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Protein

Ribonuclease mitogillin

Gene

ret

Organism
Aspergillus restrictus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei76 – 761
Active sitei122 – 1221Proton acceptor
Active sitei163 – 1631Proton donor

GO - Molecular functioni

  1. endoribonuclease activity Source: InterPro
  2. RNA binding Source: InterPro

GO - Biological processi

  1. negative regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nuclease, Protein synthesis inhibitor

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease mitogillin (EC:3.1.27.-)
Alternative name(s):
Restrictocin
Gene namesi
Name:ret
OrganismiAspergillus restrictus
Taxonomic identifieri5064 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei3050. Asp r 1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27271 PublicationAdd
BLAST
Chaini28 – 176149Ribonuclease mitogillinPRO_0000030838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 174
Disulfide bondi102 ↔ 158

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
176
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi29 – 357Combined sources
Turni39 – 424Combined sources
Beta strandi46 – 527Combined sources
Helixi53 – 6210Combined sources
Beta strandi65 – 684Combined sources
Beta strandi70 – 723Combined sources
Beta strandi75 – 784Combined sources
Beta strandi84 – 863Combined sources
Helixi100 – 1034Combined sources
Beta strandi118 – 1247Combined sources
Turni137 – 1404Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi157 – 1659Combined sources
Beta strandi171 – 1733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQZX-ray1.70A/B28-176[»]
1JBRX-ray2.15A/B28-176[»]
1JBSX-ray1.97A/B28-176[»]
1JBTX-ray2.70A/B28-176[»]
SMRiP67876. Positions 28-176.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP67876.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease U2 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
PRINTSiPR01704. FUNRIBOTOXIN.
SUPFAMiSSF53933. SSF53933. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P67876-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAIKNLFLL AATAVSVLAA PSPLDARATW TCINQQLNPK TNKWEDKRLL
60 70 80 90 100
YSQAKAESNS HHAPLSDGKT GSSYPHWFTN GYDGNGKLIK GRTPIKFGKA
110 120 130 140 150
DCDRPPKHSQ NGMGKDDHYL LEFPTFPDGH DYKFDSKKPK EDPGPARVIY
160 170
TYPNKVFCGI VAHQRGNQGD LRLCSH
Length:176
Mass (Da):19,595
Last modified:October 10, 2004 - v1
Checksum:iAAD431C57939E42C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521S → N in AAA32707 (Ref. 3) Curated
Sequence conflicti142 – 1421D → N AA sequence (PubMed:3994994).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56176 Genomic DNA. Translation: CAA39637.1.
M55508 mRNA. Translation: AAA32706.1.
M65257 Genomic DNA. Translation: AAA32707.1.
PIRiS22294. NRASMR.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X56176 Genomic DNA. Translation: CAA39637.1.
M55508 mRNA. Translation: AAA32706.1.
M65257 Genomic DNA. Translation: AAA32707.1.
PIRiS22294. NRASMR.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AQZX-ray1.70A/B28-176[»]
1JBRX-ray2.15A/B28-176[»]
1JBSX-ray1.97A/B28-176[»]
1JBTX-ray2.70A/B28-176[»]
SMRiP67876. Positions 28-176.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

Allergomei3050. Asp r 1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP67876.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamiPF00545. Ribonuclease. 1 hit.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
PRINTSiPR01704. FUNRIBOTOXIN.
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

Publicationsi

  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(1990) [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(1990) [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 (APR-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(1984) [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(1995) [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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 28-176.

Entry informationi

Entry nameiRNMG_ASPRE
AccessioniPrimary (citable) accession number: P67876
Secondary accession number(s): P04389, P19792
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 19, 1987
Last sequence update: October 10, 2004
Last modified: March 31, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.