CAPSD_CGMVW
ID CAPSD_CGMVW Reviewed; 161 AA.
AC P69475; P19521;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 02-JUN-2021, entry version 52.
DE RecName: Full=Capsid protein;
DE AltName: Full=Coat protein;
GN Name=CP;
OS Cucumber green mottle mosaic virus (strain watermelon W) (CGMMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Virgaviridae; Tobamovirus.
OX NCBI_TaxID=12237;
OH NCBI_TaxID=3653; Citrullus.
OH NCBI_TaxID=3659; Cucumis sativus (Cucumber).
OH NCBI_TaxID=3668; Lagenaria siceraria (Bottle gourd) (Lagenaria leucantha).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Meshi T., Kiyama R., Ohno T., Okada Y.;
RT "Nucleotide sequence of the coat protein cistron and the 3' noncoding
RT region of cucumber green mottle mosaic virus (watermelon strain) RNA.";
RL Virology 127:54-64(1983).
RN [2]
RP PROTEIN SEQUENCE OF 2-161, AND ACETYLATION AT ALA-2.
RA Nozu Y., Tsugita A.;
RT "The amino acid sequence of cucumber green mottle mosaic virus (watermelon
RT strain) protein.";
RL Plant Sci. 44:47-51(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE OF 1-45.
RX PubMed=3201760; DOI=10.1016/s0042-6822(88)90132-8;
RA Saito T., Imai Y., Meshi T., Okada Y.;
RT "Interviral homologies of the 30K proteins of tobamoviruses.";
RL Virology 167:653-656(1988).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1-161.
RX PubMed=8201619; DOI=10.1006/jmbi.1994.1379;
RA Wang H., Stubbs G.;
RT "Structure determination of cucumber green mottle mosaic virus by X-ray
RT fiber diffraction. Significance for the evolution of tobamoviruses.";
RL J. Mol. Biol. 239:371-384(1994).
CC -!- FUNCTION: Capsid protein self-assembles to form rod-shaped virions
CC about 18 nm in diameter with a central canal enclosing the viral
CC genomic RNA.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the virgaviridae capsid protein family.
CC {ECO:0000305}.
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DR EMBL; V01551; CAA24792.1; -; mRNA.
DR EMBL; J04322; AAA46384.1; -; Genomic_RNA.
DR PIR; JQ1160; VCTMSH.
DR PDB; 1CGM; Fiber; 3.40 A; E=2-161.
DR PDBsum; 1CGM; -.
DR SMR; P69475; -.
DR EvolutionaryTrace; P69475; -.
DR GO; GO:0019029; C:helical viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR Gene3D; 1.20.120.70; -; 1.
DR InterPro; IPR001337; TMV-like_coat.
DR InterPro; IPR036417; TMV-like_coat_sf.
DR Pfam; PF00721; TMV_coat; 1.
DR SUPFAM; SSF47195; SSF47195; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Capsid protein; Direct protein sequencing;
KW Helical capsid protein; Virion.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 2..161
FT /note="Capsid protein"
FT /id="PRO_0000144929"
FT MOD_RES 2
FT /note="N-acetylalanine; by host"
FT /evidence="ECO:0000269|Ref.2"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:1CGM"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1CGM"
FT HELIX 22..30
FT /evidence="ECO:0007829|PDB:1CGM"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:1CGM"
FT HELIX 40..51
FT /evidence="ECO:0007829|PDB:1CGM"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1CGM"
FT TURN 74..79
FT /evidence="ECO:0007829|PDB:1CGM"
FT HELIX 80..87
FT /evidence="ECO:0007829|PDB:1CGM"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1CGM"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:1CGM"
FT HELIX 112..134
FT /evidence="ECO:0007829|PDB:1CGM"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1CGM"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1CGM"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1CGM"
SQ SEQUENCE 161 AA; 17394 MW; 2119F359A096D925 CRC64;
MAYNPITPSK LIAFSASYVP VRTLLNFLVA SQGTAFQTQA GRDSFRESLS ALPSSVVDIN
SRFPDAGFYA FLNGPVLRPI FVSLLSSTDT RNRVIEVVDP SNPTTAESLN AVKRTDDAST
AARAEIDNLI ESISKGFDVY DRASFEAAFS VVWSEATTSK A