ID   CAPSD_BFDV              Reviewed;         247 AA.
AC   Q9YUC8;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   02-JUN-2021, entry version 71.
DE   RecName: Full=Capsid protein;
GN   Name=Cap; ORFNames=ORF2;
OS   Beak and feather disease virus (BFDV).
OC   Viruses; Monodnaviria; Shotokuvirae; Cressdnaviricota; Arfiviricetes;
OC   Cirlivirales; Circoviridae; Circovirus.
OX   NCBI_TaxID=77856;
OH   NCBI_TaxID=116991; Gracula.
OH   NCBI_TaxID=9223; Psittaciformes.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9791035; DOI=10.1006/viro.1998.9324;
RA   Bassami M.R., Berryman D., Wilcox G.E., Raidal S.R.;
RT   "Psittacine beak and feather disease virus nucleotide sequence analysis and
RT   its relationship to porcine circovirus, plant circoviruses, and chicken
RT   anaemia virus.";
RL   Virology 249:453-459(1998).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REP, AND DNA-BINDING.
RX   PubMed=16809327; DOI=10.1128/jvi.02559-05;
RA   Heath L., Williamson A.L., Rybicki E.P.;
RT   "The capsid protein of beak and feather disease virus binds to the viral
RT   DNA and is responsible for transporting the replication-associated protein
RT   into the nucleus.";
RL   J. Virol. 80:7219-7225(2006).
CC   -!- FUNCTION: Self-assembles to form the virion icosahedral capsid with a
CC       T=1 symmetry. This very small capsid (17 - 22 nm in diameter) allows
CC       the virus to be very stable in the environment and resistant to some
CC       disinfectants, including detergents. Essential for the initial
CC       attachment to heparan sulfate moieties and chondroitin sulfate B of the
CC       host cell surface proteoglycans. After attachment, the virus is
CC       endocytosed and traffics to the nucleus. The capsid protein binds and
CC       transports the viral genome and Rep across the nuclear envelope.
CC       {ECO:0000269|PubMed:16809327}.
CC   -!- SUBUNIT: Homomultimer. Assembles in the nucleus, presumably in an
CC       immature form, then migrates to the cytoplasm once assembled as mature
CC       virion (By similarity). Interacts with Rep; this interaction relocates
CC       Rep into the nucleus. {ECO:0000250, ECO:0000269|PubMed:16809327}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:16809327}.
CC       Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the circoviridae capsid protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF080560; AAC69862.1; -; Genomic_DNA.
DR   SMR; Q9YUC8; -.
DR   Proteomes; UP000007454; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039615; C:T=1 icosahedral viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019069; P:viral capsid assembly; IEA:InterPro.
DR   GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.950; -; 1.
DR   InterPro; IPR003383; Circovirus_capsid.
DR   InterPro; IPR038652; Circovirus_capsid_sf.
DR   Pfam; PF02443; Circo_capsid; 1.
PE   1: Evidence at protein level;
KW   Capsid protein; DNA-binding; Host nucleus; Host-virus interaction;
KW   T=1 icosahedral capsid protein; Viral attachment to host cell;
KW   Viral penetration into host cytoplasm; Viral penetration into host nucleus;
KW   Virion; Virus endocytosis by host; Virus entry into host cell.
FT   CHAIN           1..247
FT                   /note="Capsid protein"
FT                   /id="PRO_0000319848"
FT   REGION          1..40
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          15..44
FT                   /note="Nuclear localization signals"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   247 AA;  28942 MW;  25E086A559ABAB7E CRC64;
     MWGTSNCACA KFQIRRRYAR PYRRRHIRRY RRRRRHFRRR RFTTNRVYTL RLTRQFQFKI
     QKQTTSVGNL IFNADYITFA LDDFLQAVPN PHALNFEDYR IKLAKMEMRP TGGHYTVQSN
     GFGHTAVIQD SRITKFKTTA DQTQDPLAPF DGAKKWFVSR GFKRLLRPKP QITIEDLTTA
     NQSAALWLNS ARTGWIPLQG GPNSAGTKVR HYGIAFSFPQ PEQTITYVTK LTLYVQFRQF
     APNNPST