DNB2_ADE05
ID DNB2_ADE05 Reviewed; 529 AA.
AC P03265;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 130.
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 5 (HAdV-5) (Human adenovirus 5).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus.
OX NCBI_TaxID=28285;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6117824; DOI=10.1093/nar/9.18.4439;
RA Kruijer W., van Schaik F.M.A., Sussenbach J.S.;
RT "Structure and organization of the gene coding for the DNA binding protein
RT of adenovirus type 5.";
RL Nucleic Acids Res. 9:4439-4457(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1727603; DOI=10.1016/0042-6822(92)90082-z;
RA Chroboczek J., Bieber F., Jacrot B.;
RT "The sequence of the genome of adenovirus type 5 and its comparison with
RT the genome of adenovirus type 2.";
RL Virology 186:280-285(1992).
RN [3]
RP FUNCTION.
RX PubMed=12502807; DOI=10.1128/jvi.77.2.915-922.2003;
RA van Breukelen B., Brenkman A.B., Holthuizen P.E., van der Vliet P.C.;
RT "Adenovirus type 5 DNA binding protein stimulates binding of DNA polymerase
RT to the replication origin.";
RL J. Virol. 77:915-922(2003).
RN [4]
RP FUNCTION, AND IDENTIFICATION IN THE INITIATION COMPLEX.
RX PubMed=12747549; DOI=10.1007/978-3-662-05597-7_5;
RA Liu H., Naismith J.H., Hay R.T.;
RT "Adenovirus DNA replication.";
RL Curr. Top. Microbiol. Immunol. 272:131-164(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 176-529.
RX PubMed=8039495; DOI=10.1002/j.1460-2075.1994.tb06598.x;
RA Tucker P.A., Tsernoglou D., Tucker A.D., Coenjaerts F.E.J., Leenders H.,
RA van der Vliet P.C.;
RT "Crystal structure of the adenovirus DNA binding protein reveals a hook-on
RT model for cooperative DNA binding.";
RL EMBO J. 13:2994-3002(1994).
RN [6] {ECO:0007744|PDB:1ANV}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 174-529 IN COMPLEX WITH ZINC.
RX PubMed=15299602; DOI=10.1107/s0907444996005525;
RA Kanellopoulos P.N., Tsernoglou D., van der Vliet P.C., Tucker P.A.;
RT "Conformational change of the adenovirus DNA-binding protein induced by
RT soaking crystals with K3UO2F5 solutions.";
RL Acta Crystallogr. D 52:942-945(1996).
RN [7] {ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 174-529 IN COMPLEX WITH ZINC.
RX PubMed=8632448; DOI=10.1006/jmbi.1996.0141;
RA Kanellopoulos P.N., Tsernoglou D., van der Vliet P.C., Tucker P.A.;
RT "Alternative arrangements of the protein chain are possible for the
RT adenovirus single-stranded DNA binding protein.";
RL J. Mol. Biol. 257:1-8(1996).
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 relese 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:12502807,
CC ECO:0000269|PubMed:12747549}.
CC -!- SUBUNIT: Homomultimerizes on viral ssDNA bound to pTP. Forms a
CC initiation complex with viral polymerase, pTP and hosts NFIA and
CC POU2F1/OCT1. Interacts with host SRCAP. {ECO:0000255|HAMAP-
CC Rule:MF_04054}.
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 -!- SIMILARITY: Belongs to the adenoviridae E2A DNA-binding protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04054}.
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DR EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X02997; CAA26755.1; ALT_SEQ; Genomic_DNA.
DR PIR; A03833; W7AD25.
DR RefSeq; AP_000213.1; AC_000008.1.
DR PDB; 1ADU; X-ray; 3.00 A; A/B=174-529.
DR PDB; 1ADV; X-ray; 3.20 A; A/B=174-529.
DR PDB; 1ANV; X-ray; 2.70 A; A=174-529.
DR PDB; 2WAZ; X-ray; 2.30 A; X=174-529.
DR PDB; 2WB0; X-ray; 1.95 A; X=174-529.
DR PDBsum; 1ADU; -.
DR PDBsum; 1ADV; -.
DR PDBsum; 1ANV; -.
DR PDBsum; 2WAZ; -.
DR PDBsum; 2WB0; -.
DR SMR; P03265; -.
DR IntAct; P03265; 5.
DR MINT; P03265; -.
DR EvolutionaryTrace; P03265; -.
DR Proteomes; UP000004992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
DR GO; GO:0019028; C:viral capsid; IDA:CACAO.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:CAFA.
DR GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
DR GO; GO:0039687; P:viral DNA strand displacement replication; IDA:UniProtKB.
DR DisProt; DP00003; -.
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 3D-structure; DNA replication; DNA-binding; Early protein; Host nucleus;
KW Host-virus interaction; Metal-binding; Phosphoprotein;
KW Viral DNA replication; Zinc.
FT CHAIN 1..529
FT /note="DNA-binding protein"
FT /id="PRO_0000221679"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..166
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 137..156
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
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 ECO:0007744|PDB:1ADU, ECO:0007744|PDB:1ADV,
FT ECO:0007744|PDB:1ANV, ECO:0007744|PDB:2WAZ,
FT ECO:0007744|PDB:2WB0"
FT MOD_RES 195
FT /note="Phosphotyrosine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04054"
FT HELIX 180..194
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 213..226
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 237..256
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 331..338
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:1ANV"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 362..379
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:1ADV"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:1ANV"
FT STRAND 415..419
FT /evidence="ECO:0007829|PDB:2WB0"
FT TURN 421..424
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 428..430
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 434..441
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 444..449
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:2WB0"
FT HELIX 473..488
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 491..493
FT /evidence="ECO:0007829|PDB:1ANV"
FT HELIX 506..508
FT /evidence="ECO:0007829|PDB:2WB0"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:2WB0"
SQ SEQUENCE 529 AA; 59139 MW; AC1582B80F370E23 CRC64;
MASREEEQRE TTPERGRGAA RRPPTMEDVS SPSPSPPPPR APPKKRMRRR IESEDEEDSS
QDALVPRTPS PRPSTSAADL AIAPKKKKKR PSPKPERPPS PEVIVDSEEE REDVALQMVG
FSNPPVLIKH GKGGKRTVRR LNEDDPVARG MRTQEEEEEP SEAESEITVM NPLSVPIVSA
WEKGMEAARA LMDKYHVDND LKANFKLLPD QVEALAAVCK TWLNEEHRGL QLTFTSKKTF
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
