RNS1_PYRPY
ID RNS1_PYRPY Reviewed; 228 AA.
AC O80322;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Ribonuclease S-1;
DE EC=4.6.1.19;
DE AltName: Full=S1-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-87; ASN-101; ASN-144; ASN-157 AND ASN-175, 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 (By
CC similarity). {ECO:0000250}.
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: N-linked core structure at Asn-87 and Asn-101 contains xylose and
CC fucose or consists of disaccharide (GlcNAc-GlcNAc). N-linked core
CC structure at Asn-144 contains xylose. {ECO:0000269|PubMed:10469125}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; AB002139; BAA32412.1; -; mRNA.
DR AlphaFoldDB; O80322; -.
DR SMR; O80322; -.
DR iPTMnet; O80322; -.
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..228
FT /note="Ribonuclease S-1"
FT /id="PRO_0000030977"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT DISULFID 75..119
FT /evidence="ECO:0000250"
FT DISULFID 183..210
FT /evidence="ECO:0000250"
SQ SEQUENCE 228 AA; 25791 MW; 95AF4EB28E6D571E CRC64;
MGVTGMTYMF TMVFSLIVLI LSSSTVGYDY FQFTQQYQPA VCNSNPTPCN DPTDKLFTVH
GLWPSNRNGP DPEKCKTTAL NSQKIGNMTA QLEIIWPNVL NRSDHVGFWE KEWIKHGTCG
YPTIKDDMHY LQTVIRMYIT QKQNVSAILS KAAIQPNGTN RPLVDIENAI RRGTNNTKPK
FKCQKNTRTT TELVEVTLCS DRDLKKFINC PHGPPQGSRF SCPSSVQY
