RNY1_ASHGO
ID RNY1_ASHGO Reviewed; 292 AA.
AC Q75BW5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Ribonuclease T2-like;
DE Short=RNase T2-like;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNY1; OrderedLocusNames=ACR156W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016816; AAS51382.1; -; Genomic_DNA.
DR RefSeq; NP_983558.1; NM_208911.1.
DR AlphaFoldDB; Q75BW5; -.
DR SMR; Q75BW5; -.
DR STRING; 33169.AAS51382; -.
DR EnsemblFungi; AAS51382; AAS51382; AGOS_ACR156W.
DR GeneID; 4619690; -.
DR KEGG; ago:AGOS_ACR156W; -.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_037966_1_0_1; -.
DR InParanoid; Q75BW5; -.
DR OMA; WPIHNDG; -.
DR Proteomes; UP000000591; Chromosome III.
DR GO; GO:0005829; C:cytosol; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
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:0006915; P:apoptotic process; IEA:EnsemblFungi.
DR GO; GO:0000902; P:cell morphogenesis; IEA:EnsemblFungi.
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; 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..23
FT /evidence="ECO:0000255"
FT CHAIN 24..292
FT /note="Ribonuclease T2-like"
FT /id="PRO_0000042716"
FT ACT_SITE 96
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 162
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 42..61
FT /evidence="ECO:0000250"
FT DISULFID 50..103
FT /evidence="ECO:0000250"
FT DISULFID 60..177
FT /evidence="ECO:0000250"
FT DISULFID 111..169
FT /evidence="ECO:0000250"
FT DISULFID 246..280
FT /evidence="ECO:0000250"
SQ SEQUENCE 292 AA; 33434 MW; 42EB4F6AE49980B4 CRC64;
MAKTASAMLF LYLLLSRCLL SHAFQEFITK FPMPMMYNFP SCSSTIPSTC RNETAIADTC
CFEYPGGLIL HSQFWNAPYR KRSYRDFGPD DSFTIHGLWN DRCDGSWDQF CRRGSSIRSV
VDILSKDSLN RGGLPITGKA LLRQMSMYWK GDRGDENLWV HEYNKHGLCL NTLRPECYQR
WGSVASAEDQ AIYDYFRIAM NLHLKIDAYH ALSRQGIKPR CDAPYDAVRM QNALADDFGR
EVQMQCTGNR LTGVTYYYLL RGGILSENFQ PVDPTQSSSC RGKIYWIPKS GC
