ID   RNOY_CRAGI              Reviewed;         213 AA.
AC   Q7M456;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=Ribonuclease Oy;
DE            Short=RNase Oy;
DE            EC=3.1.27.-;
OS   Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX   NCBI_TaxID=29159;
RN   [1]
RP   PROTEIN SEQUENCE, AND CHARACTERIZATION.
RX   PubMed=8138535; DOI=10.1093/oxfordjournals.jbchem.a124259;
RA   Watanabe H., Narumi H., Inaba T., Ohgi K., Irie M.;
RT   "Purification, some properties, and primary structure of a base non-
RT   specific ribonuclease from oyster (Crussdstrea grigus).";
RL   J. Biochem. 114:800-807(1993).
CC   -!- FUNCTION: Releases mononucleotides from RNA in the order of 3'-GMP, 3'-
CC       AMP and 3'-UMP.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   PIR; JX0295; JX0295.
DR   AlphaFoldDB; Q7M456; -.
DR   SMR; Q7M456; -.
DR   PRIDE; Q7M456; -.
DR   Proteomes; UP000005408; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033897; F:ribonuclease T2 activity; IEA:InterPro.
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; Nuclease; Reference proteome; Secreted.
FT   CHAIN           1..213
FT                   /note="Ribonuclease Oy"
FT                   /id="PRO_0000206510"
FT   ACT_SITE        35
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        89
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        93
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        51..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        160..198
FT                   /evidence="ECO:0000250"
FT   DISULFID        178..188
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   213 AA;  24360 MW;  8C8A9852C330738A CRC64;
     KDWNYFTFAQ QWPIAVCAEH KSCFIPDSVV GWGIHGLWPS SDTESKGPEN CNGSWPFDIN
     NVMPLVPELK KYWPNLYPDT KANSFWEHEW SKHGTCATSL PATSNELKYF GMGLKLHAKY
     NISRILVNQG ILPSKTAGYM INETEAAVKR ELGVDAVIEC VYDKEKTKKQ LLYEISICLT
     KEFELISCNK KEVSETTCPR KEPFFYPPVH DNN