ID D3YPI8_HHV1 Unreviewed; 1235 AA.
AC D3YPI8;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 06-MAR-2013, entry version 17.
DE RecName: Full=DNA polymerase;
DE EC=2.7.7.7;
GN Name=UL30;
OS Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1).
OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
OC Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10298;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=08050286;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H129;
RX PubMed=20219902; DOI=10.1128/JVI.00312-10;
RA Szpara M.L., Parsons L., Enquist L.W.;
RT "Sequence variability in clinical and laboratory isolates of herpes
RT simplex virus 1 reveals new mutations.";
RL J. Virol. 84:5303-5313(2010).
CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
CC diphosphate + DNA(n+1).
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
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DR EMBL; GU734772; ADD60110.1; -; Genomic_DNA.
DR EMBL; HQ123096; ADM52114.1; -; 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:ribonuclease H activity; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; RNaseH_fold; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Nucleotidyltransferase; Transferase.
SQ SEQUENCE 1235 AA; 136519 MW; BFD1010E56AFB816 CRC64;
MFSGGGGPLS PGGKSAARAA SGFFAPAGPR GAGRGPPPCL 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 GRNNTLAQPR APMAFGTSSD VEFNCTADNL AIEGGMSDLP
AYKLMCFDIE CKAGGEDELA FPVAGHPEDL VIQISCLLYD LSTTALEHVL LFSLGSCDLP
ESHLTELAAR 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 AALRELDATA PGDEPAPPAA LPCPAKRPRE TPSHADPPGG ASKPRKLLVS
ELAEDPAYAI AHGVALNTDY YFSHLLGAAC VTFKALFGNN AKITESLLKR FIPEVWHPPD
DVAARLRAAG FGAVGAGATA EETRRMLHRA FDTLA
//