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P67876 (RNMG_ASPRE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease mitogillin

EC=3.1.27.-
Alternative name(s):
Restrictocin
Gene names
Name:ret
OrganismAspergillus restrictus
Taxonomic identifier5064 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length176 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This purine-specific ribonuclease cleaves 28S RNA in eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor activity.

Subcellular location

Secreted.

Sequence similarities

Belongs to the ribonuclease U2 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
Nuclease
Protein synthesis inhibitor
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processnegative regulation of translation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

endoribonuclease activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.4
Chain28 – 176149Ribonuclease mitogillin
PRO_0000030838

Sites

Active site761
Active site1221Proton acceptor
Active site1631Proton donor

Amino acid modifications

Disulfide bond32 ↔ 174
Disulfide bond102 ↔ 158

Experimental info

Sequence conflict521S → N in AAA32707. Ref.3
Sequence conflict1421D → N AA sequence Ref.4

Secondary structure

............................ 176
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P67876 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: AAD431C57939E42C

FASTA17619,595
        10         20         30         40         50         60 
MVAIKNLFLL AATAVSVLAA PSPLDARATW TCINQQLNPK TNKWEDKRLL YSQAKAESNS 

        70         80         90        100        110        120 
HHAPLSDGKT GSSYPHWFTN GYDGNGKLIK GRTPIKFGKA DCDRPPKHSQ NGMGKDDHYL 

       130        140        150        160        170 
LEFPTFPDGH DYKFDSKKPK EDPGPARVIY TYPNKVFCGI VAHQRGNQGD LRLCSH 

« Hide

References

[1]"Isolation and nucleotide sequence of the Aspergillus restrictus gene coding for the ribonucleolytic toxin restrictocin and its expression in Aspergillus nidulans: the leader sequence protects producing strains from suicide."
Lamy B., Davies J.
Nucleic Acids Res. 19:1001-1006(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 34475 / NRRL 2869.
[2]"Secretion of a potential virulence factor, a fungal ribonucleotoxin, during human aspergillosis infections."
Lamy B., Moutaouakil M., Latge J.P., Davies J.
Mol. Microbiol. 5:1811-1815(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 34475 / NRRL 2869.
[3]"Regulation and sequence of the restrictocin gene of Aspergillus restrictus."
Yang R., Kenealy W.R.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Strain: ATCC 34475 / NRRL 2869.
[4]"Complete amino acid sequence of the Aspergillus cytotoxin mitogillin."
Fernandez-Luna J.L., Lopez-Otin C., Soriano F., Mendez E.
Biochemistry 24:861-867(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 28-176.
[5]"Insights into specificity of cleavage and mechanism of cell entry from the crystal structure of the highly specific Aspergillus ribotoxin, restrictocin."
Yang X., Moffat K.
Structure 4:837-852(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-176.
[6]"Crystal structures of restrictocin-inhibitor complexes with implications for RNA recognition and base flipping."
Yang X., Gerczei T., Glover L.T., Correll C.C.
Nat. Struct. Biol. 8:968-973(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 28-176.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56176 Genomic DNA. Translation: CAA39637.1.
M55508 mRNA. Translation: AAA32706.1.
M65257 Genomic DNA. Translation: AAA32707.1.
PIRNRASMR. S22294.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQZX-ray1.70A/B28-176[»]
1JBRX-ray2.15A/B28-176[»]
1JBSX-ray1.97A/B28-176[»]
1JBTX-ray2.70A/B28-176[»]
ProteinModelPortalP67876.
SMRP67876. Positions 28-176.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

Allergome3050. Asp r 1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFPIRSF037430. RNase_U2. 1 hit.
PRINTSPR01704. FUNRIBOTOXIN.
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP67876.

Entry information

Entry nameRNMG_ASPRE
AccessionPrimary (citable) accession number: P67876
Secondary accession number(s): P04389, P19792
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: October 11, 2004
Last modified: April 16, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references