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Protein

Nuclear shuttle protein

Gene

BV1

Organism
Sida golden mosaic Honduras virus
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Binds to the genomic viral ssDNA, shuttles it into and out of the cell nucleus. Begomoviruses use 2 proteins to transport their DNA from cell to cell. The nuclear shuttle protein (NSP) shuttles it between nucleus and cytoplasm and the movement protein (MP) probably transports the DNA-NSP complex to the cell periphery and facilitates movement across the cell wall.UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Viral movement proteinUniRule annotation

Keywords - Biological processi

Host-virus interactionUniRule annotation, Transport

Keywords - Ligandi

DNA-bindingUniRule annotation

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear shuttle proteinUniRule annotation
Short name:
NSPUniRule annotation
Gene namesi
Name:BV1Imported
OrganismiSida golden mosaic Honduras virusImported
Taxonomic identifieri223316 [NCBI]
Taxonomic lineageiVirusesssDNA virusesGeminiviridaeBegomovirus

Subcellular locationi

  • Host cell membrane UniRule annotation; Peripheral membrane protein UniRule annotation; Cytoplasmic side UniRule annotation
  • Host cytoplasm UniRule annotation
  • Host nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host cell membraneUniRule annotation, Host cytoplasmUniRule annotation, Host membrane, Host nucleusUniRule annotation, Membrane

Interactioni

Subunit structurei

Binds to single-stranded and double-stranded viral DNA. Interacts with the host nuclear shuttle interacting (NSI) protein. This interaction may allow NSP to recruit NSI monomers to the viral genome and thus regulate nuclear export of viral genome by NSP.UniRule annotation

Family & Domainsi

Sequence similaritiesi

Belongs to the begomovirus nuclear shuttle protein family.UniRule annotation

Family and domain databases

InterProiIPR001530. Gemini_BR1.
IPR000263. GV_A/BR1_coat.
[Graphical view]
PfamiPF00844. Gemini_coat. 1 hit.
[Graphical view]
PRINTSiPR00223. GEMCOATARBR1.
PR00225. GEMCOATBR1.

Sequencei

Sequence statusi: Complete.

P89119-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYHFRTKRGS AFTPRRYYAR NNVFKRSAPF KRDEGKRRPV NSNKAHDEPK
60 70 80 90 100
MKAQRIHENQ FGPDFVMAHN SAISTFISYP SLGKTEPNRS RSYIKLKRLR
110 120 130 140 150
VKGTVKIERV QADMNMDGAT PKVEGVFSLV VVVDRKPHLG SSGCLHTFDE
160 170 180 190 200
LFGARIHSHG NLSITPSLKD RFYIRHVFKR VLSVEKDTMM VDVEGSTTLS
210 220 230 240 250
NRRYNCWSTF KDLDHDSCNG VYGNISKNAL LVYYCWMSDT VSKASTFVSF

DLDYVG
Length:256
Mass (Da):29,381
Last modified:May 1, 1997 - v1
Checksum:i3E74464462EC67BE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11098 Genomic DNA. Translation: CAA71978.1.
RefSeqiNP_808898.1. NC_004660.1.

Genome annotation databases

GeneIDi988181.
KEGGivg:988181.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y11098 Genomic DNA. Translation: CAA71978.1.
RefSeqiNP_808898.1. NC_004660.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi988181.
KEGGivg:988181.

Family and domain databases

InterProiIPR001530. Gemini_BR1.
IPR000263. GV_A/BR1_coat.
[Graphical view]
PfamiPF00844. Gemini_coat. 1 hit.
[Graphical view]
PRINTSiPR00223. GEMCOATARBR1.
PR00225. GEMCOATBR1.
ProtoNetiSearch...

Entry informationi

Entry nameiP89119_9GEMI
AccessioniPrimary (citable) accession number: P89119
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1997
Last sequence update: May 1, 1997
Last modified: June 8, 2016
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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.