RNAS_ASPGI
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 03-AUG-2022, entry version 120.
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}.
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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 PRIDE; 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:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0033902; F:rRNA endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:2000766; P:negative regulation of cytoplasmic translation; IDA:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
DR InterPro; IPR004025; Fun_ribotoxin.
DR InterPro; IPR000026; Gua-sp_ribonuclease_N1/T1/U2.
DR InterPro; IPR016191; Ribonuclease/ribotoxin.
DR PIRSF; PIRSF037430; RNase_U2; 1.
DR PRINTS; PR01704; FUNRIBOTOXIN.
DR SUPFAM; SSF53933; SSF53933; 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
