ID DPOL_HHV11 Reviewed; 1235 AA. AC P04293; B9VQF8; Q09IA3; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 2. DT 03-NOV-2009, entry version 67. 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 1 (strain 17) (HHV-1) (Human herpes simplex virus OS 1). OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Alphaherpesvirinae; Simplexvirus. OX NCBI_TaxID=10299; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=88274327; PubMed=2839594; RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., RA McNab D., Perry L.J., Scott J.E., Taylor P.; RT "The complete DNA sequence of the long unique region in the genome of RT herpes simplex virus type 1."; RL J. Gen. Virol. 69:1531-1574(1988). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86067223; PubMed=2999714; DOI=10.1093/nar/13.22.8143; RA Quinn J.P., McGeoch D.J.; RT "DNA sequence of the region in the genome of herpes simplex virus type RT 1 containing the genes for DNA polymerase and the major DNA binding RT protein."; RL Nucleic Acids Res. 13:8143-8163(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nonneuroinvasive mutant HF10; RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019; RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.; RT "Determination and analysis of the DNA sequence of highly attenuated RT herpes simplex virus type 1 mutant HF10, a potential oncolytic RT virus."; RL Microbes Infect. 9:142-149(2007). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=17 syn+; RA Cunningham C., Davison A.J.; RT "Herpes simplex virus type 1 bacterial artificial chromosome."; RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases. RN [5] RP FUNCTION. RX PubMed=2553735; RA Crute J.J., Lehman I.R.; RT "Herpes simplex-1 DNA polymerase. Identification of an intrinsic RT 5'----3' exonuclease with ribonuclease H activity."; RL J. Biol. Chem. 264:19266-19270(1989). RN [6] RP INTERACTION WITH UL8. RX PubMed=9261356; RA Marsden H.S., McLean G.W., Barnard E.C., Francis G.J., MacEachran K., RA Murphy M., McVey G., Cross A., Abbotts A.P., Stow N.D.; RT "The catalytic subunit of the DNA polymerase of herpes simplex virus RT type 1 interacts specifically with the C terminus of the UL8 component RT of the viral helicase-primase complex."; RL J. Virol. 71:6390-6397(1997). 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. 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 (Potential). Note=The protein CC 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. CC -!- SEQUENCE CAUTION: CC Sequence=CAA26941.1; Type=Frameshift; Positions=114; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14112; CAA32323.1; -; Genomic_DNA. DR EMBL; X03181; CAA26941.1; ALT_FRAME; Genomic_DNA. DR EMBL; DQ889502; ABI63492.1; -; Genomic_DNA. DR EMBL; FJ593289; ACM62253.1; -; Genomic_DNA. DR PIR; A00715; DJBEV1. DR PIR; C30085; DJBEH7. DR RefSeq; NP_044632.1; -. DR SMR; P04293; 60-640, 700-1110. DR GeneID; 2703462; -. DR DrugBank; DB00787; Aciclovir. DR DrugBank; DB00426; Famciclovir. DR DrugBank; DB00529; Foscarnet. DR DrugBank; DB01004; Ganciclovir. DR DrugBank; DB00249; Idoxuridine. DR DrugBank; DB00299; Penciclovir. DR DrugBank; DB00432; Trifluridine. DR DrugBank; DB00577; Valaciclovir. DR DrugBank; DB01610; Valganciclovir. