ID   RNM_ASPPH               Reviewed;         238 AA.
AC   P19791;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Ribonuclease M;
DE            Short=RNase M;
DE            EC=4.6.1.19;
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=2229029; DOI=10.1093/oxfordjournals.jbchem.a123198;
RA   Watanabe H., Naitoh A., Suyama Y., Inokuchi N., Shimada H., Koyama T.,
RA   Ohgi K., Irie M.;
RT   "Primary structure of a base non-specific and adenylic acid preferential
RT   ribonuclease from Aspergillus saitoi.";
RL   J. Biochem. 108:303-310(1990).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; P19791; -.
DR   SMR; P19791; -.
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..238
FT                   /note="Ribonuclease M"
FT                   /id="PRO_0000206504"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        115
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        5..22
FT                   /evidence="ECO:0000250"
FT   DISULFID        13..58
FT                   /evidence="ECO:0000250"
FT   DISULFID        21..126
FT                   /evidence="ECO:0000250"
FT   DISULFID        66..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..225
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   238 AA;  26607 MW;  D34F53073C8E0125 CRC64;
     TIDTCSSDSP LSCQTDNEAS CCFNSPGGSL LQTQFWDYDP SDGPSDSWTI HGLWPDNCDG
     SYQEYCDDSR EYSNITSILE AQDRTELLSY MKEYWPDYEG ADEDESFWEH EWNKHGTCIN
     TIDPSCYTDY YAQEEVGDFF QQVVDLFKTL DSYTALSDAG ITPSEDATYK LSDIEDALAA
     IHDGYPPYVG CEDGALSQLY YYFNVKGSAI GGTYVASERL EDSNCKGSGI KYPPKSSS