DPOL_HCMVA
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 23-FEB-2022, entry version 129.
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; Herpesviridae; Betaherpesvirinae; 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}.
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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: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; 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 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
