RNS6_PYRPY
ID RNS6_PYRPY Reviewed; 229 AA.
AC O80324;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Ribonuclease S-6;
DE EC=4.6.1.19;
DE AltName: Full=S6-RNase;
DE Flags: Precursor;
OS Pyrus pyrifolia (Chinese pear) (Pyrus serotina).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Pyrus.
OX NCBI_TaxID=3767;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Imamuraaki; TISSUE=Style;
RX PubMed=9700066; DOI=10.1023/a:1006078500664;
RA Ishimizu T., Shinkawa T., Sakiyama F., Norioka S.;
RT "Primary structural features of rosaceous S-RNases associated with
RT gametophytic self-incompatibility.";
RL Plant Mol. Biol. 37:931-941(1998).
RN [2]
RP GLYCOSYLATION AT ASN-77; ASN-87; ASN-145; ASN-188 AND ASN-203, AND
RP STRUCTURE OF CARBOHYDRATES.
RC STRAIN=cv. Imamuraaki; TISSUE=Style;
RX PubMed=10469125; DOI=10.1046/j.1432-1327.1999.00499.x;
RA Ishimizu T., Mitsukami Y., Shinkawa T., Natsuka S., Hase S., Miyagi M.,
RA Sakiyama F., Norioka S.;
RT "Presence of asparagine-linked N-acetylglucosamine and chitobiose in Pyrus
RT pyrifolia S-RNases associated with gametophytic self-incompatibility.";
RL Eur. J. Biochem. 263:624-634(1999).
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};
CC -!- PTM: The N-glycans attached at Asn-188 and Asn-203 consist of either
CC monosaccharide (GlcNAc) or disaccharide (GlcNAc-GlcNAc) that could not
CC be distinguished.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
CC -!- CAUTION: Gln-112 is present instead of the conserved Glu which is
CC expected to act as an active site proton donor. {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 EMBL; AB002142; BAA32415.1; -; mRNA.
DR AlphaFoldDB; O80324; -.
DR SMR; O80324; -.
DR iPTMnet; O80324; -.
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 PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00530; RNASE_T2_1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Endonuclease; Glycoprotein;
KW Hydrolase; Lyase; Nuclease; Signal.
FT SIGNAL 1..27
FT CHAIN 28..229
FT /note="Ribonuclease S-6"
FT /id="PRO_0000030982"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine; alternate"
FT /evidence="ECO:0000269|PubMed:10469125"
FT DISULFID 75..119
FT /evidence="ECO:0000250"
FT DISULFID 184..210
FT /evidence="ECO:0000250"
SQ SEQUENCE 229 AA; 26278 MW; 907C5231E0B612A3 CRC64;
MGITGMIYMV PMVFSLIVLI SCSSTMGYNY FQFTQQYQPA VCNSNPTPCK DPPDKLFTVH
GLWPSNDVGD DPIYCKNKTI KSQQIGNLTA QLIIIWPNVL DRTDHVGFWN RQWNKHGSCG
KAPTIKDEMH YFKTVIKMYI TQKQNVSEIL SRAKIEPEGK IRRRDDIINA IRLGTKDKKP
KLKCQKNNQT TELVEITICS DRNLTQFIDC PRSSFKGSPF HCPTNHILY
