RNS3_PYRPY
ID RNS3_PYRPY Reviewed; 222 AA.
AC O80323;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Ribonuclease S-3;
DE EC=4.6.1.19;
DE AltName: Full=S3-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. 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 [2]
RP PROTEIN SEQUENCE OF 23-36.
RX PubMed=8232200; DOI=10.1007/bf00280196;
RA Sassa H., Hirano H., Ikehashi H.;
RT "Identification and characterization of stylar glycoproteins associated
RT with self-incompatibility genes of Japanese pear, Pyrus serotina Rehd.";
RL Mol. Gen. Genet. 241:17-25(1993).
RN [3]
RP GLYCOSYLATION AT ASN-40 AND ASN-138, 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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=11577107; DOI=10.1074/jbc.m107617200;
RA Matsuura T., Sakai H., Unno M., Ida K., Sato M., Sakiyama F., Norioka S.;
RT "Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil
RT ribonuclease responsible for gametophytic self-incompatibility.";
RL J. Biol. Chem. 276:45261-45269(2001).
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-linked core structure at Asn-138 contains xylose.
CC {ECO:0000269|PubMed:10469125}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; AB002140; BAA32413.1; -; mRNA.
DR PIR; S39930; S39930.
DR PDB; 1IQQ; X-ray; 1.50 A; A=23-222.
DR PDBsum; 1IQQ; -.
DR AlphaFoldDB; O80323; -.
DR SMR; O80323; -.
DR iPTMnet; O80323; -.
DR EvolutionaryTrace; O80323; -.
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 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Glycoprotein; Hydrolase; Lyase; Nuclease; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:8232200"
FT CHAIN 23..222
FT /note="Ribonuclease S-3"
FT /id="PRO_0000030979"
FT ACT_SITE 55
FT ACT_SITE 106
FT ACT_SITE 109
FT ACT_SITE 110
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:10469125"
FT DISULFID 37..44
FT DISULFID 70..113
FT DISULFID 177..215
FT DISULFID 192..203
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 50..60
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 99..109
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1IQQ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 121..132
FT /evidence="ECO:0007829|PDB:1IQQ"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:1IQQ"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:1IQQ"
FT TURN 166..170
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 183..193
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 197..201
FT /evidence="ECO:0007829|PDB:1IQQ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:1IQQ"
SQ SEQUENCE 222 AA; 25747 MW; C3B3A6FEB53D91C1 CRC64;
MVHVVMMVFL LIVLILCSST VGYDYFQFTQ QYQLAVCNSN RTLCKDPPDK LFTVHGLWPS
NMVGPDPSKC PIKNIRKREK LLEHQLEIIW PNVFDRTKNN LFWDKEWMKH GSCGYPTIDN
ENHYFETVIK MYISKKQNVS RILSKAKIEP DGKKRALLDI ENAIRNGADN KKPKLKCQKK
GTTTELVEIT LCSDKSGEHF IDCPHPFEPI SPHYCPTNNI KY
