(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 104.
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=RNA + H(2)O = an (RNA fragment)-3'-nucleoside-3'-phosphate + a
CC         5'-hydroxy-ribonucleotide-3'-(RNA fragment).; EC=4.6.1.19;
CC         Evidence={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}.
DR   EMBL; AE016816; AAS51382.1; -; Genomic_DNA.
DR   RefSeq; NP_983558.1; NM_208911.1.
DR   STRING; 33169.AAS51382; -.
DR   EnsemblFungi; AAS51382; AAS51382; AGOS_ACR156W.
DR   GeneID; 4619690; -.
DR   KEGG; ago:AGOS_ACR156W; -.
DR   InParanoid; Q75BW5; -.
DR   KO; K01166; -.
DR   OMA; EDTCCFI; -.
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:0016829; F:lyase activity; IEA:UniProtKB-KW.
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;
DR   PRODOM; Q75BW5.
DR   SWISS-2DPAGE; Q75BW5.
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
//

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