ID   CAPSD_CERV              Reviewed;         494 AA.
AC   P05399;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   02-JUN-2021, entry version 88.
DE   RecName: Full=Probable capsid protein;
DE            Short=CP;
DE   AltName: Full=Coat protein;
GN   ORFNames=ORF IV;
OS   Carnation etched ring virus (CERV).
OC   Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC   Ortervirales; Caulimoviridae; Caulimovirus.
OX   NCBI_TaxID=10640;
OH   NCBI_TaxID=3570; Dianthus caryophyllus (Carnation) (Clove pink).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16453731; DOI=10.1002/j.1460-2075.1986.tb04614.x;
RA   Hull R., Sadler J., Longstaff M.;
RT   "The sequence of carnation etched ring virus DNA: comparison with
RT   cauliflower mosaic virus and retroviruses.";
RL   EMBO J. 5:3083-3090(1986).
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   -!- 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; X04658; CAA28359.1; -; Genomic_DNA.
DR   PIR; S00853; VCCVCE.
DR   RefSeq; NP_612576.1; NC_003498.1.
DR   SMR; P05399; -.
DR   GeneID; 935427; -.
DR   KEGG; vg:935427; -.
DR   Proteomes; UP000008446; 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   3: Inferred from homology;
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..494
FT                   /note="Probable capsid protein"
FT                   /id="PRO_0000222034"
FT   ZN_FING         418..435
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          474..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           120..123
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        480..494
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   494 AA;  56886 MW;  26825539E512D54E CRC64;
     MNREAILWKN INSIPEEPDL IKSLEVLSME QNDRERELEH NLILNKQISE QIPEWIIPDS
     LSELSSGIDL NFVLEEQEVN DNNSQPSLEE EVVSESDVES MRSFNVAMNR GEVGESSNKR
     PKREPDLFTS FGKIREDIGD KNPSLNILNL DCVNSPSDRK NKIDKWAAEL GLVFLTNPEA
     YTTAPNAARA RLAYMEHKSL GIVNRFIKST QWTQMNGDIL LNVVSGLYTM FLGEDYTGNQ
     EKTLEQERAK ASLRLINLQL CDICSLQSFF CDYESNLYKL PQNEYPSLVK QYLAKIPIVG
     EKASKRFEEE ASAATSYSLG FAHKLVNEEL AKICELSKKQ KKLKRFNKNC CSTFEKPYEY
     GCKPSYSKKK KYSKKYKPKY TKYKVIRKKK KFSPGKYFKP KDKKSEKAKY CPKGKKTCRC
     WVCNIEGHYA NECPNRQTSE KFKLIQIAEN YGLEPIENPY EDQQEICLLE QIQLSSSDSE
     LDDTCEESSS EESE