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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   14-MAY-2014, entry version 82.
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
OS   2).
OC   Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
OC   Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10315;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9499055;
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-
CC       binding protein. Additionally, the polymerase contains an
CC       intrinsic ribonuclease H (RNase H) activity that specifically
CC       degrades RNA/DNA heteroduplexes or duplex DNA substrates in the 5'
CC       to 3' direction. Therefore, it can catalyze the excision of the
CC       RNA primers that initiate the synthesis of Okazaki fragments at a
CC       replication fork during viral DNA replication (By similarity).
CC   -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC       diphosphate + DNA(n+1).
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester.
CC   -!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL29, the
CC       DNA polymerase processivity factor, and the alkaline exonuclease.
CC       Interacts with the putative helicase-primase complex subunit UL8;
CC       this interaction may coordinate leading and lagging strand DNA
CC       synthesis at the replication fork (By similarity).
CC   -!- SUBCELLULAR LOCATION: Host nucleus (By similarity). Note=the
CC       protein is present at discrete sites in nuclei, called replication
CC       compartments where viral DNA replication occurs (By similarity).
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
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DR   EMBL; Z86099; CAB06755.1; -; Genomic_DNA.
DR   RefSeq; NP_044500.1; NC_001798.1.
DR   ProteinModelPortal; P89453; -.
DR   GeneID; 1487316; -.
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   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 2.
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; IPR023211; DNA_pol_palm_dom.
DR   InterPro; IPR021639; DNAPolymera_Pol_C.
DR   InterPro; IPR012337; RNaseH-like_dom.
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; 2.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   Complete proteome; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Endonuclease; Host nucleus; Hydrolase;
KW   Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN         1   1240       DNA polymerase catalytic subunit.
FT                                /FTId=PRO_0000385160.
FT   COMPBIAS    667    685       Asp-rich.
FT   COMPBIAS    991    996       Poly-Ala.
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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