ID I3TC89_HHV1 Unreviewed; 1235 AA.
AC I3TC89;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN Name=UL30 {ECO:0000313|EMBL:AFK50376.1};
GN ORFNames=hmpv214_0031 {ECO:0000313|EMBL:AOY34298.1};
OS Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus humanalpha1.
OX NCBI_TaxID=10298 {ECO:0000313|EMBL:AFK50376.1};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AFK50376.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=McKrae {ECO:0000313|EMBL:AFK50376.1};
RX PubMed=23021301; DOI=10.1016/j.virol.2012.08.043;
RA Watson G., Xu W., Reed A., Babra B., Putman T., Wick E., Wechsler S.L.,
RA Rohrmann G.F., Jin L.;
RT "Sequence and comparative analysis of the genome of HSV-1 strain McKrae.";
RL Virology 433:528-537(2012).
RN [2] {ECO:0000313|EMBL:ALM22599.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=McKrae {ECO:0000313|EMBL:ALM22599.1};
RA Renner D.W., Tafuri Y.R., Parsons L., Shreve J.T., Neumann D., Szpara M.L.;
RT "Genome Sequence of a UL56 Defective HSV-1 Strain McKrae.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AOY34298.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=McKrae {ECO:0000313|EMBL:AOY34298.1};
RX PubMed=27739035;
RA Danaher R.J., Fouts D.E., Chan A.P., Choi Y., DePew J., McCorrison J.M.,
RA Nelson K.E., Wang C., Miller C.S.;
RT "HSV-1 clinical isolates with unique in vivo and in vitro phenotypes and
RT insight into genomic differences.";
RL J. Neurovirol. 0:0-0(2016).
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. {ECO:0000256|ARBA:ARBA00025601}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
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 Evidence={ECO:0000256|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
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. {ECO:0000256|ARBA:ARBA00025814}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; JQ730035; AFK50376.1; -; Genomic_DNA.
DR EMBL; KT425107; ALM22599.1; -; Genomic_DNA.
DR EMBL; KX791987; AOY34298.1; -; Genomic_DNA.
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; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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 PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
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; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Host nucleus {ECO:0000256|ARBA:ARBA00022562};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109}.
FT DOMAIN 246..543
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 607..1175
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1200..1235
FT /note="DNA polymerase catalytic subunit Pol C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11590"
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..677
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1235 AA; 136550 MW; 0D0BBA2E8C7677F4 CRC64;
MFSGGGGPLS PGGKSAARAA SGFFAPAGPR GAGRGPPPCL RQNFYNPYLA PVGTQQKPTG
PTQRHTYYSE CDEFRFIAPR VLDEDAPPEK RAGVHDGHLK RAPKVYCGGD ERDVLRVGSG
GFWPRRSRLW GGVDHAPAGF DPTVTVFHVY 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 PAYYAAGPAQ RGVIGEYCIQ DSLLVGQLFF KFLPHLELSA
VARLAGINIT RTIYDGQQIR VFTCLLRLAD QKGFILPDTQ GRFRGAGGEA PKRPAAARED
EERPEEEGED ENEREEGGGE REPEGARETA GRHVGYQGAR VLDPTSGFHV NPVVVFDFAS
LYPSIIQAHN LCFSTLSLRA DAVAHLEAGK DYLEIEMGGR 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
//
