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P00652 (RNC2_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 76. 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:
Guanyl-specific ribonuclease C2

Short name=RNase C-2
EC=3.1.27.3
Gene names
ORF Names:ACLA_055300
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length132 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Two-stage endonucleolytic cleavage to nucleoside 3'-phosphates and 3'-phosphooligonucleotides ending in G-P with 2',3'-cyclic phosphate intermediates.

Subcellular location

Secreted.

Sequence similarities

Belongs to the ribonuclease N1/T1 family.

Sequence caution

The sequence EAW13482.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   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

ribonuclease T1 activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.2
Chain27 – 132106Guanyl-specific ribonuclease C2
PRO_0000137369

Sites

Active site661 By similarity
Active site841Proton acceptor By similarity
Active site1181Proton donor By similarity

Amino acid modifications

Disulfide bond28 ↔ 36 By similarity
Disulfide bond32 ↔ 129 By similarity

Experimental info

Sequence conflict531Y → E AA sequence Ref.2
Sequence conflict981S → G AA sequence Ref.2
Sequence conflict1241N → D AA sequence Ref.2
Sequence conflict130 – 1323SGW → Y AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P00652 [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 3E2B1FEEFE0DBF84

FASTA13214,064
        10         20         30         40         50         60 
MLYNKLITIA ALLVPALAAP QGLDVRDCDY TCGSHCYSAS AVSDAQSAGY QLYSAGQSVG 

        70         80         90        100        110        120 
RSRYPHQYRN YEGFNFPVSG NYYEWPILSS GSTYNGGSPG ADRVVFNDND ELAGLITHTG 

       130 
ASGNGFVACS GW 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027048 Genomic DNA. Translation: EAW13482.1. Sequence problems.
PIRNRASTC. A00799.
RefSeqXP_001274908.1. XM_001274907.1.

3D structure databases

ProteinModelPortalP00652.
SMRP00652. Positions 28-130.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4707141.
KEGGact:ACLA_055300.

Phylogenomic databases

eggNOGNOG114265.
HOGENOMHOG000217295.
OrthoDBEOG7XSTSF.

Family and domain databases

Gene3D3.10.450.30. 1 hit.
InterProIPR000026. Gua-sp_ribonuclease_N1/T1.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PfamPF00545. Ribonuclease. 1 hit.
[Graphical view]
SUPFAMSSF53933. SSF53933. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRNC2_ASPCL
AccessionPrimary (citable) accession number: P00652
Secondary accession number(s): A1C9F8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 3, 2007
Last modified: April 16, 2014
This is version 76 of the entry and version 2 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