DPOL_HHV21
ID DPOL_HHV21 Reviewed; 1240 AA.
AC P07918;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 23-FEB-2022, entry version 105.
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 2 (strain 186) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10312;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3038677; DOI=10.1016/0378-1119(87)90039-4;
RA Tsurumi T., Maeno K., Nishiyama Y.;
RT "Nucleotide sequence of the DNA polymerase gene of herpes simplex virus
RT type 2 and comparison with the type 1 counterpart.";
RL Gene 52:129-137(1987).
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: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; M16321; AAA45853.1; -; Genomic_DNA.
DR PIR; A27315; DJBE21.
DR SMR; P07918; -.
DR PRIDE; P07918; -.
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 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..1240
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000046515"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..688
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1240 AA; 137356 MW; 1CDA4B1D11F8180E CRC64;
MFCAAGGPAS PGGKSAARAA SGFFAPHNPR GATQTAPPPC RRQNFYNPHL AQTGTQPKAP
GPAQRHTYYS ECDEFRFIAP RSLDEDAPAE QRTGVHDGRL RRAPKVYCGG DERDVLRVGP
EGFWPRRLRL WGGADHAPEG FDPTVTVFHV YDILEHVEHA YSMRAAQLHE RFMDAITPAG
TVITLLGLTP EGHRVAVHVY GTRQYFYMNK AEVDRHLQCR APRDLCERLA AALRESPGAS
FRGISADHFE AEVVERADVY YYETRPTLYY RVFVRSGRAL AYLCDNFCPA IRKYEGGVDA
TTRFILDNPG FVTFGWYRLK PGRGNAPAQP RPPTAFGTSS DVEFNCTADN LAVEGAMCDL
PAYKLMCFDI ECKAGGEDEL AFPVAERPED LVIQISCLLY DLSTTALEHI LLFSLGSCDL
PESHLSDLAS RGLPAPVVLE FDSEFEMLLA FMTFVKQYGP EFVTGYNIIN FDWPFVLTKL
TEIYKVPLDG YGRMNGRGVF RVWDIGQSHF QKRSKIKVNG MVNIDMYGII TDKVKLSSYK
LNAVAEAVLK DKKKDLSYRD IPAYYASGPA QRGVIGEYCV QDSLLVGQLF FKFLPHLELS
AVARLAGINI TRTIYDGQQI RVFTCLLRLA GQKGFILPDT QGRFRGLDKE APKRPAVPRG
EGERPGDGNG DEDKDDDEDG DEDGDEREEV ARETGGRHVG YQGARVLDPT SGFHVDPVVV
FDFASLYPSI IQAHNLCFST LSLRPEAVAH LEADRDYLEI EVGGRRLFFV KAHVRESLLS
ILLRDWLAMR KQIRSRIPQS PPEEAVLLDK QQAAIKVVCN SVYGFTGVQH GLLPCLHVAA
TVTTIGREML LATRAYVHAR WAEFDQLLAD FPEAAGMRAP GPYSMRIIYG DTDSIFVLCR
GLTGEALVAM GDKMASHISR ALFLPPIKLE CEKTFTKLLL IAKKKYIGVI CGGKMLIKGV
DLVRKNNCAF INRTSRALVD LLFYDDTVSG AAAALAERPA EEWLARPLPE GLQAFGAVLV
DAHRRITDPE RDIQDFVLTA ELSRHPRAYT NKRLAHLTVY YKLMARRAQV PSIKDRIPYV
IVAQTREVEE TVARLAALRE LDAAAPGDEP APPAALPSPA KRPRETPSHA DPPGGASKPR
KLLVSELAED PGYAIARGVP LNTDYYFSHL LGAACVTFKA LFGNNAKITE SLLKRFIPET
WHPPDDVAAR LRAAGFGPAG AGATAEETRR MLHRAFDTLA
