ID   MCP_HHV6Z               Reviewed;        1345 AA.
AC   Q9QJ26;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-DEC-2020, entry version 51.
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=U57;
OS   Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=36351;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z29;
RX   PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA   Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA   Pellett P.E.;
RT   "Human herpesvirus 6B genome sequence: coding content and comparison with
RT   human herpesvirus 6A.";
RL   J. Virol. 73:8040-8052(1999).
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; AF157706; AAD49660.1; -; Genomic_DNA.
DR   RefSeq; NP_050238.1; NC_000898.1.
DR   PDB; 6Q1F; EM; 9.00 A; A/B/C/D/E/F/G/H/I/q/r/s/t/u/v/w=1-1345.
DR   PDBsum; 6Q1F; -.
DR   SMR; Q9QJ26; -.
DR   PRIDE; Q9QJ26; -.
DR   GeneID; 1497059; -.
DR   KEGG; vg:1497059; -.
DR   Proteomes; UP000006930; 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   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host nucleus; Reference proteome;
KW   T=16 icosahedral capsid protein; Virion.
FT   CHAIN           1..1345
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000408407"
SQ   SEQUENCE   1345 AA;  152107 MW;  80746387AFC2A573 CRC64;
     MENWQATEIL PKIEAPLNIF NDIKTYTAEQ LFDNLRIYFG DDPSRYNISF EALLGIYCNK
     IEWINFFTTP IAVAANVIRF NDVSRMTLGK VLFFIQLPRV ATGNDVTAPK ETTIMVAKHS
     EKHPINISFD LSAACLEHLE NTFKNTVIDQ ILNINALHTV LRSLKNSADS LERGLIHAFM
     QTLLRKSPPQ FIVLTMNENK VHNKQALSRV QRSNMFQSLK NRLLTSLFFL NRNNNSSYIY
     RILNDMMESV TESILNDTNN YTSKENIPLD GVLLGPIGSI QKLTNILSQY ISTQVVSAPI
     SYGHFIMGKE NAVTAIAYRA IMADFTQFTV NAGTEQQDTN NKSEIFDKSR AYADLKLNTL
     KLGDKLVAFD HLHKVYKNTD VNDPLEQSLQ LTFFFPLGIY IPTETGFSTM ETRVKLNDTM
     ENNLPTSVFF HNKDQVVQRI DFADILPSVC HPIVHDSTIV ERLMKNEPLP TGHRFSQLCQ
     LKITRENPTR ILQTLYNLYE SRQEVPKNTN VLKNELNVED FYKPDNPTLP TERHPFFDLT
     YIQKNRATEV LCTPRIMIGN MPLPLAPISF HEARTNQMLE HAKTNSHNYD FTLKIVTESL
     TSGSYPELAY VIEILVHGNK HAFMILKQVI SQCISYWFNM KHILLFCNSF EMIMLISNHM
     GDELIPGAAF AHYRNLVSLI RLVKRTISIS NINEQLCGEP LVNFANALFD GRLFCPFVHT
     MPRNDTNAKI TADDTPLTQN TVRVRNYEIS DVQRMNLIDS SVVFTDNDRP SNENTILSKI
     FYFCVLPALS NNKACGAGVN VKELVLDLFY TEPFICPDDC FQENPISSDV LMSLIREAMG
     PGYTVANTSS IAKQLFKSLI YINENTKILE VEVSLDPAQR HGNSVHFQSL QHILYNGLCL
     ISPITTLRRY YQPIPFHRFF SDPGICGTMN ADIQVFLNTF PHYQRNDGGF PLPPPLALEF
     YNWQRTPFSV YSAFCPNSLL SIMTLAAMHS KLSPVAIAIQ SKSKIHPGFA ATLVRTDNFD
     VECLLYSSRA ATSIILDDPT VTAEAKDIVT TYNFTQHLSF VDMGLGFSST TATANLKRIK
     SDMGSKIQNL FSAFPIHAFT NTDINTWIRH HVGIEKPNPS EGEALNIITF GGINKNPPSI
     LLHGQQAICE VILTPVTTNI NFFKLPHNPR GRESCMMGTD PHNEEAARKA LYDHTQTDSD
     TFAATTNPWA SLPGSLGDIL YNTAHREQLC YNPKTYSPNA QFFTESDILK TNKMMYKVIN
     EYCMKSNSCL NSDSEIQYSC SEGTDSFVSR PCQFLQNALP LHCSSNQALL ESRSKTGNTQ
     ISETHYCNYA IGETIPLQLI IESSI