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Protein

Antiviral protein I

Gene

PAP1

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, 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)DescriptionActionsGraphical viewLength
Active sitei198By similarity1

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 I (EC:3.2.2.22)
Alternative name(s):
PAP-C
PAP-I
Ribosome-inactivating protein
rRNA N-glycosidase
Gene namesi
Name:PAP1
OrganismiPhytolacca americana (American pokeweed) (Phytolacca decandra)
Taxonomic identifieri3527 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesPhytolaccaceaePhytolacca

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 225 PublicationsAdd BLAST22
ChainiPRO_000003078123 – 285Antiviral protein IAdd BLAST263
PropeptideiPRO_0000030782286 – 313Add BLAST28

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi56 ↔ 281
Disulfide bondi107 ↔ 128

Keywords - PTMi

Disulfide bond

Expressioni

Tissue specificityi

Spring leaves and roots.

Structurei

Secondary structure

1313
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi25 – 32Combined sources8
Helixi35 – 49Combined sources15
Beta strandi59 – 61Combined sources3
Beta strandi71 – 77Combined sources7
Helixi79 – 81Combined sources3
Beta strandi83 – 89Combined sources7
Turni90 – 92Combined sources3
Beta strandi95 – 102Combined sources8
Turni103 – 105Combined sources3
Beta strandi106 – 112Combined sources7
Helixi118 – 127Combined sources10
Turni131 – 133Combined sources3
Beta strandi134 – 136Combined sources3
Beta strandi139 – 141Combined sources3
Helixi145 – 152Combined sources8
Helixi157 – 159Combined sources3
Helixi164 – 174Combined sources11
Helixi182 – 201Combined sources20
Helixi203 – 211Combined sources9
Turni212 – 214Combined sources3
Helixi221 – 239Combined sources19
Beta strandi244 – 252Combined sources9
Beta strandi258 – 263Combined sources6
Helixi264 – 267Combined sources4
Helixi268 – 270Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D6AX-ray2.10A/B23-284[»]
1PAFX-ray2.50A/B23-284[»]
1PAGX-ray2.80A/B23-284[»]
1QCGX-ray2.10A/B23-284[»]
1QCIX-ray2.00A/B23-284[»]
1QCJX-ray2.10A/B23-284[»]
ProteinModelPortaliP10297.
SMRiP10297.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10297.

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.
IPR016331. Shiga-like_toxin_subunit_A.
[Graphical view]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PIRSFiPIRSF001924. Shigella_toxin_subunit_A. 1 hit.
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.

P10297-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSMLVVTIS IWLILAPTST WAVNTIIYNV GSTTISKYAT FLNDLRNEAK
60 70 80 90 100
DPSLKCYGIP MLPNTNTNPK YVLVELQGSN KKTITLMLRR NNLYVMGYSD
110 120 130 140 150
PFETNKCRYH IFNDISGTER QDVETTLCPN ANSRVSKNIN FDSRYPTLES
160 170 180 190 200
KAGVKSRSQV QLGIQILDSN IGKISGVMSF TEKTEAEFLL VAIQMVSEAA
210 220 230 240 250
RFKYIENQVK TNFNRAFNPN PKVLNLQETW GKISTAIHDA KNGVLPKPLE
260 270 280 290 300
LVDASGAKWI VLRVDEIKPD VALLNYVGGS CQTTYNQNAM FPQLIMSTYY
310
NYMVNLGDLF EGF
Length:313
Mass (Da):35,219
Last modified:October 1, 1993 - v2
Checksum:i2C57B2861EBA57F5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55383 mRNA. Translation: CAA39054.1.
PIRiS17757.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X55383 mRNA. Translation: CAA39054.1.
PIRiS17757.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D6AX-ray2.10A/B23-284[»]
1PAFX-ray2.50A/B23-284[»]
1PAGX-ray2.80A/B23-284[»]
1QCGX-ray2.10A/B23-284[»]
1QCIX-ray2.00A/B23-284[»]
1QCJX-ray2.10A/B23-284[»]
ProteinModelPortaliP10297.
SMRiP10297.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.2.2.22. 4806.

Miscellaneous databases

EvolutionaryTraceiP10297.

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.
IPR016331. Shiga-like_toxin_subunit_A.
[Graphical view]
PfamiPF00161. RIP. 1 hit.
[Graphical view]
PIRSFiPIRSF001924. Shigella_toxin_subunit_A. 1 hit.
PRINTSiPR00396. SHIGARICIN.
SUPFAMiSSF56371. SSF56371. 1 hit.
PROSITEiPS00275. SHIGA_RICIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRIP1_PHYAM
AccessioniPrimary (citable) accession number: P10297
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1993
Last modified: November 2, 2016
This is version 100 of the entry and version 2 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.