RNY1A_CANAL
ID RNY1A_CANAL Reviewed; 399 AA.
AC Q5AK94; A0A1D8PNY7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Ribonuclease T2-like 1-A;
DE Short=RNase T2-like A;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNY1-A; OrderedLocusNames=CAALFM_C504400WA;
GN ORFNames=CaO19.11408, CaO19.3926;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(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; CP017627; AOW29848.1; -; Genomic_DNA.
DR RefSeq; XP_721836.2; XM_716743.2.
DR AlphaFoldDB; Q5AK94; -.
DR SMR; Q5AK94; -.
DR STRING; 237561.Q5AK94; -.
DR GeneID; 3636408; -.
DR KEGG; cal:CAALFM_C504400WA; -.
DR CGD; CAL0000196842; RNY11.
DR VEuPathDB; FungiDB:C5_04400W_A; -.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_037966_0_1_1; -.
DR InParanoid; Q5AK94; -.
DR OMA; QLSCHNT; -.
DR OrthoDB; 994722at2759; -.
DR PRO; PR:Q5AK94; -.
DR Proteomes; UP000000559; Chromosome 5.
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; 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..17
FT /evidence="ECO:0000255"
FT CHAIN 18..399
FT /note="Ribonuclease T2-like 1-A"
FT /id="PRO_0000043251"
FT REGION 259..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 24..43
FT /evidence="ECO:0000250"
FT DISULFID 32..79
FT /evidence="ECO:0000250"
FT DISULFID 42..150
FT /evidence="ECO:0000250"
FT DISULFID 87..142
FT /evidence="ECO:0000250"
FT DISULFID 214..249
FT /evidence="ECO:0000250"
SQ SEQUENCE 399 AA; 42733 MW; CBE909B5994F7E03 CRC64;
MLSILSIAAL LIATVQAADF SSSCPIDSPI SCSSNGDTSN SCCYENPGGI ILFTQFWDYN
PASGPADSFT IHSIWNDYCS GGYPQFCDTS LEIDSTGSTI ESIVVDQFGD QTLYDNMNKY
WTDINGNNKK FWAHEFNKHG TCLNTLNPSC YSNYKQNENV YDYYSLVYQL FQKLPTYQWL
VSAGIKPSTT ATYTLSQIQS ALKSKFGAEV YIACDSNNAI NEVWYFYNIK GSILQQNYLP
IDTVSKTNCP SSGIKFPPKG NSGANTLTTK TTGTTTSGSG STSVPATSYI NLTGKSGCLI
SNGKYYTSGT CATYHFNAGS SGNTQITSSK GNCGIDSSNQ FTCSSSTSAT DFQVSGGSIG
YNGNFDWCLG AVTGSGSTAQ TSVKLSDGSC SSFKLTLSS
