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Database: UniProt
Entry: P04292
LinkDB: P04292
Original site: P04292 
ID   DPOL_HHV1K              Reviewed;        1235 AA.
AC   P04292;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   26-NOV-2014, entry version 84.
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 KOS) (HHV-1) (Human herpes simplex virus
OS   1).
OC   Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
OC   Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10306;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2999787; DOI=10.1073/pnas.82.23.7969;
RA   Gibbs J.S., Chiou H.C., Hall J.D., Mount D.W., Retondo M.J.,
RA   Weller S.K., Coen D.M.;
RT   "Sequence and mapping analyses of the herpes simplex virus DNA
RT   polymerase gene predict a C-terminal substrate binding domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 82:7969-7973(1985).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS) OF 43-1235.
RX   PubMed=17997600; DOI=10.1371/journal.ppat.0030160;
RA   Goodman L.B., Loregian A., Perkins G.A., Nugent J., Buckles E.L.,
RA   Mercorelli B., Kydd J.H., Palu G., Smith K.C., Osterrieder N.,
RA   Davis-Poynter N.;
RT   "A point mutation in a herpesvirus polymerase determines
RT   neuropathogenicity.";
RL   PLoS Pathog. 3:E160-E160(2007).
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       {ECO:0000250}.
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). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. Note=The protein
CC       is present at discrete sites in nuclei, called replication
CC       compartments where viral DNA replication occurs. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000305}.
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DR   EMBL; M10792; AAA66438.1; -; Genomic_DNA.
DR   PIR; A00714; DJBEK1.
DR   PDB; 2GV9; X-ray; 2.68 A; A/B=43-1235.
DR   PDBsum; 2GV9; -.
DR   ProteinModelPortal; P04292; -.
DR   SMR; P04292; 59-639, 1200-1235.
DR   BindingDB; P04292; -.
DR   ChEMBL; CHEMBL5944; -.
DR   EvolutionaryTrace; P04292; -.
DR   GO; GO:0042025; C:host cell 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: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   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Endonuclease; Host nucleus; Hydrolase;
KW   Multifunctional enzyme; Nuclease; Nucleotidyltransferase; Transferase.
FT   CHAIN         1   1235       DNA polymerase catalytic subunit.
FT                                /FTId=PRO_0000046513.
FT   COMPBIAS      4      7       Poly-Gly.
FT   COMPBIAS    659    688       Glu-rich.
FT   COMPBIAS    986    991       Poly-Ala.
FT   STRAND       72     79       {ECO:0000244|PDB:2GV9}.
FT   HELIX        80     82       {ECO:0000244|PDB:2GV9}.
FT   STRAND       92    101       {ECO:0000244|PDB:2GV9}.
FT   STRAND      104    107       {ECO:0000244|PDB:2GV9}.
FT   STRAND      110    113       {ECO:0000244|PDB:2GV9}.
FT   STRAND      128    130       {ECO:0000244|PDB:2GV9}.
FT   STRAND      145    157       {ECO:0000244|PDB:2GV9}.
FT   HELIX       160    162       {ECO:0000244|PDB:2GV9}.
FT   HELIX       169    174       {ECO:0000244|PDB:2GV9}.
FT   STRAND      179    187       {ECO:0000244|PDB:2GV9}.
FT   STRAND      193    199       {ECO:0000244|PDB:2GV9}.
FT   STRAND      203    208       {ECO:0000244|PDB:2GV9}.
FT   HELIX       209    214       {ECO:0000244|PDB:2GV9}.
FT   HELIX       221    234       {ECO:0000244|PDB:2GV9}.
FT   STRAND      235    237       {ECO:0000244|PDB:2GV9}.
FT   HELIX       245    247       {ECO:0000244|PDB:2GV9}.
FT   STRAND      249    259       {ECO:0000244|PDB:2GV9}.
FT   STRAND      266    274       {ECO:0000244|PDB:2GV9}.
FT   HELIX       276    285       {ECO:0000244|PDB:2GV9}.
FT   STRAND      288    290       {ECO:0000244|PDB:2GV9}.
FT   STRAND      292    294       {ECO:0000244|PDB:2GV9}.
FT   HELIX       299    306       {ECO:0000244|PDB:2GV9}.
FT   STRAND      312    318       {ECO:0000244|PDB:2GV9}.
FT   TURN        322    324       {ECO:0000244|PDB:2GV9}.
FT   HELIX       332    334       {ECO:0000244|PDB:2GV9}.
FT   STRAND      336    338       {ECO:0000244|PDB:2GV9}.
FT   STRAND      340    346       {ECO:0000244|PDB:2GV9}.
FT   HELIX       347    349       {ECO:0000244|PDB:2GV9}.
FT   STRAND      350    352       {ECO:0000244|PDB:2GV9}.
FT   STRAND      363    372       {ECO:0000244|PDB:2GV9}.
FT   STRAND      389    400       {ECO:0000244|PDB:2GV9}.
FT   TURN        401    403       {ECO:0000244|PDB:2GV9}.
FT   STRAND      406    415       {ECO:0000244|PDB:2GV9}.
FT   HELIX       421    429       {ECO:0000244|PDB:2GV9}.
FT   STRAND      436    442       {ECO:0000244|PDB:2GV9}.
FT   HELIX       443    457       {ECO:0000244|PDB:2GV9}.
FT   STRAND      460    466       {ECO:0000244|PDB:2GV9}.
FT   TURN        467    470       {ECO:0000244|PDB:2GV9}.
FT   HELIX       471    481       {ECO:0000244|PDB:2GV9}.
