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Conserved domains on  [gi|31339721|gb|AAP49207|]
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protein VII precursor [Human adenovirus 11]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Adeno_VII super family cl03945
Adenoviral core protein VII; The function of this protein is unknown. It has a conserved amino ...
 1-94 2.29e-31

Adenoviral core protein VII; The function of this protein is unknown. It has a conserved amino terminus of 50 residues followed by a positively charged tail, suggesting it may interact with nucleic acid. The major core protein of the adenovirus, protein VII, was found to be associated with viral DNA throughout infection. The precursor to protein VII were shown to be in vivo and in vitro acceptors of ADP-ribose. The ADP-ribosylated core proteins were assembled into mature virus particles. ADP-ribosylation of adenovirus core proteins may have a role in virus decapsidation.


The actual alignment was detected with superfamily member pfam03228:

Pssm-ID: 281252  Cd Length: 142  Bit Score: 110.93  E-value: 2.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31339721     1 MSILISPSNNTGWGLRAPSKMYGGARKRSTQHPVRVRGHFRAPWGALKGRTRVRTTVDDVIDQVVADARNYTPT-APTST 79
Cdd:pfam03228   1 MSILISPSDNTGWGIGFPSKMFAGAKKFSDKHPVRVRGHYRAPWGAHKRGLNARTSLDDAIDAVVEEARNYTPTpPPVST 80

                          90
                  ....*....|....*
gi 31339721    80 VDAVIDSVVADARNY 94
Cdd:pfam03228  81 VDAAIKTKLRGAKRY 95
 
Name Accession Description Interval E-value
Adeno_VII pfam03228
Adenoviral core protein VII; The function of this protein is unknown. It has a conserved amino ...
 1-94 2.29e-31

Adenoviral core protein VII; The function of this protein is unknown. It has a conserved amino terminus of 50 residues followed by a positively charged tail, suggesting it may interact with nucleic acid. The major core protein of the adenovirus, protein VII, was found to be associated with viral DNA throughout infection. The precursor to protein VII were shown to be in vivo and in vitro acceptors of ADP-ribose. The ADP-ribosylated core proteins were assembled into mature virus particles. ADP-ribosylation of adenovirus core proteins may have a role in virus decapsidation.


Pssm-ID: 281252  Cd Length: 142  Bit Score: 110.93  E-value: 2.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31339721     1 MSILISPSNNTGWGLRAPSKMYGGARKRSTQHPVRVRGHFRAPWGALKGRTRVRTTVDDVIDQVVADARNYTPT-APTST 79
Cdd:pfam03228   1 MSILISPSDNTGWGIGFPSKMFAGAKKFSDKHPVRVRGHYRAPWGAHKRGLNARTSLDDAIDAVVEEARNYTPTpPPVST 80

                          90
                  ....*....|....*
gi 31339721    80 VDAVIDSVVADARNY 94
Cdd:pfam03228  81 VDAAIKTKLRGAKRY 95
 
Name Accession Description Interval E-value
Adeno_VII pfam03228
Adenoviral core protein VII; The function of this protein is unknown. It has a conserved amino ...
 1-94 2.29e-31

Adenoviral core protein VII; The function of this protein is unknown. It has a conserved amino terminus of 50 residues followed by a positively charged tail, suggesting it may interact with nucleic acid. The major core protein of the adenovirus, protein VII, was found to be associated with viral DNA throughout infection. The precursor to protein VII were shown to be in vivo and in vitro acceptors of ADP-ribose. The ADP-ribosylated core proteins were assembled into mature virus particles. ADP-ribosylation of adenovirus core proteins may have a role in virus decapsidation.


Pssm-ID: 281252  Cd Length: 142  Bit Score: 110.93  E-value: 2.29e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31339721     1 MSILISPSNNTGWGLRAPSKMYGGARKRSTQHPVRVRGHFRAPWGALKGRTRVRTTVDDVIDQVVADARNYTPT-APTST 79
Cdd:pfam03228   1 MSILISPSDNTGWGIGFPSKMFAGAKKFSDKHPVRVRGHYRAPWGAHKRGLNARTSLDDAIDAVVEEARNYTPTpPPVST 80

                          90
                  ....*....|....*
gi 31339721    80 VDAVIDSVVADARNY 94
Cdd:pfam03228  81 VDAAIKTKLRGAKRY 95
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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