CAPSH_ASFK5
ID CAPSH_ASFK5 Reviewed; 646 AA.
AC Q5IZJ5;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Major capsid protein;
DE Short=MCP;
DE AltName: Full=p72;
DE AltName: Full=p73;
GN OrderedLocusNames=Ken-093;
OS African swine fever virus (isolate Pig/Kenya/KEN-50/1950) (ASFV).
OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Pokkesviricetes;
OC Asfuvirales; Asfarviridae; Asfivirus.
OX NCBI_TaxID=561445;
OH NCBI_TaxID=6937; Ornithodoros (relapsing fever ticks).
OH NCBI_TaxID=85517; Phacochoerus aethiopicus (Warthog).
OH NCBI_TaxID=41426; Phacochoerus africanus (Warthog).
OH NCBI_TaxID=273792; Potamochoerus larvatus (Bushpig).
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15634958; DOI=10.1128/jcm.43.1.112-119.2005;
RA Zsak L., Borca M.V., Risatti G.R., Zsak A., French R.A., Lu Z.,
RA Kutish G.F., Neilan J.G., Callahan J.D., Nelson W.M., Rock D.L.;
RT "Preclinical diagnosis of African swine fever in contact-exposed swine by a
RT real-time PCR assay.";
RL J. Clin. Microbiol. 43:112-119(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kutish G.F., Rock D.L.;
RT "African swine fever virus genomes.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Capsid protein that self-assembles to form the pseudo-
CC hexameric capsomers of the icosahedral capsid (By similarity). The
CC capsid is constructed of 2760 pseudo-hexameric capsomers and 12
CC pentameric capsomers, with a T=277 symmetry, about 200 nm in diameter
CC (By similarity). The capsid encapsulates the DNA-containing nucleoid,
CC the core shell and the inner membrane (By similarity). Plays an
CC essential role in virion assembly (By similarity). Involved in virus
CC attachment to the host cell (By similarity).
CC {ECO:0000250|UniProtKB:P22776}.
CC -!- SUBUNIT: Homotrimer (By similarity). The membrane-bound form, but not
CC the cytosolic one, assembles into large complexes (By similarity).
CC Interacts with the minor capsid proteins M1249L and p17; these
CC interactions form a rigid zipper structure that stabilizes the
CC capsomers (By similarity). {ECO:0000250|UniProtKB:P22776}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P22776}. Host
CC endoplasmic reticulum membrane; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P22776}. Host cytoplasm, host cytosol
CC {ECO:0000250|UniProtKB:P22776}. Note=Present in the outer part of the
CC capsid shell (By similarity). Localizes to the viral factory at 16 hpi
CC (By similarity). {ECO:0000250|UniProtKB:P22776}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NCLDV major capsid protein family.
CC {ECO:0000305}.
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DR EMBL; AY261360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AY578698; AAT84447.1; -; Genomic_DNA.
DR SMR; Q5IZJ5; -.
DR Proteomes; UP000000861; Genome.
DR GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.70.9.20; -; 1.
DR InterPro; IPR007542; MCP_C.
DR InterPro; IPR038519; MCP_C_sf.
DR InterPro; IPR016112; VP_dsDNA_II.
DR Pfam; PF04451; Capsid_NCLDV; 1.
DR SUPFAM; SSF49749; SSF49749; 2.
PE 3: Inferred from homology;
KW Capsid protein; Host cytoplasm; Host endoplasmic reticulum; Host membrane;
KW Host-virus interaction; Late protein; Membrane;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..646
FT /note="Major capsid protein"
FT /id="PRO_0000373385"
SQ SEQUENCE 646 AA; 73211 MW; F5C5DEBBDFDDEEBA CRC64;
MASGGAFCLI ANDGKADKII LAQDLLNSRI SNIKNVNKSY GKPDPEPTLS QIEETHMVHF
NAHFKPYVPI GFEYNKVRPH TGTPTLGNKL TFGIPQYGDF FHDMVGHHIL GACHSSWQDA
PIQGSSQMGA HGQLQTFPRN GYDWDNQTPL EGAVYTLVDP FGRPIVPGTK NAYRNLVYYC
EYPGERLYEN VRFDVNGNSL DEYSSDVTTL VRKFCIPGDK MTGYKHLVGQ EVSVEGTSGP
LLCNVQDMHK PHQSKPILTD ENDTQRTCTH TNPKFLSQHF PENSHNIQTA GKQDITPITD
ATYLDIRRNV HYSCNGPQTP KYYQPPLALW IKLRFWFNEN VNLAIPSVSI PFGERFITIK
LASQKDLVNE FPGLFIRQSR FIPGRPSRRN IRFKPWFIPG VISEISLTNN ELYINNLFVT
PEIHNLFVKR VRFSLIRVHK TQVTHTNNNH HDEKLMSALK WPIEYMFIGL KPTWNISDQN
PHQHRDWHKF GHVVNAIMQP THHAEVSFQD RDTALPDACS SISDISPITY PITLPIIKNI
SVTAHGINLI DKFPSKFCSS YIPFHYGGNS IKTPDDPGAM MITFALKPRE EYQPSGHINV
SRAREFYISW DTDYVGSITT ADLVVSASAI NFLLLQNGSA VLRYST