RNL2_LENED
ID RNL2_LENED Reviewed; 239 AA.
AC P81296;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Ribonuclease Le2;
DE Short=RNase Le2;
DE EC=4.6.1.19;
OS Lentinula edodes (Shiitake mushroom) (Lentinus edodes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Omphalotaceae; Lentinula.
OX NCBI_TaxID=5353;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=1369096; DOI=10.1271/bbb.56.2003;
RA Kobayashi H., Inokuchi N., Koyama T., Watanabe H., Iwama M., Ohgi K.,
RA Irie M.;
RT "Primary structure of a base non-specific and adenylic acid preferential
RT ribonuclease from the fruit bodies of Lentinus edodes.";
RL Biosci. Biotechnol. Biochem. 56:2003-2010(1992).
RN [2]
RP PROTEIN SEQUENCE OF 1-40.
RX PubMed=1368676; DOI=10.1271/bbb1961.55.1167;
RA Shimada H., Inokuchi N., Okuwaki H., Koyama T., Irie M.;
RT "Purification and characterization of a base non-specific and adenylic acid
RT preferring ribonuclease from the fruit bodies of Lentinus edodes.";
RL Agric. Biol. Chem. 55:1167-1169(1991).
CC -!- FUNCTION: This is a base non-specific and adenylic acid preferential
CC ribonuclease.
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 -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR PIR; JC1373; JC1373.
DR AlphaFoldDB; P81296; -.
DR SMR; P81296; -.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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 Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW Nuclease.
FT CHAIN 1..239
FT /note="Ribonuclease Le2"
FT /id="PRO_0000206505"
FT ACT_SITE 51
FT /evidence="ECO:0000250"
FT ACT_SITE 111
FT /evidence="ECO:0000250"
FT ACT_SITE 115
FT /evidence="ECO:0000250"
FT DISULFID 5..22
FT /evidence="ECO:0000250"
FT DISULFID 13..58
FT /evidence="ECO:0000250"
FT DISULFID 21..126
FT /evidence="ECO:0000250"
FT DISULFID 66..118
FT /evidence="ECO:0000250"
FT DISULFID 191..225
FT /evidence="ECO:0000250"
SQ SEQUENCE 239 AA; 25877 MW; 3277B8DC3B498E04 CRC64;
ISSGCGTTGA LSCSSNAKGT CCFEAPGGLI LQTQFWDTSP ETGPTDSWTI HGLWPDNCDG
SFSEDCDPSR DYTGISSLLT AQGASDTLQF MNQFWLNDPD DGSNEELWEH EWATHGTCYS
TLQTSCLPEG SPKGAEAVAF FEQVVTLFKT LPTYEWLTNQ GIKPSSSTTH TYSALTAALE
AEAGVIPALN CDGSDLDEIY WYFHLRGSVI DGEFEPISAP EKGDCPSSGI KWLPKNNEK
