ID   DPOL_ELHVK              Reviewed;        1041 AA.
AC   Q9DKT8;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-FEB-2022, entry version 97.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
DE            EC=3.1.26.4;
OS   Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS   (Elephant endotheliotropic herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Proboscivirus.
OX   NCBI_TaxID=654902;
OH   NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH   NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH   NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA   Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA   Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA   Bennett M., Stewart J.P., Ulrich R.G.;
RT   "Identification of novel rodent herpesviruses, including the first
RT   gammaherpesvirus of Mus musculus.";
RL   J. Virol. 81:8091-8100(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA   Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA   Hentschke J.;
RT   "Genetic and ultrastructural characterization of a European isolate of the
RT   fatal endotheliotropic elephant herpesvirus.";
RL   J. Gen. Virol. 82:475-482(2001).
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   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF322977; AAG41999.1; -; Genomic_DNA.
DR   SMR; Q9DKT8; -.
DR   PRIDE; Q9DKT8; -.
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:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
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; Endonuclease;
KW   Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Transferase; Viral DNA replication.
FT   CHAIN           1..1041
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000408152"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1041 AA;  118411 MW;  28F13228D4428E55 CRC64;
     MAFFNPYFKS KNKGSDMPPK QSMSFTKQHK TKESAFLSIT PECIIKPKSS KLLKKYNGEQ
     PRLFYNGEPV LLYTVREISQ WPVKDIMKVN NGTVDGSCNV VSTSHEPDSP VKNNCEETVV
     FHIYEQCVFC AHDVSYEYLP WRYKRFLSPT GTIISLIGKT EDGTDVCVNV HGQAYYFYVA
     MKDEAATRDA VSKVMSNLEK ESSSCSYVMK SVNKMSLMGF NTNTSSYLMM IFSNHFVGKE
     AARNLKDLDF EIFEHLVEPN TRFLVDNEFC SFGWYSLKTP YVRQTSKDSN CELELDCCVG
     DLQVLRDRVD WPNYKCMAFD IECLSGSVDD AFPDATNPDD IIIQISCVCF DIKNTIETQH
     LFTLGSCAEI PGVYIYECAS EYELIESFLT FVRVYGPNFI TGYNINAFDI PYVIGRCRYY
     NIQCGAFTKM KRGRMTCFKG MESFLNRCQC KVTISGIVII DMYRVCMDKV SAPNHKLDTV
     VDMLLGEKKH SVSYKQIPVL FRRDDDGRAV VGAYCVHDSV LVHKLFCKLL FHYEASAIAR
     LSNISINKVV FDGQQSRIFT CMLAAARREG LIIPSIDEAG EDTYQGATVL EPKTGFYNTP
     VAVFDFASLY PSIIQAYNLC YCTLITDNYV ASLREEDITM VTTNTGRVHR FVKPHVRKSI
     LSQLLTSWLA ERKAVREKLK HCKDPLMQIL LDKQQLALKL TCNAVYGFTG VSKGMFPCLA
     IAESVTAQGR QLLAVTKQYI CDRFNDWTFL TQIAPELVDC PVDSNRFKID VVYGDTDSVF
     VLLCGIENAD RLYSALPNFV AHITKTLFPP PIKLEVDKVF EKLLLLCKKR YVGVLHGEEK
     LSMKGIDLVR RNVCGFVKNT TLAVIKSLFS DNVISEAVQK MSGMTQDQVC KEGLPPGFFK
     LVALITDARE RLYENRVDIH ELQLSATLTQ ACDKYKQQNL PHLTVVRKKL ERREEIPNTG
     DRIFYVLLAH PDERVANYVI AEDPDYVETH RLQINCSKYF SNLISSITHS ISPIFPEFIS
     KPDRFLMSCV PRKTYPKPIL N