ID   RNST_SACER              Reviewed;         101 AA.
AC   P00650;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Guanyl-specific ribonuclease St;
DE            Short=RNase St;
DE            EC=4.6.1.24;
OS   Saccharopolyspora erythraea (Streptomyces erythraeus).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=1836;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=1269746; DOI=10.1016/0014-5793(76)80264-5;
RA   Yoshida N., Sasaki A., Rashid M.A., Otsuka H.;
RT   "The amino acid sequence of ribonuclease St.";
RL   FEBS Lett. 64:122-125(1976).
RN   [2]
RP   SEQUENCE REVISION.
RA   Yoshida N., Sasaki A., Rashid M.A., Otsuka H.;
RL   Submitted (JUN-1977) to the PIR data bank.
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; A91429; NRSMTE.
DR   AlphaFoldDB; P00650; -.
DR   SMR; P00650; -.
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..101
FT                   /note="Guanyl-specific ribonuclease St"
FT                   /id="PRO_0000137368"
FT   ACT_SITE        61
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        91
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   DISULFID        4..54
FT                   /evidence="ECO:0000269|PubMed:1269746"
SQ   SEQUENCE   101 AA;  11354 MW;  E739ADB75A61A9FB CRC64;
     EAPCGDTSGF EQVRLADLPP EATDTYELIE KGGPYPYPED GTVFENREGI LPDCAEGYYH
     EYTVKTPSGD DRGARRFVVG DGGEYFYTED HYESFRLTIV N