DPOL_VZVO
ID DPOL_VZVO Reviewed; 1194 AA.
AC Q4JQU7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 23-FEB-2022, entry version 55.
DE RecName: Full=DNA polymerase catalytic subunit;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
GN ORFNames=ORF28;
OS Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax (V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
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, the DNA
CC polymerase processivity factor, and the alkaline exonuclease. Interacts
CC with the helicase-primase complex composed of the primase, the helicase
CC and the primase-associated factor; this interaction may coordinate
CC leading and lagging strand DNA synthesis at the replication fork (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. 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; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57642.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57713.1; -; Genomic_DNA.
DR SMR; Q4JQU7; -.
DR IntAct; Q4JQU7; 10.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; Genome.
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; 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 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..1194
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000385161"
SQ SEQUENCE 1194 AA; 134117 MW; 3270DDD74508A6F6 CRC64;
MAIRTGFCNP FLTQASGIKY NPRTGRGSNR EFLHSYKTTM SSFQFLAPKC LDEDVPMEER
KGVHVGTLSR PPKVYCNGKE VPILDFRCSS PWPRRVNIWG EIDFRGDKFD PRFNTFHVYD
IVETTEAASN GDVSRFATAT RPLGTVITLL GMSRCGKRVA VHVYGICQYF YINKAEVDTA
CGIRSCSELS VLLAECLRSS MITQNDATLN GDKNAFHGTS FKSASPESFR VEVIERTDVY
YYDTQPCAFY RVYSPSSKFT NYLCDNFHPE LKKYEGRVDA TTRFLMDNPG FVSFGWYQLK
PGVDGERVRV RPASRQLTLS DVEIDCMSDN LQAIPNDDSW PDYKLLCFDI ECKSGGSNEL
AFPDATHLED LVIQISCLLY SIPRQSLEHI LLFSLGSCDL PQRYVQEMKD AGLPEPTVLE
FDSEFELLIA FMTLVKQYAP EFATGYNIVN FDWAFIMEKL NSIYSLKLDG YGSINRGGLF
KIWDVGKSGF QRRSKVKING LISLDMYAIA TEKLKLSSYK LDSVAREALN ESKRDLPYKD
IPGYYASGPN TRGIIGEYCI QDSALVGKLF FKYLPHLELS AVARLARITL TKAIYDGQQV
RIYTCLLGLA SSRGFILPDG GYPATFEYKD VIPDVGDVEE EMDEDESVSP TGTSSGRNVG
YKGARVFDPD TGFYIDPVVV LDFASLYPSI IQAHNLCFTT LTLNFETVKR LNPSDYATFT
VGGKRLFFVR SNVRESLLGV LLKDWLAMRK AIRARIPGSS SDEAVLLDKQ QAAIKVVCNS
VYGFTGVAQG FLPCLYVAAT VTTIGRQMLL STRDYIHNNW AAFERFITAF PDIESSVLSQ
KAYEVKVIYG DTDSVFIRFK GVGVEGIAKI GEKMAHIIST ALFCPPIKLE CEKTFIKLLL
ITKKKYIGVI YGGKVLMKGV DLVRKNNCQF INDYARKLVE LLLYDDTVSR AAAEASCVSI
AEWNRRAMPS GMAGFGRIIA DAHRQITSPK LDINKFVMTA ELSRPPSAYI NRRLAHLTVY
YKLVMRQGQI PNVRERIPYV IVAPTDEVEA DAKSVALLRG DPLQNTAGKR CGEAKRKLII
SDLAEDPIHV TSHGLSLNID YYFSHLIGTA SVTFKALFGN DTKLTERLLK RFIPETRVVN
VKMLNRLQAA GFVCIHAPRW DNKMNTEAEI TEEEQSHQIM RRVFCIPKAI LHQS