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Database: UniProt
Entry: E1B1V7_HHV2
LinkDB: E1B1V7_HHV2
Original site: E1B1V7_HHV2 
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}.
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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
//
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