ID   RNT1_TRIHA              Reviewed;         106 AA.
AC   P26875;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   RecName: Full=Guanyl-specific ribonuclease Th1;
DE            Short=RNase Th1;
DE            EC=4.6.1.24;
OS   Trichoderma harzianum (Hypocrea lixii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5544;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=01;
RX   PubMed=3139001;
RA   Bezborodova S.I., Vasileva-Tonkova E.S., Polyakov K.M., Shlyapnikov S.V.;
RT   "Isolation, analysis of amino acid sequence and crystallization of the
RT   extracellular ribonuclease Th1 from Trichoderma harzianum-01.";
RL   Bioorg. Khim. 14:453-466(1988).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[RNA] containing guanosine + H2O = an [RNA fragment]-3'-
CC         guanosine-3'-phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA
CC         fragment].; EC=4.6.1.24;
CC   -!- SIMILARITY: Belongs to the ribonuclease N1/T1 family. {ECO:0000305}.
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DR   PIR; JN0428; JN0428.
DR   AlphaFoldDB; P26875; -.
DR   SMR; P26875; -.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046589; F:ribonuclease T1 activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   Gene3D; 3.10.450.30; Microbial ribonucleases; 1.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   PANTHER; PTHR42104; EXTRACELLULAR GUANYL-SPECIFIC RIBONUCLEASE RNTA (AFU_ORTHOLOGUE AFUA_4G03230); 1.
DR   PANTHER; PTHR42104:SF1; EXTRACELLULAR GUANYL-SPECIFIC RIBONUCLEASE RNTA (AFU_ORTHOLOGUE AFUA_4G03230); 1.
DR   SUPFAM; SSF53933; Microbial ribonucleases; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease.
FT   CHAIN           1..106
FT                   /note="Guanyl-specific ribonuclease Th1"
FT                   /id="PRO_0000137375"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        58
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        92
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        5..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        23..84
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   106 AA;  10750 MW;  892A8BFE043AA022 CRC64;
     DTATCGKVFY SASAVSAASN AACNYVRAGS TAGGSTYPHV YNNYEGFRFK GLSKPFYEFP
     ILSSGKTYTG GSPGADRVVI NGQCSIAGII THTGASGNAF VACGGT
//