ID   TRS1_HCMVM              Reviewed;         788 AA.
AC   Q6SVX2; D2K3Y4;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Protein TRS1;
GN   Name=TRS1;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
CC   -!- FUNCTION: Inhibits the establishment of the antiviral state in the
CC       infected cell. Prevents the phosphorylation of the host eukaryotic
CC       translation initiation factor eIF-2alpha/EIF2S1 and thus the shutoff of
CC       viral and cellular protein synthesis by directly interacting with
CC       EIF2AK2/PKR. Also inhibits host autophagy by interacting with host
CC       Beclin-1/BECN1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with host EIF2AK2/PKR; this interaction retains
CC       EIF2AK2 to the host nucleus and prevents its activation. Interaction
CC       (via N-terminus) with host BECN1; this interaction inhibits host
CC       autophagy. Interacts with the viral DNA polymerase accessory subunit
CC       UL44. Interacts with host HSPA5 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250}. Host cytoplasm
CC       {ECO:0000250}. Host nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae US22 family. {ECO:0000305}.
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DR   EMBL; AY446894; AAR31723.1; -; Genomic_DNA.
DR   RefSeq; YP_081619.1; NC_006273.2.
DR   BioGRID; 1678076; 1.
DR   PRIDE; Q6SVX2; -.
DR   GeneID; 3077523; -.
DR   KEGG; vg:3077523; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; TAS:Reactome.
DR   GO; GO:0030291; F:protein serine/threonine kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0039521; P:suppression by virus of host autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0039580; P:suppression by virus of host PKR signaling; IEA:UniProtKB-KW.
DR   GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
DR   InterPro; IPR003360; US22-like.
DR   Pfam; PF02393; US22; 2.
PE   3: Inferred from homology;
KW   Host cytoplasm; Host nucleus; Host-virus interaction;
KW   Inhibition of host autophagy by virus;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host interferon signaling pathway by virus;
KW   Inhibition of host PKR by virus; Reference proteome; Viral immunoevasion;
KW   Virion.
FT   CHAIN           1..788
FT                   /note="Protein TRS1"
FT                   /id="PRO_0000418273"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          610..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..634
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..663
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   788 AA;  83959 MW;  79DACA06405652E6 CRC64;
     MAQRNGMSPR PPPLGRGRGA GGPSGVGSSP PSSCVPMGAT STAGTGASAA PTATPGHGVH
     RVEPRGPPGA PPSSGNNSNF WHGPERLLLS QIPVERQALT ELEYQAMGAV WRAAFLANST
     GRAMRKWSQR DAGTLLPLGR PYGFYARVTP RSQMNGVGAT DLRQLSPRDA WIVLVATVVH
     EVDPAADPTV GDKAGHPEGL CAQDGLYLAL GAGFRVFVYD LANNTLILAA RDADEWFRHG
     AGEVVRLYRC NRLGVGTPRA TLLPQPALRQ TLLRAEEATA LGRELRRRWA GTTVALQTPG
     RRLQPMVLLG AWQELAQYEP FASAPHPASL LTAVRRHLNQ RLCCGWLALG AVLPARWLGC
     AAGPATGTTS PPAASGTETE AAGGDAPCAM AGAVGSAVTI PPQPYGGAGG SAICVPNADA
     HAVVGADATA AAAAAAAAPT VMVGPTAMAG PAASGTVPRA MLVVVLDELG AVFGYCPLDG
     HVYPLAAELS HFLRAGVLGA LALGRESAPA AEAARRLLPE LDREQWERPR WDALHLHPRA
     ALWAREPHGQ LAFLLRPGRG EAEVLTLATK HPVICANVED YLQDARRRAD AQALGLDLAT
     VVMEAGGQMI HKKTKKPKGK EDESVMKGKH SRYTRPTEPP LTPQASLGRA LRRDDEDWKP
     SRVPGEDSWY DLDETFWVLG SNRKNDVYQR RWKKTVLRCG LEIDRPMPTV PKGCRPQTFT
     HEGIQLMGGA TQEPLDTGLY APSHVTSAFV PSVYMPPTVP YPDPAARLCR DMRRVTFSNV
     ATHYHYNA