ID   RNMS_ASPPH              Reviewed;         105 AA.
AC   P00653;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Guanyl-specific ribonuclease Ms;
DE            Short=RNase Ms;
DE            EC=4.6.1.24;
OS   Aspergillus phoenicis (Aspergillus saitoi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5063;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=7096302; DOI=10.1093/oxfordjournals.jbchem.a133841;
RA   Watanabe H., Ohgi K., Irie M.;
RT   "Primary structure of a minor ribonuclease from Aspergillus saitoi.";
RL   J. Biochem. 91:1495-1509(1982).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND SEQUENCE REVISION TO 52-54; 80
RP   AND 95.
RX   PubMed=1646118; DOI=10.1016/0014-5793(91)80589-u;
RA   Nonaka T., Mitsui Y., Irie M., Nakamura K.T.;
RT   "Three-dimensional structure of ribonuclease Ms*3'-guanylic acid complex at
RT   2.5-A resolution.";
RL   FEBS Lett. 283:207-209(1991).
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; A00800; NRASTP.
DR   PDB; 1RDS; X-ray; 1.80 A; A=1-105.
DR   PDB; 1RMS; X-ray; 1.90 A; A=1-105.
DR   PDBsum; 1RDS; -.
DR   PDBsum; 1RMS; -.
DR   AlphaFoldDB; P00653; -.
DR   SMR; P00653; -.
DR   EvolutionaryTrace; P00653; -.
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   3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW   Hydrolase; Lyase; Nuclease.
FT   CHAIN           1..105
FT                   /note="Guanyl-specific ribonuclease Ms"
FT                   /id="PRO_0000137370"
FT   ACT_SITE        39
FT   ACT_SITE        57
FT                   /note="Proton acceptor"
FT   ACT_SITE        91
FT                   /note="Proton donor"
FT   DISULFID        3..11
FT   DISULFID        7..102
FT   STRAND          4..7
FT                   /evidence="ECO:0007829|PDB:1RDS"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:1RDS"
FT   HELIX           14..30
FT                   /evidence="ECO:0007829|PDB:1RDS"
FT   STRAND          37..41
FT                   /evidence="ECO:0007829|PDB:1RDS"
FT   STRAND          55..60
FT                   /evidence="ECO:0007829|PDB:1RDS"
FT   STRAND          74..80
FT                   /evidence="ECO:0007829|PDB:1RDS"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:1RDS"
FT   STRAND          94..97
FT                   /evidence="ECO:0007829|PDB:1RDS"
SQ   SEQUENCE   105 AA;  11332 MW;  94CF56D109242EFD CRC64;
     ESCEYTCGST CYWSSDVSAA KAKGYSLYES GDTIDDYPHG YHDYEGFDFP VSGTYYEYPI
     MSDYDVYTGG SPGADRVIFN GDDELAGVIT HTGASGDDFV ACSSS