FT   TURN        488    490       {ECO:0000244|PDB:2GV9}.
FT   STRAND      491    496       {ECO:0000244|PDB:2GV9}.
FT   STRAND      499    501       {ECO:0000244|PDB:2GV9}.
FT   STRAND      515    517       {ECO:0000244|PDB:2GV9}.
FT   STRAND      520    524       {ECO:0000244|PDB:2GV9}.
FT   HELIX       525    529       {ECO:0000244|PDB:2GV9}.
FT   HELIX       540    546       {ECO:0000244|PDB:2GV9}.
FT   TURN        557    559       {ECO:0000244|PDB:2GV9}.
FT   HELIX       560    566       {ECO:0000244|PDB:2GV9}.
FT   HELIX       568    592       {ECO:0000244|PDB:2GV9}.
FT   HELIX       594    605       {ECO:0000244|PDB:2GV9}.
FT   HELIX       609    611       {ECO:0000244|PDB:2GV9}.
FT   HELIX       619    632       {ECO:0000244|PDB:2GV9}.
FT   STRAND      707    709       {ECO:0000244|PDB:2GV9}.
FT   STRAND      713    719       {ECO:0000244|PDB:2GV9}.
FT   HELIX       721    728       {ECO:0000244|PDB:2GV9}.
FT   TURN        733    735       {ECO:0000244|PDB:2GV9}.
FT   STRAND      736    738       {ECO:0000244|PDB:2GV9}.
FT   TURN        748    751       {ECO:0000244|PDB:2GV9}.
FT   STRAND      752    756       {ECO:0000244|PDB:2GV9}.
FT   STRAND      758    765       {ECO:0000244|PDB:2GV9}.
FT   TURN        767    769       {ECO:0000244|PDB:2GV9}.
FT   HELIX       773    791       {ECO:0000244|PDB:2GV9}.
FT   HELIX       792    794       {ECO:0000244|PDB:2GV9}.
FT   HELIX       797    814       {ECO:0000244|PDB:2GV9}.
FT   HELIX       817    822       {ECO:0000244|PDB:2GV9}.
FT   STRAND      826    828       {ECO:0000244|PDB:2GV9}.
FT   HELIX       831    856       {ECO:0000244|PDB:2GV9}.
FT   HELIX       859    865       {ECO:0000244|PDB:2GV9}.
FT   HELIX       867    872       {ECO:0000244|PDB:2GV9}.
FT   STRAND      879    885       {ECO:0000244|PDB:2GV9}.
FT   STRAND      887    895       {ECO:0000244|PDB:2GV9}.
FT   HELIX       902    917       {ECO:0000244|PDB:2GV9}.
FT   STRAND      923    937       {ECO:0000244|PDB:2GV9}.
FT   STRAND      940    945       {ECO:0000244|PDB:2GV9}.
FT   STRAND      950    954       {ECO:0000244|PDB:2GV9}.
FT   HELIX       964    979       {ECO:0000244|PDB:2GV9}.
FT   HELIX       981    989       {ECO:0000244|PDB:2GV9}.
FT   HELIX       990    992       {ECO:0000244|PDB:2GV9}.
FT   HELIX       995   1000       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1005   1007       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1008   1022       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1029   1031       {ECO:0000244|PDB:2GV9}.
FT   TURN       1069   1071       {ECO:0000244|PDB:2GV9}.
FT   STRAND     1074   1077       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1146   1151       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1158   1172       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1174   1177       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1181   1189       {ECO:0000244|PDB:2GV9}.
FT   HELIX      1194   1196       {ECO:0000244|PDB:2GV9}.
SQ   SEQUENCE   1235 AA;  136520 MW;  90415EF72ED2A607 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
     ESHLNELAAR GLPTPVVLEF DSEFEMLLAF MTLVKQYGPE FVTGYNIINF DWPFLLAKLT
     DIYKVPLDGY GRMNGRGVFR VWDIGQSHFQ KRSKIKVNGM VNIDMYGIIT DKIKLSSYKL
     NAVAEAVLKD KKKDLSYRDI PAYYATGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA
     VARLAGINIT RTIYDGQQIR VFTCLLRLAD QKGFILPDTQ GRFRGAGGEA PKRPAAARED
     EERPEEEGED EDEREEGGGE REPEGARETA GRHVGYQGAK VLDPTSGFHV NPVVVFDFAS
     LYPSIIQAHN LCFSTLSLRA DAVAHLEAGK DYLEIEVGGR RLFFVKAHVR ESLLSILLRD
     WLAMRKQIRS RIPQSSPEEA VLLDKQQAAI KVVCNSVYGF TGVQHGLLPC LHVAATVTTI
     GREMLLATRE YVHARWAAFE QLLADFPEAA DMRAPGPYSM RIIYGDTDSI FVLCRGLTAA
     GLTAMGDKMA SHISRALFLP PIKLECEKTF TKLLLIAKKK YIGVIYGGKM LIKGVDLVRK
     NNCAFINRTS RALVDLLFYD DTVSGAAAAL AERPAEEWLA RPLPEGLQAF GAVLVDAHRR
     ITDPERDIQD FVLTAELSRH PRAYTNKRLA HLTVYYKLMA RRAQVPSIKD RIPYVIVAQT
     REVEETVARL AALRELDAAA PGDEPAPPAA LPSPAKRPRE TPSHADPPGG ASKPRKLLVS
     ELAEDPAYAI AHGVALNTDY YFSHLLGAAC VTFKALFGNN AKITESLLKR FIPEVWHPPD
     DVAARLRAAG FGAVGAGATA EETRRMLHRA FDTLA
//
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