ID   DPOL_HHV1A              Reviewed;        1235 AA.
AC   P07917;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   23-FEB-2022, entry version 116.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
DE            EC=3.1.26.4;
GN   ORFNames=UL30;
OS   Human herpesvirus 1 (strain Angelotti) (HHV-1) (Human herpes simplex virus
OS   1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10301;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3022246; DOI=10.1093/nar/14.20.8225;
RA   Knopf C.W.;
RT   "Nucleotide sequence of the DNA polymerase gene of herpes simplex virus
RT   type 1 strain Angelotti.";
RL   Nucleic Acids Res. 14:8225-8226(1986).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1200-1235.
RX   PubMed=15048824; DOI=10.1002/prot.10630;
RA   Hicks J.M., Hsu V.L.;
RT   "The extended left-handed helix: a simple nucleic acid-binding motif.";
RL   Proteins 55:330-338(2004).
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 UL29, the DNA
CC       polymerase processivity factor, and the alkaline exonuclease. Interacts
CC       with the putative helicase-primase complex subunit UL8; this
CC       interaction may coordinate leading and lagging strand DNA synthesis at
CC       the replication fork (By similarity). {ECO:0000250}.
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}.
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DR   EMBL; X04495; CAA28183.1; -; Genomic_DNA.
DR   PIR; A25552; DJBEAN.
DR   PDB; 1DML; X-ray; 2.70 A; B/D/F/H=1200-1235.
DR   PDBsum; 1DML; -.
DR   SMR; P07917; -.
DR   IntAct; P07917; 1.
DR   EvolutionaryTrace; P07917; -.
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; IPR021639; DNAPolymera_Pol_C.
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   Pfam; PF11590; DNAPolymera_Pol; 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   Endonuclease; Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Transferase; Viral DNA replication.
FT   CHAIN           1..1235
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000046512"
FT   REGION          640..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1098..1134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..678
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           1201..1208
FT                   /evidence="ECO:0007829|PDB:1DML"
FT   STRAND          1212..1215
FT                   /evidence="ECO:0007829|PDB:1DML"
FT   HELIX           1220..1234
FT                   /evidence="ECO:0007829|PDB:1DML"
SQ   SEQUENCE   1235 AA;  136603 MW;  4CDB3B8AE73663BF CRC64;
     MFSGGGGPLS PGGKSAARAA SGFFVPAGPR GAGRGPPPCL RQNFYNPYLA PVGTQQKPTG
     PTQRHTYYSE CDEFRFIAPR VLDEDAPPEK RAGVHDGHLK RAPKVYCGGD ERDVLRVGSG
     GFWPRRSRLW GGVDHAPAGF NPTVTVFHVY DILENVEHAY GMRAAQFHAR FMDAITPTGT
     VITLLGLTPE GHRVAVHVYG TRQYFYMNKE EVDRHLQCRA PRDLCERMAA ALRESPGASF
     RGISADHFEA EVVERTDVYY YETRPALFYR VYVRSGRVLS YLCDNFCPAI KKYEGGVDAT
     TRFILDNPGF VTFGWYRLKP GRNNTLAQPR VPMAFGTSSD VEFNCTADNL AIEGGMSDLP
     AYKLMCFDIE CKAGGEDELA FPVAGHPEDL VIQISCLLYD LSTTALEHVL LFSLGSCDLP
     ESHLTELAAR GLPTPVVLEF DSEFEMLLAF MTLVKQYGPE FVTGYNIINF DWPFLLAKLT
     DIYKVPLDGY GRMNGRGVFR VWDIGQSHFQ KRSKIKVNGM VNIDMYGIIT DKIKLSSYKL
     NAVAEAVLKD KKKDLSYRDI PAYYAAGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA
     VARLAGINIT RTIYDGQQIR VFTCLLRLAD QKGFILPDTQ GRFRGAGGEA PKRPAAARED
     EERPEEEGED EDEREEGGGE REPEGARETA GRHVGYQGAR VLDPTSGFHV NPVVVFDFAS
     LYPSIIQAHN LCFSTLSLRA DAVAHLEAGK DYLEIEVGGR RLFFVKAHVR ESLLSILLRD
     WLAMRKQIRS RIPQSSPEEA VLLDKQQAAI KVVCNSVYGF TGVQHGLLPC LHVAATVTTI
     GREMLLATRE YVHARWAAFE QLLADFPEAA DMRAPGPYSM RIIYGDTDSI FVLCRGLTAA
     GLTAVGDKMA SHISRALFLP PIKLECEKTF TKLLLIAKKK YIGVIYGGKM LIKGVDLVRK
     NNCAFINRTS RALVDLLFYD DTVSGAAAAL AERPAEEWLA RPLPEGLQAF GAVLVDAHRR
     ITDPERDIQD FVLTAELSRH PRAYTNKRLA HLTVYYKLMA RRAQVPSIKD RIPYVIVAQT
     REVEETVARL AALRELDATA PGDEPAPPAA LPCPAKRPRE TPSHADPPGG ASKPRKLLVS
     ELAEDPAYAI AHGVALNTDY YFSHLLGVAC VTFKALFGNN AKITESLLKR FIPEVWHPPD
     DVAARLRAAG FGAVGAGATA EETRRMLHRA FDTLA