RNMG_ASPRE
ID RNMG_ASPRE Reviewed; 176 AA.
AC P67876; P04389; P19792;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Ribonuclease mitogillin;
DE EC=3.1.27.-;
DE AltName: Full=Restrictocin;
DE Flags: Precursor;
GN Name=ret;
OS Aspergillus restrictus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Aspergillus.
OX NCBI_TaxID=5064;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34475 / NRRL 2869;
RX PubMed=2020539; DOI=10.1093/nar/19.5.1001;
RA Lamy B., Davies J.;
RT "Isolation and nucleotide sequence of the Aspergillus restrictus gene
RT coding for the ribonucleolytic toxin restrictocin and its expression in
RT Aspergillus nidulans: the leader sequence protects producing strains from
RT suicide.";
RL Nucleic Acids Res. 19:1001-1006(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 34475 / NRRL 2869;
RX PubMed=1943712; DOI=10.1111/j.1365-2958.1991.tb01930.x;
RA Lamy B., Moutaouakil M., Latge J.P., Davies J.;
RT "Secretion of a potential virulence factor, a fungal ribonucleotoxin,
RT during human aspergillosis infections.";
RL Mol. Microbiol. 5:1811-1815(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=ATCC 34475 / NRRL 2869;
RA Yang R., Kenealy W.R.;
RT "Regulation and sequence of the restrictocin gene of Aspergillus
RT restrictus.";
RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 28-176.
RX PubMed=3994994; DOI=10.1021/bi00325a008;
RA Fernandez-Luna J.L., Lopez-Otin C., Soriano F., Mendez E.;
RT "Complete amino acid sequence of the Aspergillus cytotoxin mitogillin.";
RL Biochemistry 24:861-867(1985).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-176.
RX PubMed=8805570; DOI=10.1016/s0969-2126(96)00090-1;
RA Yang X., Moffat K.;
RT "Insights into specificity of cleavage and mechanism of cell entry from the
RT crystal structure of the highly specific Aspergillus ribotoxin,
RT restrictocin.";
RL Structure 4:837-852(1996).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 28-176.
RX PubMed=11685244; DOI=10.1038/nsb1101-968;
RA Yang X., Gerczei T., Glover L.T., Correll C.C.;
RT "Crystal structures of restrictocin-inhibitor complexes with implications
RT for RNA recognition and base flipping.";
RL Nat. Struct. Biol. 8:968-973(2001).
CC -!- FUNCTION: This purine-specific ribonuclease cleaves 28S RNA in
CC eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor
CC activity.
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; X56176; CAA39637.1; -; Genomic_DNA.
DR EMBL; M55508; AAA32706.1; -; mRNA.
DR EMBL; M65257; AAA32707.1; -; Genomic_DNA.
DR PIR; S22294; NRASMR.
DR PDB; 1AQZ; X-ray; 1.70 A; A/B=28-176.
DR PDB; 1JBR; X-ray; 2.15 A; A/B=28-176.
DR PDB; 1JBS; X-ray; 1.97 A; A/B=28-176.
DR PDB; 1JBT; X-ray; 2.70 A; A/B=28-176.
DR PDBsum; 1AQZ; -.
DR PDBsum; 1JBR; -.
DR PDBsum; 1JBS; -.
DR PDBsum; 1JBT; -.
DR AlphaFoldDB; P67876; -.
DR SMR; P67876; -.
DR Allergome; 3050; Asp r 1.
DR BRENDA; 4.6.1.23; 8124.
DR EvolutionaryTrace; P67876; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
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;
KW Nuclease; Protein synthesis inhibitor; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:3994994"
FT CHAIN 28..176
FT /note="Ribonuclease mitogillin"
FT /id="PRO_0000030838"
FT ACT_SITE 76
FT ACT_SITE 122
FT /note="Proton acceptor"
FT ACT_SITE 163
FT /note="Proton donor"
FT DISULFID 32..174
FT DISULFID 102..158
FT CONFLICT 52
FT /note="S -> N (in Ref. 3; AAA32707)"
FT /evidence="ECO:0000305"
FT CONFLICT 142
FT /note="D -> N (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:1AQZ"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:1JBS"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1AQZ"
FT HELIX 53..62
FT /evidence="ECO:0007829|PDB:1AQZ"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1JBS"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1JBS"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1AQZ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:1JBT"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1AQZ"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1AQZ"
FT TURN 137..140
FT /evidence="ECO:0007829|PDB:1JBT"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:1AQZ"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:1AQZ"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1AQZ"
SQ SEQUENCE 176 AA; 19595 MW; AAD431C57939E42C CRC64;
MVAIKNLFLL AATAVSVLAA PSPLDARATW TCINQQLNPK TNKWEDKRLL YSQAKAESNS
HHAPLSDGKT GSSYPHWFTN GYDGNGKLIK GRTPIKFGKA DCDRPPKHSQ NGMGKDDHYL
LEFPTFPDGH DYKFDSKKPK EDPGPARVIY TYPNKVFCGI VAHQRGNQGD LRLCSH
