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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   16-APR-2014, entry version 81.
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   -!- 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.
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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-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   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
FT   HELIX        80     82
FT   STRAND       92    101
FT   STRAND      104    107
FT   STRAND      110    113
FT   STRAND      128    130
FT   STRAND      145    157
FT   HELIX       160    162
FT   HELIX       169    174
FT   STRAND      179    187
FT   STRAND      193    199
FT   STRAND      203    208
FT   HELIX       209    214
FT   HELIX       221    234
FT   STRAND      235    237
FT   HELIX       245    247
FT   STRAND      249    259
FT   STRAND      266    274
FT   HELIX       276    285
FT   STRAND      288    290
FT   STRAND      292    294
FT   HELIX       299    306
FT   STRAND      312    318
FT   TURN        322    324
FT   HELIX       332    334
FT   STRAND      336    338
FT   STRAND      340    346
FT   HELIX       347    349
FT   STRAND      350    352
FT   STRAND      363    372
FT   STRAND      389    400
FT   TURN        401    403
FT   STRAND      406    415
FT   HELIX       421    429
FT   STRAND      436    442
FT   HELIX       443    457
FT   STRAND      460    466
FT   TURN        467    470
FT   HELIX       471    481
FT   TURN        488    490
FT   STRAND      491    496
FT   STRAND      499    501
FT   STRAND      515    517
FT   STRAND      520    524
FT   HELIX       525    529
FT   HELIX       540    546
FT   TURN        557    559
FT   HELIX       560    566
FT   HELIX       568    592
FT   HELIX       594    605
FT   HELIX       609    611
FT   HELIX       619    632
FT   STRAND      707    709
FT   STRAND      713    719
FT   HELIX       721    728
FT   TURN        733    735
FT   STRAND      736    738
FT   TURN        748    751
FT   STRAND      752    756
FT   STRAND      758    765
FT   TURN        767    769
FT   HELIX       773    791
FT   HELIX       792    794
FT   HELIX       797    814
FT   HELIX       817    822
FT   STRAND      826    828
FT   HELIX       831    856
FT   HELIX       859    865
FT   HELIX       867    872
FT   STRAND      879    885
FT   STRAND      887    895
FT   HELIX       902    917
FT   STRAND      923    937
FT   STRAND      940    945
FT   STRAND      950    954
FT   HELIX       964    979
FT   HELIX       981    989
FT   HELIX       990    992
FT   HELIX       995   1000
FT   HELIX      1005   1007
FT   HELIX      1008   1022
FT   HELIX      1029   1031
FT   TURN       1069   1071
FT   STRAND     1074   1077
FT   HELIX      1146   1151
FT   HELIX      1158   1172
FT   HELIX      1174   1177
FT   HELIX      1181   1189
FT   HELIX      1194   1196
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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