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Database: UniProt
Entry: DPOL_HHV2H
LinkDB: DPOL_HHV2H
Original site: DPOL_HHV2H 
ID   DPOL_HHV2H              Reviewed;        1240 AA.
AC   P89453;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   24-JAN-2024, entry version 117.
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 HG52) (HHV-2) (Human herpes simplex virus 2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha2; Human herpesvirus 2.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA   Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT   "The genome sequence of herpes simplex virus type 2.";
RL   J. Virol. 72:2010-2021(1998).
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; Z86099; CAB06755.1; -; Genomic_DNA.
DR   RefSeq; YP_009137182.1; NC_001798.2.
DR   SMR; P89453; -.
DR   GeneID; 1487316; -.
DR   KEGG; vg:1487316; -.
DR   Proteomes; UP000001874; Genome.
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; 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; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW   Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW   Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1240
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000385160"
FT   REGION          1..44
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        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;  137328 MW;  D271B71706C025A6 CRC64;
     MFCAAGGPAS PGGKPAARAA SGFFAPHNPR GATQTAPPPC RRQNFYNPHL AQTGTQPKAL
     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 TPEEAVLLDK QQAAIKVVCN SVYGFTGVQH GLLPCLHVAA
     TVTTIGREML LATRAYVHAR WAEFDQLLAD FPEAAGMRAP GPYSMRIIYG DTDSIFVLCR
     GLTAAGLVAM 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
//
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