ID   DPOL_HCMVM              Reviewed;        1242 AA.
AC   Q6SW77; D2K3M2;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 98.
DE   RecName: Full=DNA polymerase catalytic subunit;
DE            EC=2.7.7.7;
GN   Name=UL54;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(2004).
CC   -!- FUNCTION: Replicates viral genomic DNA in the late phase of lytic
CC       infection, producing long concatemeric 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 (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   -!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL57, the DNA
CC       polymerase processivity factor UL44, and the alkaline exonuclease UL98.
CC       Interacts with the putative helicase-primase complex composed of UL70,
CC       UL102 and UL105 proteins; these interactions may coordinate leading and
CC       lagging strand DNA synthesis at the replication fork (By similarity).
CC       {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; AY446894; AAR31619.1; -; Genomic_DNA.
DR   RefSeq; YP_081513.1; NC_006273.2.
DR   SMR; Q6SW77; -.
DR   PRIDE; Q6SW77; -.
DR   DNASU; 3077501; -.
DR   GeneID; 3077501; -.
DR   KEGG; vg:3077501; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; Genome.
DR   GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019033; C:viral tegument; TAS:Reactome.
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; 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; Early protein;
KW   Host nucleus; Nucleotidyltransferase; Reference proteome; Transferase;
KW   Viral DNA replication.
FT   CHAIN           1..1242
FT                   /note="DNA polymerase catalytic subunit"
FT                   /id="PRO_0000417828"
FT   REGION          14..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1109..1162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1112..1128
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1141..1159
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1242 AA;  137158 MW;  48C8C64299ED10EF CRC64;
     MFFNPYLSGG VTGGAVAGGR RQRSQPGSAQ GSGKRPPQKQ FLQIVPRGVM FDGQTGLIKH
     KTGRLPLMFY REIKHLLSHD MVWPCPWRET LVGRVVGPIR FHTYDQTDAV LFFDSPENVS
     PRYRQHLVPS GNVLRFFGAT EHGYSICVNV FGQRSYFYCE YSDTDRLREV IASVGELVPE
     PRTPYAVSVT PATKTSIYGY GTRPVPDLQC VSISNWTMAR KIGEYLLEQG FPVYEVRVDP
     LTRLVIDRRI TTFGWCSVNR YDWRQQGRAS TCDIEVDCDV SDLVAVPDDS SWPRYRCLSF
     DIECMSGEGG FPCAEKSDDI VIQISCVCYE TGGNTAVDQG IPNGNDGRGC TSEGVIFGHS
     GLHLFTIGTC GQVGPDVDVY EFPSEYELLL GFMLFFQRYA PAFVTGYNIN SFDLKYILTR
     LEYLYKVDSQ RFCKLPTAQG GRFFLHSPAV GFKRQYAAAF PSASHNNPAS TAATKVYIAG
     SVVIDMYPVC MAKTNSPNYK LNTMAELYLR QRKDDLSYKD IPRCFVANAE GRAQVGRYCL
     QDAVLVRDLF NTINFHYEAG AIARLAKIPL RRVIFDGQQI RIYTSLLDEC ACRDFILPNH
     YSKGTTVPET NSVAVSPNAA IISTAAVPGD AGSVAAMFQM SPPLQSAPSS QDGVSPGSGS
     NSSSSVGVFS VGSGSSGGVG VSNDNHGAGG TAAVSYQGAT VFEPEVGYYN DPVAVFDFAS
     LYPSIIMAHN LCYSTLLVPG GEYPVDPADV YSVTLENGVT HRFVRASVRV SVLSELLNKW
     VSQRRAVREC MRECQDPVRR MLLDKEQMAL KVTCNAFYGF TGVVNGMMPC LPIAASITRI
     GRDMLERTAR FIKDNFSEPC FLHNFFNQED YVVGTREGDS EESSTLPEGL ETSSGGLNER
     RVEARVIYGD TDSVFVRFRG LTPQALVARG PSLAHYVTAC LFVEPVKLEF EKVFVSLMMI
     CKKRYIGKVE GASGLSMKGV DLVRKTACEF VKGVTRDVLS LLFEDREVSE AAVRLSRLSL
     DEVKKYGVPR GFWRILRRLV QARDDLYLHR VRVEDLVLSS VLSKDISLYR QSNLPHIAVI
     KRLAARSEEL PSVGDRVFYV LTAPGVRAAP QGSSDNGDSV TTGVVSRSDA IDGTDDDADG
     GGVEESNRRG GEPAKKRARK PPSAVCNYEV AEDPSYVREH GVPIHADKYF EQVLKAVTNV
     LSPVFPGGET ARKDKFLHMV LPRRLHLEPA FLPYSVKAHE CC