MTP_EBVA8
ID MTP_EBVA8 Reviewed; 1318 AA.
AC Q1HVJ0;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 23-FEB-2022, entry version 63.
DE RecName: Full=Major tegument protein;
DE Short=MTP;
DE AltName: Full=Protein p140;
GN ORFNames=BNRF1;
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: 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. May also play a role in virus
CC entry at attachment or membrane fusion steps.
CC {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. {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; DQ279927; ABB89216.1; -; Genomic_DNA.
DR RefSeq; YP_001129438.1; NC_009334.1.
DR PDB; 5KDM; X-ray; 3.50 A; D=381-599.
DR PDBsum; 5KDM; -.
DR SMR; Q1HVJ0; -.
DR PRIDE; Q1HVJ0; -.
DR GeneID; 5176185; -.
DR KEGG; vg:5176185; -.
DR Proteomes; UP000007639; 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; 3.30.1330.10; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 3.90.650.10; -; 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 Pfam; PF02769; AIRS_C; 1.
DR Pfam; PF12818; Tegument_dsDNA; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR SUPFAM; SSF55326; SSF55326; 1.
DR SUPFAM; SSF56042; SSF56042; 1.
DR TIGRFAMs; TIGR01739; tegu_FGAM_synt; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host nucleus; Host-virus interaction; Late protein;
KW Reference proteome; Virion; Virion tegument.
FT CHAIN 1..1318
FT /note="Major tegument protein"
FT /id="PRO_0000382437"
FT STRAND 393..398
FT /evidence="ECO:0007829|PDB:5KDM"
FT HELIX 415..433
FT /evidence="ECO:0007829|PDB:5KDM"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:5KDM"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:5KDM"
FT STRAND 460..468
FT /evidence="ECO:0007829|PDB:5KDM"
FT HELIX 473..476
FT /evidence="ECO:0007829|PDB:5KDM"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:5KDM"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:5KDM"
FT STRAND 508..512
FT /evidence="ECO:0007829|PDB:5KDM"
FT HELIX 524..534
FT /evidence="ECO:0007829|PDB:5KDM"
FT STRAND 539..548
FT /evidence="ECO:0007829|PDB:5KDM"
FT STRAND 550..554
FT /evidence="ECO:0007829|PDB:5KDM"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:5KDM"
FT TURN 563..566
FT /evidence="ECO:0007829|PDB:5KDM"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:5KDM"
SQ SEQUENCE 1318 AA; 142856 MW; 891F86C984F4F838 CRC64;
MEDRGRETQM 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
VSAIASSLGW YYQTATGPGA DARAAARRQQ AFQTRAAAEC HAKSGVPVVA GFYRTINATL
KGGEGLQPTM FNGELGAIKH QALDTVRYDY GHYLIMLGPF QPWSGLTAPP CPYAESSWAQ
AAVQTALELF SALYPAPCIS GYARPPGPSA VIEHLGSLVP KGGLLLFLSH LPDDVKDGLG
EMGPARATGP GMQQFVSSYF LNPACSNVFI TVRQRGEKIN GRTVLQALGR ACDMAGCQHY
VLGSTVPLGG LNFVNDLASP VSTAEMMDDF SPFFTVEFPP IQEEGARSPV PLDVDESMDI
SPSYELPWLS LESCLTSILS HPTVGSKEHL VRHTDRVSGG RVAQQPGVGP LDLPLADYAF
VAHSQVWTRP GGAPPLPYRT WDRMTEKLLV SAKPGGENVK VSGTVITLGE QGYKVSLDLR
EGTRLAMAEA LLNAAFAPIL DPEDVLLTLH LHLDPRRADN SVVMEAMTAA 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