DPOL_HHV1S
ID DPOL_HHV1S Reviewed; 1235 AA.
AC P09854;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 103.
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 SC16) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10309;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3034575; DOI=10.1002/j.1460-2075.1987.tb04735.x;
RA Larder B.A., Kemp S.D., Darby G.;
RT "Related functional domains in virus DNA polymerases.";
RL EMBO J. 6:169-175(1987).
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; X04771; CAA28464.1; -; Genomic_DNA.
DR PIR; A26163; DJBE16.
DR SMR; P09854; -.
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 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW 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_0000046514"
FT REGION 640..691
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 COMPBIAS 1105..1129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 136467 MW; A13605B7EBD774AA 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 VSIDMYGIIT DKIKLSSYKL
NAVAEAVLKD KKKDLSYRDI PAYYAAGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA
VARLAGINIT RTIYDGQQIR VFTCLLRLAD QKGFILPDTQ GRFRGAGGEA PKRPAAARED
EERPEEEGED EDEREEGGGE REPDGARETA GRHVGYQGAR 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 TPSPADPPGG ASKPRKLLVS
ELAEDPAYAI AHGVALNTDY YFSHLLGAAC VTFKALFGNN AKITESLLKR FIPEVWHPPD
DVTARLRAAG FGAVGAGATA EETRRMLHRA FDTLA
