ID   MTP_EBVG                Reviewed;        1318 AA.
AC   Q3KSV4;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   24-JAN-2024, entry version 65.
DE   RecName: Full=Major tegument protein;
DE            Short=MTP;
DE   AltName: Full=Protein p140;
GN   ORFNames=BNRF1;
OS   Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Gammaherpesvirinae; Lymphocryptovirus;
OC   Lymphocryptovirus humangamma4.
OX   NCBI_TaxID=10376;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA   Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA   Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT   "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT   nasopharyngeal carcinoma patient.";
RL   J. Virol. 79:15323-15330(2005).
CC   -!- FUNCTION: Tegument protein that plays a role in the inhibition of host
CC       intrinsic defenses to promote viral early gene activation. Interacts
CC       with host DAXX and thereby disrupts the complex between DAXX and ATRX.
CC       Suppresses the DAXX-ATRX dependent deposition of histone H3.3 on viral
CC       chromatin allowing viral transcription. Targets also host SMC5/6 for
CC       proteasomal degradation in a CUL7 and calpain-dependent manner to
CC       support nuclear membrane-less replication compartment formation and
CC       lytic virus replication. {ECO:0000250|UniProtKB:P03179}.
CC   -!- SUBUNIT: Interacts with host DAXX; this interaction disrupts the
CC       chromatin remodeling complex ATRX:DAXX and thus allows viral
CC       transcription. Interacts with host SMC6; this interaction targets SMC5-
CC       SMC6 complex for proteasomal degradation.
CC       {ECO:0000250|UniProtKB:P03179}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument {ECO:0000250|UniProtKB:P03179}.
CC       Host nucleus {ECO:0000250|UniProtKB:P03179}. Note=Colocalizes with host
CC       DAXX at PML nuclear bodies. {ECO:0000250|UniProtKB:P03179}.
CC   -!- SIMILARITY: Belongs to the herpesviridae MTP family. {ECO:0000305}.
CC   -!- CAUTION: Controvertial experiments have localized MTP at the virion
CC       surface. {ECO:0000305}.
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DR   EMBL; AY961628; AAY41097.1; -; Genomic_DNA.
DR   SMR; Q3KSV4; -.
DR   Proteomes; UP000007641; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; IEA:UniProtKB-SubCell.
DR   GO; GO:0075733; P:intracellular transport of virus; IEA:InterPro.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1.
DR   Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR010077; Herpes_virus_tegument.
DR   InterPro; IPR010918; PurM-like_C_dom.
DR   InterPro; IPR036676; PurM-like_C_sf.
DR   InterPro; IPR036921; PurM-like_N_sf.
DR   InterPro; IPR024346; Tegument_herpes_virus_N.
DR   NCBIfam; TIGR01739; tegu_FGAM_synt; 1.
DR   PANTHER; PTHR10099; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   PANTHER; PTHR10099:SF1; PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   Pfam; PF13507; GATase_5; 1.
DR   Pfam; PF12818; Tegument_dsDNA; 1.
DR   SMART; SM01211; GATase_5; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR   SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Host nucleus; Host-virus interaction; Late protein; Virion;
KW   Virion tegument.
FT   CHAIN           1..1318
FT                   /note="Major tegument protein"
FT                   /id="PRO_0000382438"
SQ   SEQUENCE   1318 AA;  142800 MW;  10913AC520BB34A1 CRC64;
     MEERGRETQM PVARYGGPFI MVRLFGQDGE ANIQEQRLYE LLSDPRSALG LDPGPLIAEN
     LLLVALRGTN NDPRPQRQER ARELALVGIL LGNGEQGEHL GTESALEASG NNYVYAYGPD
     WMARPSTWSA EIQQFLRLLG ATYVLRVEMG RQFGFEVHRS RPSFRQFQAI NHLVLFDNAL
     RKYDSGQVAA GFQRALLVAG PETADTRPDL RKLNEWVFGG RAAGGRQLAD ELKIVSALRD
     TYSGHLVLQP TETLDTWKVL SRDTRTAHSL EHGFIHAAGT IQANCPQLFM RRQHPGLFPF
     VNAIASSLGW YYQTATGPGA DARAAARRQQ AFQTRAAAEC HAKSGVPVVA GFYRTINATL
     KGGEGLQPTM FNGELGAIKH QALDTVRYDY GHYLIMLGPF QPWSGLTAPP CPYAESSWAQ
     AAVQTALELF SALYPAPCIS GYARPPGPSA VIEHLRSLVP KGGLLLFLSH LPDDVKDGLG
     EMGPARATGP GMQQFVGSYF LNPACSNVFI TVRQRGEKIN GRTVLQALGR ACDMAGCQHY
     VLGSTVPLGG LNFVNDLASP VSTAEMMDDF SPFFTVEFPP IQEEGASSPV PLDVDESMDI
     SPSYELPWLS LESCLTSILS HPTVGSKEHL VRHTDRVSGG RVAQQPGVGP LDLPLADYAF
     VAHSQVWTRP GGAPPLPYRT WDRMTEKLLV SAKPGGENVK VSGTVITLGE QGYKVSLDLR
     EGTRLAMAEA LLNAAFAPIL DPEDVLLTLH LHLDPSRADN SAVMEAMTAA SDYARGLGVK
     LTFGSASCPE TGSSASSFMT VVASVSAPGE FSGPLITPVL QKTGSLLIAV RCGDGKIQGG
     SLFEQLFSDV ATTPRAPEAL SLKNLFRAVQ QLVKSGIVLS GHDISDGGLV TCLVEMALAG
     QRGVTITMPV ASDYLPEMFA EHPGLVFEVE ERSVGEVLQT LRSMNMYPAV LGRVGEQGPD
     QMFEVQHGPE TVLRQSLRLL LGTWSSFASE QYECLRPDRI NRSMHVSDYG YNEALAVSPL
     TGKNLSPRRL VTEPDPRCQV AVLCAPGTRG HESLLAAFTN AGCLCRRVFF REVRDNTFLD
     KYVGLAIGGV HGARDSALAG RATVALINRS PALRDAILKF LNRPDTFSVA LGELGVQVLA
     GLGAVGSTDN PPAPGVEVNV QRSPLILAPN ASGMFESRWL NISIPATTSS VMLRGLRGCV
     LPCWVQGSCL GLQFTNLGMP YVLQNAHQIA CHFHSNGTDA WRFAMNYPRN PTEQGNIAGL
     CSRDGRHLAL LCDPSLCTDF WQWEHIPPAF GHPTGCSPWT LMFQAAHLWS LRHGRPSE
//