ID   CAPSD_CAMVS             Reviewed;         489 AA.
AC   P03542;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   23-FEB-2022, entry version 92.
DE   RecName: Full=Capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
GN   ORFNames=ORF IV;
OS   Cauliflower mosaic virus (strain Strasbourg) (CaMV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Caulimoviridae; Caulimovirus.
OX   NCBI_TaxID=10648;
OH   NCBI_TaxID=3702; Arabidopsis thaliana (Mouse-ear cress).
OH   NCBI_TaxID=3705; Brassica.
OH   NCBI_TaxID=3725; Raphanus.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7407912; DOI=10.1016/0092-8674(80)90136-1;
RA   Franck A., Guilley H., Jonard G., Richards K., Hirth L.;
RT   "Nucleotide sequence of cauliflower mosaic virus DNA.";
RL   Cell 21:285-294(1980).
RN   [2]
RP   FUNCTION, NUCLEAR LOCALIZATION SIGNAL, AND INTERACTION WITH HOST IMPORTIN
RP   ALPHA.
RX   PubMed=12075100; DOI=10.1099/0022-1317-83-7-1783;
RA   Karsies A., Merkle T., Szurek B., Bonas U., Hohn T., Leclerc D.;
RT   "Regulated nuclear targeting of cauliflower mosaic virus.";
RL   J. Gen. Virol. 83:1783-1790(2002).
CC   -!- FUNCTION: Self assembles to form an icosahedral capsid, about 50 nm in
CC       diameter, nm, composed of 420 subunits of the viral capsid protein. The
CC       capsid encapsulates the genomic dsDNA. Following virus entry into host
CC       cell, provides nuclear import of the viral genome. Virus particles do
CC       not enter the nucleus, but dock at the nuclear membrane through the
CC       interaction with host importins (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:12075100}.
CC   -!- SUBUNIT: Interacts (via nuclear localization signal) with host importin
CC       alpha. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the caulimoviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; V00141; CAA23459.1; -; Genomic_DNA.
DR   PIR; A04153; VCCV.
DR   RefSeq; NP_056727.1; NC_001497.1.
DR   PRIDE; P03542; -.
DR   GeneID; 1489541; -.
DR   KEGG; vg:1489541; -.
DR   Proteomes; UP000002501; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039620; C:T=7 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR   InterPro; IPR001988; Caulimo_coat.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PRINTS; PR00221; CAULIMOCOAT.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; Host nucleus; Metal-binding; Reference proteome;
KW   T=7 icosahedral capsid protein; Viral penetration into host nucleus;
KW   Virion; Virus entry into host cell; Zinc; Zinc-finger.
FT   CHAIN           1..489
FT                   /note="Capsid protein"
FT                   /id="PRO_0000222033"
FT   ZN_FING         412..429
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          79..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           122..125
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000269|PubMed:12075100"
FT   COMPBIAS        92..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  56664 MW;  9A61A59AC00D99AE CRC64;
     MAESILDRTI NRFWYNLGED CLSESQFDLM IRLMEESLDG DQIIDLTSLP SDNLQVEQVM
     TTTEDSISEE ESEFLLAIGE TSEEESDSGE EPEFEQVRMD RTGGTEIPKE EDGEGPSRYN
     ERKRKTPEDR YFPTQPKTIP GQKQTSMGML NIDCQTNRRT LIDDWAAEIG LIVKTNREDY
     LDPETILLLM EHKTSGIAKE LIRNTRWNRT TGDIIEQVID AMYTMFLGLN YSDNKVAEKI
     DEQEKAKIRM TKLQLCDICY LEEFTCDYEK NMYKTELADF PGYINQYLSK IPIIGEKALT
     RFRHEANGTS IYSLGFAAKI VKEELSKICD LSKKQKKLKK FNKKCCSIGE ASTEYGCKKT
     STKKYHKKRY KKKYKAYKPY KKKKKFRSGK YFKPKEKKGS KQKYCPKGKK DCRCWICNIE
     GHYANECPNR QSSEKAHILQ QAEKLGLQPI EEPYEGVQEV FILEYKEEEE ETSTEESDGS
     STSEDSDSD