P03265 (DNB2_ADE05) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Early E2A DNA-binding protein

Gene names

Name:

DBP

Organism

Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5) [Complete proteome]

Taxonomic identifier

28285 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Adenoviridae › Mastadenovirus › Human adenovirus C

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds cooperatively single-stranded DNA in a sequence-independent manner. Involved in DNA-replication, regulation of mRNA formation, and host-range specificity. Zinc is required for DNA binding.
Subunit structure	Interacts with human SRCAP By similarity.
Subcellular location	Host nucleus. Note: Accumulates in infected cells.
Sequence similarities	Belongs to the adenoviridae E2A DNA-binding protein family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Host nucleus
Developmental stage	Early protein
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological_process	DNA replication Inferred from electronic annotation. Source: InterPro transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 529

529

Early E2A DNA-binding protein

PRO_0000221679

Regions

Zinc finger

273 – 286

14

Potential

Amino acid modifications

Modified residue

195

1

Phosphotyrosine Probable

Secondary structure

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529

Helix Strand Turn

Details...

Helix

180 – 194

15

Helix

199 – 204

6

Helix

213 – 226

14

Helix

237 – 256

20

Beta strand

268 – 272

5

Beta strand

275 – 278

4

Beta strand

287 – 289

3

Beta strand

291 – 297

7

Beta strand

331 – 338

8

Helix

340 – 342

3

Beta strand

343 – 346

4

Beta strand

358 – 360

3

Helix

362 – 379

18

Beta strand

389 – 394

6

Helix

397 – 399

3

Beta strand

401 – 403

3

Beta strand

415 – 419

5

Turn

421 – 424

4

Helix

428 – 430

3

Helix

434 – 441

8

Beta strand

444 – 449

6

Beta strand

470 – 472

3

Helix

473 – 488

16

Beta strand

491 – 493

3

Helix

506 – 508

3

Beta strand

524 – 526

3

Sequences

	Sequence		Length	Mass (Da)
	P03265 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: AC1582B80F370E23	FASTA	529	59,139
	10 20 30 40 50 60 MASREEEQRE TTPERGRGAA RRPPTMEDVS SPSPSPPPPR APPKKRMRRR IESEDEEDSS 70 80 90 100 110 120 QDALVPRTPS PRPSTSAADL AIAPKKKKKR PSPKPERPPS PEVIVDSEEE REDVALQMVG 130 140 150 160 170 180 FSNPPVLIKH GKGGKRTVRR LNEDDPVARG MRTQEEEEEP SEAESEITVM NPLSVPIVSA 190 200 210 220 230 240 WEKGMEAARA LMDKYHVDND LKANFKLLPD QVEALAAVCK TWLNEEHRGL QLTFTSKKTF 250 260 270 280 290 300 VTMMGRFLQA YLQSFAEVTY KHHEPTGCAL WLHRCAEIEG ELKCLHGSIM INKEHVIEMD 310 320 330 340 350 360 VTSENGQRAL KEQSSKAKIV KNRWGRNVVQ ISNTDARCCV HDAACPANQF SGKSCGMFFS 370 380 390 400 410 420 EGAKAQVAFK QIKAFMQALY PNAQTGHGHL LMPLRCECNS KPGHAPFLGR QLPKLTPFAL 430 440 450 460 470 480 SNAEDLDADL ISDKSVLASV HHPALIVFQC CNPVYRNSRA QGGGPNCDFK ISAPDLLNAL 490 500 510 520 VMVRSLWSEN FTELPRMVVP EFKWSTKHQY RNVSLPVAHS DARQNPFDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure and organization of the gene coding for the DNA binding protein of adenovirus type 5." Kruijer W., van Schaik F.M.A., Sussenbach J.S. Nucleic Acids Res. 9:4439-4457(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The sequence of the genome of adenovirus type 5 and its comparison with the genome of adenovirus type 2." Chroboczek J., Bieber F., Jacrot B. Virology 186:280-285(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." Tucker P.A., Tsernoglou D., Tucker A.D., Coenjaerts F.E.J., Leenders H., van der Vliet P.C. EMBO J. 13:2994-3002(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 176-529.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M73260 Genomic DNA. No translation available.
X02997 Genomic DNA. Translation: CAA26755.1. Sequence problems.

PIR

W7AD25. A03833.

RefSeq

AP_000213.1. AC_000008.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ADU	X-ray	3.00	A/B	174-529	[»]
1ADV	X-ray	3.20	A/B	174-529	[»]
1ANV	X-ray	2.70	A	174-529	[»]
2WAZ	X-ray	2.30	X	174-529	[»]
2WB0	X-ray	1.95	X	174-529	[»]

DisProt

DP00003.

ProteinModelPortal

P03265.

SMR

P03265. Positions 179-529.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-216016.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.269.10. 1 hit.
3.90.148.10. 2 hits.

InterPro

IPR005376. Adenovirus_DNA-bd_C.
IPR003176. Adenovirus_DNA-bd_N.
[Graphical view]

Pfam

PF02236. Viral_DNA_bi. 1 hit.
PF03728. Viral_DNA_Zn_bi. 2 hits.
[Graphical view]

SUPFAM

SSF57917. E2A_DNA_Zn_bd. 2 hits.
SSF47724. Vir_DNA_bd. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P03265.

Entry information

Entry name

DNB2_ADE05

Accession

Primary (citable) accession number: P03265

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	April 3, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program