DNB2_ADE02
ID DNB2_ADE02 Reviewed; 529 AA.
AC P03264;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04054};
DE Short=DBP {ECO:0000255|HAMAP-Rule:MF_04054};
DE AltName: Full=Early 2A protein {ECO:0000255|HAMAP-Rule:MF_04054};
DE AltName: Full=Early E2A DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04054};
GN Name=DBP {ECO:0000255|HAMAP-Rule:MF_04054};
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=6985485; DOI=10.1093/nar/10.15.4493;
RA Kruijer W., van Schaik F.M.A., Sussenbach J.S.;
RT "Nucleotide sequence of the gene encoding adenovirus type 2 DNA binding
RT protein.";
RL Nucleic Acids Res. 10:4493-4500(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 438-529.
RX PubMed=6259616; DOI=10.1093/nar/9.1.1;
RA Akusjaervi G., Zabielski J., Perricaudet M., Pettersson U.;
RT "The sequence of the 3' non-coding region of the hexon mRNA discloses a
RT novel adenovirus gene.";
RL Nucleic Acids Res. 9:1-17(1981).
RN [3]
RP PHOSPHORYLATION.
RX PubMed=2607338; DOI=10.1099/0022-1317-70-12-3249;
RA Russell W.C., Webster A., Leith I.R., Kemp G.D.;
RT "Phosphorylation of adenovirus DNA-binding protein.";
RL J. Gen. Virol. 70:3249-3259(1989).
RN [4]
RP SUBUNIT, AND DOMAIN.
RX PubMed=9135160; DOI=10.1093/emboj/16.6.1455;
RA Dekker J., Kanellopoulos P.N., Loonstra A.K., van Oosterhout J.A.,
RA Leonard K., Tucker P.A., van der Vliet P.C.;
RT "Multimerization of the adenovirus DNA-binding protein is the driving force
RT for ATP-independent DNA unwinding during strand displacement synthesis.";
RL EMBO J. 16:1455-1463(1997).
RN [5]
RP FUNCTION.
RX PubMed=9545375; DOI=10.1006/jmbi.1998.1652;
RA Dekker J., Kanellopoulos P.N., van Oosterhout J.A., Stier G., Tucker P.A.,
RA van der Vliet P.C.;
RT "ATP-independent DNA unwinding by the adenovirus single-stranded DNA
RT binding protein requires a flexible DNA binding loop.";
RL J. Mol. Biol. 277:825-838(1998).
RN [6]
RP INTERACTION WITH HOST SRCAP.
RX PubMed=11581372; DOI=10.1128/jvi.75.21.10033-10040.2001;
RA Xu X., Chackalaparampil I., Monroy M.A., Cannella M.T., Pesek E.,
RA Chrivia J., Yaciuk P.;
RT "Adenovirus DNA binding protein interacts with the SNF2-related CBP
RT activator protein (SrCap) and inhibits SrCap-mediated transcription.";
RL J. Virol. 75:10033-10040(2001).
RN [7]
RP FUNCTION.
RX PubMed=12747551; DOI=10.1007/978-3-662-05597-7_7;
RA de Jong R.N., van der Vliet P.C., Brenkman A.B.;
RT "Adenovirus DNA replication: protein priming, jumping back and the role of
RT the DNA binding protein DBP.";
RL Curr. Top. Microbiol. Immunol. 272:187-211(2003).
RN [8]
RP FUNCTION.
RX PubMed=12954226; DOI=10.1016/s0042-6822(03)00386-6;
RA Xu X., Tarakanova V., Chrivia J., Yaciuk P.;
RT "Adenovirus DNA binding protein inhibits SrCap-activated CBP and CREB-
RT mediated transcription.";
RL Virology 313:615-621(2003).
CC -!- FUNCTION: Plays a role in the elongation phase of viral strand
CC displacement replication by unwinding the template in an ATP-
CC independent fashion, employing its capacity to form multimers. Also
CC enhances the rate of initiation. Released from template upon second
CC strand synthesis. Assembles in complex with viral pTP, viral pol, host
CC NFIA and host POU2F1/OCT1 on viral origin of replication. Covers the
CC whole ssDNA genome during synthesis. The complementary strand synthesis
CC induces its release from DNA template. May inhibit cellular
CC transcription mediated by the interaction between host SRCAP and CBP.
CC {ECO:0000255|HAMAP-Rule:MF_04054, ECO:0000269|PubMed:12747551,
CC ECO:0000269|PubMed:12954226, ECO:0000269|PubMed:9545375}.
