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Conserved domains on  [gi|6730536|pdb|1QS1|D]
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Chain D, ADP-RIBOSYLTRANSFERASE

Protein Classification

tetratricopeptide repeat protein( domain architecture ID 10213767)

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

 Zoom to residue level

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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 ...
 264-460 1.31e-77

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: 240.38  E-value: 1.31e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D      264 KSLDFKNDInAEAHSWGMKNYEEWAKDLTDSQREALDGYARQDYKEINNYLRNQGG---SGNEKLDAQIKNISDALGKKP 340
Cdd:cd00233   1 KTLDFKNDI-DEAEAWGNKNYKKWLKKLSPSEKEAIREYTGSDYKKINNYLRGNGGpenSLNSELDKQIENIDSAFKKKP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D      341 IPENITVYRWCGMPEFGYQISDP-----LPSLKDFEEQFLNTIKEDKGYMSTSLSSERlaAFGSRKIILRLQVPKGSTGA 415
Cdd:cd00233  80 IPENITVYRGVDMTYLGLIFQSTdgtinKTVNKQFEAKFLGKIYKDDGFMSTSLVSES--AFGGRPIILRLTVPKGSKGA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1QS1_D      416 YLSAIGGFASEKEILLDKDSKYHIDKVTEVIIKgVKRYVVDATLL 460
Cdd:cd00233 158 YISPISGFPGELEVLLPRGSTYKINKITVSSDG-NKQIVIDAELI 201
VIP2 super family cl00173
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 86-239 5.95e-10

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.


The actual alignment was detected with superfamily member pfam03496:

Pssm-ID: 469640 [Multi-domain]  Cd Length: 199  Bit Score: 58.53  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D         86 LTATEKGKMNNFLDNK-----NDIKTNYKEITFSMAGSFEDEIKDlkeIDKMFDKTNLSNSIITYKNVEPTTIG--FNKS 158
Cdd:pfam03496  16 LTSSEKEAIRGYTGSDyspinNYLRQNKGDINGLDASDLEKKIKN---IDSAFSKSPIPENIIVYRRVGEDYFGldGGLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D        159 LTEGNTINSDAMAQFKEQFLDRDIKFDSYLDTHLTAQQVSS--KERVILKVTVPSGkgsttpTKAGVI----LNNSEYKM 232
Cdd:pfam03496  93 LNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDVAASfgGRPIILRITVPKG------TKGAYIsplsGYPGEQEV 166


                  ....*..
1QS1_D        233 LIDNGYM 239
Cdd:pfam03496 167 LLPRGST 173
 
Name Accession Description Interval E-value
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 264-460 1.31e-77

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: 240.38  E-value: 1.31e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D      264 KSLDFKNDInAEAHSWGMKNYEEWAKDLTDSQREALDGYARQDYKEINNYLRNQGG---SGNEKLDAQIKNISDALGKKP 340
Cdd:cd00233   1 KTLDFKNDI-DEAEAWGNKNYKKWLKKLSPSEKEAIREYTGSDYKKINNYLRGNGGpenSLNSELDKQIENIDSAFKKKP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D      341 IPENITVYRWCGMPEFGYQISDP-----LPSLKDFEEQFLNTIKEDKGYMSTSLSSERlaAFGSRKIILRLQVPKGSTGA 415
Cdd:cd00233  80 IPENITVYRGVDMTYLGLIFQSTdgtinKTVNKQFEAKFLGKIYKDDGFMSTSLVSES--AFGGRPIILRLTVPKGSKGA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1QS1_D      416 YLSAIGGFASEKEILLDKDSKYHIDKVTEVIIKgVKRYVVDATLL 460
Cdd:cd00233 158 YISPISGFPGELEVLLPRGSTYKINKITVSSDG-NKQIVIDAELI 201
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 276-462 3.81e-74

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: 231.49  E-value: 3.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D        276 AHSWGMKNYEEWAKDLTDSQREALDGYARQDYKEINNYLRNQGGSGN----EKLDAQIKNISDALGKKPIPENITVYRWC 351
Cdd:pfam03496   1 ANSWGNKNYKDWKENLTSSEKEAIRGYTGSDYSPINNYLRQNKGDINgldaSDLEKKIKNIDSAFSKSPIPENIIVYRRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D        352 GMPEFG--------YQISDPLPSLKDFEEQFLNTIKEDKGYMSTSLSSERLAAFGSRKIILRLQVPKGSTGAYLSAIGGF 423
Cdd:pfam03496  81 GEDYFGldgglplnNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDVAASFGGRPIILRITVPKGTKGAYISPLSGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
1QS1_D        424 ASEKEILLDKDSKYHIDKVTEVIIKGVKRYVVDATLLTN 462
Cdd:pfam03496 161 PGEQEVLLPRGSTYKINKITIVESKGHTKLIIDATVLKK 199
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 86-239 5.95e-10

