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Conserved domains on  [gi|939186911|pdb|5DZQ|O]
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Chain O, Toxin-like protein

Protein Classification

ADP-ribosyltransferase( domain architecture ID 10507422)

ADP-ribosyltransferase such as C3 exoenzyme, a mono-ADP-ribosyltransferase that catalyzes transfer of an ADP-ribose moiety from NAD(+) to Rho GTPases.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 25-211 4.62e-58

ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ADP-ribosyltransferases, where, in Swiss:Q93Q17, E403 is the catalytic residue and E401 contributes to the transfer of ADP-ribose to the target protein. In clostridial species it is actin that is being ADP-ribosylated; this result is lethal and dermonecrotic in infected mammals.


:

Pssm-ID: 427336 [Multi-domain]  Cd Length: 199  Bit Score: 181.80  E-value: 4.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O         25 GEKEYKAWEKKLRANEKELVKEYT-ANAKPFNTYLRANEGKLGFKP--EIDKKILKLDEALKKSKLSETVQVYRGDDTSI 101
Cdd:pfam03496   5 GNKNYKDWKENLTSSEKEAIRGYTgSDYSPINNYLRQNKGDINGLDasDLEKKIKNIDSAFSKSPIPENIIVYRRVGEDY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O        102 FGKEFQNSIYQGNKVNRELFRKLRDEYQGKIRTEYGYLSTSIVSN--QQFAMRPVLTTLKVPKGAHAGYVDKISQYKGQY 179
Cdd:pfam03496  85 FGLDGGLPLNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDvaASFGGRPIILRITVPKGTKGAYISPLSGYPGEQ 164

                         170       180       190
                  ....*....|....*....|....*....|..
5DZQ_O        180 ELLLPRNTKYKIDKMYIIVNKGSETIKIEATV 211
Cdd:pfam03496 165 EVLLPRGSTYKINKITIVESKGHTKLIIDATV 196
 
Name Accession Description Interval E-value
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 25-211 4.62e-58

ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ADP-ribosyltransferases, where, in Swiss:Q93Q17, E403 is the catalytic residue and E401 contributes to the transfer of ADP-ribose to the target protein. In clostridial species it is actin that is being ADP-ribosylated; this result is lethal and dermonecrotic in infected mammals.


Pssm-ID: 427336 [Multi-domain]  Cd Length: 199  Bit Score: 181.80  E-value: 4.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O         25 GEKEYKAWEKKLRANEKELVKEYT-ANAKPFNTYLRANEGKLGFKP--EIDKKILKLDEALKKSKLSETVQVYRGDDTSI 101
Cdd:pfam03496   5 GNKNYKDWKENLTSSEKEAIRGYTgSDYSPINNYLRQNKGDINGLDasDLEKKIKNIDSAFSKSPIPENIIVYRRVGEDY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O        102 FGKEFQNSIYQGNKVNRELFRKLRDEYQGKIRTEYGYLSTSIVSN--QQFAMRPVLTTLKVPKGAHAGYVDKISQYKGQY 179
Cdd:pfam03496  85 FGLDGGLPLNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDvaASFGGRPIILRITVPKGTKGAYISPLSGYPGEQ 164

                         170       180       190
                  ....*....|....*....|....*....|..
5DZQ_O        180 ELLLPRNTKYKIDKMYIIVNKGSETIKIEATV 211
Cdd:pfam03496 165 EVLLPRGSTYKINKITIVESKGHTKLIIDATV 196
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 25-211 2.34e-50

VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative insecticidal proteins (VIPs) possesses high specificity against the major insect pest, corn rootworms, and belongs to a classs of binary toxins and regulators of biological pathways distinct from classical A-B toxins. A novel family of insecticidal ADP-ribosyltransferses were isolated from Bacillus cereus during vegetative growth, where VIP1 likely targets insect cells and VIP2 ribosylates actin. VIP2 shares significant sequence similarity with enzymatic components of other binary toxins, Clostridium botulinum C2 toxin, C. perfringens iota toxin, C. piroforme toxin, C. piroforme toxin and C. difficile toxin.


Pssm-ID: 238144 [Multi-domain]  Cd Length: 201  Bit Score: 162.19  E-value: 2.34e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O       25 GEKEYKAWEKKLRANEKELVKEYTAN-AKPFNTYLRANEGKL-GFKPEIDKKILKLDEALKKSKLSETVQVYRGDDTSIF 102
Cdd:cd00233  16 GNKNYKKWLKKLSPSEKEAIREYTGSdYKKINNYLRGNGGPEnSLNSELDKQIENIDSAFKKKPIPENITVYRGVDMTYL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O      103 GKEFQNSIYQGNKVNRELFRKLrdeYQGKIRTEYGYLSTSIVSNQQFAMRPVLTTLKVPKGAHAGYVDKISQYKGQYELL 182
Cdd:cd00233  96 GLIFQSTDGTINKTVNKQFEAK---FLGKIYKDDGFMSTSLVSESAFGGRPIILRLTVPKGSKGAYISPISGFPGELEVL 172

                       170       180
                ....*....|....*....|....*....
5DZQ_O      183 LPRNTKYKIDKMYIIVNKGSETIkIEATV 211
Cdd:cd00233 173 LPRGSTYKINKITVSSDGNKQIV-IDAEL 200
PRK15244 PRK15244
type III secretion system effector NAD(+)--protein-arginine ADP-ribosyltransferase SpvB;
110-203 4.98e-04

type III secretion system effector NAD(+)--protein-arginine ADP-ribosyltransferase SpvB;


