKPIV YTLYGIFIVI CKTEALISID VNSGSHSSRV
     SQNLSLHTNL IASKSIIKEI KLRNLAGVIV IDFVDMIHQK DQIHLLAFFR YLLNINSVMI
     TLIQLSDIGL LELTRKRQDQ SIYDVFQIGN ISKSSFLYDR ILSLNKNLFK TNLLINYTLF
     SNVKLIYNY