ID   DPOL_EBVB9              Reviewed;        1015 AA.
AC   P03198; Q777B1;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
GN   ORFNames=BALF5;
OS   Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=10377;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6092825;
RA   Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.;
RT   "Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8
RT   Epstein-Barr virus.";
RL   Mol. Biol. Med. 1:21-45(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6087149; DOI=10.1038/310207a0;
RA   Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA   Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA   Tuffnell P.S., Barrell B.G.;
RT   "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL   Nature 310:207-211(1984).
RN   [3]
RP   INTERACTION WITH BALF2, BMRF1, AND BGL5.
RX   PubMed=9434720; DOI=10.1006/viro.1997.8891;
RA   Zeng Y., Middeldorp J., Madjar J.J., Ooka T.;
RT   "A major DNA binding protein encoded by BALF2 open reading frame of
RT   Epstein-Barr virus (EBV) forms a complex with other EBV DNA-binding
RT   proteins: DNAase, EA-D, and DNA polymerase.";
RL   Virology 239:285-295(1997).
RN   [4]
RP   INTERACTION WITH THE PUTATIVE PRIMASE-HELICASE COMPLEX.
RX   PubMed=10684269; DOI=10.1128/jvi.74.6.2550-2557.2000;
RA   Fujii K., Yokoyama N., Kiyono T., Kuzushima K., Homma M., Nishiyama Y.,
RA   Fujita M., Tsurumi T.;
RT   "The Epstein-Barr virus pol catalytic subunit physically interacts with the
RT   BBLF4-BSLF1-BBLF2/3 complex.";
RL   J. Virol. 74:2550-2557(2000).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15731235; DOI=10.1128/jvi.79.6.3409-3418.2005;
RA   Daikoku T., Kudoh A., Fujita M., Sugaya Y., Isomura H., Shirata N.,
RA   Tsurumi T.;
RT   "Architecture of replication compartments formed during Epstein-Barr virus
RT   lytic replication.";
RL   J. Virol. 79:3409-3418(2005).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 628-641 IN COMPLEX WITH
RP   HLA-DRA/HLA-DRB5 HETERODIMER.
RX   PubMed=12244309; DOI=10.1038/ni835;
RA   Lang H.L.E., Jacobsen H., Ikemizu S., Andersson C., Harlos K., Madsen L.,
RA   Hjorth P., Sondergaard L., Svejgaard A., Wucherpfennig K., Stuart D.I.,
RA   Bell J.I., Jones E.Y., Fugger L.;
RT   "A functional and structural basis for TCR cross-reactivity in multiple
RT   sclerosis.";
RL   Nat. Immunol. 3:940-943(2002).
CC   -!- FUNCTION: Replicates viral genomic DNA in the late phase of lytic
CC       infection, producing long concatemeric DNA. The replication complex is
CC       composed of six viral proteins: the DNA polymerase, processivity
CC       factor, primase, primase-associated factor, helicase, and ssDNA-binding
CC       protein.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC   -!- SUBUNIT: Forms a complex with the ssDNA-binding protein BALF2, the DNA
CC       polymerase processivity factor BMRF1, and the alkaline exonuclease
CC       BGLF5. Interacts with the putative helicase-primase complex composed of
CC       BBLF4, BSLF1 and BBLF2/3 proteins; these interactions may coordinate
CC       leading and lagging strand DNA synthesis at the replication fork.
CC       {ECO:0000269|PubMed:10684269, ECO:0000269|PubMed:12244309,
CC       ECO:0000269|PubMed:9434720}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000269|PubMed:15731235}.
CC       Note=the protein is present at discrete sites in nuclei, called
CC       replication compartments where viral DNA replication occurs.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; V01555; CAA24805.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53462.1; -; Genomic_DNA.
DR   PIR; A00713; DJBE2L.
DR   RefSeq; YP_401712.1; NC_007605.1.
DR   PDB; 1H15; X-ray; 3.10 A; C/F=628-641.
DR   PDBsum; 1H15; -.
DR   SMR; P03198; -.
DR   BioGRID; 971723; 3.
DR   PRIDE; P03198; -.
DR   DNASU; 3783681; -.
DR   GeneID; 3783681; -.
DR   KEGG; vg:3783681; -.
DR   EvolutionaryTrace; P03198; -.
DR   Proteomes; UP000153037; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 1.
DR   InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR   InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR   InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR   InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW   Early protein; Host nucleus; Nucleotidyltransferase; Reference proteome;
KW   Transferase; Viral DNA replication.
FT   CHAIN           1..1015
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000046505"
SQ   SEQUENCE   1015 AA;  113418 MW;  0503B5E269399812 CRC64;
     MSGGLFYNPF LRPNKGLLKK PDKEYLRLIP KCFQTPGAAG VVDVRGPQPP LCFYQDSLTV
     VGGDEDGKGM WWRQRAQEGT ARPEADTHGS PLDFHVYDIL ETVYTHEKCA VIPSDKQGYV
     VPCGIVIKLL GRRKADGASV CVNVFGQQAY FYASAPQGLD VEFAVLSALK ASTFDRRTPC
     RVSVEKVTRR SIMGYGNHAG DYHKITLSHP NSVCHVATWL QDKHGCRIFE ANVDATRRFV
     LDNDFVTFGW YSCRRAIPRL QHRDSYAELE YDCEVGDLSV RREDSSWPSY QALAFDIECL
     GEEGFPTATN EADLILQISC VLWSTGEEAG RYRRILLTLG TCEDIEGVEV YEFPSELDML
     YAFFQLIRDL SVEIVTGYNV ANFDWPYILD RARHIYSINP ASLGKIRAGG VCEVRRPHDA
     GKGFLRANTK VRITGLIPID MYAVCRDKLS LSDYKLDTVA RHLLGAKKED VHYKEIPRLF
     AAGPEGRRRL GMYCVQDSAL VMDLLNHFVI HVEVAEIAKI AHIPCRRVLD DGQQIRVFSC
     LLAAAQKENF ILPMPSASDR DGYQGATVIQ PLSGFYNSPV LVVDFASLYP SIIQAHNLCY
     STMITPGEEH RLAGLRPGED YESFRLTGGV YHFVKKHVHE SFLASLLTSW LAKRKAIKKL
     LAACEDPRQR TILDKQQLAI KCTCNAVYGF TGVANGLFPC LSIAETVTLQ GRTMLERAKA
     FVEALSPANL QALAPSPDAW APLNPEGQLR VIYGDTDSLF IECRGFSESE TLRFADALAA
     HTTRSLFVAP ISLEAEKTFS CLMLITKKRY VGVLTDGKTL MKGVELVRKT ACKFVQTRCR
     RVLDLVLADA RVKEAASLLS HRPFQESFTQ GLPVGFLPVI DILNQAYTDL REGRVPMGEL
     CFSTELSRKL SAYKSTQMPH LAVYQKFVER NEELPQIHDR IQYVFVEPKG GVKGARKTEM
     AEDPAYAERH GVPVAVDHYF DKLLQGAANI LQCLFDNNSG AALSVLQNFT ARPPF