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Protein

Ribonuclease alpha-sarcin

Gene

sar

Organism
Aspergillus giganteus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Hydrolysis of the phosphodiester linkage between guanosine and adenosine residues at one specific position in 28S rRNA from rat ribosomes.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei771
Active sitei123Proton acceptor1
Active sitei164Proton donor1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nuclease, Protein synthesis inhibitor

Enzyme and pathway databases

BRENDAi3.1.27.10. 510.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease alpha-sarcin (EC:3.1.27.10)
Alternative name(s):
rRNA endonuclease
Gene namesi
Name:sar
OrganismiAspergillus giganteus
Taxonomic identifieri5060 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 271 PublicationAdd BLAST27
ChainiPRO_000003083628 – 177Ribonuclease alpha-sarcinAdd BLAST150

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 175
Disulfide bondi103 ↔ 159

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1177
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi30 – 39Combined sources10
Turni40 – 43Combined sources4
Beta strandi44 – 53Combined sources10
Helixi54 – 60Combined sources7
Turni61 – 63Combined sources3
Beta strandi66 – 69Combined sources4
Beta strandi71 – 73Combined sources3
Beta strandi76 – 78Combined sources3
Beta strandi85 – 87Combined sources3
Turni101 – 103Combined sources3
Beta strandi111 – 113Combined sources3
Beta strandi115 – 117Combined sources3
Beta strandi122 – 124Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi146 – 151Combined sources6
Beta strandi153 – 155Combined sources3
Beta strandi158 – 166Combined sources9
Turni167 – 169Combined sources3
Beta strandi172 – 174Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DE3NMR-A28-177[»]
1R4YNMR-A28-177[»]
ProteinModelPortaliP00655.
SMRiP00655.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00655.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribonuclease U2 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1/U2.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
PRINTSiPR01704. FUNRIBOTOXIN.
SUPFAMiSSF53933. SSF53933. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00655-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAIKNLVLV ALTAVTALAV PSPLEARAVT WTCLNDQKNP KTNKYETKRL
60 70 80 90 100
LYNQNKAESN SHHAPLSDGK TGSSYPHWFT NGYDGDGKLP KGRTPIKFGK
110 120 130 140 150
SDCDRPPKHS KDGNGKTDHY LLEFPTFPDG HDYKFDSKKP KENPGPARVI
160 170
YTYPNKVFCG IIAHTKENQG ELKLCSH
Length:177
Mass (Da):19,724
Last modified:March 1, 1992 - v2
Checksum:i6C711D9482DC9DD1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13704 mRNA. Translation: BAA02863.1.
X60770 Genomic DNA. Translation: CAA43180.1.
PIRiJU0138. NRASSG.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13704 mRNA. Translation: BAA02863.1.
X60770 Genomic DNA. Translation: CAA43180.1.
PIRiJU0138. NRASSG.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DE3NMR-A28-177[»]
1R4YNMR-A28-177[»]
ProteinModelPortaliP00655.
SMRiP00655.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.27.10. 510.

Miscellaneous databases

EvolutionaryTraceiP00655.

Family and domain databases

Gene3Di3.10.450.30. 1 hit.
InterProiIPR004025. Fun_ribotoxin.
IPR000026. Gua-sp_ribonuclease_N1/T1/U2.
IPR016191. Ribonuclease/ribotoxin.
[Graphical view]
PIRSFiPIRSF037430. RNase_U2. 1 hit.
PRINTSiPR01704. FUNRIBOTOXIN.
SUPFAMiSSF53933. SSF53933. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRNAS_ASPGI
AccessioniPrimary (citable) accession number: P00655
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 1, 1992
Last modified: November 2, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.