RNY1B_CANAL
ID RNY1B_CANAL Reviewed; 413 AA.
AC Q5AKB1; A0A1D8PNX5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Ribonuclease T2-like 1-B;
DE Short=RNase T2-like B;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=RNY1-B; OrderedLocusNames=CAALFM_C504260WA;
GN ORFNames=CaO19.11391, CaO19.3910;
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; AOW29834.1; -; Genomic_DNA.
DR RefSeq; XP_721820.1; XM_716727.2.
DR AlphaFoldDB; Q5AKB1; -.
DR SMR; Q5AKB1; -.
DR STRING; 237561.Q5AKB1; -.
DR PRIDE; Q5AKB1; -.
DR GeneID; 3636451; -.
DR KEGG; cal:CAALFM_C504260WA; -.
DR CGD; CAL0000201046; orf19.11391.
DR VEuPathDB; FungiDB:C5_04260W_A; -.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_037966_0_1_1; -.
DR InParanoid; Q5AKB1; -.
DR OrthoDB; 994722at2759; -.
DR PRO; PR:Q5AKB1; -.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..413
FT /note="Ribonuclease T2-like 1-B"
FT /id="PRO_0000043252"
FT ACT_SITE 84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT ACT_SITE 151
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10046"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..55
FT /evidence="ECO:0000250"
FT DISULFID 41..91
FT /evidence="ECO:0000250"
FT DISULFID 54..162
FT /evidence="ECO:0000250"
FT DISULFID 99..154
FT /evidence="ECO:0000250"
FT DISULFID 227..262
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 45726 MW; 05DAC88BDFBD1FDA CRC64;
MKYSILAILA HLLTNIKATQ EVFTLSDLPP DSCPIDSPIS CSKNAQELEN VNSCCYESPA
GVILLTQFWD YNPATGPDNL FTQHGLWGNM CSYGYPQFCD PSLEINPNGE IIRSIIVDQF
GDEELYNNMS YSWKDYHGKD SSFWAHEYNK HGTCFSTIKP SCYLSNTPKN QNLYDFFRIA
IGLFNKLPTY DWLAEAGIVP TNSKTYSLSE IQSALNDKFG ANVFIKCDYN HAINEIWYYH
HVKGSLLQHN FLPIDSVAHT NCPSTGIKYP PKGKVAHPTL TTKTTTGTST TIHNPTGIPA
RSYVHLSGKS GCLISNGKWY TSGTCATYHF KKTIDDSNIE IRSSKGICGI NGNEEFTCSR
AVSGGTDFQI KDGKIGYQDK FDWCFGSTTG SGSTAQTSVK LADGSCDSFQ LLI
