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 05-DEC-2018, entry version 115. 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; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Betaherpesvirinae; Cytomegalovirus. OX NCBI_TaxID=10360; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3023690; RA Kouzarides T., Bankier A.T., Satchwell S.C., Weston K.M., RA Tomlinson P., 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., RA Tomlinson P., Barrell B.G.; RT "Large-scale rearrangement of homologous regions in the genomes of RT HCMV and EBV."; RL Virology 157:397-413(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2161319; 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., RA Alcendor D.J., McGeoch D.J., Hayward G.S.; RT "The human cytomegalovirus genome revisited: comparison with the RT chimpanzee cytomegalovirus genome."; RL J. Gen. Virol. 84:17-28(2003). RN [5] RP ERRATUM. RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., RA Alcendor D.J., 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: RT the HCMV proteome."; RL J. Virol. 78:10960-10966(2004). RN [7] RP ERRATUM. 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., RA Hogle J.M.; RT "Crystal structure of the cytomegalovirus DNA polymerase subunit UL44 RT in complex with the C terminus from the catalytic subunit. Differences RT in 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 CC complex is composed of six viral proteins: the DNA polymerase, CC processivity factor, primase, primase-associated factor, helicase, CC and ssDNA-binding 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- CC COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7; CC -!- SUBUNIT: Forms a complex with the ssDNA-binding protein UL57, the CC DNA polymerase processivity factor UL44, and the alkaline CC exonuclease UL98. Interacts with the putative helicase-primase CC complex composed of UL70, UL102 and UL105 proteins; these CC interactions may coordinate leading and lagging strand DNA CC synthesis at the replication fork (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250}. Note=the protein CC is present at discrete sites in nuclei, called replication CC compartments where viral DNA replication occurs. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. CC {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 ProteinModelPortal; P08546; -. 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 PRIDE; P08546; -. DR OrthoDB; VOG0900001M; -. 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: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:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 3.30.420.10; -; 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; 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 PROSITE; PS00116; DNA_POLYMERASE_B; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Host nucleus; Nucleotidyltransferase; KW Reference proteome; Transferase; Viral DNA replication. FT CHAIN 1 1242 DNA polymerase catalytic subunit. FT /FTId=PRO_0000046507. FT COMPBIAS 658 665 Poly-Ser. FT CONFLICT 942 943 FV -> VF (in Ref. 3). {ECO:0000305}. FT HELIX 1229 1234 {ECO:0000244|PDB:1YYP}. FT STRAND 1235 1237 {ECO:0000244|PDB:1YYP}. FT HELIX 1238 1240 {ECO:0000244|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 //