CAPSD_SCPMV
ID CAPSD_SCPMV Reviewed; 279 AA.
AC P03607;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE Flags: Precursor;
GN ORFNames=ORF3;
OS Southern cowpea mosaic virus (SCPMV) (Southern bean mosaic virus (strain
OS cowpea)).
OC Viruses; Riboviria; Orthornavirae; Pisuviricota; Pisoniviricetes;
OC Sobelivirales; Solemoviridae; Sobemovirus.
OX NCBI_TaxID=196398;
OH NCBI_TaxID=3847; Glycine max (Soybean) (Glycine hispida).
OH NCBI_TaxID=3885; Phaseolus vulgaris (Kidney bean) (French bean).
OH NCBI_TaxID=3915; Vigna mungo (Black gram) (Phaseolus mungo).
OH NCBI_TaxID=3917; Vigna unguiculata (Cowpea).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2823471; DOI=10.1016/0042-6822(87)90172-3;
RA Wu S., Rinehart C.A., Kaesberg P.;
RT "Sequence and organization of southern bean mosaic virus genomic RNA.";
RL Virology 161:73-80(1987).
RN [2]
RP PROTEIN SEQUENCE OF 20-279, AND ACETYLATION AT ALA-20.
RX PubMed=18635141; DOI=10.1016/0042-6822(82)90071-x;
RA Hermodson M.A., Abad-Zapatero C., Abdel-Meguid S.S., Pundak S.,
RA Rossmann M.G., Tremaine J.H.;
RT "Amino acid sequence of southern bean mosaic virus coat protein and its
RT relation to the three-dimensional structure of the virus.";
RL Virology 119:133-149(1982).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=19711553; DOI=10.1038/286033a0;
RA Abad-Zapatero C., Abdel-Meguid S.S., Johnson J.E., Leslie A.G., Rayment I.,
RA Rossmann M.G., Suck D., Tsukihara T.;
RT "Structure of southern bean mosaic virus at 2.8 A resolution.";
RL Nature 286:33-39(1980).
CC -!- SUBUNIT: The virus particle has a shell of 180 protein subunits
CC arranged with T=3 icosahedral symmetry around a core of RNA. Each
CC icosahedral unit contains three protein subunits.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the icosahedral plant coat protein family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Virus Particle ExploreR db; Note=Icosahedral capsid
CC structure;
CC URL="https://viperdb.scripps.edu/Info_Page.php?VDB=4sbv";
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DR EMBL; M23021; AAA46567.1; -; Genomic_RNA.
DR PIR; A04218; VCBW.
DR PIR; D33739; VCBWSC.
DR RefSeq; NP_042303.1; NC_001625.2.
DR PDB; 4SBV; X-ray; 2.80 A; A/B/C=20-279.
DR PDBsum; 4SBV; -.
DR SMR; P03607; -.
DR iPTMnet; P03607; -.
DR GeneID; 1481841; -.
DR KEGG; vg:1481841; -.
DR EvolutionaryTrace; P03607; -.
DR Proteomes; UP000008033; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IDA:CAFA.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0008289; F:lipid binding; IDA:CAFA.
DR GO; GO:0003723; F:RNA binding; IDA:CAFA.
DR GO; GO:0039660; F:structural constituent of virion; IDA:CAFA.
DR Gene3D; 2.60.120.20; -; 1.
DR InterPro; IPR000937; Capsid_prot_S-dom_vir.
DR InterPro; IPR029053; Viral_coat.
DR Pfam; PF00729; Viral_coat; 1.
DR PRINTS; PR00233; ICOSAHEDRAL.
DR PROSITE; PS00555; ICOSAH_VIR_COAT_S; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Capsid protein; Direct protein sequencing;
KW Disulfide bond; Reference proteome; T=3 icosahedral capsid protein; Virion.
FT PROPEP 1..19
FT /evidence="ECO:0000269|PubMed:18635141"
FT /id="PRO_0000040209"
FT CHAIN 20..279
FT /note="Capsid protein"
FT /id="PRO_0000040210"
FT REGION 20..83
FT /note="R domain, interaction with RNA"
FT REGION 31..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..269
FT /note="S domain, virion shell"
FT REGION 270..279
FT /note="P domain, projecting"
FT MOD_RES 20
FT /note="N-acetylalanine; by host"
FT /evidence="ECO:0000269|PubMed:18635141"
FT DISULFID 188..195
FT VARIANT 101
FT /note="V -> D"
FT VARIANT 245
FT /note="T -> I"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 86..99
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:4SBV"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:4SBV"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 126..140
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 149..155
FT /evidence="ECO:0007829|PDB:4SBV"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:4SBV"
FT TURN 185..192
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:4SBV"
FT HELIX 221..228
FT /evidence="ECO:0007829|PDB:4SBV"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 242..248
FT /evidence="ECO:0007829|PDB:4SBV"
FT STRAND 256..269
FT /evidence="ECO:0007829|PDB:4SBV"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:4SBV"
SQ SEQUENCE 279 AA; 30527 MW; 9B1BD427642493C1 CRC64;
MSGLFHHRTK PREIRAFVMA TRLTKKQLAQ AIQNTLPNPP RRKRRAKRRA AQVPKPTQAG
VSMAPIAQGT MVKLRPPMLR SSMDVTILSH CELSTELAVT VTIVVTSELV MPFTVGTWLR
GVAQNWSKYA WVAIRYTYLP SCPTTTSGAI HMGFQYDMAD TLPVSVNQLS NLKGYVTGPV
WEGQSGLCFV NNTKCPDTSR AITIALDTNE VSEKRYPFKT ATDYATAVGV NANIGNILVP
ARLVTAMEGG SSKTAVNTGR LYASYTIRLI EPIAAALNL
