Q02933 · RNY1_YEAST
- ProteinRibonuclease T2-like
- GeneRNY1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids434 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Rnase which modulates cell survival under stress conditions. Released from the vacuole to the cytoplasm during stress to promote tRNA and rRNA cleavage and to activate separately a downstream pathway that promotes cell death. Involved in cell size, vacuolar morphology and growth at high temperatures and high salt concentration.
Miscellaneous
Present with 504 molecules/cell in log phase SD medium.
Catalytic activity
- a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H+
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 87 | |||||
Sequence: H | ||||||
Active site | 156 | |||||
Sequence: E | ||||||
Active site | 160 | |||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | fungal-type vacuole | |
Cellular Component | vacuolar lumen | |
Cellular Component | vacuole | |
Molecular Function | ribonuclease T2 activity | |
Molecular Function | RNA binding | |
Molecular Function | RNA endonuclease activity | |
Biological Process | apoptotic process | |
Biological Process | cell morphogenesis | |
Biological Process | mRNA catabolic process | |
Biological Process | RNA catabolic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonuclease T2-like
- EC number
- Short namesRNase T2-like
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ02933
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Is released from the vacuole to the cytoplasm during stress conditions like oxidative stress or stationary phase stress.
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 87 | Impairs cytosolic tRNA-cleaving activity; when associated with F-160. | ||||
Sequence: H → F | ||||||
Mutagenesis | 160 | Impairs cytosolic tRNA-cleaving activity; when associated with F-87. | ||||
Sequence: H → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 7 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MLLKNLHSLLQLPIFSNG | ||||||
Chain | PRO_0000042717 | 19-434 | Ribonuclease T2-like | |||
Sequence: ADKGIEPNCPINIPLSCSNKTDIDNSCCFEYPGGIFLQTQFWNYFPSKNDLNETELVKELGPLDSFTIHGLWPDNCHGGYQQFCNRSLQIDDVYYLLHDKKFNNNDTSLQISGEKLLEYLDLYWKSNNGNHESLWIHEFNKHGTCISTIRPECYTEWGANSVDRKRAVYDYFRITYNLFKKLDTFSTLEKNNIVPSVDNSYSLEQIEAALSKEFEGKKVFIGCDRHNSLNEVWYYNHLKGSLLSEMFVPMDSLAIRTNCKKDGIKFFPKGYVPTFRRRPNKGARYRGVVRLSNINNGDQMQGFLIKNGHWMSQGTPANYELIKSPYGNYYLRTNQGFCDIISSSSNELVCKFRNIKDAGQFDFDPTKGGDGYIGYSGNYNWGGDTYPRRRNQSPIFSVDDEQNSKKYKFKLKFIKN | ||||||
Disulfide bond | 27↔46 | |||||
Sequence: CPINIPLSCSNKTDIDNSCC | ||||||
Disulfide bond | 35↔94 | |||||
Sequence: CSNKTDIDNSCCFEYPGGIFLQTQFWNYFPSKNDLNETELVKELGPLDSFTIHGLWPDNC | ||||||
Glycosylation | 37 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 45↔171 | |||||
Sequence: CCFEYPGGIFLQTQFWNYFPSKNDLNETELVKELGPLDSFTIHGLWPDNCHGGYQQFCNRSLQIDDVYYLLHDKKFNNNDTSLQISGEKLLEYLDLYWKSNNGNHESLWIHEFNKHGTCISTIRPEC | ||||||
Glycosylation | 70 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 102↔163 | |||||
Sequence: CNRSLQIDDVYYLLHDKKFNNNDTSLQISGEKLLEYLDLYWKSNNGNHESLWIHEFNKHGTC | ||||||
Glycosylation | 103 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 123 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 241↔277 | |||||
Sequence: CDRHNSLNEVWYYNHLKGSLLSEMFVPMDSLAIRTNC |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Up-regulated by heat shock and osmotic stress.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length434
- Mass (Da)50,171
- Last updated1996-11-01 v1
- Checksum0BBE8B3C5C7351E1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U43503 EMBL· GenBank· DDBJ | AAB68239.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY692990 EMBL· GenBank· DDBJ | AAT93009.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006949 EMBL· GenBank· DDBJ | DAA11310.1 EMBL· GenBank· DDBJ | Genomic DNA |