RNY1_EMENI
ID RNY1_EMENI Reviewed; 417 AA.
AC Q5B3K6; C8V9U6;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Ribonuclease T2-like;
DE Short=RNase T2-like;
DE EC=4.6.1.19;
DE Flags: Precursor;
GN Name=rny1; ORFNames=AN4874;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000084; EAA60952.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF76577.1; -; Genomic_DNA.
DR RefSeq; XP_662478.1; XM_657386.1.
DR AlphaFoldDB; Q5B3K6; -.
DR SMR; Q5B3K6; -.
DR STRING; 227321.Q5B3K6; -.
DR PRIDE; Q5B3K6; -.
DR EnsemblFungi; CBF76577; CBF76577; ANIA_04874.
DR EnsemblFungi; EAA60952; EAA60952; AN4874.2.
DR GeneID; 2872672; -.
DR KEGG; ani:AN4874.2; -.
DR VEuPathDB; FungiDB:AN4874; -.
DR eggNOG; KOG1642; Eukaryota.
DR HOGENOM; CLU_037966_0_1_1; -.
DR InParanoid; Q5B3K6; -.
DR OMA; QLSCHNT; -.
DR OrthoDB; 994722at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..417
FT /note="Ribonuclease T2-like"
FT /id="PRO_0000043255"
FT REGION 274..296
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 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 45..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 229..264
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 46091 MW; A351825D40273352 CRC64;
MSSISGFLGA IPGAQQILQT MAGSLGLAPL SHPEIASSGS TFQQCGKLEL SCQTSYHGQD
TCCFNYPGGQ MLQTQFWDAD PAVGPENSWT IHGLWPDHCN GGFDQFCDSH RKYSNISLIL
IDAGRRDLLD EMSTYWKDYR GDDPNLWEHE WNKHGTCVST LETHCYSEYY PQQEVVDYFD
KTVELFHDLP TYMTLANAGI VPSYTQTYTR HEVEDALSKA HGATVTVRCR SQRLQEVWYF
FNVEGPLQTG KFVPSEPDGQ TSNCPAKGII YQPKTPNKDP GHGHEPTKTR HPHGPTGAPF
IGKGNLVVST MGQQRGCIIG RGTWYSSGTC ADFRAKRASG DTFTLSSRKG PCAFKDDIFT
CGSYISSPAE FSAEDGKLSY HGNTTFFADK APKGKVQSDI FVSEADHPIE LSIAWRG
