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Protein

Antiviral protein 2

Gene

PAP2

Organism
Phytolacca americana (American pokeweed) (Phytolacca decandra)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Inhibits viral infection of plants. Inhibits protein synthesis in both prokaryotes and eukaryotes.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei197 – 1971By 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

Enzyme and pathway databases

BRENDAi3.2.2.22. 4806.

Names & Taxonomyi

Protein namesi
Recommended name:
Antiviral protein 2 (EC:3.2.2.22)
Alternative name(s):
PAP-II
Ribosome-inactivating protein
rRNA N-glycosidase
Gene namesi
Name:PAP2
Synonyms:PAPII
OrganismiPhytolacca americana (American pokeweed) (Phytolacca decandra)
Taxonomic identifieri3527 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesPhytolaccaceaePhytolacca

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 310PRO_0000030784
Signal peptidei1 – 25251 PublicationAdd
BLAST
Chaini26 – ?Antiviral protein 2PRO_0000030783

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi57 ↔ 284By similarity
Disulfide bondi106 ↔ 123By similarity

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Expressed in late summer leaves.

Developmental stagei

Expressed progressively with the aging of the plant.

Structurei

Secondary structure

1
310
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi27 – 315Combined sources
Helixi36 – 5015Combined sources
Beta strandi51 – 577Combined sources
Beta strandi60 – 634Combined sources
Beta strandi66 – 694Combined sources
Beta strandi71 – 799Combined sources
Beta strandi82 – 898Combined sources
Turni90 – 923Combined sources
Beta strandi95 – 1028Combined sources
Beta strandi105 – 1106Combined sources
Helixi118 – 1225Combined sources
Turni123 – 1253Combined sources
Turni132 – 1343Combined sources
Helixi142 – 1498Combined sources
Helixi152 – 1543Combined sources
Helixi159 – 16911Combined sources
Turni177 – 1793Combined sources
Helixi180 – 20021Combined sources
Helixi202 – 2109Combined sources
Turni211 – 2133Combined sources
Helixi222 – 2287Combined sources
Helixi231 – 24010Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi260 – 2623Combined sources
Beta strandi265 – 2673Combined sources
Helixi268 – 2736Combined sources
Beta strandi276 – 2794Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LLNX-ray1.60A26-287[»]
ProteinModelPortaliQ40772.
SMRiQ40772. Positions 26-287.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ40772.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

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.

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

Q40772-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKMKVLEVVG LAISIWLMLT PPASSNIVFD VENATPETYS NFLTSLREAV
60 70 80 90 100
KDKKLTCHGM IMATTLTEQP KYVLVDLKFG SGTFTLAIRR GNLYLEGYSD
110 120 130 140 150
IYNGKCRYRI FKDSESDAQE TVCPGDKSKP GTQNNIPYEK SYKGMESKGG
160 170 180 190 200
ARTKLGLGKI TLKSRMGKIY GKDATDQKQY QKNEAEFLLI AVQMVTEASR
210 220 230 240 250
FKYIENKVKA KFDDANGYQP DPKAISLEKN WDSVSKVIAK VGTSGDSTVT
260 270 280 290 300
LPGDLKDENN KPWTTATMND LKNDIMALLT HVTCKVKSSM FPEIMSYYYR
310
TSISNLGEFE
Length:310
Mass (Da):34,694
Last modified:November 1, 1996 - v1
Checksum:i4D3BB001D7259D9F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78628 mRNA. Translation: CAA55342.1.
PIRiS32610.
S46239.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78628 mRNA. Translation: CAA55342.1.
PIRiS32610.
S46239.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LLNX-ray1.60A26-287[»]
ProteinModelPortaliQ40772.
SMRiQ40772. Positions 26-287.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.2.22. 4806.

Miscellaneous databases

EvolutionaryTraceiQ40772.

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...

Entry informationi

Entry nameiRIP2_PHYAM
AccessioniPrimary (citable) accession number: Q40772
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 8, 2000
Last sequence update: November 1, 1996
Last modified: October 14, 2015
This is version 78 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.