ID   DPOL_TUHV2              Reviewed;        1171 AA.
AC   Q9YUS2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   23-FEB-2022, entry version 97.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
GN   Name=DPOL;
OS   Tupaiid herpesvirus (strain 2) (TuHV-2) (Herpesvirus tupaia (strain 2)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae.
OX   NCBI_TaxID=132678;
OH   NCBI_TaxID=37347; Tupaia belangeri (Common tree shrew) (Tupaia glis belangeri).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9880021; DOI=10.1099/0022-1317-79-12-3049;
RA   Springfeld C., Tidona C.A., Kehm R., Bahr U., Darai G.;
RT   "Identification and characterization of the Tupaia herpesvirus DNA
RT   polymerase gene.";
RL   J. Gen. Virol. 79:3049-3053(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10392721; DOI=10.1016/s0168-1702(99)00012-x;
RA   Bahr U., Springfeld C., Tidona C.A., Darai G.;
RT   "Structural organization of a conserved gene cluster of Tupaia herpesvirus
RT   encoding the DNA polymerase, glycoprotein B, a probable processing and
RT   transport protein, and the major DNA binding protein.";
RL   Virus Res. 60:123-136(1999).
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   -!- SUBCELLULAR LOCATION: Host nucleus.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family. {ECO:0000305}.
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DR   EMBL; AF074328; AAD08667.1; -; Genomic_DNA.
DR   EMBL; AF084543; AAD42936.1; -; Genomic_DNA.
DR   SMR; Q9YUS2; -.
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: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; 2.
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; Host nucleus;
KW   Nucleotidyltransferase; Transferase; Viral DNA replication.
FT   CHAIN           1..1171
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000046524"
FT   REGION          647..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1149..1171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..663
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1171 AA;  128591 MW;  D2D64897FD5E70E8 CRC64;
     MSTVTFFNPY LCGPRKPRAP SAGEGGAEGA AAARARAASA PFLQIVPRGC LYDGERGLLK
     HNCALAPRMF FRDRPYVLSK DLVWPTLPPP AVPASTTERA PRAPAPSADL LFHMYDQAET
     VVSADSKELI HPGYRHRITP CGVVLRLFGR TADGASLCVN VFGQDAYFYC RYGDAQSLHD
     RLYRLSDTLE LAPVFHVRVR RVQRCSIYGY GTRPFADLYL VACGNWHVLK KMGQCLLDEG
     VEVFEVGVSP LTRFLLDKKI PSFGWCRLRR WHARPAHGRL STAELEVDCE VADVRGVDDV
     AWPLYRCLSF DIECLSGGGA FPVAENLDDV VIQISCVCYP VGGTEEQRAA FPVAERHLFT
     LGPCAPIPGV LVYEFPSEFE LLCGFFTFFG RYAPEFVTGY NINNFDWRYL LTRAERVYRW
     PVAEYTRLRF GGRFCAYVPG GGGRQPGFRT AQTKVLITGT VVLDLYPVCM AKVSAPDYKL
     NTVCELYLGR QKEDLSYKEL PRAFLSGDAG RARVGRYCVQ DAVLVKELFE KLNYHYEAAA
     VARLARISLR KVIFEGQQIR IYTCLLEEAA ARQMVVPTFR SGAQRGAAPG AGGGGGEETT
     YQGATVFEPT VGYHHAPVAV FDFASLYPSI IMAHNLCYST WLRDDPGTPA RPPETPARPP
     ETPAAGPSGA AHAGGVPGAT FRTPFRTPAG VPAAAAGGAG AGPPGGGAVS SASVGGRAAV
     SPSETPAERE PEPAPEDVFV VHVGQGVSYR FVRENVRASI LSELLRRWLA QRRAVREAMR
     ECEDETRRLL LDKEQLALKV TCNAFYGFTG FSQGMLPCLP VAASITTIGR DMLSRTSAYI
     EAHFAEPAFL ARFFEPGDLP RADEPPPTVR VIYGDTDSVF VRFGGVRAGA IVARGEDLAA
     AVTEALFTEP VKLEFEKLFV ALMMICKKRY IGRVFGSDAL VMKGVDLVRK TACRFVKTVV
     RDVVELVFRD AAVAEAATRM SELTLEEMRR VGVPAGFHVL LQRLARARDD LFSGRVETAA
     LVLSSVLSQD VSRYKQLNLP HLAVIRRLAA RSEELPSVGD RVSYVLTAGP PDGRANAPNY
     ELAEDPDYVA AHRVPIHAAK YFEQVVKAVT NTLYPVFPRG VVRRDRFLAD LVPKRVYLGD
     EFKRHARPVE EEVCESERGG SGLLSSLDSS R