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P08056 (RNRH_RHINI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 84. 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 Rh

Short name=RNase Rh
EC=3.1.27.1
OrganismRhizopus niveus
Taxonomic identifier4844 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisEarly diverging fungal lineagesMucoromycotinaMucoralesMucorineaeRhizopodaceaeRhizopus

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This is a base non-specific ribonuclease.

Catalytic activity

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

Sequence similarities

Belongs to the RNase T2 family.

Ontologies

Keywords
   DomainSignal
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMDisulfide bond
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Molecular_functionRNA binding

Inferred from electronic annotation. Source: InterPro

ribonuclease T2 activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Ref.1
Chain17 – 238222Ribonuclease Rh
PRO_0000030964

Sites

Active site621
Active site1211
Active site1251

Amino acid modifications

Disulfide bond19 ↔ 36 Ref.4
Disulfide bond26 ↔ 69 Ref.4
Disulfide bond35 ↔ 136 Ref.4
Disulfide bond79 ↔ 128 Ref.4
Disulfide bond198 ↔ 229 Ref.4

Experimental info

Sequence conflict82 – 843NRA → SLY in BAA00167. Ref.1

Secondary structure

..................................... 238
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08056 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: A3BAB811D24334B3

FASTA23825,635
        10         20         30         40         50         60 
MKAVLALATL IGSTLASSCS STALSCSNSA NSDTCCSPEY GLVVLNMQWA PGYGPDNAFT 

        70         80         90        100        110        120 
LHGLWPDKCS GAYAPSGGCD SNRASSSIAS VIKSKDSSLY NSMLTYWPSN QGNNNVFWSH 

       130        140        150        160        170        180 
EWSKHGTCVS TYDPDCYDNY EEGEDIVDYF QKAMDLRSQY NVYKAFSSNG ITPGGTYTAT 

       190        200        210        220        230 
EMQSAIESYF GAKAKIDCSS GTLSDVALYF YVRGRDTYVI TDALSTGSCS GDVEYPTK 

« Hide

References

[1]"Primary structure of a base non-specific ribonuclease from Rhizopus niveus."
Horiuchi H., Yanai K., Takagi M., Yano K., Wakabayashi E., Sanda A., Mine S., Ohgi K., Irie M.
J. Biochem. 103:408-418(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 17-238.
Strain: NBRC 4810 / AS 3.4817.
[2]"Expression of RNase Rh from Rhizopus niveus in yeast and characterization of the secreted proteins."
Ohgi K., Horiuchi H., Watanabe H., Takagi M., Yano K., Irie M.
J. Biochem. 109:776-785(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
Strain: NBRC 4810 / AS 3.4817.
[3]"Crystal and molecular structure of RNase Rh, a new class of microbial ribonuclease from Rhizopus niveus."
Kurihara H., Mitsui Y., Ohgi K., Irie M., Mizuno H., Nakamura K.T.
FEBS Lett. 306:189-192(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[4]"The crystal structure of ribonuclease Rh from Rhizopus niveus at 2.0-A resolution."
Kurihara H., Nonaka T., Mitsui Y., Ohgi K., Irie M., Nakamura K.T.
J. Mol. Biol. 255:310-320(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00238 Genomic DNA. Translation: BAA00167.1.
D12476 mRNA. Translation: BAA02042.1.
PIRJH0367.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOLX-ray2.00A17-238[»]
ProteinModelPortalP08056.
SMRP08056. Positions 17-238.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.90.730.10. 1 hit.
InterProIPR001568. RNase_T2-like.
IPR018188. RNase_T2_AS.
[Graphical view]
PANTHERPTHR11240. PTHR11240. 1 hit.
PfamPF00445. Ribonuclease_T2. 1 hit.
[Graphical view]
SUPFAMSSF55895. SSF55895. 1 hit.
PROSITEPS00530. RNASE_T2_1. 1 hit.
PS00531. RNASE_T2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP08056.

Entry information

Entry nameRNRH_RHINI
AccessionPrimary (citable) accession number: P08056
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: April 16, 2014
This is version 84 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