CAPSD_CMVFN
ID CAPSD_CMVFN Reviewed; 218 AA.
AC P69466; P14767;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 02-JUN-2021, entry version 67.
DE RecName: Full=Capsid protein;
DE Short=CP;
DE AltName: Full=Coat protein;
GN ORFNames=ORF3b;
OS Cucumber mosaic virus (strain FNY) (CMV).
OC Viruses; Riboviria; Orthornavirae; Kitrinoviricota; Alsuviricetes;
OC Martellivirales; Bromoviridae; Cucumovirus.
OX NCBI_TaxID=12307;
OH NCBI_TaxID=3663; Cucurbita pepo (Vegetable marrow) (Summer squash).
OH NCBI_TaxID=4097; Nicotiana tabacum (Common tobacco).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=2230731; DOI=10.1099/0022-1317-71-10-2243;
RA Owen J., Shintaku M., Aeschleman P., Tahar S., Palukaitis P.;
RT "Nucleotide sequence and evolutionary relationships of cucumber mosaic
RT virus (CMV) strains: CMV RNA 3.";
RL J. Gen. Virol. 71:2243-2249(1990).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=10906212; DOI=10.1128/jvi.74.16.7578-7586.2000;
RA Smith T.J., Chase E., Schmidt T., Perry K.L.;
RT "The structure of cucumber mosaic virus and comparison to cowpea chlorotic
RT mottle virus.";
RL J. Virol. 74:7578-7586(2000).
CC -!- FUNCTION: Capsid protein. Probably binds RNA and plays a role in
CC packaging (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- DOMAIN: The N-terminal arginine-rich stretch does not seem to be the
CC major RNA-binding region that allows formation of an infectious
CC ribonucleoprotein complex. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cucumovirus capsid protein family.
CC {ECO:0000305}.
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DR EMBL; D10538; BAA01397.1; -; Genomic_RNA.
DR RefSeq; NP_040777.1; NC_001440.1.
DR PDB; 1F15; X-ray; 3.20 A; A/B/C=1-218.
DR PDBsum; 1F15; -.
DR SMR; P69466; -.
DR GeneID; 962640; -.
DR KEGG; vg:962640; -.
DR EvolutionaryTrace; P69466; -.
DR Proteomes; UP000002502; Genome.
DR GO; GO:0039617; C:T=3 icosahedral viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR Gene3D; 2.60.120.530; -; 1.
DR InterPro; IPR000247; Cucumovirus_coat.
DR InterPro; IPR023800; Cucumovirus_coat_A.
DR InterPro; IPR037137; Cucumovirus_coat_Asu_sf.
DR Pfam; PF00760; Cucumo_coat; 1.
DR PRINTS; PR00222; CUCUMOCOAT.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome;
KW T=3 icosahedral capsid protein; Virion.
FT CHAIN 1..218
FT /note="Capsid protein"
FT /id="PRO_0000083204"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 32..47
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:1F15"
FT HELIX 94..97
FT /evidence="ECO:0007829|PDB:1F15"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 102..113
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:1F15"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:1F15"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1F15"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:1F15"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:1F15"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:1F15"
FT STRAND 198..208
FT /evidence="ECO:0007829|PDB:1F15"
SQ SEQUENCE 218 AA; 24141 MW; C4B4FCB21F197F98 CRC64;
MDKSESTSAG RNRRRRPRRG SRSAPSSADA NFRVLSQQLS RLNKTLAAGR PTINHPTFVG
SERCRPGYTF TSITLKPPKI DRGSYYGKRL LLPDSVTEYD KKLVSRIQIR VNPLPKFDST
VWVTVRKVPA SSDLSVAAIS AMFADGASPV LVYQYAASGV QANNKLLYDL SAMRADIGDM
RKYAVLVYSK DDALETDELV LHVDIEHQRI PTSGVLPV