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: 58.53  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D         86 LTATEKGKMNNFLDNK-----NDIKTNYKEITFSMAGSFEDEIKDlkeIDKMFDKTNLSNSIITYKNVEPTTIG--FNKS 158
Cdd:pfam03496  16 LTSSEKEAIRGYTGSDyspinNYLRQNKGDINGLDASDLEKKIKN---IDSAFSKSPIPENIIVYRRVGEDYFGldGGLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D        159 LTEGNTINSDAMAQFKEQFLDRDIKFDSYLDTHLTAQQVSS--KERVILKVTVPSGkgsttpTKAGVI----LNNSEYKM 232
Cdd:pfam03496  93 LNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDVAASfgGRPIILRITVPKG------TKGAYIsplsGYPGEQEV 166


                  ....*..
1QS1_D        233 LIDNGYM 239
Cdd:pfam03496 167 LLPRGST 173
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 87-231 1.29e-08

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: 54.71  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D       87 TATEKGKMNNFLD-NKNDIKTNYKEItfsmagsfEDEIKDlkeIDKMFDKTNLSNSIITYKNVEPTTIGFNKSLTEGnTI 165
Cdd:cd00233  39 TGSDYKKINNYLRgNGGPENSLNSEL--------DKQIEN---IDSAFKKKPIPENITVYRGVDMTYLGLIFQSTDG-TI 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1QS1_D      166 NSDAMAQFKEQFLDRDIKFDSYLDTHLTAQQVSSKERVILKVTVPSGKG-------STTPTKAGVILN-NSEYK 231
Cdd:cd00233 107 NKTVNKQFEAKFLGKIYKDDGFMSTSLVSESAFGGRPIILRLTVPKGSKgayispiSGFPGELEVLLPrGSTYK 180
PRK15244 PRK15244
type III secretion system effector NAD(+)--protein-arginine ADP-ribosyltransferase SpvB;
286-442 2.06e-05

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


Pssm-ID: 185156 [Multi-domain]  Cd Length: 591  Bit Score: 47.03  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D       286 EWAKDLTDSQREALDGYARQDYKEINNYLRNQGG---------------SGNEKLDAQIKN--------ISDALGKKPIP 342
Cdd:PRK15244 385 KWAIVEESKQIQALRYYSAQGYSVINKYLRGDDYpetqaketllsrdylSTNEPSDEEFKNamsvyindIAEGLSSLPET 464

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D       343 ENITVYRwcgmpefGYQISDplPSLKDFEEQF--LNTIKEDKGYMSTSLSSERLaafgsRKIILRLQVPKGSTGAYLSAI 420
Cdd:PRK15244 465 DHRVVYR-------GLKLDK--PALSDVLKEYttIGNIIIDKAFMSTSPDKAWI-----NDTILNIYLEKGHKGRILGDV 530

                        170       180
                 ....*....|....*....|..
1QS1_D       421 GGFASEKEILLDKDSKYHIDKV 442
Cdd:PRK15244 531 AHFKGEAEMLFPPNTKLKIESI 552
 
Name Accession Description Interval E-value
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 264-460 1.31e-77

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: 240.38  E-value: 1.31e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D      264 KSLDFKNDInAEAHSWGMKNYEEWAKDLTDSQREALDGYARQDYKEINNYLRNQGG---SGNEKLDAQIKNISDALGKKP 340
Cdd:cd00233   1 KTLDFKNDI-DEAEAWGNKNYKKWLKKLSPSEKEAIREYTGSDYKKINNYLRGNGGpenSLNSELDKQIENIDSAFKKKP 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D      341 IPENITVYRWCGMPEFGYQISDP-----LPSLKDFEEQFLNTIKEDKGYMSTSLSSERlaAFGSRKIILRLQVPKGSTGA 415
Cdd:cd00233  80 IPENITVYRGVDMTYLGLIFQSTdgtinKTVNKQFEAKFLGKIYKDDGFMSTSLVSES--AFGGRPIILRLTVPKGSKGA 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
1QS1_D      416 YLSAIGGFASEKEILLDKDSKYHIDKVTEVIIKgVKRYVVDATLL 460
Cdd:cd00233 158 YISPISGFPGELEVLLPRGSTYKINKITVSSDG-NKQIVIDAELI 201
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 276-462 3.81e-74

