ID   EBNA1_EBVG              Reviewed;         641 AA.
AC   Q3KSS4;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   23-FEB-2022, entry version 78.
DE   RecName: Full=Epstein-Barr nuclear antigen 1;
DE            Short=EBNA-1;
DE            Short=EBV nuclear antigen 1;
GN   Name=EBNA1; ORFNames=BKRF1;
OS   Epstein-Barr virus (strain GD1) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
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: Plays an essential role in replication and partitioning of
CC       viral genomic DNA during latent viral infection. During this phase, the
CC       circular double-stranded viral DNA undergoes replication once per cell
CC       cycle and is efficiently partitioned to the daughter cells. EBNA1
CC       activates the initiation of viral DNA replication through binding to
CC       specific sites in the viral latent origin of replication, oriP.
CC       Additionally, it governs the segregation of viral episomes by mediating
CC       their attachment to host cell metaphase chromosomes. Also activates the
CC       transcription of several viral latency genes. Finally, it can
CC       counteract the stabilization of host p53/TP53 by host USP7, thereby
CC       decreasing apoptosis and increasing host cell survival.
CC       {ECO:0000250|UniProtKB:P03211}.
CC   -!- SUBUNIT: Interacts with human USP7. Interacts with human EBP2; this
CC       interaction is important for the stable segregation of EBV episomes
CC       during cell division but not for the replication of the episomes.
CC       Interacts with BGLF4; this interaction facilitates the switch from
CC       latent to lytic DNA replication by down-regulating EBNA1 replication
CC       function. Interacts with human PAX5; this interaction promotes EBNA1-
CC       dependent transcription. {ECO:0000250|UniProtKB:P03211}.
CC   -!- INTERACTION:
CC       Q3KSS4; Q3KSS4: EBNA1; NbExp=2; IntAct=EBI-2621046, EBI-2621046;
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03211}.
CC   -!- SIMILARITY: Belongs to the herpesviridae EBNA1 family. {ECO:0000305}.
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DR   EMBL; AY961628; AAY41125.1; -; Genomic_DNA.
DR   PDB; 4PR5; X-ray; 1.80 A; C=407-417.
DR   PDB; 4PRD; X-ray; 1.75 A; C=407-417.
DR   PDB; 4PRH; X-ray; 2.50 A; C=407-417.
DR   PDB; 5T7X; X-ray; 2.35 A; A/B=459-607.
DR   PDBsum; 4PR5; -.
DR   PDBsum; 4PRD; -.
DR   PDBsum; 4PRH; -.
DR   PDBsum; 5T7X; -.
DR   SMR; Q3KSS4; -.
DR   IntAct; Q3KSS4; 7.
DR   Proteomes; UP000007641; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   GO; GO:0039588; P:suppression by virus of host antigen processing and presentation; IEA:UniProtKB-KW.
DR   GO; GO:0039644; P:suppression by virus of host NF-kappaB cascade; IEA:UniProtKB-KW.
DR   GO; GO:0019042; P:viral latency; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.390; -; 1.
DR   InterPro; IPR035975; E2/EBNA1_C_sf.
DR   InterPro; IPR004186; EBNA1_DNA-bd.
DR   InterPro; IPR037007; EBNA1_DNA-bd_sf.
DR   Pfam; PF02905; EBV-NA1; 1.
DR   SUPFAM; SSF54957; SSF54957; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; DNA-binding; Host nucleus; Host-virus interaction;
KW   Inhibition of host adaptive immune response by virus;
KW   Inhibition of host NF-kappa-B by virus;
KW   Inhibition of host proteasome antigen processing by virus; Transcription;
KW   Transcription regulation; Viral immunoevasion; Viral latency;
KW   Viral latency initiation and maintenance.
FT   CHAIN           1..641
FT                   /note="Epstein-Barr nuclear antigen 1"
FT                   /id="PRO_0000375932"
FT   REGION          1..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..478
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..450
FT                   /note="Interaction with USP7"
FT                   /evidence="ECO:0000250"
FT   REGION          612..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..381
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        619..641
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   TURN            412..414
FT                   /evidence="ECO:0007829|PDB:4PR5"
FT   HELIX           476..489
FT                   /evidence="ECO:0007829|PDB:5T7X"
FT   STRAND          503..512
FT                   /evidence="ECO:0007829|PDB:5T7X"
FT   HELIX           514..527
FT                   /evidence="ECO:0007829|PDB:5T7X"
FT   STRAND          537..540
FT                   /evidence="ECO:0007829|PDB:5T7X"
FT   STRAND          556..567
FT                   /evidence="ECO:0007829|PDB:5T7X"
FT   HELIX           569..584
FT                   /evidence="ECO:0007829|PDB:5T7X"
FT   HELIX           590..592
FT                   /evidence="ECO:0007829|PDB:5T7X"
FT   STRAND          593..604
FT                   /evidence="ECO:0007829|PDB:5T7X"
SQ   SEQUENCE   641 AA;  56731 MW;  8AFF6E7AB7D40EDD CRC64;
     MSDEGPGTGP GNGLGQKEDS SGPEGSGGSG PQRRGGDNHG RGRGRGRGRG GGRPGAPGGS
     GSGPRHRDGV RRPQKRPSCI GCKGAHGGTG SGAGAGGAGA GGAGAGGGAG AGGGAGGAGG
     AGGAGAGGGA GAGGGAGGAG GAGAGGGAGA GGGAGGAGAG GGAGGAGGAG AGGGAGAGGG
     AGGAGAGGGA GGAGGAGAGG GAGAGGAGGA GGAGAGGAGA GGGAGGAGGA GAGGAGAGGA
     GAGGAGAGGA GGAGAGGAGG AGAGGAGGAG AGEEAGGAGA GGGAGGAGAG GAGGAGAGGA
     GGAGAGGAGG AGAGGGAGAG GAGAGGGGRG RGGSGGRGRG GSGGRGRGGS GGRRGRGRER
     ARGRSRERAR GRGRGRGEKR PRSPSSQSSS SGSPPRRPPP GRRPFFHPVG DADYFEYLQE
     GGPDGEPDVP PGAIEQGPTD DPGEGPSTGP RGQGDGGRRK KGGWFGKHRG QGGSNPKFEN
     IAEGLRVLLA RSHVERTTEE GNWVAGVFVY GGSKTSLYNL RRGIALAVPQ CRITPLSRLP
     FGMAPGPGPQ PGPLRESIVC YFMVFLQTHI FAEVLKDAIK DLVMTKPAPT CNIKVTVCSF
     DDGVDLPPWF PPMVEGAAAE GDDGDDGDEG GDGDEGEEGQ E