RNY1_YARLI
ID RNY1_YARLI Reviewed; 406 AA.
AC Q6CAV7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Ribonuclease T2-like;
DE Short=RNase T2-like;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNY1; OrderedLocusNames=YALI0C23991g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382129; CAG82527.1; -; Genomic_DNA.
DR RefSeq; XP_502205.1; XM_502205.1.
DR AlphaFoldDB; Q6CAV7; -.
DR SMR; Q6CAV7; -.
DR STRING; 4952.CAG82527; -.
DR EnsemblFungi; CAG82527; CAG82527; YALI0_C23991g.
DR GeneID; 2909604; -.
DR KEGG; yli:YALI0C23991g; -.
DR VEuPathDB; FungiDB:YALI0_C23991g; -.
DR HOGENOM; CLU_037966_0_1_1; -.
DR InParanoid; Q6CAV7; -.
DR OMA; QLSCHNT; -.
DR Proteomes; UP000001300; Chromosome C.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central.
DR GO; GO:0033897; F:ribonuclease T2 activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..406
FT /note="Ribonuclease T2-like"
FT /id="PRO_0000043257"
FT REGION 268..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 92
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /evidence="ECO:0000250"
FT ACT_SITE 154
FT /evidence="ECO:0000250"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..63
FT /evidence="ECO:0000250"
FT DISULFID 52..99
FT /evidence="ECO:0000250"
FT DISULFID 62..165
FT /evidence="ECO:0000250"
FT DISULFID 107..157
FT /evidence="ECO:0000250"
FT DISULFID 231..265
FT /evidence="ECO:0000250"
SQ SEQUENCE 406 AA; 42796 MW; F4231091A6828938 CRC64;
MQFSLATIAT VAAAVSALVC PYTKRDAVAA FTSPPLSSAD HKSCPADTPV SCSSGAGSAD
LCCTESPGGV LVLTQFWDWT PAIGPDDLFT LHGLWPDNCD GSYAQFCDKS MEVQSVAAVL
QQLGETELLD KMNKIWIPNR GSTDSFWTHE WNKHATCMST LKDKCYSSDA PQYQSLADWA
HTVVNVFETV NTYKFLEAAG ITPDSSKTYA KTDFLNALNS NFDGKQVHIS CKSGYISEVW
YYFHLKGSVV SGQYLPIDDI GSSSCPDQIK FPPKDGSGGT PPPTDPSDPP TGGSKGFINI
SGQSGCLISN GNWYTSGTCA TYTLGESQYG GVTLTSSKGP CDVVNGKFSC ASGNNAGQFT
QDGSNIVYGG KSDWSAPSVP SGSQQVGVSP GSAGGSVSFN LVFAAK