Pssm-ID: 185156 [Multi-domain]  Cd Length: 591  Bit Score: 40.48  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O       110 IYQGNKVNRELFRKLRDEYQ--GKIRTEYGYLSTSivsNQQFAMRPVLTTLKVPKGAHAGYVDKISQYKGQYELLLPRNT 187
Cdd:PRK15244 469 VYRGLKLDKPALSDVLKEYTtiGNIIIDKAFMSTS---PDKAWINDTILNIYLEKGHKGRILGDVAHFKGEAEMLFPPNT 545

                         90
                 ....*....|....*.
5DZQ_O       188 KYKIDKmyiIVNKGSE 203
Cdd:PRK15244 546 KLKIES---IVNCGSQ 558
 
Name Accession Description Interval E-value
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 25-211 4.62e-58

ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ADP-ribosyltransferases, where, in Swiss:Q93Q17, E403 is the catalytic residue and E401 contributes to the transfer of ADP-ribose to the target protein. In clostridial species it is actin that is being ADP-ribosylated; this result is lethal and dermonecrotic in infected mammals.


Pssm-ID: 427336 [Multi-domain]  Cd Length: 199  Bit Score: 181.80  E-value: 4.62e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O         25 GEKEYKAWEKKLRANEKELVKEYT-ANAKPFNTYLRANEGKLGFKP--EIDKKILKLDEALKKSKLSETVQVYRGDDTSI 101
Cdd:pfam03496   5 GNKNYKDWKENLTSSEKEAIRGYTgSDYSPINNYLRQNKGDINGLDasDLEKKIKNIDSAFSKSPIPENIIVYRRVGEDY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O        102 FGKEFQNSIYQGNKVNRELFRKLRDEYQGKIRTEYGYLSTSIVSN--QQFAMRPVLTTLKVPKGAHAGYVDKISQYKGQY 179
Cdd:pfam03496  85 FGLDGGLPLNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDvaASFGGRPIILRITVPKGTKGAYISPLSGYPGEQ 164

                         170       180       190
                  ....*....|....*....|....*....|..
5DZQ_O        180 ELLLPRNTKYKIDKMYIIVNKGSETIKIEATV 211
Cdd:pfam03496 165 EVLLPRGSTYKINKITIVESKGHTKLIIDATV 196
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 25-211 2.34e-50

VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative insecticidal proteins (VIPs) possesses high specificity against the major insect pest, corn rootworms, and belongs to a classs of binary toxins and regulators of biological pathways distinct from classical A-B toxins. A novel family of insecticidal ADP-ribosyltransferses were isolated from Bacillus cereus during vegetative growth, where VIP1 likely targets insect cells and VIP2 ribosylates actin. VIP2 shares significant sequence similarity with enzymatic components of other binary toxins, Clostridium botulinum C2 toxin, C. perfringens iota toxin, C. piroforme toxin, C. piroforme toxin and C. difficile toxin.


Pssm-ID: 238144 [Multi-domain]  Cd Length: 201  Bit Score: 162.19  E-value: 2.34e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O       25 GEKEYKAWEKKLRANEKELVKEYTAN-AKPFNTYLRANEGKL-GFKPEIDKKILKLDEALKKSKLSETVQVYRGDDTSIF 102
Cdd:cd00233  16 GNKNYKKWLKKLSPSEKEAIREYTGSdYKKINNYLRGNGGPEnSLNSELDKQIENIDSAFKKKPIPENITVYRGVDMTYL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O      103 GKEFQNSIYQGNKVNRELFRKLrdeYQGKIRTEYGYLSTSIVSNQQFAMRPVLTTLKVPKGAHAGYVDKISQYKGQYELL 182
Cdd:cd00233  96 GLIFQSTDGTINKTVNKQFEAK---FLGKIYKDDGFMSTSLVSESAFGGRPIILRLTVPKGSKGAYISPISGFPGELEVL 172

                       170       180
                ....*....|....*....|....*....
5DZQ_O      183 LPRNTKYKIDKMYIIVNKGSETIkIEATV 211
Cdd:cd00233 173 LPRGSTYKINKITVSSDGNKQIV-IDAEL 200
PRK15244 PRK15244
type III secretion system effector NAD(+)--protein-arginine ADP-ribosyltransferase SpvB;
110-203 4.98e-04

type III secretion system effector NAD(+)--protein-arginine ADP-ribosyltransferase SpvB;


Pssm-ID: 185156 [Multi-domain]  Cd Length: 591  Bit Score: 40.48  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
5DZQ_O       110 IYQGNKVNRELFRKLRDEYQ--GKIRTEYGYLSTSivsNQQFAMRPVLTTLKVPKGAHAGYVDKISQYKGQYELLLPRNT 187
Cdd:PRK15244 469 VYRGLKLDKPALSDVLKEYTtiGNIIIDKAFMSTS---PDKAWINDTILNIYLEKGHKGRILGDVAHFKGEAEMLFPPNT 545

                         90
                 ....*....|....*.
5DZQ_O       188 KYKIDKmyiIVNKGSE 203
Cdd:PRK15244 546 KLKIES---IVNCGSQ 558
 
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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