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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
 
 
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