P0CL70 (RNCL_ASPCV) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 9.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ribonuclease clavin EC=3.1.27.- | ||||
| Gene names |
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| Organism | Aspergillus clavatus | ||||
| Taxonomic identifier | 5057 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus![]() |
Protein attributes
| Sequence length | 177 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Clavin has the same substrate-specificity than alpha-sarcin. It is specific for purines in both single- and double-stranded RNA. Its toxic action on eukaryotic cells is the result of cleavage of a single phosphodiester bond in the 60S subunit of ribosomes. Ref.1 |
| Subcellular location | Secreted By similarity. |
| Sequence similarities | Belongs to the ribonuclease U2 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Hydrolase Nuclease Protein synthesis inhibitor |
| PTM | Disulfide bond |
| Gene Ontology (GO) | |
| Biological_process | negative regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysisInferred from electronic annotation. Source: GOC |
| Cellular_component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | RNA binding Inferred from electronic annotation. Source: InterPro endoribonuclease activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | By similarity | ||||||||
| Chain | 28 – 177 | 150 | Ribonuclease clavin | PRO_0000030835 | |||||||
Sites | |||||||||||
| Active site | 77 | 1 | By similarity | ||||||||
| Active site | 123 | 1 | Proton acceptor By similarity | ||||||||
| Active site | 164 | 1 | Proton donor By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 33 ↔ 175 | By similarity | |||||||||
| Disulfide bond | 103 ↔ 159 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 13 | 1 | T → M in AAB42201. Ref.2 | ||||||||
| Sequence conflict | 98 | 1 | W → L in AAB42201. Ref.2 | ||||||||
| Sequence conflict | 113 | 1 | G → V in AAB42201. Ref.2 | ||||||||
Sequences
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References
| [1] | "Clavin, a type-1 ribosome-inactivating protein from Aspergillus clavatus IFO 8605. cDNA isolation, heterologous expression, biochemical and biological characterization of the recombinant protein." Parente D., Raucci G., Celano B., Pacilli A., Zanoni L., Canevari S., Adobati E., Colnaghi M.I., Dosio F., Arpicco S., Cattel L., Mele A., de Santis R. Eur. J. Biochem. 239:272-280(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. Strain: NBRC 8605. |
| [2] | "Characterization of a new ribotoxin gene (c-sar) from Aspergillus clavatus." Huang K.-C., Hwang Y.-Y., Hwu L., Lin A. Toxicon 35:383-392(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BCRC 32114. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U19383 mRNA. Translation: AAC49407.1. U48731 Genomic DNA. Translation: AAB42201.1. |
3D structure databases | |
| ProteinModelPortal | P0CL70. |
| SMR | P0CL70. Positions 28-177. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 3.10.450.30. 1 hit. |
| InterPro | IPR004025. Fun_ribotoxin. IPR000026. Gua-sp_ribonuclease_N1/T1. IPR016191. Ribonuclease/ribotoxin. [Graphical view] |
| Pfam | PF00545. Ribonuclease. 1 hit. [Graphical view] |
| PIRSF | PIRSF037430. RNase_U2. 1 hit. |
| PRINTS | PR01704. FUNRIBOTOXIN. |
| SUPFAM | SSF53933. Ribonuclease/ribotoxin. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RNCL_ASPCV | ||||||||
| Accession | Primary (citable) accession number: P0CL70 Secondary accession number(s): A1C5B3, P49074, P78572 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
