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Protein

Antiviral protein S

Gene
N/A
Organism
Phytolacca americana (American pokeweed) (Phytolacca decandra)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits viral infection of plants, and protein synthesis in vitro.

Catalytic activityi

Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei175 – 1751By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein synthesis inhibitor, Toxin

Keywords - Biological processi

Antiviral defense, Plant defense

Names & Taxonomyi

Protein namesi
Recommended name:
Antiviral protein S (EC:3.2.2.22)
Alternative name(s):
PAP-S
Ribosome-inactivating protein
rRNA N-glycosidase
OrganismiPhytolacca americana (American pokeweed) (Phytolacca decandra)
Taxonomic identifieri3527 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesPhytolaccaceaePhytolacca

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261Antiviral protein SPRO_0000221415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 2581 Publication
Disulfide bondi84 ↔ 1051 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
261
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi13 – 2715Combined sources
Beta strandi34 – 363Combined sources
Beta strandi37 – 393Combined sources
Beta strandi49 – 557Combined sources
Beta strandi61 – 677Combined sources
Turni68 – 703Combined sources
Beta strandi73 – 808Combined sources
Beta strandi83 – 886Combined sources
Helixi95 – 10410Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi116 – 1183Combined sources
Helixi122 – 1298Combined sources
Helixi134 – 1363Combined sources
Helixi141 – 15111Combined sources
Helixi159 – 17214Combined sources
Helixi174 – 1785Combined sources
Helixi180 – 1889Combined sources
Beta strandi190 – 1923Combined sources
Helixi198 – 2058Combined sources
Helixi207 – 2159Combined sources
Helixi218 – 2203Combined sources
Beta strandi221 – 2299Combined sources
Beta strandi235 – 2406Combined sources
Helixi241 – 2444Combined sources
Helixi245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIKX-ray1.80A1-261[»]
1J1QX-ray1.80A1-261[»]
1J1RX-ray1.90A1-261[»]
1J1SX-ray2.00A1-261[»]
ProteinModelPortaliP23339.
SMRiP23339. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23339.

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
[Graphical view]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23339-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
INTITFDAGN ATINKYATFM ESLRNEAKDP SLKCYGIPML PNTNSTIKYL
60 70 80 90 100
LVKLQGASLK TITLMLRRNN LYVMGYSDPY DNKCRYHIFN DIKGTEYSDV
110 120 130 140 150
ENTLCPSSNP RVAKPINYNG LYPTLEKKAG VTSRNEVQLG IQILSSDIGK
160 170 180 190 200
ISGQGSFTEK IEAKFLLVAI QMVSEAARFK YIENQVKTNF NRDFSPNDKV
210 220 230 240 250
LDLEENWGKI STAIHNSKNG ALPKPLELKN ADGTKWIVLR VDEIKPDVGL
260
LNYVNGTCQA T
Length:261
Mass (Da):29,200
Last modified:November 1, 1991 - v1
Checksum:iD88B99962FE8399D
GO

Sequence databases

PIRiJE0401.

Cross-referencesi

Sequence databases

PIRiJE0401.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GIKX-ray1.80A1-261[»]
1J1QX-ray1.80A1-261[»]
1J1RX-ray1.90A1-261[»]
1J1SX-ray2.00A1-261[»]
ProteinModelPortaliP23339.
SMRiP23339. Positions 1-261.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23339.

Family and domain databases

Gene3Di3.40.420.10. 1 hit.
4.10.470.10. 1 hit.
InterProiIPR001574. Ribosome_inactivat_prot.
IPR017988. Ribosome_inactivat_prot_CS.
IPR016138. Ribosome_inactivat_prot_sub1.
IPR016139. Ribosome_inactivat_prot_sub2.
IPR017989. Ribosome_inactivat_prot_subgr.
[Graphical view]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The complete amino acid sequence of antiviral protein from the seeds of pokeweed (Phytolacca americana)."
    Kung S.S., Kimura M., Funatsu G.
    Agric. Biol. Chem. 54:3301-3318(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Seed.

Entry informationi

Entry nameiRIPS_PHYAM
AccessioniPrimary (citable) accession number: P23339
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: December 9, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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.