ID   MCP_ALHV1               Reviewed;        1370 AA.
AC   O36375;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   02-DEC-2020, entry version 60.
DE   RecName: Full=Major capsid protein {ECO:0000255|HAMAP-Rule:MF_04016};
DE            Short=MCP {ECO:0000255|HAMAP-Rule:MF_04016};
GN   Name=MCP {ECO:0000255|HAMAP-Rule:MF_04016}; Synonyms=25;
OS   Alcelaphine herpesvirus 1 (strain C500) (AlHV-1) (Malignant catarrhal fever
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Macavirus.
OX   NCBI_TaxID=654901;
OH   NCBI_TaxID=9927; Connochaetes taurinus (Blue wildebeest).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9261371; DOI=10.1128/jvi.71.9.6517-6525.1997;
RA   Ensser A., Pflanz R., Fleckenstein B.;
RT   "Primary structure of the alcelaphine herpesvirus 1 genome.";
RL   J. Virol. 71:6517-6525(1997).
CC   -!- FUNCTION: Self-assembles to form an icosahedral capsid with a T=16
CC       symmetry, about 200 nm in diameter, and consisting of 150 hexons and 12
CC       pentons (total of 162 capsomers). Hexons form the edges and faces of
CC       the capsid and are each composed of six MCP molecules. In contrast, one
CC       penton is found at each of the 12 vertices. Eleven of the pentons are
CC       MCP pentamers, while the last vertex is occupied by the portal complex.
CC       The capsid is surrounded by a layer of proteinaceous material
CC       designated the tegument which, in turn, is enclosed in an envelope of
CC       host cell-derived lipids containing virus-encoded glycoproteins.
CC       {ECO:0000255|HAMAP-Rule:MF_04016}.
CC   -!- SUBUNIT: Homomultimer. Makes the hexons and eleven out of twelve
CC       pentons. Interacts with triplex proteins 1/TRX1 and 2/TRX2; adjacent
CC       capsomers are linked together in groups of three by triplexes,
CC       heterotrimeric complexes composed of one molecule of TRX1 and two
CC       molecules of TRX2. Interacts with scaffold protein; this interaction
CC       allows efficient MCP transport to the host nucleus. Interacts with
CC       capsid vertex component 2/CVC2. Interacts with the small capsomere-
CC       interacting protein/SCP. {ECO:0000255|HAMAP-Rule:MF_04016}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04016}. Host
CC       nucleus {ECO:0000255|HAMAP-Rule:MF_04016}.
CC   -!- SIMILARITY: Belongs to the herpesviridae major capsid protein family.
CC       {ECO:0000255|HAMAP-Rule:MF_04016}.
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DR   EMBL; AF005370; AAC58072.1; -; Genomic_DNA.
DR   PIR; T03120; T03120.
DR   RefSeq; NP_065524.1; NC_002531.1.
DR   SMR; O36375; -.
DR   PRIDE; O36375; -.
DR   GeneID; 911741; -.
DR   KEGG; vg:911741; -.
DR   Proteomes; UP000000941; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0039622; C:T=16 icosahedral viral capsid; IEA:UniProtKB-UniRule.
DR   GO; GO:0005198; F:structural molecule activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_04016; HSV_MCP; 1.
DR   InterPro; IPR000912; Herpes_MCP.
DR   InterPro; IPR023233; Herpes_MCP_upper_sf.
DR   Pfam; PF03122; Herpes_MCP; 1.
DR   PRINTS; PR00235; HSVCAPSIDMCP.
DR   SUPFAM; SSF103417; SSF103417; 1.
PE   3: Inferred from homology;
KW   Capsid protein; Host nucleus; Reference proteome;
KW   T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1370
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000405715"
SQ   SEQUENCE   1370 AA;  153358 MW;  7F53E311761A5B9D CRC64;
     MEVCRLENRP LPHAAVEANL LRQVKESAAE GLFKSFQLLV GKDVRENSVR FEVLLGVYAN
     VIEFVKFLET GLAASCINTE FRDLKRMVDG KIQFKVSVPT IAHSDGRRPN KQRQYIVMKC
     TSKHHISAEI ELAIADLENM HMEPETDLDM LEYIGTVKTV TSALQFGIDA LERGLIDTVL
     SVKLRHAPPL FILQSLSDPT LTERGLKKSI KSDLVSMFKD HLITHSFFIN KAEALATPRQ
     YILGMLSSII NSVSKETVFK GTSTYTTSSG EPVAGVIETT DAILNKLLTL LGEYKTEVVG
     PAAYASYVVR GENLVTAVSY GRAMRSFEQF KNKLVDDPVG QAGSLDKNAD SDNEYSSLPQ
     TTIPVSVVKV GSQPVIVESI QKMYNEAQAP FPLNRRMQYT YFFPLGLFIP RPKYTTSTSV
     KLEDDSCLSS EVWVVNKTNT PLCFNYQNAL RTLCHPRVNS PSACLQELQR SNLADNALEA
     FRDGLRSRPM DNMNLFAHVR RFYLKRTEVV LLPIAQKCNL STDDLLHPTN HKLLQLELHP
     LFDFVVERVA AEEAAFRATH RTFSGNIPQP LAPNQFQDSR GKQFEAATSL QHAVDDATLE
     VIRSTAFDPT YPFICYIVEA MIHGQPEKFT MNIPFISLCI NTYWDNSGNL AFINSFFMVK
     NICTHMGGGL INRDAYALYR KILGEVVAIK HAIVRMCGAE QLGNNELQGY VNGLLDRQLL
     PPFAYRDTFA QLDNRGARFV IGAKEHDNSQ AFVHALPDFE NANQVAPAMY HTRNTFNWDT
     FEYITVSNGN NDADAADLEK IYYYVMLPVC TNGHMCGMGA DFENIAIVLG YNIPVFDIPQ
     FNGDDTVLEH LENGPLRDIL IASEVNPTAD MLRMMIVSYL NCPQMTQVVR VKTRRDHCQN
     LGPEQGAIIE HTVMVNGFVC FGIPERMKQV AKNMFYPVPF HRFYCDPLVA GSWDNHIQNY
     VMNNFSQRSL EAFNAPPGIM ADYAEWHKAP MAKYITSCKA STASLSAFTV MHNKLSPIAF
     IVQAKHKIHP GFALTVLRTD EVLAENVMFS ARASTSVFVG RPTVSRREVR ADAVSFEVNH
     ELATIETGLS YSSVVTPAHV ASITTDMGIY CQNLFSIFSN EIYDHADVNN YVARKIGVED
     AVNRHNPRAL IAGVGQISHP PGLVHGQYAT CEVIPTPVTA DVAYFQKSNS PRGRASCVVS
     SDINNQERAE QFLYDHSLPD PAYEYRSTVN PWASQKGSLG DVLYGSRYRQ VSSPGIYSPS
     KPFFNKEEML KNNRSFYTLV NEYAQRLAGY AATSCTDLQY VVINGTDVFL EQPCLFLQEA
     FPTLSASHRV LLDEYMSFKN THAPVHMGHY FIEEVAPVKR VFKIGNKVAS