ID RNAS_ASPGI Reviewed; 177 AA. AC P00655; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-1992, sequence version 2. DT 24-JAN-2024, entry version 126. DE RecName: Full=Ribonuclease alpha-sarcin; DE EC=4.6.1.23 {ECO:0000305}; DE AltName: Full=rRNA endonuclease; DE Flags: Precursor; GN Name=sar; OS Aspergillus giganteus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus. OX NCBI_TaxID=5060; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=MDH 18894; RX PubMed=2336369; DOI=10.1093/nar/18.7.1897; RA Oka T., Natori Y., Tanaka S., Tsurugi K., Endo Y.; RT "Complete nucleotide sequence of cDNA for the cytotoxin alpha sarcin."; RL Nucleic Acids Res. 18:1897-1897(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=MDH 18894; RA Wnendt S., Felske H., Henze P.P., Ulbrich N., Stahl U.; RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 28-177. RX PubMed=6343394; DOI=10.1016/s0021-9258(20)81966-8; RA Sacco G., Drickamer K., Wool I.G.; RT "The primary structure of the cytotoxin alpha-sarcin."; RL J. Biol. Chem. 258:5811-5818(1983). RN [4] RP FUNCTION. RX PubMed=2930482; DOI=10.1042/bj2570723; RA Brigotti M., Rambelli F., Zamboni M., Montanaro L., Sperti S.; RT "Effect of alpha-sarcin and ribosome-inactivating proteins on the RT interaction of elongation factors with ribosomes."; RL Biochem. J. 257:723-727(1989). RN [5] RP STRUCTURE BY NMR OF 28-177. RX PubMed=10843858; DOI=10.1006/jmbi.2000.3813; RA Perez-Canadillas J.M., Santoro J., Campos-Olivas R., Lacadena J., RA Martinez del Pozo A., Gavilanes J.G., Rico M., Bruix M.; RT "The highly refined solution structure of the cytotoxic ribonuclease alpha- RT sarcin reveals the structural requirements for substrate recognition and RT ribonucleolytic activity."; RL J. Mol. Biol. 299:1061-1073(2000). CC -!- FUNCTION: Alpha-sarcin is specific for purines in both single- and CC double-stranded RNA. Its toxic action on eukaryotic cells is the result CC of cleavage of a single phosphodiester bond in the 60S subunit of CC ribosomes (By similarity). Inhibits both the EFl (elongation factor 1)- CC dependent binding of aminoacyl-tRNA and the GTP-dependent binding of CC EF2 (elongation factor 2) to ribosomes (PubMed:2930482). CC {ECO:0000250|UniProtKB:P0CL70, ECO:0000269|PubMed:2930482}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 28S rRNA containing guanosine-adenosine pair + H2O = an [RNA CC fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'- CC [RNA fragment].; EC=4.6.1.23; Evidence={ECO:0000305}; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the ribonuclease U2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D13704; BAA02863.1; -; mRNA. DR EMBL; X60770; CAA43180.1; -; Genomic_DNA. DR PIR; JU0138; NRASSG. DR PDB; 1DE3; NMR; -; A=28-177. DR PDB; 1R4Y; NMR; -; A=28-177. DR PDBsum; 1DE3; -. DR PDBsum; 1R4Y; -. DR AlphaFoldDB; P00655; -. DR BMRB; P00655; -. DR SMR; P00655; -. DR KEGG; ag:BAA02863; -. DR BRENDA; 4.6.1.23; 510. DR EvolutionaryTrace; P00655; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004521; F:RNA endonuclease activity; IDA:UniProtKB. DR GO; GO:0033902; F:rRNA endonuclease activity; IEA:UniProtKB-EC. DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB. DR CDD; cd00606; fungal_RNase; 1. DR Gene3D; 3.10.450.30; Microbial ribonucleases; 1. DR InterPro; IPR004025; Fun_ribotoxin. DR InterPro; IPR016191; Ribonuclease/ribotoxin. DR InterPro; IPR048269; RNase_U2. DR PIRSF; PIRSF037430; RNase_U2; 1. DR PRINTS; PR01704; FUNRIBOTOXIN. DR SUPFAM; SSF53933; Microbial ribonucleases; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase; Lyase; KW Nuclease; Protein synthesis inhibitor; Secreted; Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:6343394" FT CHAIN 28..177 FT /note="Ribonuclease alpha-sarcin" FT /id="PRO_0000030836" FT REGION 86..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 90..118 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 77 FT ACT_SITE 123 FT /note="Proton acceptor" FT ACT_SITE 164 FT /note="Proton donor" FT DISULFID 33..175 FT DISULFID 103..159 FT STRAND 30..39 FT /evidence="ECO:0007829|PDB:1DE3" FT TURN 40..43 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 44..53 FT /evidence="ECO:0007829|PDB:1DE3" FT HELIX 54..60 FT /evidence="ECO:0007829|PDB:1DE3" FT TURN 61..63 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 66..69 FT /evidence="ECO:0007829|PDB:1R4Y" FT STRAND 71..73 FT /evidence="ECO:0007829|PDB:1R4Y" FT STRAND 76..78 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 85..87 FT /evidence="ECO:0007829|PDB:1DE3" FT TURN 101..103 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 111..113 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 115..117 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 122..124 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 134..136 FT /evidence="ECO:0007829|PDB:1R4Y" FT STRAND 146..151 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 153..155 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 158..166 FT /evidence="ECO:0007829|PDB:1DE3" FT TURN 167..169 FT /evidence="ECO:0007829|PDB:1DE3" FT STRAND 172..174 FT /evidence="ECO:0007829|PDB:1DE3" SQ SEQUENCE 177 AA; 19724 MW; 6C711D9482DC9DD1 CRC64; MVAIKNLVLV ALTAVTALAV PSPLEARAVT WTCLNDQKNP KTNKYETKRL LYNQNKAESN SHHAPLSDGK TGSSYPHWFT NGYDGDGKLP KGRTPIKFGK SDCDRPPKHS KDGNGKTDHY LLEFPTFPDG HDYKFDSKKP KENPGPARVI YTYPNKVFCG IIAHTKENQG ELKLCSH //