CAPSD_MNSV
ID CAPSD_MNSV Reviewed; 390 AA.
AC P19899;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 02-JUN-2021, entry version 76.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
DE AltName: Full=p42;
GN ORFNames=ORF4;
OS Melon necrotic spot virus (MNSV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Tolucaviricetes;
OC Tolivirales; Tombusviridae; Procedovirinae; Gammacarmovirus.
OX NCBI_TaxID=11987;
OH NCBI_TaxID=3656; Cucumis melo (Muskmelon).
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2584953; DOI=10.1099/0022-1317-70-11-3033;
RA Riviere C.J., Pot J., Tremaine J.H., Rochon D.M.;
RT "Coat protein of melon necrotic spot carmovirus is more similar to those of
RT tombusviruses than those of carmoviruses.";
RL J. Gen. Virol. 70:3033-3042(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2212985; DOI=10.1099/0022-1317-71-9-1887;
RA Riviere C.J., Rochon D.M.;
RT "Nucleotide sequence and genomic organization of melon necrotic spot
RT virus.";
RL J. Gen. Virol. 71:1887-1896(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) OF 60-390.
RC STRAIN=KS;
RX PubMed=18097092; DOI=10.1107/s1744309107066481;
RA Wada Y., Tanaka H., Yamashita E., Kubo C., Ichiki-Uehara T.,
RA Nakazono-Nagaoka E., Omura T., Tsukihara T.;
RT "The structure of melon necrotic spot virus determined at 2.8 A
RT resolution.";
RL Acta Crystallogr. F 64:8-13(2008).
CC -!- FUNCTION: Capsid protein self-assembles to form an icosahedral capsid
CC with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180
CC capsid proteins. Also acts as a suppressor of RNA-mediated gene
CC silencing, also known as post-transcriptional gene silencing (PTGS), a
CC mechanism of plant viral defense that limits the accumulation of viral
CC RNAs (By similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Note=Binds 4 Ca(2+) ions per icosahedral asymmetric unit, itself
CC composed of three capsid protein subunits. Ca(2+) ions probably promote
CC virus assembly and stabilize the virus particle.;
CC -!- SUBUNIT: Homodimer. Homomultimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the icosahedral plant coat protein family.
CC {ECO:0000305}.
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DR EMBL; M29671; AAB02435.1; -; Genomic_RNA.
DR EMBL; D00562; BAA00436.1; -; Genomic_RNA.
DR EMBL; D12536; BAA02104.1; -; Genomic_RNA.
DR PIR; JQ0169; VCVEMN.
DR RefSeq; NP_041231.1; NC_001504.1.
DR PDB; 2ZAH; X-ray; 2.81 A; A/B/C=60-390.
DR PDBsum; 2ZAH; -.
DR SMR; P19899; -.
DR GeneID; 1491981; -.
DR KEGG; vg:1491981; -.
DR EvolutionaryTrace; P19899; -.
DR Proteomes; UP000202003; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
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; Calcium; Capsid protein; Reference proteome; RNA-binding;
KW T=3 icosahedral capsid protein; Virion.
FT CHAIN 1..390
FT /note="Capsid protein"
FT /id="PRO_0000222864"
FT REGION 95..256
FT /note="S domain, virion shell"
FT REGION 257..390
FT /note="P domain, projecting"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:2ZAH"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2ZAH"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:2ZAH"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2ZAH"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2ZAH"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 145..159
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 168..175
FT /evidence="ECO:0007829|PDB:2ZAH"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2ZAH"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 231..238
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 246..256
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:2ZAH"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2ZAH"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 308..320
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 328..341
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 344..353
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:2ZAH"
FT STRAND 374..382
FT /evidence="ECO:0007829|PDB:2ZAH"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:2ZAH"
SQ SEQUENCE 390 AA; 41853 MW; 62D6AF207BC7EA03 CRC64;
MAMVKRINNL PTVKLAKQAL PLLANPKLVN KAIDVVPLVV QGGRKLSKAA KRLLGAYGGN
ISYTEGAKPG AISAPVAISR RVAGMKPRFV RSEGSVKIVH REFIASVLPS SDLTVNNGDV
NIGKYRVNPS NNALFTWLQG QAQLYDMYRF TRLRITYIPT TGSTSTGRVS LLWDRDSQDP
LPIDRAAISS YAHSADSAPW AENVLVVPCD NTWRYMNDTN AVDRKLVDFG QFLFATYSGA
GSTAHGDLYV EYAVEFKDPQ PIAGMVCMFD RLVSLSEVGS TIKGVNYIAD RDVITTGGNI
GVNINIPGTY LVTIVLNATS IGPLTFTGNS KLVGNSLNLT SSGASALTFT LNSTGVPNSS
DSSFSVGTVV ALTRVRMTIT RCSPETAYLA
