ID E1B1V7_HHV2 Unreviewed; 1236 AA.
AC E1B1V7;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=UL30 {ECO:0000313|EMBL:ADM52125.1};
OS Human herpesvirus 2 (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus humanalpha2.
OX NCBI_TaxID=10310 {ECO:0000313|EMBL:ADM52125.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:ADM52125.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=08040304 {ECO:0000313|EMBL:ADM52125.1};
RX PubMed=20733037; DOI=10.1128/AAC.00669-10;
RA Burrel S., Deback C., Agut H., Boutolleau D.;
RT "Genotypic characterization of UL23 thymidine kinase and UL30 DNA
RT polymerase of clinical isolates of herpes simplex virus: natural
RT polymorphism and mutations associated with resistance to antivirals.";
RL Antimicrob. Agents Chemother. 0:0-0(2010).
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. {ECO:0000256|ARBA:ARBA00025601}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
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 Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
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. {ECO:0000256|ARBA:ARBA00025814}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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; HQ123107; ADM52125.1; -; Genomic_DNA.
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; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT DOMAIN 247..544
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 608..1176
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1201..1236
FT /note="DNA polymerase catalytic subunit Pol C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11590"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 646..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1099..1135
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..684
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1236 AA; 136911 MW; F1D05FBB0384DEC6 CRC64;
MFCAAGGPTS PGGKSAARAA SGFFAPHNPR GATQTAPPPC RRQNFYNPHL AQTGTQPKAP
GPAQRHTYYS ECDEFRFIAP RSLDEDAPAE QRTGVHDGRL RRAPKVYCGG DERDVLRVGP
EGFWPRRLRL WGGADHAPKG 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 DEREEVARET GGRHVGYQGA RVLDPTSGFH VDPVVVFDFA
SLYPSIIQAH NLCFSTLSLR PEAVAHLEAD RDYLEIEVGG RRLFFVKAHV RESLLSILLR
DWLAMRKQIR SRIPQSPPEE AVLLDKQQAA IKVVCNSVYG FTGVQHGLLP CLHVAATVTT
IGREMLLATR AYVHARWAEF DQLLADFPEA AGMRAPGPYS MRIIYGDTDS IFVLCRGLTA
AGLVAMGDKM ASHISRALFL PPIKLECEKT FTKLLLIAKK KYIGVICGGK MLIKGVDLVR
KNNCAFINRT SRALVDLLFY DDTVSGAAAA LAERPAEEWL ARPLPEGLQA FGAVLVDAHR
RITDPERDIQ DFVLTAELSR HPRAYTNKRL AHLTVYYKLM ARRAQVPSIK DRIPYVIVAQ
TREVEETVAR LAALRELDAA APGDEPAPPA ALPSPAKRPR ETPSHADPPG GASKPRKLLV
SELAEDPGYA IARGVPLNTD YYFSHLLGAA CVTFKALFGN NAKITESLLK RFIPETWHPP
DDVAARLRAA GFGPAGAGAT AEETRRMLHR AFDTLA
//