ID   DPOL_EBVA8              Reviewed;        1015 AA.
AC   Q1HVC1;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   23-FEB-2022, entry version 71.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
GN   ORFNames=BALF5;
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: 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 (By similarity). {ECO:0000250}.
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 major DNA-binding protein BALF2, the
CC       DNA 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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus. Note=the protein is present at
CC       discrete sites in nuclei, called replication compartments where viral
CC       DNA replication occurs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; DQ279927; ABB89286.1; -; Genomic_DNA.
DR   RefSeq; YP_001129507.1; NC_009334.1.
DR   SMR; Q1HVC1; -.
DR   IntAct; Q1HVC1; 5.
DR   MINT; Q1HVC1; -.
DR   PRIDE; Q1HVC1; -.
DR   GeneID; 5176180; -.
DR   KEGG; vg:5176180; -.
DR   Proteomes; UP000007639; 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:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome 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   3: Inferred from homology;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Host nucleus;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1015
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000375925"
SQ   SEQUENCE   1015 AA;  113432 MW;  221FC425B2542EC9 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 TLRFAEALAA
     HTTRSLFVAP ISLEAEKTFS CLMLITKKRY VGVLTDGKTL MKGVELVRKT ACKFVQTRCR
     RVLDLVLADA RVKEAASLLS HRPFQESFTQ GLPVGFLPVI DILNQAYTDL REGRVPMGEL
     CFSTELSRKL SAYKSTQMPH LAVYQKFVER NEELPQIHDR IQYVFVEPKG GVKGARKTEM
     AEDPAYAERH GVPVAVDHYF DKLLQGAANI LQCLFDNNSG AALSVLQNFT ARPPF