P00655 (RNAS_ASPGI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease alpha-sarcin
EC=3.1.27.10

Alternative name(s):
rRNA endonuclease

Gene names

Name:

sar

Organism

Aspergillus giganteus

Taxonomic identifier

5060 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Pezizomycotina › leotiomyceta › 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 protein level

General annotation (Comments)

Function	Alpha-sarcin 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.
Catalytic activity	Hydrolysis of the phosphodiester linkage between guanosine and adenosine residues at one specific position in 28S rRNA from rat ribosomes.
Subcellular location	Secreted.
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
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological_process	negative regulation of translation Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred 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 rRNA endonuclease activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 27

27

Ref.3

Chain

28 – 177

150

Ribonuclease alpha-sarcin

PRO_0000030836

Sites

Active site

77

1

Active site

123

1

Proton acceptor

Active site

164

1

Proton donor

Amino acid modifications

Disulfide bond

33 ↔ 175

Disulfide bond

103 ↔ 159

Secondary structure

1

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177

Helix Strand Turn

Details...

Beta strand

30 – 39

10

Turn

40 – 43

4

Beta strand

44 – 53

10

Helix

54 – 60

7

Turn

61 – 63

3

Beta strand

66 – 69

4

Beta strand

71 – 73

3

Beta strand

76 – 78

3

Beta strand

85 – 87

3

Turn

101 – 103

3

Beta strand

111 – 113

3

Beta strand

115 – 117

3

Beta strand

122 – 124

3

Beta strand

134 – 136

3

Beta strand

146 – 151

6

Beta strand

153 – 155

3

Beta strand

158 – 166

9

Turn

167 – 169

3

Beta strand

172 – 174

3

Sequences

	Sequence		Length	Mass (Da)
	P00655 [UniParc]. Last modified March 1, 1992. Version 2. Checksum: 6C711D9482DC9DD1	FASTA	177	19,724
	10 20 30 40 50 60 MVAIKNLVLV ALTAVTALAV PSPLEARAVT WTCLNDQKNP KTNKYETKRL LYNQNKAESN 70 80 90 100 110 120 SHHAPLSDGK TGSSYPHWFT NGYDGDGKLP KGRTPIKFGK SDCDRPPKHS KDGNGKTDHY 130 140 150 160 170 LLEFPTFPDG HDYKFDSKKP KENPGPARVI YTYPNKVFCG IIAHTKENQG ELKLCSH

References

[1]	"Complete nucleotide sequence of cDNA for the cytotoxin alpha sarcin." Oka T., Natori Y., Tanaka S., Tsurugi K., Endo Y. Nucleic Acids Res. 18:1897-1897(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: MDH 18894.
[2]	Wnendt S., Felske H., Henze P.P., Ulbrich N., Stahl U. Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: MDH 18894.
[3]	"The primary structure of the cytotoxin alpha-sarcin." Sacco G., Drickamer K., Wool I.G. J. Biol. Chem. 258:5811-5818(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 28-177.
[4]	"The highly refined solution structure of the cytotoxic ribonuclease alpha-sarcin reveals the structural requirements for substrate recognition and ribonucleolytic activity." Perez-Canadillas J.M., Santoro J., Campos-Olivas R., Lacadena J., Martinez del Pozo A., Gavilanes J.G., Rico M., Bruix M. J. Mol. Biol. 299:1061-1073(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 28-177.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D13704 mRNA. Translation: BAA02863.1.
X60770 Genomic DNA. Translation: CAA43180.1.

PIR

NRASSG. JU0138.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DE3	NMR	-	A	28-177	[»]
1R4Y	NMR	-	A	50-177	[»]

ProteinModelPortal

P00655.

SMR

P00655. 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...

Other

EvolutionaryTrace

P00655.

Entry information

Entry name

RNAS_ASPGI

Accession

Primary (citable) accession number: P00655

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	March 1, 1992
Last modified:	April 3, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program