CVC2_EBVA8
ID CVC2_EBVA8 Reviewed; 570 AA.
AC P0C705; Q777B7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Capsid vertex component 2 {ECO:0000255|HAMAP-Rule:MF_04025};
GN Name=CVC2 {ECO:0000255|HAMAP-Rule:MF_04025}; ORFNames=BVRF1;
OS Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
CC -!- FUNCTION: Capsid vertex-specific component that plays a role during
CC viral DNA encapsidation, assuring correct genome cleavage and
CC presumably stabilizing capsids that contain full-length viral genomes.
CC Participates in the interaction between the capsid and the tegument
CC through interaction with the large tegument protein/LTP.
CC {ECO:0000255|HAMAP-Rule:MF_04025}.
CC -!- SUBUNIT: Heterodimerizes with CVC1. Interacts with major capsid
CC protein/MCP and triplex capsid protein 1/TRX1 at the pentamer vertices.
CC Interacts with the large tegument protein/LTP. {ECO:0000255|HAMAP-
CC Rule:MF_04025}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04025}. Host
CC nucleus {ECO:0000255|HAMAP-Rule:MF_04025}.
CC -!- SIMILARITY: Belongs to the herpesviridae CVC2 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04025}.
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DR EMBL; DQ279927; ABB89279.1; -; Genomic_DNA.
DR RefSeq; YP_001129499.1; NC_009334.1.
DR RefSeq; YP_401703.1; NC_007605.1.
DR SMR; P0C705; -.
DR DNASU; 3783732; -.
DR GeneID; 3783732; -.
DR GeneID; 5176157; -.
DR KEGG; vg:3783732; -.
DR KEGG; vg:5176157; -.
DR Proteomes; UP000007639; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0019072; P:viral genome packaging; IEA:UniProtKB-UniRule.
DR GO; GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04025; HSV_CVC2; 1.
DR InterPro; IPR002493; Herpes_UL25.
DR Pfam; PF01499; Herpes_UL25; 1.
PE 3: Inferred from homology;
KW Capsid protein; Host nucleus; Host-virus interaction; Reference proteome;
KW Viral genome packaging; Viral penetration into host nucleus;
KW Viral release from host cell; Virion; Virus entry into host cell.
FT CHAIN 1..570
FT /note="Capsid vertex component 2"
FT /id="PRO_0000408261"
FT REGION 1..54
FT /note="Interaction with major capsid protein/MCP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04025"
FT REGION 102..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 62461 MW; 7D8D7B9E67064BAB CRC64;
MALSGHVLID PARLPRDTGP ELMWAPSLRN SLRVSPEALE LAEREAERAR SERWDRCAQV
LKNRLLRVEL DGIMRDHLAR AEEIRQDLDA VVAFSDGLES MQVRSPSTGG RSAPAPPSPS
PAQPFTRLTG NAQYAVSISP TDPPLMVAGS LAQTLLGNLY GNINQWVPSF GPWYRTMSAN
AMQRRVFPKQ LRGNLNFTNS VSLKLMTEVV AVLEGTTQDF FSDVRHLPDL QAALILSVAY
LLLQGGSSHQ QRPLPASREE LLELGPESLE KIIADLKAKS PGGNFMILTS GNKEARQSIA
PLNRQAAYPP GTFADNKIYN LFVGAGLLPT TAALNVPGAA GRDRDLVYRI ANQIFGEDVP
PFSSHQWNLR VGLAALEALM LVYTLCETAN LAEAATRRLH LSSLLPQAMQ RRKPAMASAG
MPGAYPVQTL FRHGELFRFI WAHYVRPTVA ADPQASISSL FPGLVLLALE LKLMDGQAPS
HYAINLTGQK FDTLFEIINQ KLLFHDPAAM LAARTQLRLA FEDGVGVALG RPSPMLAARE
ILERQFSASD DYDRLYFLTL GYLASPVAPS