ID DPOL_HCMVA Reviewed; 1242 AA. AC P08546; Q7M6M9; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 29-MAY-2024, entry version 134. DE RecName: Full=DNA polymerase catalytic subunit; DE EC=2.7.7.7; GN Name=UL54; Synonyms=HFLF2; OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5). OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes; OC Herpesvirales; Orthoherpesviridae; Betaherpesvirinae; Cytomegalovirus; OC Cytomegalovirus humanbeta5; Human cytomegalovirus. OX NCBI_TaxID=10360; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3023690; DOI=10.1128/jvi.61.1.125-133.1987; RA Kouzarides T., Bankier A.T., Satchwell S.C., Weston K.M., Tomlinson P., RA Barrell B.G.; RT "Sequence and transcription analysis of the human cytomegalovirus DNA RT polymerase gene."; RL J. Virol. 61:125-133(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3029980; DOI=10.1016/0042-6822(87)90282-0; RA Kouzarides T., Bankier A.T., Satchwell S.C., Weston K.M., Tomlinson P., RA Barrell B.G.; RT "Large-scale rearrangement of homologous regions in the genomes of HCMV and RT EBV."; RL Virology 157:397-413(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6; RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R., RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A., RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.; RT "Analysis of the protein-coding content of the sequence of human RT cytomegalovirus strain AD169."; RL Curr. Top. Microbiol. Immunol. 154:125-169(1990). RN [4] RP GENOME REANNOTATION. RX PubMed=12533697; DOI=10.1099/vir.0.18606-0; RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., RA McGeoch D.J., Hayward G.S.; RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee RT cytomegalovirus genome."; RL J. Gen. Virol. 84:17-28(2003). RN [5] RP ERRATUM OF PUBMED:12533697. RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J., RA McGeoch D.J., Hayward G.S.; RL J. Gen. Virol. 84:1053-1053(2003). RN [6] RP IDENTIFICATION. RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004; RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J., RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W., RA Shenk T., Smith R.D., Nelson J.A.; RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the RT HCMV proteome."; RL J. Virol. 78:10960-10966(2004). RN [7] RP ERRATUM OF PUBMED:15452216. RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J., RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W., RA Shenk T., Smith R.D., Nelson J.A.; RL J. Virol. 78:13395-13395(2004). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1221-1242. RX PubMed=16371349; DOI=10.1074/jbc.m506900200; RA Appleton B.A., Brooks J., Loregian A., Filman D.J., Coen D.M., Hogle J.M.; RT "Crystal structure of the cytomegalovirus DNA polymerase subunit UL44 in RT complex with the C terminus from the catalytic subunit. Differences in RT structure and function relative to unliganded UL44."; RL J. Biol. Chem. 281:5224-5232(2006). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X17403; CAA35413.1; -; Genomic_DNA. DR EMBL; M17209; AAA46008.1; -; Genomic_DNA. DR EMBL; M14709; AAA45988.1; -; Genomic_DNA. DR EMBL; BK000394; DAA00159.1; -; Genomic_DNA. DR PIR; S09817; DJBEC1. DR PDB; 1YYP; X-ray; 2.50 A; B=1221-1242. DR PDBsum; 1YYP; -. DR SMR; P08546; -. DR DIP; DIP-46030N; -. DR IntAct; P08546; 1. DR BindingDB; P08546; -. DR ChEMBL; CHEMBL3414; -. DR DrugBank; DB00369; Cidofovir. DR DrugBank; DB00529; Foscarnet. DR DrugCentral; P08546; -. DR EvolutionaryTrace; P08546; -. DR Proteomes; UP000008991; Genome. DR Proteomes; UP000008992; Genome. DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0008296; F:3'-5'-DNA exonuclease activity; IEA:TreeGrafter. 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:0006287; P:base-excision repair, gap-filling; IEA:TreeGrafter. DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB. DR GO; GO:0045004; P:DNA replication proofreading; IEA:TreeGrafter. DR GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; IEA:TreeGrafter. DR GO; GO:0009432; P:SOS response; IEA:TreeGrafter. 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 1: Evidence at protein level; KW 3D-structure; DNA replication; DNA-binding; DNA-directed DNA polymerase; KW Host nucleus; Nucleotidyltransferase; Reference proteome; Transferase; KW Viral DNA replication. FT CHAIN 1..1242 FT /note="DNA polymerase catalytic subunit" FT /id="PRO_0000046507" 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 877..898 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1108..1163 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 1108..1123 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" FT CONFLICT 942..943 FT /note="FV -> VF (in Ref. 3)" FT /evidence="ECO:0000305" FT HELIX 1229..1234 FT /evidence="ECO:0007829|PDB:1YYP" FT STRAND 1235..1237 FT /evidence="ECO:0007829|PDB:1YYP" FT HELIX 1238..1240 FT /evidence="ECO:0007829|PDB:1YYP" SQ SEQUENCE 1242 AA; 137102 MW; FA59BFF842BED80B 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 EESSALPEGL ETSSGGSNER RVEARVIYGD TDSVFVRFRG LTPQALVARG PSLAHYVTAC LFVEPVKLEF EKVFVSLMMI CKKRYIGKVE GASGLSMKGV DLVRKTACEF VKGVTRDVLS LLFEDREVSE AAVRLSRLSL DEVKKYGVPR GFWRILRRLV QARDDLYLHR VRVEDLVLSS VLSKDISLYR QSNLPHIAVI KRLAARSEEL PSVGDRVFYV LTAPGVRTAP QGSSDNGDSV TAGVVSRSDA IDGTDDDADG GGVEESNRRG GEPAKKRARK PPSAVCNYEV AEDPSYVREH GVPIHADKYF EQVLKAVTNV LSPVFPGGET ARKDKFLHMV LPRRLHLEPA FLPYSVKAHE CC //