ID   RNF1_GIBBA              Reviewed;         105 AA.
AC   P16411;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Extracellular guanyl-specific ribonuclease Fl1;
DE            Short=RNase Fl1;
DE            EC=4.6.1.24;
OS   Gibberella baccata (Fusarium lateritium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium lateritium species complex.
OX   NCBI_TaxID=5523;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=54228;
RX   PubMed=3142486;
RA   Bezborodova S.I., Chepurnova N.K., Shlyapnikov S.V.;
RT   "Ribonuclease Fl1 from Fusarium lateriticum. Isolation, substrate
RT   specificity and amino acid sequence.";
RL   Bioorg. Khim. 14:893-904(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   AlphaFoldDB; P16411; -.
DR   SMR; P16411; -.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
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   InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR   InterPro; IPR016191; Ribonuclease/ribotoxin.
DR   Pfam; PF00545; Ribonuclease; 1.
DR   SUPFAM; SSF53933; SSF53933; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease.
FT   CHAIN           1..105
FT                   /note="Extracellular guanyl-specific ribonuclease Fl1"
FT                   /id="PRO_0000137377"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        57
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        90
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        5..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        23..82
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   105 AA;  10889 MW;  5DD5C8E56B1972D4 CRC64;
     EASTCGSTPY SASQVRAAAN AACQYYQSDD TAGSTTYPHT YNNYEGFDFA VNGPYQEFPI
     RTGGVYSGGS PGADRVIINT SCQYAGAITH TGASGNNFVG CSNST