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. 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:0006260; P:DNA replication; IEA:UniProtKB-KW. DR InterPro; IPR006172; DNA-dir_DNA_pol_B. DR InterPro; IPR006134; DNA-dir_DNA_pol_B_cons-reg. DR InterPro; IPR017966; DNA-dir_DNA_pol_B_cons_reg2. DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS. DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc. DR PANTHER; PTHR10322; DNA_pol_B; 1. DR Pfam; PF00136; DNA_pol_B; 1. DR Pfam; PF03104; DNA_pol_B_exo; 1. DR PRINTS; PR00106; DNAPOLB. DR SMART; SM00486; POLBc; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Endonuclease; Host nucleus; Hydrolase; KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Transferase; KW Virus reference strain. FT CHAIN 1 1235 DNA polymerase catalytic subunit. FT /FTId=PRO_0000046511. FT COMPBIAS 4 7 Poly-Gly. FT COMPBIAS 659 688 Glu-rich. FT COMPBIAS 986 991 Poly-Ala. FT COMPBIAS 1101 1128 Pro-rich. FT VARIANT 33 33 S -> G (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 102 102 A -> T (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 330 330 A -> R (in strain: Nonneuroinvasive FT mutant HF10 and 17 syn+). FT VARIANT 646 646 A -> T (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 802 802 L -> F (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 905 905 V -> M (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 1203 1203 A -> T (in strain: Nonneuroinvasive FT mutant HF10). FT VARIANT 1208 1209 TA -> AT (in strain: Nonneuroinvasive FT mutant HF10). SQ SEQUENCE 1235 AA; 136421 MW; E8CD41D6EDED8343 CRC64; MFSGGGGPLS PGGKSAARAA SGFFAPAGPR GASRGPPPCL RQNFYNPYLA PVGTQQKPTG PTQRHTYYSE CDEFRFIAPR VLDEDAPPEK RAGVHDGHLK RAPKVYCGGD ERDVLRVGSG GFWPRRSRLW GGVDHAPAGF NPTVTVFHVY DILENVEHAY GMRAAQFHAR FMDAITPTGT VITLLGLTPE GHRVAVHVYG TRQYFYMNKE EVDRHLQCRA PRDLCERMAA ALRESPGASF RGISADHFEA EVVERTDVYY YETRPALFYR VYVRSGRVLS YLCDNFCPAI KKYEGGVDAT TRFILDNPGF VTFGWYRLKP GRNNTLAQPA APMAFGTSSD VEFNCTADNL AIEGGMSDLP AYKLMCFDIE CKAGGEDELA FPVAGHPEDL VIQISCLLYD LSTTALEHVL LFSLGSCDLP ESHLNELAAR GLPTPVVLEF DSEFEMLLAF MTLVKQYGPE FVTGYNIINF DWPFLLAKLT DIYKVPLDGY GRMNGRGVFR VWDIGQSHFQ KRSKIKVNGM VNIDMYGIIT DKIKLSSYKL NAVAEAVLKD KKKDLSYRDI PAYYAAGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA VARLAGINIT RTIYDGQQIR VFTCLLRLAD QKGFILPDTQ GRFRGAGGEA PKRPAAARED EERPEEEGED EDEREEGGGE REPEGARETA GRHVGYQGAR VLDPTSGFHV NPVVVFDFAS LYPSIIQAHN LCFSTLSLRA DAVAHLEAGK DYLEIEVGGR RLFFVKAHVR ESLLSILLRD WLAMRKQIRS RIPQSSPEEA VLLDKQQAAI KVVCNSVYGF TGVQHGLLPC LHVAATVTTI GREMLLATRE YVHARWAAFE QLLADFPEAA DMRAPGPYSM RIIYGDTDSI FVLCRGLTAA GLTAVGDKMA SHISRALFLP PIKLECEKTF TKLLLIAKKK YIGVIYGGKM LIKGVDLVRK NNCAFINRTS RALVDLLFYD DTVSGAAAAL AERPAEEWLA RPLPEGLQAF GAVLVDAHRR ITDPERDIQD FVLTAELSRH PRAYTNKRLA HLTVYYKLMA RRAQVPSIKD RIPYVIVAQT REVEETVARL AALRELDAAA PGDEPAPPAA LPSPAKRPRE TPSPADPPGG ASKPRKLLVS ELAEDPAYAI AHGVALNTDY YFSHLLGAAC VTFKALFGNN AKITESLLKR FIPEVWHPPD DVAARLRTAG FGAVGAGATA EETRRMLHRA FDTLA //