DPOL_VZVD
ID DPOL_VZVD Reviewed; 1194 AA.
AC P09252;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 23-FEB-2022, entry version 112.
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 Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAA27911.1; -; Genomic_DNA.
DR PIR; B27214; DJBE28.
DR SMR; P09252; -.
DR BindingDB; P09252; -.
DR ChEMBL; CHEMBL4859; -.
DR DrugBank; DB00787; Acyclovir.
DR DrugBank; DB13896; Talimogene laherparepvec.
DR DrugCentral; P09252; -.
DR PRIDE; P09252; -.
DR Proteomes; UP000002602; 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; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..1194
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000046525"
SQ SEQUENCE 1194 AA; 134048 MW; C0D5F0EA8D0D81E0 CRC64;
MAIRTGFCNP FLTQASGIKY NPRTGRGSNR EFLHSYKTTM SSFQFLAPKC LDEDVPMEER
KGVHVGTLSR PPKVYCNGKE VPILDFRCSS PWPRRVNIWG EIDFRGDKFD PRFNTFHVYD
IVETTEAASN GDVSRFATAT RPLGTVITLL GMSRCGKRVA VHVYGICQYF YINKAEVDTA
CGIRSGSELS 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 GVSVEGIAKI 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 GFVCIHAPCW DNKMNTEAEI TEEEQSHQIM RRVFCIPKAI LHQS
