ID   MCP_PSHV1               Reviewed;        1413 AA.
AC   Q6UDI4;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 47.
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=UL19;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(2006).
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; AY372243; AAQ73726.1; -; Genomic_DNA.
DR   RefSeq; NP_944420.1; NC_005264.1.
DR   SMR; Q6UDI4; -.
DR   PRIDE; Q6UDI4; -.
DR   GeneID; 2657004; -.
DR   KEGG; vg:2657004; -.
DR   Proteomes; UP000006840; 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..1413
FT                   /note="Major capsid protein"
FT                   /id="PRO_0000406817"
SQ   SEQUENCE   1413 AA;  154177 MW;  603E21B15DEE43F4 CRC64;
     MDGHGCSSSQ AMCRGAFGNV ATRPAPFPRS AAPFVVAGES LGALRDKCHA YFYDSFSSFT
     GVDCCYGSRF DILLGSYFNT ITLSHFLETG LSIACICVKF PELKYAEDGI VQFVVANPMI
     ARSDCEVPSR PSYTYVTKKW SRTTLTSSLS ICGPALELLT GDALDGTEIA NFSRARAMNQ
     LARDLKLTLD SFERGTVHHV LGILIRKAPP MPLLQPLMAA MARERDMNVV ARANILSAMK
     NAVREHLFFM DKESRGDPQD IARGLLSLIN CTLPSVSDTR VTHVGPGGRP IDGVLVTTEA
     VKGLVTQALT LTASEATVPA MYGELSISGT NLVTALLMGK AIRNFNEAAR NLLNFADGNV
     DVSDFPDIPQ DGEDAPRTMS VNMSLVTVGD SLVAVEALER IYARTGVPYP LAGNVDLTFF
     FPLGLFKPHK DRYAIGGLIL PDTAEAAVDG RLFPPTEMFF FDKDEQLRSV SFESSLGTVA
     HPIAHGIMET LQELSQEQWV QARPPAPMDF TIQRMSQQPP RAQMVEFLTA VATAVTAPHP
     SATLINRRST DQFLSHTNPF LQLEVHPFYD VYRVAQDLQT PSDAALFAPV EPSTLAASRR
     LCNGDIPLPL SSADFRSSRG RQLAACGAML SSQAAAAIET TLSDPNYPVA FYVIEACLHG
     DETLFLESQR LVAQCIESYW VSAGGLAFVN SFAMIMYITH NLSSLVNRNC HALYAEIVAV
     LNSMRAAVSR FTQSGDALLQ HTQEELNHLL MDPAVFPPIL YDCDPIIRVT GAYAARNITI
     RTLGERAPVV STRDWPPQAD FGAINITLNH GPPYTARGRA DGGAHHDSEW TVLNKIFYYA
     LLPALARGRC CSVGVEFEMV YNLINTTRLP ANADDLAAPE ANPLHVNNLA PDSFNALLHN
     SGVALVDAEA LVAFIAAARL RQVAHTLPLR VSYSADPGFA TIDSPNTAFT DGVLYNGLIM
     MNYPQYDATL VASRYFYALP VNGFYANRTI VEATHRGAVN LGEVPEDLPL VPTFLGAEAY
     RSIRAPSYMY CAKQCASGTA SAGAVAYGLM AGYFKTSPVA LTHQLKSGLH PGFALTVARQ
     DRFYADQILF ARRLSESYYM GAPTTESRAE NNSLMIDIHQ PRSHVDMGLG FTASRMPAKL
     NTVVTDMGSR SQNLFDARYP GQFRYLEVAD FIASEITDDD SLAMPRARPP LMLPYEAPPL
     PPCLERGQRA TCEFLITPVT ADLKYFYGPA NPRGRSSCVA CMPHEDPSRD SVDRAMYDHT
     TPDAAFPSRA TNNPWASQRF SLGDRMYNAR RGFIVTSDFF SPLGKFMTPS RVEDKNRCLA
     RLLRESATAV SSVTGNTEFQ FVAPVGSNEL ITDPCAIFQE AYPILCASDK ALFASYENPR
     KAVGTGAREN HFAQYLIHDA SPLSGVLKCN GKL