DPOL_ADE02
ID DPOL_ADE02 Reviewed; 1198 AA.
AC P03261;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04055};
DE EC=2.7.7.7 {ECO:0000255|HAMAP-Rule:MF_04055, ECO:0000269|PubMed:6540263};
GN Name=POL {ECO:0000255|HAMAP-Rule:MF_04055};
OS Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=10515;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7142161; DOI=10.1016/s0021-9258(18)33473-2;
RA Gingeras T.R., Sciaky D., Gelinas R.E., Bing-Dong J., Yen C.E., Kelly M.M.,
RA Bullock P.A., Parsons B.L., O'Neill K.E., Roberts R.J.;
RT "Nucleotide sequences from the adenovirus-2 genome.";
RL J. Biol. Chem. 257:13475-13491(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7142162; DOI=10.1016/s0021-9258(18)33474-4;
RA Alestroem P., Akusjaervi G., Pettersson M., Pettersson U.;
RT "DNA sequence analysis of the region encoding the terminal protein and the
RT hypothetical N-gene product of adenovirus type 2.";
RL J. Biol. Chem. 257:13492-13498(1982).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=6540263; DOI=10.1016/s0021-9258(17)42726-8;
RA Field J., Gronostajski R.M., Hurwitz J.;
RT "Properties of the adenovirus DNA polymerase.";
RL J. Biol. Chem. 259:9487-9495(1984).
RN [4]
RP INTERACTION WITH THE TERMINAL PROTEIN.
RX PubMed=8985382; DOI=10.1128/jvi.71.1.539-547.1997;
RA Webster A., Leith I.R., Hay R.T.;
RT "Domain organization of the adenovirus preterminal protein.";
RL J. Virol. 71:539-547(1997).
RN [5]
RP MOTIF.
RX PubMed=11390396; DOI=10.1074/jbc.m103159200;
RA Brenkman A.B., Heideman M.R., Truniger V., Salas M., van der Vliet P.C.;
RT "The (I/Y)XGG motif of adenovirus DNA polymerase affects template DNA
RT binding and the transition from initiation to elongation.";
RL J. Biol. Chem. 276:29846-29853(2001).
RN [6]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=12134025; DOI=10.1128/jvi.76.16.8200-8207.2002;
RA Brenkman A.B., Breure E.C., van der Vliet P.C.;
RT "Molecular architecture of adenovirus DNA polymerase and location of the
RT protein primer.";
RL J. Virol. 76:8200-8207(2002).
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:0000255|HAMAP-Rule:MF_04055,
CC ECO:0000269|PubMed:12134025}.
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, ECO:0000269|PubMed:6540263};
CC -!- SUBUNIT: Heterodimer with the terminal protein; this heterodimer binds
CC to bp 9 to 18 of the genome (By similarity) (PubMed:8985382). Forms a
CC complex with viral pTP, DBP and hosts NFIA and POU2F1/OCT1 for
CC initiation of replication (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_04055, ECO:0000269|PubMed:8985382}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92206.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J01917; AAA92206.1; ALT_INIT; Genomic_DNA.
DR PIR; A92351; WMAD12.
DR RefSeq; AP_000166.1; AC_000007.1.
DR RefSeq; NP_040516.2; NC_001405.1.
DR IntAct; P03261; 1.
DR MINT; P03261; -.
DR GeneID; 2652985; -.
DR KEGG; vg:2652985; -.
DR Proteomes; UP000008167; 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; IDA:UniProtKB.
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:0039687; P:viral DNA strand displacement replication; IDA:UniProtKB.
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 1: Evidence at protein level;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Host nucleus;
KW Nucleotidyltransferase; Reference proteome; Transferase;
KW Viral DNA replication.
FT CHAIN 1..1198
FT /note="DNA polymerase"
FT /id="PRO_0000046492"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 906..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1198 AA; 135670 MW; 464EB16F37B6069E CRC64;
MALVQAHRAR RLHAEAPDSG DQPPRRRVRQ QPPRAAPAPA RARRRRAPAP SPGGSRAPPT
SGGPPASPLL DASSKDTPAA HRPPRGTVVA PRGCGLLQVI DAATNQPLEI RYHLDLARAL
TRLCEVNLQE LPPDLSPREL QTMDSSHLRD VVIKLRPPRA DIWTLGSRGV VVRSTITPLE
QPDGQGQAAE VEDHQPNPPG EGLKFPLCFL VRGRQVNLVQ DVQPVHRCQY CARFYKSQHE
CSARRRDFYF HHINSHSSNW WREIQFFPIG SHPRTERLFV TYDVETYTWM GAFGKQLVPF
MLVMKFGGDE PLVTAARDLA VDLGWDRWEQ DPLTFYCITP EKMAIGRQFR TFRDHLQMLM
ARDLWSSFVA SNPHLADWAL SEHGLSSPEE LTYEELKKLP SIKGTPRFLE LYIVGHNING
FDEIVLAAQV INNRSEVPGP FRITRNFMPR AGKILFNDVT FALPNPRSKK RTDFLLWEQG
GCDDTDFKYQ YLKVMVRDTF ALTHTSLRKA AQAYALPVEK GCCAYQAVNQ FYMLGSYRSE
ADGFPIQEYW KDREEFVLNR ELWKKKGQDK YDIIKETLDY CALDVQVTAE LVNKLRDSYA
SFVRDAVGLT DASFNVFQRP TISSNSHAIF RQIVFRAEQP ARSNLGPDLL APSHELYDYV
RASIRGGRCY PTYLGILREP LYVYDICGMY ASALTHPMPW GPPLNPYERA LAARAWQQAL
DLQGCKIDYF DARLLPGVFT VDADPPDETQ LDPLPPFCSR KGGRLCWTNE RLRGEVATSV
DLVTLHNRGW RVHLVPDERT TVFPEWRCVA REYVQLNIAA KERADRDKNQ TLRSIAKLLS
NALYGSFATK LDNKKIVFSD QMDAATLKGI TAGQVNIKSS SFLETDNLSA EVMPAFEREY
SPQQLALADS DAEESEDERA PTPFYSPPSG TPGHVAYTYK PITFLDAEEG DMCLHTLERV
DPLVDNDRYP SHLASFVLAW TRAFVSEWSE FLYEEDRGTP LEDRPLKSVY GDTDSLFVTE
RGHRLMETRG KKRIKKHGGN LVFDPERPEL TWLVECETVC GACGADAYSP ESVFLAPKLY
ALKSLHCPSC GASSKGKLRA KGHAAEGLDY DTMVKCYLAD AQGEDRQRFS TSRTSLKRTL
ASAQPGAHPF TVTQTTLTRT LRPWKDMTLA RLDEHRLLPY SESRPNPRNE EICWIEMP
