RNS5_PYRPY
ID RNS5_PYRPY Reviewed; 227 AA.
AC P93460;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Ribonuclease S-5;
DE EC=4.6.1.19;
DE AltName: Full=S5-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].
RC STRAIN=cv. Kosui; TISSUE=Style;
RA Sassa H., Hirano H.;
RT "Nucleotide sequence of a cDNA encoding S5-Rnase from Japanese pear (Pyrus
RT serotina).";
RL (er) Plant Gene Register PGR97-007(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=cv. Hosui; 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 [3]
RP GLYCOSYLATION AT ASN-45 AND ASN-143, AND STRUCTURE OF CARBOHYDRATES.
RC STRAIN=cv. Hosui; 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: N-glycan at Asn-45 consists of disaccharide (GlcNAc-GlcNAc). N-
CC linked core structure at Asn-143 contains xylose.
CC {ECO:0000269|PubMed:10469125}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; D88282; BAA13577.1; -; mRNA.
DR EMBL; AB002141; BAA32414.1; -; mRNA.
DR AlphaFoldDB; P93460; -.
DR SMR; P93460; -.
DR iPTMnet; P93460; -.
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..227
FT /note="Ribonuclease S-5"
FT /id="PRO_0000030981"
FT ACT_SITE 60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT ACT_SITE 115
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT DISULFID 75..118
FT /evidence="ECO:0000250"
FT DISULFID 182..208
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 26059 MW; 44BC2A9E9E738FCA CRC64;
MGITGMVYVV TMVFLLIVLI LSSSTVGYDY FQFTQQYQLA VCNSNRTPCK DPPDKLFTVH
GLWPSSMAGP DPSNCPIRNI RKREKLLEPQ LAIIWPNVFD RTKNKLFWDK EWMKHGTCGY
PTIDNENHYF ETVIKMYISK KQNVSRILSK AKIEPDGKKR ALLDIENAIR NGADNKKPKL
KCQKKGTTTE LVEITLCSDK SGEHFIDCPH PFEPISPHYC PTNNIKY
