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Protein

Capsid protein

Gene

ORF3b

Organism
Cowpea chlorotic mottle virus (CCMV)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Capsid protein. Probably binds RNA and plays a role in packaging.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein

Keywords - Ligandi

RNA-binding, Viral nucleoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
Capsid protein
Short name:
CP
Alternative name(s):
Coat protein
Gene namesi
ORF Names:ORF3b
OrganismiCowpea chlorotic mottle virus (CCMV)
Taxonomic identifieri12303 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageBromoviridaeBromovirus
Virus hostiGlycine max (Soybean) (Glycine hispida) [TaxID: 3847]
Vigna unguiculata (Cowpea) [TaxID: 3917]
Proteomesi
  • UP000008445 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, T=3 icosahedral capsid protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved; by host
Chaini2 – 190189Capsid proteinPRO_0000083195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine; by host

Keywords - PTMi

Acetylation

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 589Combined sources
Beta strandi67 – 715Combined sources
Helixi76 – 783Combined sources
Helixi83 – 853Combined sources
Beta strandi87 – 9711Combined sources
Beta strandi105 – 1117Combined sources
Helixi116 – 1183Combined sources
Helixi119 – 1224Combined sources
Beta strandi131 – 1333Combined sources
Beta strandi135 – 1406Combined sources
Turni141 – 1444Combined sources
Helixi147 – 1537Combined sources
Beta strandi154 – 1629Combined sources
Beta strandi168 – 17811Combined sources
Helixi181 – 1833Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWPX-ray3.20A/B/C1-190[»]
1ZA7X-ray2.70A/B/C26-190[»]
ProteinModelPortaliP03601.
SMRiP03601. Positions 26-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP03601.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 2313Arg-richAdd
BLAST

Domaini

The N-terminal arginine-rich stretch does not seem to be the major RNA-binding region that allows formation of an infectious ribonucleoprotein complex.1 Publication

Sequence similaritiesi

Belongs to the bromovirus capsid protein family.Curated

Family and domain databases

Gene3Di2.60.120.220. 1 hit.
InterProiIPR002009. Bromo_CP.
IPR010392. Satellite_virus_coat.
[Graphical view]
PfamiPF01318. Bromo_coat. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P03601-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTVGTGKLT RAQRRAAARK NKRNTRVVQP VIVEPIASGQ GKAIKAWTGY
60 70 80 90 100
SVSKWTASCA AAEAKVTSAI TISLPNELSS ERNKQLKVGR VLLWLGLLPS
110 120 130 140 150
VSGTVKSCVT ETQTTAAASF QVALAVADNS KDVVAAMYPE AFKGITLEQL
160 170 180 190
TADLTIYLYS SAALTEGDVI VHLEVEHVRP TFDDSFTPVY
Length:190
Mass (Da):20,343
Last modified:January 23, 2007 - v4
Checksum:i36BD1DA882D27EAD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti151 – 1511T → A in AAA46370 (PubMed:6895941).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28818 Genomic RNA. Translation: AAA46373.1.
J02052 Genomic RNA. Translation: AAA46370.1.
PIRiA04212. VCBVC.
RefSeqiNP_613277.1. NC_003542.1.

Genome annotation databases

GeneIDi962152.
KEGGivg:962152.

Cross-referencesi

Web resourcesi

Virus Particle ExploreR db

Icosahedral capsid structure

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M28818 Genomic RNA. Translation: AAA46373.1.
J02052 Genomic RNA. Translation: AAA46370.1.
PIRiA04212. VCBVC.
RefSeqiNP_613277.1. NC_003542.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWPX-ray3.20A/B/C1-190[»]
1ZA7X-ray2.70A/B/C26-190[»]
ProteinModelPortaliP03601.
SMRiP03601. Positions 26-190.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi962152.
KEGGivg:962152.

Miscellaneous databases

EvolutionaryTraceiP03601.

Family and domain databases

Gene3Di2.60.120.220. 1 hit.
InterProiIPR002009. Bromo_CP.
IPR010392. Satellite_virus_coat.
[Graphical view]
PfamiPF01318. Bromo_coat. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence of cowpea chlorotic mottle virus RNAs 2 and 3 and evidence of a recombination event during bromovirus evolution."
    Allison R.F., Janda M., Ahlquist P.
    Virology 172:321-330(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  2. "Complete nucleotide sequences of the coat protein messenger RNAs of brome mosaic virus and cowpea chlorotic mottle virus."
    Dasgupta R., Kaesberg P.
    Nucleic Acids Res. 10:703-713(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
  3. "Deletion of highly conserved arginine-rich RNA binding motif in cowpea chlorotic mottle virus capsid protein results in virion structural alterations and RNA packaging constraints."
    Annamalai P., Apte S., Wilkens S., Rao A.L.
    J. Virol. 79:3277-3288(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN ARG-RICH MOTIF.
  4. "Structures of the native and swollen forms of cowpea chlorotic mottle virus determined by X-ray crystallography and cryo-electron microscopy."
    Speir J.A., Munshi S., Wang G., Baker T.S., Johnson J.E.
    Structure 3:63-78(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
  5. "Conformational studies on a peptide fragment representing the RNA-binding N-terminus of a viral coat protein using circular dichroism and NMR spectroscopy."
    van der Graaf M., Hemminga M.A.
    Eur. J. Biochem. 201:489-494(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-26.
  6. "Solution conformation of a peptide fragment representing a proposed RNA-binding site of a viral coat protein studied by two-dimensional NMR."
    van der Graaf M., van Mierlo C.P.M., Hemminga M.A.
    Biochemistry 30:5722-5727(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-26.
  7. "Conformation and mobility of the RNA-binding N-terminal part of the intact coat protein of cowpea chlorotic mottle virus. A two-dimensional proton nuclear magnetic resonance study."
    van der Graaf M., Kroon G.J.A., Hemminga M.A.
    J. Mol. Biol. 220:701-709(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-34.

Entry informationi

Entry nameiCAPSD_CCMV
AccessioniPrimary (citable) accession number: P03601
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 102 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

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.