ID DPOL_ELHVK Reviewed; 1041 AA.
AC Q9DKT8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 102.
DE RecName: Full=DNA polymerase catalytic subunit;
DE EC=2.7.7.7;
DE EC=3.1.26.4;
OS Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998) (EIHV-1)
OS (Elephant endotheliotropic herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Proboscivirus;
OC Proboscivirus elephantidbeta1; Elephantid herpesvirus 1.
OX NCBI_TaxID=654902;
OH NCBI_TaxID=9783; Elephas maximus (Indian elephant).
OH NCBI_TaxID=9785; Loxodonta africana (African elephant).
OH NCBI_TaxID=99490; Loxodonta cyclotis (African forest elephant).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17507487; DOI=10.1128/jvi.00255-07;
RA Ehlers B., Kuchler J., Yasmum N., Dural G., Voigt S., Schmidt-Chanasit J.,
RA Jakel T., Matuschka F.R., Richter D., Essbauer S., Hughes D.J., Summers C.,
RA Bennett M., Stewart J.P., Ulrich R.G.;
RT "Identification of novel rodent herpesviruses, including the first
RT gammaherpesvirus of Mus musculus.";
RL J. Virol. 81:8091-8100(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11172087; DOI=10.1099/0022-1317-82-3-475;
RA Ehlers B., Burkhardt S., Goltz M., Bergmann V., Ochs A., Weiler H.,
RA Hentschke J.;
RT "Genetic and ultrastructural characterization of a European isolate of the
RT fatal endotheliotropic elephant herpesvirus.";
RL J. Gen. Virol. 82:475-482(2001).
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 -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. 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; AF322977; AAG41999.1; -; Genomic_DNA.
DR SMR; Q9DKT8; -.
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; 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 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; DNA-binding; DNA-directed DNA polymerase; Endonuclease;
KW Host nucleus; Hydrolase; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; Transferase; Viral DNA replication.
FT CHAIN 1..1041
FT /note="DNA polymerase catalytic subunit"
FT /id="PRO_0000408152"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 118411 MW; 28F13228D4428E55 CRC64;
MAFFNPYFKS KNKGSDMPPK QSMSFTKQHK TKESAFLSIT PECIIKPKSS KLLKKYNGEQ
PRLFYNGEPV LLYTVREISQ WPVKDIMKVN NGTVDGSCNV VSTSHEPDSP VKNNCEETVV
FHIYEQCVFC AHDVSYEYLP WRYKRFLSPT GTIISLIGKT EDGTDVCVNV HGQAYYFYVA
MKDEAATRDA VSKVMSNLEK ESSSCSYVMK SVNKMSLMGF NTNTSSYLMM IFSNHFVGKE
AARNLKDLDF EIFEHLVEPN TRFLVDNEFC SFGWYSLKTP YVRQTSKDSN CELELDCCVG
DLQVLRDRVD WPNYKCMAFD IECLSGSVDD AFPDATNPDD IIIQISCVCF DIKNTIETQH
LFTLGSCAEI PGVYIYECAS EYELIESFLT FVRVYGPNFI TGYNINAFDI PYVIGRCRYY
NIQCGAFTKM KRGRMTCFKG MESFLNRCQC KVTISGIVII DMYRVCMDKV SAPNHKLDTV
VDMLLGEKKH SVSYKQIPVL FRRDDDGRAV VGAYCVHDSV LVHKLFCKLL FHYEASAIAR
LSNISINKVV FDGQQSRIFT CMLAAARREG LIIPSIDEAG EDTYQGATVL EPKTGFYNTP
VAVFDFASLY PSIIQAYNLC YCTLITDNYV ASLREEDITM VTTNTGRVHR FVKPHVRKSI
LSQLLTSWLA ERKAVREKLK HCKDPLMQIL LDKQQLALKL TCNAVYGFTG VSKGMFPCLA
IAESVTAQGR QLLAVTKQYI CDRFNDWTFL TQIAPELVDC PVDSNRFKID VVYGDTDSVF
VLLCGIENAD RLYSALPNFV AHITKTLFPP PIKLEVDKVF EKLLLLCKKR YVGVLHGEEK
LSMKGIDLVR RNVCGFVKNT TLAVIKSLFS DNVISEAVQK MSGMTQDQVC KEGLPPGFFK
LVALITDARE RLYENRVDIH ELQLSATLTQ ACDKYKQQNL PHLTVVRKKL ERREEIPNTG
DRIFYVLLAH PDERVANYVI AEDPDYVETH RLQINCSKYF SNLISSITHS ISPIFPEFIS
KPDRFLMSCV PRKTYPKPIL N
//