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: 231.49  E-value: 3.81e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D        276 AHSWGMKNYEEWAKDLTDSQREALDGYARQDYKEINNYLRNQGGSGN----EKLDAQIKNISDALGKKPIPENITVYRWC 351
Cdd:pfam03496   1 ANSWGNKNYKDWKENLTSSEKEAIRGYTGSDYSPINNYLRQNKGDINgldaSDLEKKIKNIDSAFSKSPIPENIIVYRRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D        352 GMPEFG--------YQISDPLPSLKDFEEQFLNTIKEDKGYMSTSLSSERLAAFGSRKIILRLQVPKGSTGAYLSAIGGF 423
Cdd:pfam03496  81 GEDYFGldgglplnNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDVAASFGGRPIILRITVPKGTKGAYISPLSGY 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
1QS1_D        424 ASEKEILLDKDSKYHIDKVTEVIIKGVKRYVVDATLLTN 462
Cdd:pfam03496 161 PGEQEVLLPRGSTYKINKITIVESKGHTKLIIDATVLKK 199
ADPrib_exo_Tox pfam03496
ADP-ribosyltransferase exoenzyme; This is a family of bacterial and viral bi-glutamic acid ...
 86-239 5.95e-10

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: 58.53  E-value: 5.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D         86 LTATEKGKMNNFLDNK-----NDIKTNYKEITFSMAGSFEDEIKDlkeIDKMFDKTNLSNSIITYKNVEPTTIG--FNKS 158
Cdd:pfam03496  16 LTSSEKEAIRGYTGSDyspinNYLRQNKGDINGLDASDLEKKIKN---IDSAFSKSPIPENIIVYRRVGEDYFGldGGLP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D        159 LTEGNTINSDAMAQFKEQFLDRDIKFDSYLDTHLTAQQVSS--KERVILKVTVPSGkgsttpTKAGVI----LNNSEYKM 232
Cdd:pfam03496  93 LNNNGTINEELVSAFKEKFEGKVKTEYGYMSTSLVSDVAASfgGRPIILRITVPKG------TKGAYIsplsGYPGEQEV 166


                  ....*..
1QS1_D        233 LIDNGYM 239
Cdd:pfam03496 167 LLPRGST 173
VIP2 cd00233
VIP2; A family of actin-ADP-ribosylating toxin. A member of the Bacillus-prodiced vegetative ...
 87-231 1.29e-08

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: 54.71  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D       87 TATEKGKMNNFLD-NKNDIKTNYKEItfsmagsfEDEIKDlkeIDKMFDKTNLSNSIITYKNVEPTTIGFNKSLTEGnTI 165
Cdd:cd00233  39 TGSDYKKINNYLRgNGGPENSLNSEL--------DKQIEN---IDSAFKKKPIPENITVYRGVDMTYLGLIFQSTDG-TI 106

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1QS1_D      166 NSDAMAQFKEQFLDRDIKFDSYLDTHLTAQQVSSKERVILKVTVPSGKG-------STTPTKAGVILN-NSEYK 231
Cdd:cd00233 107 NKTVNKQFEAKFLGKIYKDDGFMSTSLVSESAFGGRPIILRLTVPKGSKgayispiSGFPGELEVLLPrGSTYK 180
PRK15244 PRK15244
type III secretion system effector NAD(+)--protein-arginine ADP-ribosyltransferase SpvB;
286-442 2.06e-05

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


Pssm-ID: 185156 [Multi-domain]  Cd Length: 591  Bit Score: 47.03  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D       286 EWAKDLTDSQREALDGYARQDYKEINNYLRNQGG---------------SGNEKLDAQIKN--------ISDALGKKPIP 342
Cdd:PRK15244 385 KWAIVEESKQIQALRYYSAQGYSVINKYLRGDDYpetqaketllsrdylSTNEPSDEEFKNamsvyindIAEGLSSLPET 464

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D       343 ENITVYRwcgmpefGYQISDplPSLKDFEEQF--LNTIKEDKGYMSTSLSSERLaafgsRKIILRLQVPKGSTGAYLSAI 420
Cdd:PRK15244 465 DHRVVYR-------GLKLDK--PALSDVLKEYttIGNIIIDKAFMSTSPDKAWI-----NDTILNIYLEKGHKGRILGDV 530

                        170       180
                 ....*....|....*....|..
1QS1_D       421 GGFASEKEILLDKDSKYHIDKV 442
Cdd:PRK15244 531 AHFKGEAEMLFPPNTKLKIESI 552
alt PHA02566
ADP-ribosyltransferase; Provisional
 289-389 3.35e-03

ADP-ribosyltransferase; Provisional


Pssm-ID: 222881 [Multi-domain]  Cd Length: 684  Bit Score: 40.11  E-value: 3.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1QS1_D       289 KDLTDSQREALDGYARQDYKEINNYLRNQGGSGNEKLDAQIKNISDAL------GKKpIPENITVYRwcGMpEFGYQISD 362
Cdd:PHA02566 423 KKLTPAESRAIREYCASGYIDINNFLLGRYKPEFYMDEEEAEKAIDNLdsafknGDK-LPEGTTLYR--GQ-SVTSKIYE 498

                         90       100
                 ....*....|....*....|....*..
1QS1_D       363 PLPSLKDFeeQFLNtikedkgYMSTSL 389
Cdd:PHA02566 499 ALVKNKVF--YFKN-------FVSTSL 516
 
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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