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 13-SEP-2023, entry version 78. 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; OC Gammacarmovirus melonis. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 OrthoDB; 10131at10239; -. 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 Gene3D; 2.60.40.4030; -; 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 SUPFAM; SSF88633; Positive stranded ssRNA viruses; 1. 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 //