DPOL_HHV1K
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 23-FEB-2022, entry version 108.
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 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; 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., Weller S.K.,
RA Coen D.M.;
RT "Sequence and mapping analyses of the herpes simplex virus DNA polymerase
RT 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-binding
CC protein. Additionally, the polymerase contains an intrinsic
CC ribonuclease H (RNase H) activity that specifically degrades RNA/DNA
CC heteroduplexes or duplex DNA substrates in the 5' to 3' direction.
CC Therefore, it can catalyze the excision of the RNA primers that
CC initiate the synthesis of Okazaki fragments at a replication fork
CC during viral DNA replication (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC -!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL29, the DNA
CC polymerase processivity factor, and the alkaline exonuclease. Interacts
CC with the putative helicase-primase complex subunit UL8; this
CC interaction may coordinate leading and lagging strand DNA synthesis at
CC the replication fork (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. Note=The protein is
CC present at discrete sites in nuclei, called replication compartments
CC where viral DNA replication occurs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {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 SMR; P04292; -.
DR BindingDB; P04292; -.
DR ChEMBL; CHEMBL5944; -.
DR PRIDE; P04292; -.
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 GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.132.60; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.90.1600.10; -; 1.
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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR021639; DNAPolymera_Pol_C.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
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; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase;
KW Endonuclease; Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; Transferase; Viral DNA replication.
FT CHAIN 1..1235
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000046513"
FT REGION 640..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1098..1134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..678
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 92..101
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 145..157
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 169..174
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 209..214
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 221..234
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 249..259
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 266..274
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 276..285
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 312..318
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 340..346
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 389..400
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 406..415
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 421..429
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 436..442
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 443..457
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 460..466
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 471..481
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 525..529
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 540..546
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 557..559
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 560..566
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 568..592
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 594..605
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 609..611
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 619..632
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 713..719
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 721..728
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 733..735
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 736..738
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 748..751
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 752..756
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 758..765
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 767..769
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 773..791
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 792..794
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 797..814
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 817..822
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 826..828
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 831..856
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 859..865
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 867..872
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 879..885
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 887..895
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 902..917
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 923..937
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 940..945
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 950..954
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 964..979
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 981..989
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 990..992
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 995..1000
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1005..1007
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1008..1022
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1029..1031
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1041..1043
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1050..1060
FT /evidence="ECO:0007829|PDB:2GV9"
FT TURN 1069..1071
FT /evidence="ECO:0007829|PDB:2GV9"
FT STRAND 1074..1077
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1081..1085
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1087..1095
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1146..1151
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1158..1172
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1174..1177
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1181..1189
FT /evidence="ECO:0007829|PDB:2GV9"
FT HELIX 1194..1196
FT /evidence="ECO:0007829|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
