ID   DPOL_EHV1B              Reviewed;        1220 AA.
AC   P28858; Q6DLI1;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   23-FEB-2022, entry version 118.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
DE            EC=3.1.26.4;
GN   OrderedLocusNames=30;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
CC   -!- FUNCTION: Replicates viral genomic 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. Additionally, the polymerase contains an intrinsic
CC       ribonuclease H (RNase H) activity that specifically degrades RNA/DNA
CC       heteroduplexes or duplex DNA substrates in the 5' to 3' direction.
CC       Therefore, it can catalyze the excision of the RNA primers that
CC       initiate the synthesis of Okazaki fragments at a replication fork
CC       during viral DNA replication (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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC   -!- SUBUNIT: Forms a complex with the ssDNA-binding protein, the DNA
CC       polymerase processivity factor, and the alkaline exonuclease. Interacts
CC       with the helicase-primase complex composed of the primase, the helicase
CC       and the primase-associated factor; this interaction may coordinate
CC       leading and lagging strand DNA synthesis at the replication fork (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Note=The protein is
CC       present at discrete sites in nuclei, called replication compartments
CC       where viral DNA replication occurs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; AY665713; AAT67287.1; -; Genomic_DNA.
DR   PIR; D36798; DJBEC3.
DR   RefSeq; YP_053075.1; NC_001491.2.
DR   SMR; P28858; -.
DR   IntAct; P28858; 1.
DR   GeneID; 1487570; -.
DR   KEGG; vg:1487570; -.
DR   Proteomes; UP000001189; 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:0034061; F:DNA polymerase activity; IDA:AgBase.
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:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:1902074; P:response to salt; IDA:AgBase.
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; Endonuclease;
KW   Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1220
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000046518"
FT   REGION          21..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        644..659
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1220 AA;  135956 MW;  858C14DCCC71A65B CRC64;
     MAAREQANSV RRSGFFNPFI GKRPFFRPGS GQTAETERPR PPQHSYCTEV GSFKFIAPRC
     LDEEAPADQR RGVHVGTLER PPKVYCDGSE YDVLNFASGG CWPRRIRVWN GQDFRGDGFN
     PRFERFHVYD IVETSESASH DDPSRFAELS RPSGSVVTLL GMSECGKRVA VHVYGVRHYF
     YMAKAEVDSA CGITTEAELV RAMVDCAHSS ALSAALGNGN GGKQSGGSGG GWWGGKHVSA
     DCFKVETVCH TTLYYFGSKP ALYYRVSASS SRLGGFICDN FHPEITKFEG SVDVTTRLLL
     DNENFTSFGW YRLRPGTHGE RVQLRPVERH VTSSDVEINC TPDNLEPIPD EAAWPDYKLM
     CFDIECKAGT GNEMAFPVAT NQEDLVIQIS CLLYSLATQN HEHTLLFSLG SCDISEEYSF
     ACVQRGEPRP TVLEFDSEYE LLVAFLTFLK QYSPEFATGY NIVNFDWAYI VNKVTSVYNI
     KLDGYGKFNK GGLFKVWDIA TNHFQKKSKV KINGLISLDM YSVATEKLKL PSYKLDAVVG
     DVLGEHKIDL PYKEIPSYYA GGPDRRGVIG EYCIQDSRLV GKLFFKYLPH LELSAVAKLA
     RITLTRVIFD GQQIRVYTCL LKLARERNFI LPDNRRRFDS QADAASETSE LAMDSQSHAF
     DSTDEPDGVD GTPDAAGSGA TSENGGGKPG VGRAVGYQGA KVLDPVSGFH VDPVVVFDFA
     SLYPSIIQAH NLCFTTLALD EVDLAGLQPS VDYSTFEVGD QKLFFVHAHI RESLLGILLR
     DWLAMRKAVR ARIPTSTPEE AVLLDKQQSA IKVICNSVYG FTGVANGLLP CLRIAATVTT
     IGRDMLLKTR DYVHSRWATR ELLEDNFPGA IGFRNHKPYS VRVIYGDTDS VFIKFVGLTY
     EGVSELGDAM SRQISADLFR APIKLECEKT FQRLLLITKK KYIGVINGGK MLMKGVDLVR
     KNNCSFINLY ARHLVDLLLY DEDVATAAAE VTDVPPAEWV GRPLPSGFDK FGRVLVEAYN
     RITAPNLDVR EFVMTAELSR SPESYTNKRL PHLTVYFKLA MRNEELPSVK ERIPYVIVAQ
     TEAAEREAGV VNSMRGTAQN PVVTKTARPQ PKRKLLVSDL AEDPTYVSEN DVPLNTDYYF
     SHLLGTISVT FKALFGNDVR TTENLLKRFI PETPHKTPTK TQALLERAGF EKLTPFTPEE
     ESRRILHTVF CTLEAAPHQS