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P0CL70 (RNCL_ASPCV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 clavin

EC=3.1.27.-
Gene names
Name:cla
Synonyms:c-sar
OrganismAspergillus clavatus
Taxonomic identifier5057 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length177 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Clavin has the same substrate specificity as 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 componentSecreted
   DomainSignal
   Molecular functionHydrolase
Nuclease
Protein synthesis inhibitor
   PTMDisulfide bond
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 By similarity
Chain28 – 177150Ribonuclease clavin
PRO_0000030835

Sites

Active site771 By similarity
Active site1231Proton acceptor By similarity
Active site1641Proton donor By similarity

Amino acid modifications

Disulfide bond33 ↔ 175 By similarity
Disulfide bond103 ↔ 159 By similarity

Experimental info

Sequence conflict131T → M in AAB42201. Ref.2
Sequence conflict981W → L in AAB42201. Ref.2
Sequence conflict1131G → V in AAB42201. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0CL70 [UniParc].

Last modified April 5, 2011. Version 1.
Checksum: EA602B8555D7022D

FASTA17719,855
        10         20         30         40         50         60 
MVAIKNLVLV ALTAVTALAM PSPLEERAAT WTCMNEQKNP KTNKYENKRL LYNQNNAESN 

        70         80         90        100        110        120 
AHHAPLSDGK TGSSYPHWFT NGYDGDGKIL KGRTPIKWGN SDCDRPPKHS KNGDGKNDHY 

       130        140        150        160        170 
LLEFPTFPDG HQYNFDSKKP KEDPGPARVI YTYPNKVFCG IVAHTRENQG DLKLCSH 

« Hide

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

ProteinModelPortalP0CL70.
SMRP0CL70. Positions 28-177.
ModBaseSearch...
MobiDBSearch...

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...

Entry information

Entry nameRNCL_ASPCV
AccessionPrimary (citable) accession number: P0CL70
Secondary accession number(s): A1C5B3, P49074, P78572
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: April 5, 2011
Last modified: April 16, 2014
This is version 14 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