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Conserved domains on  [gi|686386753|ref|WP_031903306|]
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ADP-ribosyltransferase, partial [Staphylococcus aureus]

Protein Classification

ADP-ribosyltransferase family protein; tetratricopeptide repeat protein( domain architecture ID 10083253)

ADP-ribosyltransferase family protein similar to mono (ADP-ribosyl) transferases, which exist in vertebrates and transfer ADP-ribose to arginine| tetratricopeptide repeat (TPR) protein may adopt a right-handed helical structure with an amphipathic channel and may function as an interaction scaffold in the formation of multi-protein complexes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 15-225 4.57e-66

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: 202.63  E-value: 4.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  15 AADVKNftDLNEATDWGNKLIKKA--GYSSNDKRAIYEYTK-DSSKINGPLRAAGGDINKLDSTVQEKVRRLDLSISKST 91
Cdd:cd00233    2 TLDFKN--DIDEAEAWGNKNYKKWlkKLSPSEKEAIREYTGsDYKKINNYLRGNGGPENSLNSELDKQIENIDSAFKKKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  92 TPESVYVYRLLNLDYLTSIVGFTsedLHKLQQTNNGQYDENLVrklnnvmnSRIYREDGYSSTQLVSGAAMGGRPIELRL 171
Cdd:cd00233   80 IPENITVYRGVDMTYLGLIFQST---DGTINKTVNKQFEAKFL--------GKIYKDDGFMSTSLVSESAFGGRPIILRL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 686386753 172 ELPKGTKAAYVNnrELTAYYGQQEVLLPRGTEYAVGSVNLSNDK-RKIIITAIVF 225
Cdd:cd00233  149 TVPKGSKGAYIS--PISGFPGELEVLLPRGSTYKINKITVSSDGnKQIVIDAELI 201
 
Name Accession Description Interval E-value
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 15-225 4.57e-66

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: 202.63  E-value: 4.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  15 AADVKNftDLNEATDWGNKLIKKA--GYSSNDKRAIYEYTK-DSSKINGPLRAAGGDINKLDSTVQEKVRRLDLSISKST 91
Cdd:cd00233    2 TLDFKN--DIDEAEAWGNKNYKKWlkKLSPSEKEAIREYTGsDYKKINNYLRGNGGPENSLNSELDKQIENIDSAFKKKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  92 TPESVYVYRLLNLDYLTSIVGFTsedLHKLQQTNNGQYDENLVrklnnvmnSRIYREDGYSSTQLVSGAAMGGRPIELRL 171
Cdd:cd00233   80 IPENITVYRGVDMTYLGLIFQST---DGTINKTVNKQFEAKFL--------GKIYKDDGFMSTSLVSESAFGGRPIILRL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 686386753 172 ELPKGTKAAYVNnrELTAYYGQQEVLLPRGTEYAVGSVNLSNDK-RKIIITAIVF 225
Cdd:cd00233  149 TVPKGSKGAYIS--PISGFPGELEVLLPRGSTYKINKITVSSDGnKQIVIDAELI 201
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 27-227 7.65e-66

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: 202.21  E-value: 7.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753   27 ATDWGNKLIKKAGY--SSNDKRAIYEYTK-DSSKINGPLRAAGGDINKLD-STVQEKVRRLDLSISKSTTPESVYVYRLL 102
Cdd:pfam03496   1 ANSWGNKNYKDWKEnlTSSEKEAIRGYTGsDYSPINNYLRQNKGDINGLDaSDLEKKIKNIDSAFSKSPIPENIIVYRRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  103 NLDYLTSIVGftsedlhkLQQTNNGQYDENLVRKLNNVMNSRIYREDGYSSTQLVSG--AAMGGRPIELRLELPKGTKAA 180
Cdd:pfam03496  81 GEDYFGLDGG--------LPLNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDvaASFGGRPIILRITVPKGTKGA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 686386753  181 YVNNreLTAYYGQQEVLLPRGTEYAVGSV--NLSNDKRKIIITAIVFKK 227
Cdd:pfam03496 153 YISP--LSGYPGEQEVLLPRGSTYKINKItiVESKGHTKLIIDATVLKK 199
 
Name Accession Description Interval E-value
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 15-225 4.57e-66

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: 202.63  E-value: 4.57e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  15 AADVKNftDLNEATDWGNKLIKKA--GYSSNDKRAIYEYTK-DSSKINGPLRAAGGDINKLDSTVQEKVRRLDLSISKST 91
Cdd:cd00233    2 TLDFKN--DIDEAEAWGNKNYKKWlkKLSPSEKEAIREYTGsDYKKINNYLRGNGGPENSLNSELDKQIENIDSAFKKKP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  92 TPESVYVYRLLNLDYLTSIVGFTsedLHKLQQTNNGQYDENLVrklnnvmnSRIYREDGYSSTQLVSGAAMGGRPIELRL 171
Cdd:cd00233   80 IPENITVYRGVDMTYLGLIFQST---DGTINKTVNKQFEAKFL--------GKIYKDDGFMSTSLVSESAFGGRPIILRL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 686386753 172 ELPKGTKAAYVNnrELTAYYGQQEVLLPRGTEYAVGSVNLSNDK-RKIIITAIVF 225
Cdd:cd00233  149 TVPKGSKGAYIS--PISGFPGELEVLLPRGSTYKINKITVSSDGnKQIVIDAELI 201
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 27-227 7.65e-66

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: 202.21  E-value: 7.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753   27 ATDWGNKLIKKAGY--SSNDKRAIYEYTK-DSSKINGPLRAAGGDINKLD-STVQEKVRRLDLSISKSTTPESVYVYRLL 102
Cdd:pfam03496   1 ANSWGNKNYKDWKEnlTSSEKEAIRGYTGsDYSPINNYLRQNKGDINGLDaSDLEKKIKNIDSAFSKSPIPENIIVYRRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 686386753  103 NLDYLTSIVGftsedlhkLQQTNNGQYDENLVRKLNNVMNSRIYREDGYSSTQLVSG--AAMGGRPIELRLELPKGTKAA 180
Cdd:pfam03496  81 GEDYFGLDGG--------LPLNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDvaASFGGRPIILRITVPKGTKGA 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 686386753  181 YVNNreLTAYYGQQEVLLPRGTEYAVGSV--NLSNDKRKIIITAIVFKK 227
Cdd:pfam03496 153 YISP--LSGYPGEQEVLLPRGSTYKINKItiVESKGHTKLIIDATVLKK 199
 
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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