DPOL_EHV1V
ID DPOL_EHV1V Reviewed; 1220 AA.
AC Q6S6P1;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=DNA polymerase catalytic subunit;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
GN OrderedLocusNames=30;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45914.1; -; Genomic_DNA.
DR SMR; Q6S6P1; -.
DR PRIDE; Q6S6P1; -.
DR Proteomes; UP000008296; 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..1220
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000046519"
FT REGION 21..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1220 AA; 135955 MW; 062483351A1A14ED CRC64;
MAAREQANSV RRSGFFNPFI GKRPFFRPGS GQTAETERPR PPQHSYCTEV GSFKFIAPRC
LDEEAPADQR RGVHVGTLER PPKVYCDGSE YDVLNFASGG CWPRRIRVWN GQDFRGDGFN
PRFERFHVYD IVETSESASH DDPSRFAELS RPSGSVVTLL GMSECGKRVA VHVYGVRHYF
YMAKAEVDSA CGITTEAELV RAMVDCAHSS ALSAALGNGN GGKQSGGSGG GWWGGKHVSA
DCFKVETVCH TTLYYFGSKP ALYYRVSASS SRLGGFICDN FHPEITKFEG SVDVTTRLLL
DNENFTSFGW YRLRPGTHGE RVQLRPVERH VTSSDVEINC TPDNLEPIPD EAAWPDYKLM
CFDIECKAGT GNEMAFPVAT NQEDLVIQIS CLLYSLATQN HEHTLLFSLG SCDISEEYSF
ACVQRGEPRP TVLEFDSEYE LLVAFLTFLK QYSPEFATGY NIVNFDWAYI VNKVTSVYNI
KLDGYGKFNK GGLFKVWDIA TNHFQKKSKV KINGLISLDM YSVATEKLKL PSYKLDAVVG
DVLGEHKIDL PYKEIPSYYA GGPDRRGVIG EYCIQDSRLV GKLFFKYLPH LELSAVAKLA
RITLTRVIFD GQQIRVYTCL LKLARERNFI LPDNRRRFDS QADAASETSE LAMDSQSHAF
DSTDEPDGVD GTPDAAGSGA TSENGGGKPG VGRAVGYQGA KVLDPVSGFH VDPVVVFDFA
SLYPSIIQAH NLCFTTLALD EVDLAGLQPS VNYSTFEVGD QKLFFVHAHI RESLLGILLR
DWLAMRKAVR ARIPTSTPEE AVLLDKQQSA IKVICNSVYG FTGVANGLLP CLRIAATVTT
IGRDMLLKTR DYVHSRWATR ELLEDNFPGA IGFRNHKPYS VRVIYGDTDS VFIKFVGLTY
EGVSELGDAM SRQISADLFR APIKLECEKT FQRLLLITKK KYIGVINGGK MLMKGVDLVR
KNNCSFINLY ARHLVDLLLY DEDVATAAAK VTDVPPAEWV GRPLPSGFDK FGRVLVEAYN
RITAPNLDVR EFVMTAELSR SPESYTNKRL PHLTVYFKLA MRNEELPSVK ERIPYVIVAQ
TEAAEREAGV VNSMRGTAQN PVVTKTARPQ PKRKLLVSDL AEDPTYVSEN DVPLNTDYYF
SHLLGTISVT FKALFGNDVR TTENLLKRFI PETPHKTPTK TQALLERAGF EKLTPFTPEE
ESRRILHTVF CTLEAAPHQS
