RNY1_KLULA
ID RNY1_KLULA Reviewed; 425 AA.
AC Q6CRT6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Ribonuclease T2-like;
DE Short=RNase T2-like;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNY1; OrderedLocusNames=KLLA0D06567g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: Rnase which modulates cell survival under stress conditions.
CC Released from the vacuole to the cytoplasm during stress to promote
CC tRNA and rRNA cleavage and to activate separately a downstream pathway
CC that promotes cell death. Involved in cell size, vacuolar morphology
CC and growth at high temperatures and high salt concentration (By
CC similarity). {ECO:0000250}.
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:PRU10046};
CC -!- SUBCELLULAR LOCATION: Vacuole lumen. Cytoplasm. Note=Is released from
CC the vacuole to the cytoplasm during stress conditions like oxidative
CC stress or stationary phase stress. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNase T2 family. {ECO:0000305}.
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DR EMBL; CR382124; CAH00449.1; -; Genomic_DNA.
DR RefSeq; XP_453353.1; XM_453353.1.
DR AlphaFoldDB; Q6CRT6; -.
DR SMR; Q6CRT6; -.
DR STRING; 28985.XP_453353.1; -.
DR EnsemblFungi; CAH00449; CAH00449; KLLA0_D06567g.
DR GeneID; 2893049; -.
DR KEGG; kla:KLLA0_D06567g; -.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_037966_0_1_1; -.
DR InParanoid; Q6CRT6; -.
DR OMA; LWIHEFN; -.
DR Proteomes; UP000000598; Chromosome D.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IEA:EnsemblFungi.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:EnsemblFungi.
DR GO; GO:0000902; P:cell morphogenesis; IEA:EnsemblFungi.
DR GO; GO:0006401; P:RNA catabolic process; IEA:EnsemblFungi.
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; IPR033130; RNase_T2_His_AS_2.
DR PANTHER; PTHR11240; PTHR11240; 1.
DR Pfam; PF00445; Ribonuclease_T2; 1.
DR SUPFAM; SSF55895; SSF55895; 1.
DR PROSITE; PS00531; RNASE_T2_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase;
KW Nuclease; Reference proteome; Signal; Vacuole.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..425
FT /note="Ribonuclease T2-like"
FT /id="PRO_0000043256"
FT ACT_SITE 92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 160
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..51
FT /evidence="ECO:0000250"
FT DISULFID 40..99
FT /evidence="ECO:0000250"
FT DISULFID 50..175
FT /evidence="ECO:0000250"
FT DISULFID 107..167
FT /evidence="ECO:0000250"
FT DISULFID 245..281
FT /evidence="ECO:0000250"
SQ SEQUENCE 425 AA; 48137 MW; E8372E5AB392B319 CRC64;
MLLNKGLLAS LLAYTTTAFD LQHIFYKEQY SCPISLPASC SNNTEIKDSC CFEFPGGIML
QTQFWDYIPP KGVSDPDELV RHLGPLDSFT NHGLWPDNCD GTYAQFCNRE SNIDDVWHLL
NDDQFNGRDD LPINGTDLLE TMDMYWKSNT GDDESLWVHE YNKHGTCIRT LYPDCYKKWG
VAGNSKKQAV YDYFRIAMKL FHDKDTYQTL KSAGIEPSVE KSYTKLEISN ALKEGHSGEV
VHFLCDRHGS LNQIWYFHSL KGSLLGEKFV PISALPKGSN CPDDNIKWYP KGHVPSSYRP
PNGNHPGTRG VVRIGNGKGF LIKNGHWYLK GTPANFFLIE APFGNYYLKT RMGYCGIDNS
NKVLACNKNV AQAAQFEYDA KKGYIGYNGA YDWYATKYPR GNQQAPVYAG SNDDGYNFQL
KFVKA
