RNY1_CANGA
ID RNY1_CANGA Reviewed; 433 AA.
AC Q6FP42;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Ribonuclease T2-like;
DE Short=RNase T2-like;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNY1; OrderedLocusNames=CAGL0J06820g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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:PRU10045, ECO:0000255|PROSITE-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; CR380956; CAG60953.1; -; Genomic_DNA.
DR RefSeq; XP_448002.1; XM_448002.1.
DR AlphaFoldDB; Q6FP42; -.
DR SMR; Q6FP42; -.
DR STRING; 5478.XP_448002.1; -.
DR EnsemblFungi; CAG60953; CAG60953; CAGL0J06820g.
DR GeneID; 2889620; -.
DR KEGG; cgr:CAGL0J06820g; -.
DR CGD; CAL0133378; CAGL0J06820g.
DR VEuPathDB; FungiDB:CAGL0J06820g; -.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_037966_0_1_1; -.
DR InParanoid; Q6FP42; -.
DR OMA; LWIHEFN; -.
DR Proteomes; UP000002428; Chromosome J.
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; IPR018188; RNase_T2_His_AS_1.
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; PS00530; RNASE_T2_1; 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..?
FT /evidence="ECO:0000255"
FT CHAIN ?..433
FT /note="Ribonuclease T2-like"
FT /id="PRO_0000043253"
FT ACT_SITE 88
FT /evidence="ECO:0000250"
FT ACT_SITE 156
FT /evidence="ECO:0000250"
FT ACT_SITE 160
FT /evidence="ECO:0000250"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 28..47
FT /evidence="ECO:0000250"
FT DISULFID 36..95
FT /evidence="ECO:0000250"
FT DISULFID 46..171
FT /evidence="ECO:0000250"
FT DISULFID 103..163
FT /evidence="ECO:0000250"
FT DISULFID 247..283
FT /evidence="ECO:0000250"
SQ SEQUENCE 433 AA; 49674 MW; 0D9C24B324520463 CRC64;
MILASVLKAF QGLQTGLQHS YQDGSPSCPI NLPLSCGNET AISDLCCFEY PGGILLMTQF
WNYAPSKPNL NRTELEEELG PVDSFTIHGL WPDDCMGGYP QFCKRDLFID DVDYLLKSDA
FNNDDTLPIQ GEELLNNLNK YWKSNNGNHE SLWIHEYNKH GTCLSTLQPQ CYSRWNPTTS
QKGPKYYKKK AVYDYFRISY DLFQKLNTYE MLAKHNITPS NDTSYTKSEI LSALSSEFQG
TQAHINCNSQ NALTEVWYYH QLNGSILNED FIPLDPLRSM SRCKDQGIKY YPKGYQRRDN
RGPNKKPISR GTIRISQYGG FLIKTGRWMK RGTPANFELI ESKYGNYLLK SRMGYCTVHN
DKSQLDCSSR SPDYATQFDY NEEKGILGYS GSFEWGAESA PKNGRTSRSV VFAVSNEKNS
NLKYKFQLKF NRK
