ID   RNTR_HYPRU              Reviewed;         234 AA.
AC   P24657;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Ribonuclease Trv;
DE            Short=RNase Trv;
DE            EC=4.6.1.19;
OS   Hypocrea rufa (Trichoderma viride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5547;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1794979; DOI=10.1093/oxfordjournals.jbchem.a123686;
RA   Inada Y., Watanabe H., Ohgi K., Irie M.;
RT   "Isolation, characterization, and primary structure of a base non-specific
RT   and adenylic acid preferential ribonuclease with higher specific activity
RT   from Trichoderma viride.";
RL   J. Biochem. 110:896-904(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; JX0197; JX0197.
DR   AlphaFoldDB; P24657; -.
DR   SMR; P24657; -.
DR   iPTMnet; P24657; -.
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; Glycoprotein;
KW   Hydrolase; Lyase; Nuclease.
FT   CHAIN           1..234
FT                   /note="Ribonuclease Trv"
FT                   /id="PRO_0000206507"
FT   ACT_SITE        52
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        15
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:1794979"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        5..24
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        23..125
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..224
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   234 AA;  25901 MW;  8B011DD65A3F909A CRC64;
     ASKTCPSNTP LSCHNTTVVQ DTCCFIPSGQ LLQTQFWDTD PSTGPSDSWT IHGLWPDNCD
     GSFPQTCDAS RAYTNITDIL TAMGADDTLQ YMQTYWKDYQ GNDESFWEHE WGKHGTCITT
     LDPGCYDDYV PTEEAADFFS KTVSLFKTLP TYQWLADAGI TPDGSKSYAL DDIQSALSQQ
     HGAEVTLGCD GKTLNEVWYH FNVKGSLQDG QFVAAEPDGA KSTCPDDVYY DPKK