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P23009 (POL2_BPMV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
RNA2 polyprotein
Alternative name(s):
Genome polyprotein M
P2

Cleaved into the following 3 chains:

  1. Movement protein
    Short name=MP
  2. Large coat protein
    Short name=LCP
    Alternative name(s):
    Coat protein VP37
  3. Small coat protein
    Short name=SCP
    Alternative name(s):
    Coat protein VP23
OrganismBean-pod mottle virus (strain Kentucky G7) (BPMV) [Complete proteome]
Taxonomic identifier31715 [NCBI]
Taxonomic lineageViruses › ssRNA positive-strand viruses, no DNA stage › Picornavirales › Secoviridae › Comovirinae › Comovirus ›
Virus hostDesmodium [TaxID: 53866]
Glycine max (Soybean) (Glycine hispida) [TaxID: 3847]
Phaseolus vulgaris (Kidney bean) (French bean) [TaxID: 3885]

Protein attributes

Sequence length1018 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Movement protein: transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Acts by forming a tubular structure at the host plasmodesmata, enlarging it enough to allow free passage of virion capsids By similarity.

Subcellular location

Movement protein: Host cell junction › host plasmodesma By similarity. Note: Assembles in tubules that are embedded within modified plasmodesmata By similarity.

Large coat protein: Virion Potential.

Post-translational modification

Specific enzymatic cleavages by RNA1 encoded picornain 3C-like protease in vivo yield mature proteins By similarity.

Miscellaneous

The virus capsid is composed of 60 icosahedral units, each of which is composed of one copy each of the two coat proteins.

Sequence similarities

Belongs to the comoviridae genome polyprotein M family.

Caution

It is uncertain whether Met-1 or Met-103 is the initiator.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 446446Movement protein By similarity
PRO_0000037031
Chain447 – 820374Large coat protein By similarity
PRO_0000037032
Chain821 – 1018198Small coat protein By similarity
PRO_0000037033

Sites

Site446 – 4472Cleavage By similarity
Site820 – 8212Cleavage By similarity

Secondary structure

1 ...................................................................................................... 1018
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23009 [UniParc].

Last modified December 1, 1992. Version 2.
Checksum: B11B35D0A7F0F872

FASTA1,018113,352
        10         20         30         40         50         60 
MFASFIFSGD NKLTEKTIFN CGDLDILVVY YTIATQFRKF LPHYIRWHLY TLLIYILPSF 

        70         80         90        100        110        120 
LTTEIKYKRN LSNIHISGLF YDNRFKFWTK HDKNLALTEE EKMEVIRNRG IPADVLAKRA 

       130        140        150        160        170        180 
HEFEKHVAHE SLKDQIPAVD KLYSTKVNKF AKIMNLRQSV VGDLKLLTDG KLYEGKHIPV 

       190        200        210        220        230        240 
SNISAGENHV VQIPLMAQEE ILSSSASDFK TAMVSKSSKP QATAMHVGAI EIIIDSFASP 

       250        260        270        280        290        300 
DCNIVGAMLL VDTYHTNPEN AVRSIFVAPF RGGRPIRVVT FPNTIVQIEP DMNSRFQLLS 

       310        320        330        340        350        360 
TTTNGDFVQG KDLAMVKVNV ACAAVGLTSS YTPTPLLESG LQKDRGLIVE YFGRMSYVAH 

       370        380        390        400        410        420 
NINQPQEKDL LEGNFSFDIK SRSRLEKVSS TKAQFVSGRT FKYDIIGAGS QSSEELSEEK 

       430        440        450        460        470        480 
IQGKAKQVDA RLRQRIDPQY NEVQAQMETN LFKLSLDDVE TPKGSMLDLK ISQSKIALPK 

       490        500        510        520        530        540 
NTVGGTILRS DLLANFLTEG NFRASVDLQR THRIKGMIKM VATVGIPENT GIALACAMNS 

       550        560        570        580        590        600 
SIRGRASSDI YTICSQDCEL WNPACTKAMT MSFNPNPCSD AWSLEFLKRT GFHCDIICVT 

       610        620        630        640        650        660 
GWTATPMQDV QVTIDWFISS QECVPRTYCV LNPQNPFVLN RWMGKLTFPQ GTSRSVKRMP 

       670        680        690        700        710        720 
LSIGGGAGAK SAILMNMPNA VLSMWRYFVG DLVFEVSKMT SPYIKCTVSF FIAFGNLADD 

       730        740        750        760        770        780 
TINFEAFPHK LVQFGEIQEK VVLKFSQEEF LTAWSTQVRP ATTLLADGCP YLYAMVHDSS 

       790        800        810        820        830        840 
VSTIPGDFVI GVKLTIIENM CAYGLNPGIS GSRLLGTIPQ SISQQTVWNQ MATVRTPLNF 

       850        860        870        880        890        900 
DSSKQSFCQF SVDLLGGGIS VDKTGDWITL VQNSPISNLL RVAAWKKGCL MVKVVMSGNA 

       910        920        930        940        950        960 
AVKRSDWASL VQVFLTNSNS TEHFDACRWT KSEPHSWELI FPIEVCGPNN GFEMWSSEWA 

       970        980        990       1000       1010 
NQTSWHLSFL VDNPKQSTTF DVLLGISQNF EIAGNTLMPA FSVPQANARS SENAESSA

« Hide

References

[1]"Analysis of the nucleotide sequence of bean pod mottle virus middle component RNA."
Macfarlane S.A., Shanks M., Davies J.W., Zlotnick A., Lomonossoff G.P.
Virology 183:405-409(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[2]"Protein-RNA interactions in an icosahedral virus at 3.0-A resolution."
Chen Z., Stauffacher C., Li Y., Schmidt T., Bomu W., Kamer G., Shanks M., Lomonossoff G., Johnson J.E.
Science 245:154-159(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 447-1018.
[3]"Evidence for assembly-dependent folding of protein and RNA in an icosahedral virus."
Lin T., Cavarelli J., Johnson J.E.
Virology 314:26-33(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 447-1005.

Web resources

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Virus Particle ExploreR db

Icosahedral capsid structure

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M62738 Genomic RNA. Translation: AAA42801.1.
PIRGNWXG7. A40321.
RefSeqNP_612348.1. NC_003495.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BMVX-ray3.001821-1018[»]
2447-820[»]
1PGLX-ray2.801821-1005[»]
2447-816[»]
1PGWX-ray2.901821-1005[»]
2466-816[»]
ProteinModelPortalP23009.
SMRP23009. Positions 447-1005.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR003181. Como_LCP.
IPR003182. Como_SCP.
[Graphical view]
PfamPF02247. Como_LCP. 1 hit.
PF02248. Como_SCP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP23009.

Entry information

Entry namePOL2_BPMV
AccessionPrimary (citable) accession number: P23009
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: December 1, 1992
Last modified: April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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