DPOL_ADE40
ID DPOL_ADE40 Reviewed; 1188 AA.
AC P48311;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04055};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_04055};
GN Name=POL {ECO:0000255|HAMAP-Rule:MF_04055};
OS Human adenovirus F serotype 40 (HAdV-40) (Human adenovirus 40).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=28284;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugan;
RX PubMed=8263936; DOI=10.1006/jmbi.1993.1687;
RA Davison A.J., Telford E.A., Watson M.S., McBride K., Mautner V.;
RT "The DNA sequence of adenovirus type 40.";
RL J. Mol. Biol. 234:1308-1316(1993).
CC -!- FUNCTION: Eukaryotic-type DNA polymerase involved in viral genomic
CC replication. DNA synthesis is protein primed, and acts in a strand
CC displacement replication. Assembles in complex with viral pTP, DBP,
CC host NFIA and host POU2F1/OCT1 on viral origin of replication. The
CC polymerase covalently transfers dCMP onto pTP, thereby initiating
CC complementary strand synthesis. {ECO:0000250|UniProtKB:P03261,
CC ECO:0000250|UniProtKB:P04495, ECO:0000255|HAMAP-Rule:MF_04055}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04055};
CC -!- SUBUNIT: Heterodimer with the terminal protein; this heterodimer binds
CC to bp 9 to 18 of the genome. Forms a complex with viral pTP, DBP and
CC hosts NFIA and POU2F1/OCT1 for initiation of replication.
CC {ECO:0000250|UniProtKB:P04495, ECO:0000255|HAMAP-Rule:MF_04055}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03261,
CC ECO:0000255|HAMAP-Rule:MF_04055}.
CC -!- MISCELLANEOUS: This DNA polymerase requires a protein as a primer.
CC {ECO:0000255|HAMAP-Rule:MF_04055}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000255|HAMAP-Rule:MF_04055, ECO:0000305}.
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DR EMBL; L19443; AAC13953.1; -; Genomic_DNA.
DR RefSeq; NP_040853.1; NC_001454.1.
DR GeneID; 2715933; -.
DR KEGG; vg:2715933; -.
DR Proteomes; UP000151954; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.1600.10; -; 1.
DR HAMAP; MF_04055; ADV_DPOL; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR014382; DNA-dir_DNA_pol_B_adenovir.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR004868; DNA-dir_DNA_pol_B_mt/vir.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR Pfam; PF03175; DNA_pol_B_2; 1.
DR PIRSF; PIRSF000788; DPol_ADV; 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; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..1188
FT /note="DNA polymerase"
FT /id="PRO_0000046497"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 135289 MW; 338106E30E2753BC CRC64;
MALVPSPRAG GFLPAETHSG PQPPRRRVRQ STAGAAPTAT RAPRRRAATA SPGEPPSTTA
SGRPPAANNV SLTPNSRLRG TIVAPRGQGL LYAIDTATNS PMEIKFHRRL ASALTRLLQV
NLRSVPADLN EAFLDSLDSS QIRTLALKLK VPRVEVWTCG SRGVVVPSII HPQQERAGAE
EGDEGERQDT EDFLNFPLRF LVRGRQVHLI QEMQSVQRCE YCARFYKYQH ECTVRRRDFY
FHHINAHSSG WWQKINFFPI GSHPRVERLF VTYDVETYTW MGAFGKQLVP FMLVMHLSGE
EALVKEACRL ACELQWDTWG NDERTFYVVT PEKLAVGKKF REYRNRLQAH FALQLWRGFL
AANPQLAEWA CLEMGLFSPD YLTYEELQKA PKLQGRPRFL ELYIVGHNIN GFDEIVLAAQ
VINNRSDVPG PFKITRNFMP RAGKILFNDI TFALPNPSSK KRTDYRLWEQ GACDDSDFKY
QFLKVMVRDT FALTHTSLRK AAQAYTLPVE KGCCPYKAVN EFYMLGSYRA DERGFPAEDY
WKDREEYLLN RELWEKKQCP HYDLVRETLD YCALDVLVTA ALVQKLRESY AQFIRDAVGL
PEASFNVFQR PTISSNSHAI FRQILYRTVK PQRSDLGGSL LAPSHEMYDY VRASIRGGRC
YPTYIGVLRE PLYVYDICGM YASALTHPMP WGFPLNPYER ALAVRDWEHA LLQVGTPIDY
FNRTLLPGIF TIDADPPPEN LLDVLPPLCS RKGGRLCWTN EPLRGEVVTS VDLITLHNRG
WHVRLLPDER ATVFPEWRCV AKEYVHLNIT AKERADREKN QTLRSIAKLL SNALYGSFAT
KLDNKKIVFS DQMDSATIKS IAAGQINIKS TSFVETDTLS AEVMPTFQRA YSPEQLAVVH
SDAEESDEEP GHAPFYTPTH KPNDHVTYTY KPITFMDAEE DDLCLHTLEK VDPLVENNRY
PSQIASFVLA WTRAFVSEWS EILYAEDRGT PLEQRTLKSV YGDTDSLFVT EAGYRLMETR
GKKRIKKHGG NLVFDPKHPE LAWLVECETV CAQCGADAYS PESVFLAPKL YALKCLRCPS
CQQISKGKLR AKGHAAETLN YDLMLKCYLA DFQGEDARFH TSRMSLKRTL ASAQPGARPF
TVTETNLTRT LRPWKDITLA PLDAHRLVPY SQSRPNPRNQ EVCWIEMP
