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RNS7_PYRPY
ID   RNS7_PYRPY              Reviewed;         226 AA.
AC   O80325;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Ribonuclease S-7;
DE            EC=4.6.1.19;
DE   AltName: Full=S7-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. Okusankichi; 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-74; ASN-77; ASN-126; ASN-144 AND ASN-172, AND
RP   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: The N-glycans attached at Asn-74 and Asn-77 consist of either
CC       monosaccharide (GlcNAc) or disaccharide (GlcNAc-GlcNAc) that could not
CC       be distinguished. The N-glycan at Asn-144 contains mannose and xylose,
CC       and at Asn-126 contains mannose, xylose and fucose. The N-glycan at
CC       Asn-172 consists of disaccharide (GlcNAc-GlcNAc).
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}.
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DR   EMBL; AB002143; BAA32416.1; -; mRNA.
DR   AlphaFoldDB; O80325; -.
DR   SMR; O80325; -.
DR   iPTMnet; O80325; -.
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   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Signal.
FT   SIGNAL          1..27
FT   CHAIN           28..226
FT                   /note="Ribonuclease S-7"
FT                   /id="PRO_0000030983"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   ACT_SITE        116
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10045"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc) asparagine; alternate"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine; alternate"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc) asparagine; alternate"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine; alternate"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   CARBOHYD        126
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        172
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:10469125"
FT   DISULFID        75..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        183..209
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   226 AA;  25470 MW;  75062DEAA6172714 CRC64;
     MGITGMIYIV TMVFSLIVLI LSSSTVGYDY FQFTQQYQPA VCNSKPTPCK DPPDKLFTVH
     GLWPSNLNGP HPENCTNATV NPHRIKNIQA QLKIIWPNVL DRTNHVGFWN KQWIKHGSCG
     YPAIMNDTHY FQTVINMYIT QKQNVSEILS KAKIEPLGIQ RPLVHIENAI RNSTNNKKPK
     FKCQKNSGVT ELVEVGLCSD GSLTQFRNCP HPPPGSPYLC PADVKY
 
 
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