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O80323 (RNS3_PYRPY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ribonuclease S-3

EC=3.1.27.1
Alternative name(s):
S3-RNase
OrganismPyrus pyrifolia (Chinese pear) (Pyrus serotina)
Taxonomic identifier3767 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsfabidsRosalesRosaceaeAmygdaloideaeMaleaePyrus

Protein attributes

Sequence length222 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species, self-incompatibility is controlled by the single, multiallelic locus S.

Catalytic activity

Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides with 2',3'-cyclic phosphate intermediates.

Post-translational modification

N-linked core structure at Asn-138 contains xylose.

Sequence similarities

Belongs to the RNase T2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Ref.2
Chain23 – 222200Ribonuclease S-3
PRO_0000030979

Sites

Active site551
Active site1061
Active site1091
Active site1101

Amino acid modifications

Glycosylation401N-linked (GlcNAc...) Ref.3
Glycosylation1381N-linked (GlcNAc...) Ref.3
Disulfide bond37 ↔ 44
Disulfide bond70 ↔ 113
Disulfide bond177 ↔ 215
Disulfide bond192 ↔ 203

Secondary structure

.................................... 222
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O80323 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C3B3A6FEB53D91C1

FASTA22225,747
        10         20         30         40         50         60 
MVHVVMMVFL LIVLILCSST VGYDYFQFTQ QYQLAVCNSN RTLCKDPPDK LFTVHGLWPS 

        70         80         90        100        110        120 
NMVGPDPSKC PIKNIRKREK LLEHQLEIIW PNVFDRTKNN LFWDKEWMKH GSCGYPTIDN 

       130        140        150        160        170        180 
ENHYFETVIK MYISKKQNVS RILSKAKIEP DGKKRALLDI ENAIRNGADN KKPKLKCQKK 

       190        200        210        220 
GTTTELVEIT LCSDKSGEHF IDCPHPFEPI SPHYCPTNNI KY 

« Hide

References

[1]"Primary structural features of rosaceous S-RNases associated with gametophytic self-incompatibility."
Ishimizu T., Shinkawa T., Sakiyama F., Norioka S.
Plant Mol. Biol. 37:931-941(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: cv. Hosui.
Tissue: Style.
[2]"Identification and characterization of stylar glycoproteins associated with self-incompatibility genes of Japanese pear, Pyrus serotina Rehd."
Sassa H., Hirano H., Ikehashi H.
Mol. Gen. Genet. 241:17-25(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 23-36.
[3]"Presence of asparagine-linked N-acetylglucosamine and chitobiose in Pyrus pyrifolia S-RNases associated with gametophytic self-incompatibility."
Ishimizu T., Mitsukami Y., Shinkawa T., Natsuka S., Hase S., Miyagi M., Sakiyama F., Norioka S.
Eur. J. Biochem. 263:624-634(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-40 AND ASN-138, STRUCTURE OF CARBOHYDRATES.
Strain: cv. Hosui.
Tissue: Style.
[4]"Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility."
Matsuura T., Sakai H., Unno M., Ida K., Sato M., Sakiyama F., Norioka S.
J. Biol. Chem. 276:45261-45269(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB002140 mRNA. Translation: BAA32413.1.
PIRS39930.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IQQX-ray1.50A23-222[»]
ProteinModelPortalO80323.
SMRO80323. Positions 23-222.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.730.10. 1 hit.
InterProIPR001568. RNase_T2-like.
IPR018188. RNase_T2_AS.
[Graphical view]
PANTHERPTHR11240. PTHR11240. 1 hit.
PfamPF00445. Ribonuclease_T2. 1 hit.
[Graphical view]
SUPFAMSSF55895. RNase_T2. 1 hit.
PROSITEPS00530. RNASE_T2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO80323.

Entry information

Entry nameRNS3_PYRPY
AccessionPrimary (citable) accession number: O80323
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1998
Last modified: April 3, 2013
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families