ID   EAD_EBVA8               Reviewed;         404 AA.
AC   P0C6Z0; Q777F9;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   02-JUN-2021, entry version 48.
DE   RecName: Full=DNA polymerase processivity factor BMRF1;
DE   AltName: Full=Early antigen protein D;
DE            Short=EA-D;
DE   AltName: Full=Polymerase accessory subunit;
GN   ORFNames=BMRF1;
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: Plays an essential role in the viral lytic DNA replication by
CC       acting as the polymerase accessory subunit. Stimulates the viral DNA
CC       polymerase activity and appears to function with it as a holoenzyme.
CC       Increases the processivity of the viral polymerase, probably by acting
CC       as a sliding clamp that prevents dissociation of the polymerase from
CC       the active template. In addition, BMRF1 transcriptionally activates the
CC       early BHLF1 promoter (By similarity). {ECO:0000250|UniProtKB:P03191}.
CC   -!- SUBUNIT: Homodimer. Homooligomerizes and adopts an oligomeric ring-
CC       shaped structure composed of 6 subunits. Forms a complex with the DNA-
CC       binding protein BALF2, the DNA polymerase subunit BALF5, and the
CC       alkaline exonuclease BGLF5. Interacts with BZLF1; this interaction may
CC       inhibit BZLF1-induced transcription of the BMRF1 promoter (By
CC       similarity). {ECO:0000250|UniProtKB:P03191}.
CC   -!- SUBCELLULAR LOCATION: Virion tegument. Host nucleus. Note=BMRF1 shows
CC       homogeneous, not dot-like, distribution in the replication
CC       compartments, which coincides with the newly synthesized viral DNA.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylated by the viral BGLF4 kinase.
CC       {ECO:0000250|UniProtKB:P03191}.
CC   -!- SIMILARITY: Belongs to the herpesviridae DNA polymerase accessory
CC       subunit family. {ECO:0000305}.
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DR   EMBL; DQ279927; ABB89234.1; -; Genomic_DNA.
DR   RefSeq; YP_001129454.1; NC_009334.1.
DR   RefSeq; YP_401657.1; NC_007605.1.
DR   SMR; P0C6Z0; -.
DR   DNASU; 3783718; -.
DR   GeneID; 3783718; -.
DR   GeneID; 5176169; -.
DR   KEGG; vg:3783718; -.
DR   KEGG; vg:5176169; -.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   InterPro; IPR007013; DNA_pol_proc_fac_herpes.
DR   Pfam; PF04929; Herpes_DNAp_acc; 1.
PE   3: Inferred from homology;
KW   Activator; Disulfide bond; DNA-binding; Early protein; Host nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Virion; Virion tegument.
FT   CHAIN           1..404
FT                   /note="DNA polymerase processivity factor BMRF1"
FT                   /id="PRO_0000375930"
FT   REGION          302..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..357
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         337
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03191"
FT   MOD_RES         344
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P03191"
FT   MOD_RES         349
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P03191"
FT   MOD_RES         355
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P03191"
FT   DISULFID        95
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P03191"
FT   DISULFID        206
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250|UniProtKB:P03191"
SQ   SEQUENCE   404 AA;  43374 MW;  533B5D5ECC05F960 CRC64;
     METTQTLRFK TKALAVLSKC YDHAQTHLKG GVLQVNLLSV NYGGPRLAAV ANAGTAGLIS
     FEVSPDAVAE WQNHQSPEEA PAAVSFRNLA YGRTCVLGKE LFGSAVEQAS LQFYKRPQGG
     SRPEFVKLTM EYDDKVSKSH HTCALMPYMP PASDRLRNEQ MIGQVLLMPK TASSLQKWAR
     QQGSGGVKVT LNPDLYVTTY TSGEACLTLD YKPLSVGPYE AFTGPVAKAQ DVGAVEAHVV
     CSVAADSLAA ALSLCRIPAV SVPILRFYRS GIIAVVAGLL TSAGDLPLDL SVILFNHASE
     EAAASTASEP EDKSPRVQPL GTGLQQRPRH TVSPSPSPPP PPRTPTWESP ARPETPSPAI
     PSHSSNTALE RPLAVQLARK RTSSEARQKQ KHPKKVKQAF NPLI