ID   RNS3_PETHY              Reviewed;         222 AA.
AC   Q40875;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Ribonuclease S-3;
DE            EC=4.6.1.19;
DE   AltName: Full=S3-RNase;
DE   AltName: Full=Stylar glycoprotein 3;
DE   Flags: Precursor;
GN   Name=S3;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Okuley J.J., Sims T.L.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Self-incompatibility (SI) is the inherited ability of a
CC       flowering plant to prevent self-fertilization by discriminating between
CC       self and non-self pollen during pollination. In many species, self-
CC       incompatibility is controlled by the single, multiallelic locus S.
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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
CC   -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR   EMBL; U07363; AAA60466.1; -; Genomic_DNA.
DR   PIR; JQ1076; JQ1076.
DR   AlphaFoldDB; Q40875; -.
DR   SMR; Q40875; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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   3: Inferred from homology;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..222
FT                   /note="Ribonuclease S-3"
FT                   /id="PRO_0000030976"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        68..117
FT                   /evidence="ECO:0000250"
FT   DISULFID        177..210
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  26213 MW;  C2B3640DC4A8CAE8 CRC64;
     MFRLQLISAF FILLFSLSPV SANFDYFQLV LTWPASFCYP KNKCQRRSNN FTIHGLWPEK
     KRFRLEFCTG DKYKRFLEED NIINVLERHW IQMRFDETYA NTKQPLWEHE YNRHGICCKN
     LYDQKAYFLL AMRLKDKLDL LTTLRTHGIT PGTKHTFGEI QKAIKTVTSN NDPDLKCVEN
     IKGVMELNEI GICYTPAADR FDRCRHSNTC DETSSTKILF RG