DPOL_GAHVM
ID DPOL_GAHVM Reviewed; 1220 AA.
AC Q9E6N9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 23-FEB-2022, entry version 105.
DE RecName: Full=DNA polymerase catalytic subunit;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
GN Name=MDV043;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14223.1; -; Genomic_DNA.
DR RefSeq; YP_001033959.1; NC_002229.3.
DR SMR; Q9E6N9; -.
DR PRIDE; Q9E6N9; -.
DR GeneID; 4811504; -.
DR KEGG; vg:4811504; -.
DR Proteomes; UP000008072; 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; 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; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..1220
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000406418"
SQ SEQUENCE 1220 AA; 138472 MW; B3FC59CEA0AC1F09 CRC64;
MSVDGTKTFF NPYIGARKRS LEARNGLSFS TGQNYDEKNN RRDRNSITYV TTIDEFKYIA
PKCLDDKDVK QKGTHIGKLK RSPVLYKNGE EYVFLNFEDC EDVWPRRCSI WNNRSFLPAD
FDPRFSRFHV YDMIETVEFA SAAIDRDKNR FLELLRPMGT IVTMMGITEC GKRVAVHVYG
IKPYFYMRKV DTDTICGSRC PRELAEKLAN VVRSSVNEVA NAKRFCTPVT RTVSADCFEV
DVVQRKDIYY YGTGHDEFYR VKSQSGKFIT LLCDNFYPSI IKYEGNIDAI TRMVLDNNGF
STFGWYSFKV GNNGEKVQVR APCHHCTSCD IEINCTVDNL IGYPEDDAWP DYKLLCFDIE
CKSGGVNECA FPCATNEEDV VIQISCLLYS INTKQLEHAL LFALGACDLP QTFKETFQSS
YNILPIVLEF DSEFELLLAF MTFIKQYAPE FVTGYNIVNF DWAFIVTKLT TVYNMRLDGY
GVVNQKGMFK VWDAGTNRFQ KKGKFKATGM ITLDMYSIAT EKLKLQSYKL DVVAEAALGE
RKKELSYKEI PSHFAAGPEK RGIIGEYCLQ DSLLVGKLFF KYIPHLELSA IAKLAGILLS
KAIFDGQQIR VYTCLLRLAR SHGFILPEKN KKFAETVSLT CEEDQTEICE HDSPQEPIHN
IKQSSLCHSN SGRTIGYQGA KVLDPISGFH VDPVMVFDFA SLYPSIIQAH NLCFTTLVHD
DTNLSNLRPQ DDYLEINVQG KLLRFVKPHI RESLLAILLK DWLAMRKAIR AKIPESCDEI
AVLLDKQQAA IKVVCNSVYG FCGVSNGLLP CIDVAATVTT IGRNMLLTVR DYIHKQWGTR
DALLREFPNL SNFMRPEDYS VSVIYGDTDS VFIKFKGVDI HGLVTTGDDM AKRVSSDLFP
KPIKLECEKT FNKLLLITKK KYMGTIHGGR MLMKGVDIVR KNNCRFINTY AKKLSDLLFL
DDTVAKAAAT VAEKPPSFWA TSPLPEGLNS FGGVLAEAYT RMMINNITEV EDFAMSAELS
RPPDAYTNKR IPHLTVYYKL AMRSEQLPVV KDRISYVIAA ATPEVVRDSA RVAEFRGELD
LCHQNSNTSC PGDSVMTNKE TYVRHSPRNK LLISDMAEDP KYLLANNIPL NTDYYLSHLL
GTLCVTFKAL FGNDVKITET VLRRFIPETF TEDCSYTERV SSEMFTTIRS GIGLQVNEEE
ETRRKLNIAF RILTATPHRY
