DP00003: Early E2A DNA-binding proteinFASTA viewXML view

General information
DisProt:DP00003
Name:Early E2A DNA-binding protein
Synonym(s):DNB2_ADE05
Adenovirus ssDNA binding protein
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P03265
UniGene: 
SwissProt: DNB2_ADE05
TrEMBL:  
NCBI (GI): 118736
Source organism:Human adenovirus C serotype 5 (HAdV-5)(Human adenovirus 5)
Sequence length:529
Percent disordered:10%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MASREEEQRE TTPERGRGAA RRPPTMEDVS SPSPSPPPPR APPKKRMRRR IESEDEEDSS - 60
QDALVPRTPS PRPSTSAADL AIAPKKKKKR PSPKPERPPS PEVIVDSEEE REDVALQMVG - 120
FSNPPVLIKH GKGGKRTVRR LNEDDPVARG MRTQEEEEEP SEAESEITVM NPLSVPIVSA - 180
WEKGMEAARA LMDKYHVDND LKANFKLLPD QVEALAAVCK TWLNEEHRGL QLTFTSNKTF - 240
VTMMGRFLQA YLQSFAEVTY KHHEPTGCAL WLHRCAEIEG ELKCLHGSIM INKEHVIEMD - 300
VTSENGQRAL KEQSSKAKIV KNRWGRNVVQ ISNTDARCCV HDAACPANQF SGKSCGMFFS - 360
EGAKAQVAFK QIKAFMQALY PNAQTGHGHL LMPLRCECNS KPGHAPFLGR QLPKLTPFAL - 420
SNAEDLDADL ISDKSVLASV HHPALIVFQC CNPVYRNSRA QGGGPNCDFK ISAPDLLNAL - 480
VMVRSLWSEN FTELPRMVVP EFKWSTKHQY RNVSLPVAHS DARQNPFDF



Functional narrative    

The human adenovirus type 5 is a virus that attacks the respiratory system. Often if causes infections in the upper respiratory system, and is accompanied by fever and a runny nose. Occasionally it may cause pneumonia. It accumulates in the nucleus of infected cells. The adenovirus binding protein is essential in the unwinding and replication of DNA. It also helps in viron assembly, host range determination, control of transcription, and stability of RNA. It is also stabilizes the DNA binding complex after binding to DNA has taken place.

Region 4: 174-296 Region 1: 297-331 Region 5: 332-400 Region 2: 401-406 Region 6: 407-452 Region 3: 453-464 Region 7: 465-529

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered - Extended
Name:Flexible Loop
Location:297 - 331
Length:35
Region sequence:

IEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQI

Modification type: Native
PDB: 1ADT:A, 1ADV:A, 1ADV:B, 1ANV:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular recognition effectors
Functional subclasses: DNA unwinding
Protein-DNA binding
Detection methods:
  1. X-ray crystallography (pH: 7.2; ethanol 5 %; NaCl 1.6 M; phosphate (buffer) 100 mM; protein 0.5 %)

References:
  1. Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC. "ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop." J Mol Biol. 1998; 277(4): 825-38. PubMed: 9545375

  2. Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC. "Characterization of the chymotryptic core of the adenovirus DNA-binding protein." FEBS Lett. 1985; 188(2): 248-52. PubMed: 4040872

  3. Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." 1994; 13(13): 2994-3002. PubMed: 8039495

Comments:
This region is known as the flexible loop. It goes from disordered to ordered upon binding to DNA, helps to stabilize the binding complex and plays an important role in DNA replication.




Region 2
Type:Disordered - Extended
Name: 
Location:401 - 406
Length:6
Region sequence:

KPGHAP

Modification type: Native
PDB: 1ADT:A, 1ADV:A, 1ADV:B, 1ANV:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (pH: 7.2; ethanol 5 %; NaCl 1.6 M; phosphate (buffer) 100 mM; protein 0.5 %)

References:
  1. Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC. "ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop." J Mol Biol. 1998; 277(4): 825-38. PubMed: 9545375

  2. Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC. "Characterization of the chymotryptic core of the adenovirus DNA-binding protein." FEBS Lett. 1985; 188(2): 248-52. PubMed: 4040872

  3. Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." 1994; 13(13): 2994-3002. PubMed: 8039495

Comments:
This region is part of the C-terminal portion of the protein which is important in chain formation and DNA replication.




Region 3
Type:Disordered - Extended
Name: 
Location:453 - 464
Length:12
Region sequence:

PVYRNSRAQGGG

Modification type: Native
PDB: 1ADT:A, 1ADV:A, 1ADV:B, 1ANV:A
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. X-ray crystallography (pH: 7.2; ethanol 5 %; NaCl 1.6 M; phosphate (buffer) 100 mM; protein 0.5 %)

References:
  1. Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC. "ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop." J Mol Biol. 1998; 277(4): 825-38. PubMed: 9545375

  2. Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC. "Characterization of the chymotryptic core of the adenovirus DNA-binding protein." FEBS Lett. 1985; 188(2): 248-52. PubMed: 4040872

  3. Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." 1994; 13(13): 2994-3002. PubMed: 8039495

Comments:
This region is part of the C-terminal portion of the protein which is important for chain formation and DNA replication.




Region 4
Type:Ordered
Name: 
Location:174 - 296
Length:123
Region sequence:

SVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLT
FTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINK
EHV

Modification type:  
PDB: 1ADT:A, 1ADV:A, 1ADV:B, 1ANV:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC. "ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop." J Mol Biol. 1998; 277(4): 825-38. PubMed: 9545375

  2. Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC. "Characterization of the chymotryptic core of the adenovirus DNA-binding protein." FEBS Lett. 1985; 188(2): 248-52. PubMed: 4040872

  3. Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." 1994; 13(13): 2994-3002. PubMed: 8039495

Comments:
 



Region 5
Type:Ordered
Name: 
Location:332 - 400
Length:69
Region sequence:

SNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLL
MPLRCECNS

Modification type:  
PDB: 1ADT:A, 1ADV:A, 1ADV:B, 1ANV:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC. "ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop." J Mol Biol. 1998; 277(4): 825-38. PubMed: 9545375

  2. Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC. "Characterization of the chymotryptic core of the adenovirus DNA-binding protein." FEBS Lett. 1985; 188(2): 248-52. PubMed: 4040872

  3. Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." 1994; 13(13): 2994-3002. PubMed: 8039495

Comments:
 



Region 6
Type:Ordered
Name: 
Location:407 - 452
Length:46
Region sequence:

FLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCN

Modification type:  
PDB: 1ADT:A, 1ADV:A, 1ADV:B, 1ANV:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC. "ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop." J Mol Biol. 1998; 277(4): 825-38. PubMed: 9545375

  2. Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC. "Characterization of the chymotryptic core of the adenovirus DNA-binding protein." FEBS Lett. 1985; 188(2): 248-52. PubMed: 4040872

  3. Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." 1994; 13(13): 2994-3002. PubMed: 8039495

Comments:
 



Region 7
Type:Ordered
Name: 
Location:465 - 529
Length:65
Region sequence:

PNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQ
NPFDF

Modification type:  
PDB: 1ADT:A, 1ADV:A, 1ADV:B, 1ANV:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC. "ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop." J Mol Biol. 1998; 277(4): 825-38. PubMed: 9545375

  2. Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC. "Characterization of the chymotryptic core of the adenovirus DNA-binding protein." FEBS Lett. 1985; 188(2): 248-52. PubMed: 4040872

  3. Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. "Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding." 1994; 13(13): 2994-3002. PubMed: 8039495

Comments:
 


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