CC -!- SUBUNIT: Homomultimerizes on viral ssDNA bound to pTP (PubMed:9135160).
CC Forms an initiation complex with viral polymerase, pTP and hosts NFIA
CC and POU2F1/OCT1 (By similarity). Interacts with host SRCAP
CC (PubMed:11581372). {ECO:0000255|HAMAP-Rule:MF_04054,
CC ECO:0000269|PubMed:11581372, ECO:0000269|PubMed:9135160}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04054}.
CC Note=Accumulates in infected cells. {ECO:0000255|HAMAP-Rule:MF_04054}.
CC -!- DOMAIN: The C-terminal arm bridges DBP molecules together, thereby
CC creating a chain. {ECO:0000255|HAMAP-Rule:MF_04054,
CC ECO:0000269|PubMed:9135160}.
CC -!- SIMILARITY: Belongs to the adenoviridae E2A DNA-binding protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04054}.
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DR EMBL; J01917; AAA92217.1; -; Genomic_DNA.
DR PIR; B03833; W7AD22.
DR RefSeq; AP_000177.1; AC_000007.1.
DR RefSeq; NP_040527.1; NC_001405.1.
DR SMR; P03264; -.
DR IntAct; P03264; 1.
DR MINT; P03264; -.
DR iPTMnet; P03264; -.
DR GeneID; 5739977; -.
DR KEGG; vg:5739976; -.
DR Proteomes; UP000008167; Genome.
DR GO; GO:0039715; C:nuclear viral factory; IDA:UniProtKB.
DR GO; GO:0019028; C:viral capsid; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IDA:CAFA.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039687; P:viral DNA strand displacement replication; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.269.10; -; 1.
DR Gene3D; 3.90.148.10; -; 2.
DR HAMAP; MF_04054; ADV_DNB2; 1.
DR InterPro; IPR036367; Ad_DBP_C_sf.
DR InterPro; IPR036368; ADBP_zn-bd_sf.
DR InterPro; IPR003176; Adenovirus_DNA-bd_a.
DR InterPro; IPR036362; Adenovirus_DNA-bd_N_sf.
DR InterPro; IPR005376; Adenovirus_DNA-bd_zn-bd.
DR InterPro; IPR037540; ADV_DNB2.
DR Pfam; PF02236; Viral_DNA_bi; 1.
DR Pfam; PF03728; Viral_DNA_Zn_bi; 2.
DR SUPFAM; SSF47724; SSF47724; 1.
DR SUPFAM; SSF57917; SSF57917; 2.
PE 1: Evidence at protein level;
KW DNA replication; DNA-binding; Early protein; Host nucleus;
KW Host-virus interaction; Metal-binding; Phosphoprotein; Reference proteome;
KW Viral DNA replication; Zinc.
FT CHAIN 1..529
FT /note="DNA-binding protein"
FT /id="PRO_0000221677"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..331
FT /note="Flexible loop"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT REGION 513..529
FT /note="C-terminal arm, DBP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 339
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 450
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT MOD_RES 195
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
SQ SEQUENCE 529 AA; 59086 MW; 114F8F02A77B28F1 CRC64;
MASREEEQRE TTPERGRGAA RRPPTMEDVS SPSPSPPPPR APPKKRLRRR LESEDEEDSS
QDALVPRTPS PRPSTSTADL AIASKKKKKR PSPKPERPPS PEVIVDSEEE REDVALQMVG
FSNPPVLIKH GKGGKRTVRR LNEDDPVARG MRTQEEKEES SEAESESTVI NPLSLPIVSA
WEKGMEAARA LMDKYHVDND LKANFKLLPD QVEALAAVCK TWLNEEHRGL QLTFTSNKTF
VTMMGRFLQA YLQSFAEVTY KHHEPTGCAL WLHRCAEIEG ELKCLHGSIM INKEHVIEMD
VTSENGQRAL KEQSSKAKIV KNRWGRNVVQ ISNTDARCCV HDAACPANQF SGKSCGMFFS
EGAKAQVAFK QIKAFMQALY PNAQTGHGHL LMPLRCECNS KPGHAPFLGR QLPKLTPFAL
SNAEDLDADL ISDKSVLASV HHPALIVFQC CNPVYRNSRA QGGGPNCDFK ISAPDLLNAL
VMVRSLWSEN FTELPRMVVP EFKWSTKHQY RNVSLPVAHS DARQNPFDF
