P93460 · RNS5_PYRPY

Function

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.

Features

Showing features for binding site, active site.

122720406080100120140160180200220
TypeIDPosition(s)Description
Binding site36a 3'-terminal ribonucleotide 3'-phosphate residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI)
Active site60Proton donor
Binding site60a 3'-terminal ribonucleotide 3'-phosphate residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI)
Binding site97-98a 3'-terminal ribonucleotide 3'-phosphate residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI)
Binding site107a 3'-terminal ribonucleotide 3'-phosphate residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI)
Binding site110-111a 3'-terminal ribonucleotide 3'-phosphate residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI)
Active site111
Binding site114-115a 3'-terminal ribonucleotide 3'-phosphate residue (UniProtKB | ChEBI) of RNA (UniProtKB | ChEBI)
Active site115Proton acceptor

GO annotations

all annotationsall molecular functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Molecular Functionribonuclease T2 activity
Molecular FunctionRNA binding
Biological ProcessRNA catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ribonuclease S-5
  • EC number
  • Alternative names
    • S5-RNase

Organism names

  • Taxonomic identifier
  • Strains
    • cv. Kosui
    • cv. Hosui
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Rosales > Rosaceae > Amygdaloideae > Maleae > Pyrus

Accessions

  • Primary accession
    P93460

Subcellular Location

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_000003098128-227Ribonuclease S-5
Disulfide bond42↔49
Glycosylation45N-linked (GlcNAc...) asparagine
Disulfide bond75↔118
Glycosylation143N-linked (GlcNAc...) asparagine
Disulfide bond182↔220
Disulfide bond197↔208

Post-translational modification

N-glycan at Asn-45 consists of disaccharide (GlcNAc-GlcNAc). N-linked core structure at Asn-143 contains xylose.

Keywords

PTM databases

Structure

Family & Domains

Sequence similarities

Belongs to the RNase T2 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    227
  • Mass (Da)
    26,059
  • Last updated
    1997-05-01 v1
  • Checksum
    44BC2A9E9E738FCA
MGITGMVYVVTMVFLLIVLILSSSTVGYDYFQFTQQYQLAVCNSNRTPCKDPPDKLFTVHGLWPSSMAGPDPSNCPIRNIRKREKLLEPQLAIIWPNVFDRTKNKLFWDKEWMKHGTCGYPTIDNENHYFETVIKMYISKKQNVSRILSKAKIEPDGKKRALLDIENAIRNGADNKKPKLKCQKKGTTTELVEITLCSDKSGEHFIDCPHPFEPISPHYCPTNNIKY

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
D88282
EMBL· GenBank· DDBJ
BAA13577.1
EMBL· GenBank· DDBJ
mRNA
AB002141
EMBL· GenBank· DDBJ
BAA32414.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp