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DNA-binding protein (DBP) (Early 2A protein) (Early E2A DNA-binding protein)

 DNB2_ADE05              Reviewed;         529 AA.
P03265;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
10-OCT-2018, entry version 114.
RecName: Full=DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04054};
Short=DBP {ECO:0000255|HAMAP-Rule:MF_04054};
AltName: Full=Early 2A protein {ECO:0000255|HAMAP-Rule:MF_04054};
AltName: Full=Early E2A DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04054};
Name=DBP {ECO:0000255|HAMAP-Rule:MF_04054};
Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5).
Viruses; dsDNA viruses, no RNA stage; Adenoviridae; Mastadenovirus.
NCBI_TaxID=28285;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6117824; DOI=10.1093/nar/9.18.4439;
Kruijer W., van Schaik F.M.A., Sussenbach J.S.;
"Structure and organization of the gene coding for the DNA binding
protein of adenovirus type 5.";
Nucleic Acids Res. 9:4439-4457(1981).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=1727603; DOI=10.1016/0042-6822(92)90082-Z;
Chroboczek J., Bieber F., Jacrot B.;
"The sequence of the genome of adenovirus type 5 and its comparison
with the genome of adenovirus type 2.";
Virology 186:280-285(1992).
[3]
FUNCTION.
PubMed=12502807; DOI=10.1128/JVI.77.2.915-922.2003;
van Breukelen B., Brenkman A.B., Holthuizen P.E., van der Vliet P.C.;
"Adenovirus type 5 DNA binding protein stimulates binding of DNA
polymerase to the replication origin.";
J. Virol. 77:915-922(2003).
[4]
FUNCTION, AND IDENTIFICATION IN THE INITIATION COMPLEX.
PubMed=12747549;
Liu H., Naismith J.H., Hay R.T.;
"Adenovirus DNA replication.";
Curr. Top. Microbiol. Immunol. 272:131-164(2003).
[5]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 176-529.
PubMed=8039495;
Tucker P.A., Tsernoglou D., Tucker A.D., Coenjaerts F.E.J.,
Leenders H., van der Vliet P.C.;
"Crystal structure of the adenovirus DNA binding protein reveals a
hook-on model for cooperative DNA binding.";
EMBO J. 13:2994-3002(1994).
[6] {ECO:0000244|PDB:1ANV}
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 174-529 IN COMPLEX WITH
ZINC.
PubMed=15299602; DOI=10.1107/S0907444996005525;
Kanellopoulos P.N., Tsernoglou D., van der Vliet P.C., Tucker P.A.;
"Conformational change of the adenovirus DNA-binding protein induced
by soaking crystals with K3UO2F5 solutions.";
Acta Crystallogr. D 52:942-945(1996).
[7] {ECO:0000244|PDB:1ADU, ECO:0000244|PDB:1ADV}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 174-529 IN COMPLEX WITH
ZINC.
PubMed=8632448; DOI=10.1006/jmbi.1996.0141;
Kanellopoulos P.N., Tsernoglou D., van der Vliet P.C., Tucker P.A.;
"Alternative arrangements of the protein chain are possible for the
adenovirus single-stranded DNA binding protein.";
J. Mol. Biol. 257:1-8(1996).
-!- FUNCTION: Plays a role in the elongation phase of viral strand
displacement replication by unwinding the template in an ATP-
independent fashion, employing its capacity to form multimers.
Also enhances the rate of initiation. Released from template upon
second strand synthesis. Assembles in complex with viral pTP,
viral pol, host NFIA and host POU2F1/OCT1 on viral origin of
replication. Covers the whole ssDNA genome during synthesis. The
complementary strand synthesis induces its relese from DNA
template. May inhibit cellular transcription mediated by the
interaction between host SRCAP and CBP. {ECO:0000255|HAMAP-
Rule:MF_04054, ECO:0000269|PubMed:12502807,
ECO:0000269|PubMed:12747549}.
-!- SUBUNIT: Homomultimerizes on viral ssDNA bound to pTP. Forms a
initiation complex with viral polymerase, pTP and hosts NFIA and
POU2F1/OCT1. Interacts with host SRCAP. {ECO:0000255|HAMAP-
Rule:MF_04054}.
-!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-
Rule:MF_04054}. Note=Accumulates in infected cells.
{ECO:0000255|HAMAP-Rule:MF_04054}.
-!- DOMAIN: The C-terminal arm bridges DBP molecules together, thereby
creating a chain. {ECO:0000255|HAMAP-Rule:MF_04054}.
-!- SIMILARITY: Belongs to the adenoviridae E2A DNA-binding protein
family. {ECO:0000255|HAMAP-Rule:MF_04054}.
-----------------------------------------------------------------------
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EMBL; M73260; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X02997; CAA26755.1; ALT_SEQ; Genomic_DNA.
PIR; A03833; W7AD25.
RefSeq; AP_000213.1; AC_000008.1.
PDB; 1ADU; X-ray; 3.00 A; A/B=174-529.
PDB; 1ADV; X-ray; 3.20 A; A/B=174-529.
PDB; 1ANV; X-ray; 2.70 A; A=174-529.
PDB; 2WAZ; X-ray; 2.30 A; X=174-529.
PDB; 2WB0; X-ray; 1.95 A; X=174-529.
PDBsum; 1ADU; -.
PDBsum; 1ADV; -.
PDBsum; 1ANV; -.
PDBsum; 2WAZ; -.
PDBsum; 2WB0; -.
DisProt; DP00003; -.
ProteinModelPortal; P03265; -.
SMR; P03265; -.
IntAct; P03265; 5.
MINT; P03265; -.
OrthoDB; VOG0900009A; -.
EvolutionaryTrace; P03265; -.
Proteomes; UP000004992; Genome.
GO; GO:0042025; C:host cell nucleus; IDA:UniProtKB.
GO; GO:0019028; C:viral capsid; IDA:CACAO.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:CAFA.
GO; GO:0003697; F:single-stranded DNA binding; IDA:CAFA.
GO; GO:0008270; F:zinc ion binding; IDA:CAFA.
GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
GO; GO:0039687; P:viral DNA strand displacement replication; IDA:UniProtKB.
Gene3D; 1.10.269.10; -; 2.
Gene3D; 3.90.148.10; -; 1.
HAMAP; MF_04054; ADV_DNB2; 1.
InterPro; IPR036367; Ad_DBP_C_sf.
InterPro; IPR036368; ADBP_zn-bd_sf.
InterPro; IPR003176; Adenovirus_DNA-bd_a.
InterPro; IPR036362; Adenovirus_DNA-bd_N_sf.
InterPro; IPR005376; Adenovirus_DNA-bd_zn-bd.
InterPro; IPR037540; ADV_DNB2.
Pfam; PF02236; Viral_DNA_bi; 1.
Pfam; PF03728; Viral_DNA_Zn_bi; 2.
SUPFAM; SSF47724; SSF47724; 1.
SUPFAM; SSF57917; SSF57917; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA replication; DNA-binding;
Early protein; Host nucleus; Host-virus interaction; Metal-binding;
Phosphoprotein; Reference proteome; Viral DNA replication; Zinc.
CHAIN 1 529 DNA-binding protein.
/FTId=PRO_0000221679.
REGION 297 331 Flexible loop. {ECO:0000255|HAMAP-
Rule:MF_04054}.
REGION 513 529 C-terminal arm, DBP binding.
{ECO:0000255|HAMAP-Rule:MF_04054}.
METAL 284 284 Zinc 1. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
METAL 286 286 Zinc 1. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
METAL 339 339 Zinc 1. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
METAL 355 355 Zinc 1. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
METAL 396 396 Zinc 2. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
METAL 398 398 Zinc 2. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
METAL 450 450 Zinc 2. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
METAL 467 467 Zinc 2. {ECO:0000244|PDB:1ADU,
ECO:0000244|PDB:1ADV,
ECO:0000244|PDB:1ANV,
ECO:0000244|PDB:2WAZ,
ECO:0000244|PDB:2WB0, ECO:0000255|HAMAP-
Rule:MF_04054}.
MOD_RES 195 195 Phosphotyrosine; by host.
{ECO:0000255|HAMAP-Rule:MF_04054}.
HELIX 180 194 {ECO:0000244|PDB:2WB0}.
HELIX 199 204 {ECO:0000244|PDB:2WB0}.
HELIX 213 226 {ECO:0000244|PDB:2WB0}.
HELIX 237 256 {ECO:0000244|PDB:2WB0}.
STRAND 268 272 {ECO:0000244|PDB:2WB0}.
STRAND 275 278 {ECO:0000244|PDB:2WB0}.
STRAND 287 289 {ECO:0000244|PDB:2WB0}.
STRAND 291 297 {ECO:0000244|PDB:2WB0}.
STRAND 331 338 {ECO:0000244|PDB:2WB0}.
HELIX 340 342 {ECO:0000244|PDB:2WB0}.
STRAND 343 346 {ECO:0000244|PDB:1ANV}.
STRAND 358 360 {ECO:0000244|PDB:2WB0}.
HELIX 362 379 {ECO:0000244|PDB:2WB0}.
STRAND 389 394 {ECO:0000244|PDB:2WB0}.
HELIX 397 399 {ECO:0000244|PDB:1ADV}.
STRAND 401 403 {ECO:0000244|PDB:1ANV}.
STRAND 415 419 {ECO:0000244|PDB:2WB0}.
TURN 421 424 {ECO:0000244|PDB:2WB0}.
HELIX 428 430 {ECO:0000244|PDB:2WB0}.
HELIX 434 441 {ECO:0000244|PDB:2WB0}.
STRAND 444 449 {ECO:0000244|PDB:2WB0}.
STRAND 470 472 {ECO:0000244|PDB:2WB0}.
HELIX 473 488 {ECO:0000244|PDB:2WB0}.
STRAND 491 493 {ECO:0000244|PDB:1ANV}.
HELIX 506 508 {ECO:0000244|PDB:2WB0}.
STRAND 524 526 {ECO:0000244|PDB:2WB0}.
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


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