ID   RNLX_SOLLC              Reviewed;         237 AA.
AC   P80196;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Intracellular ribonuclease LX;
DE            Short=RNase LX;
DE            EC=4.6.1.19;
DE   Flags: Precursor;
GN   Name=RNALX;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=cv. Lukullus; TISSUE=Hypocotyl;
RX   PubMed=7894013; DOI=10.1007/bf00019315;
RA   Koeck M., Loeffler A., Abel S., Glund K.;
RT   "cDNA structure and regulatory properties of a family of starvation-induced
RT   ribonucleases from tomato.";
RL   Plant Mol. Biol. 27:477-485(1995).
RN   [2]
RP   PROTEIN SEQUENCE OF 25-237.
RC   STRAIN=cv. Lukullus;
RX   PubMed=8319673; DOI=10.1111/j.1432-1033.1993.tb17962.x;
RA   Loeffler A., Glund K., Irie M.;
RT   "Amino acid sequence of an intracellular, phosphate-starvation-induced
RT   ribonuclease from cultured tomato (Lycopersicon esculentum) cells.";
RL   Eur. J. Biochem. 214:627-633(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-
CC         phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA +
CC         H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-
CC         COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:138284,
CC         ChEBI:CHEBI:173118; EC=4.6.1.19; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10045, ECO:0000255|PROSITE-ProRule:PRU10046};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Intracellular, but extravacuolar.
CC   -!- INDUCTION: By phosphate starvation.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; X79338; CAA55896.1; -; mRNA.
DR   PIR; S53507; S53507.
DR   RefSeq; NP_001234551.2; NM_001247622.2.
DR   AlphaFoldDB; P80196; -.
DR   SMR; P80196; -.
DR   STRING; 4081.Solyc05g007940.2.1; -.
DR   PaxDb; P80196; -.
DR   GeneID; 544193; -.
DR   KEGG; sly:544193; -.
DR   eggNOG; KOG1642; Eukaryota.
DR   InParanoid; P80196; -.
DR   OrthoDB; 994722at2759; -.
DR   BRENDA; 4.6.1.19; 3101.
DR   Proteomes; UP000004994; Unplaced.
DR   ExpressionAtlas; P80196; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR   CDD; cd01061; RNase_T2_euk; 1.
DR   Gene3D; 3.90.730.10; -; 1.
DR   InterPro; IPR033697; Ribonuclease_T2_eukaryotic.
DR   InterPro; IPR001568; RNase_T2-like.
DR   InterPro; IPR036430; RNase_T2-like_sf.
DR   InterPro; IPR018188; RNase_T2_His_AS_1.
DR   InterPro; IPR033130; RNase_T2_His_AS_2.
DR   PANTHER; PTHR11240; PTHR11240; 1.
DR   Pfam; PF00445; Ribonuclease_T2; 1.
DR   SUPFAM; SSF55895; SSF55895; 1.
DR   PROSITE; PS00530; RNASE_T2_1; 1.
DR   PROSITE; PS00531; RNASE_T2_2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Disulfide bond; Endonuclease;
KW   Hydrolase; Lyase; Nuclease; Reference proteome; Stress response; Zymogen.
FT   PROPEP          1..24
FT                   /evidence="ECO:0000269|PubMed:8319673"
FT                   /id="PRO_0000030970"
FT   CHAIN           25..237
FT                   /note="Intracellular ribonuclease LX"
FT                   /id="PRO_0000030971"
FT   ACT_SITE        63
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        117
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..124
FT                   /evidence="ECO:0000250"
FT   DISULFID        183..219
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   237 AA;  27018 MW;  54D03F8D6EEBD463 CRC64;
     MMKSQKKLLI KIIVVQCLLV LCVTSQDFDF FYFVQQWPAS YCDTRRSCCY PTTGKPDEDF
     SIHGLWPNYK DGKWPQNCDR ESSLDESEFS DLISTMEKNW PSLACPSSDG LKFWSHEWLK
     HGTCSALNQH AYFQTALDFK TKSNLLQNLN NAGIKPRNGD YYGVESIKKA IEKGVGHTPF
     IECNVDSQGN HQLYQVYLCV DSSASKFIDC PIFPHGGKCG SKIEFPSFST NDDHDEF