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Conserved domains on  [gi|310909417|emb|CBX51773|]
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unnamed protein product, partial [synthetic construct]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADP_ribosyl super family cl00283
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 2-188 4.38e-143

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


The actual alignment was detected with superfamily member pfam02763:

Pssm-ID: 444809  Cd Length: 187  Bit Score: 404.16  E-value: 4.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417    2 GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGV 81
Cdd:pfam02763   1 GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKEFYSTDNKYDAAGYSVDNENPLSGKAGGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417   82 VKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALS 161
Cdd:pfam02763  81 VKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALS 160

                         170       180
                  ....*....|....*....|....*..
gi 310909417  162 VELEINFETRGKRGQDAMYEYMAQACA 188
Cdd:pfam02763 161 VELEINFETRGKRGQDAMYEYMAQACA 187
Diphtheria_T pfam02764
Diphtheria toxin, T domain; Central domain of diphtheria toxin is the translocation (T) domain. ...
 205-370 9.76e-79

Diphtheria toxin, T domain; Central domain of diphtheria toxin is the translocation (T) domain. pH induced conformational change in this domain triggers insertion into the endosomal membrane and facilitates the transfer of the catalytic domain into the cytoplasm.


:

Pssm-ID: 460683  Cd Length: 161  Bit Score: 239.72  E-value: 9.76e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  205 LDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALehpelSELKTVTGTNPVFAGANYAAWAV 284
Cdd:pfam02764   1 LDWDKVRDKAQTIVKSLKEHGPIKNKMSRSPNKPVSEEKAKSTLEEFHDTAL-----AALKEVTGTNPAFSAANLAAWAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  285 NVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVES 364
Cdd:pfam02764  76 DVAQTFSSENADGLDKTAAVTAIVPGLGQALGIADGIVHHDPEAIAVNSIALSALMVAQAIPVVGELADIGFAAYNLVES 155


                  ....*.
gi 310909417  365 IINLFQ 370
Cdd:pfam02764 156 LAQLFQ 161
 
Name Accession Description Interval E-value
Diphtheria_C pfam02763
Diphtheria toxin, C domain; N-terminal catalytic (C) domain - blocks protein synthesis by ...
 2-188 4.38e-143

Diphtheria toxin, C domain; N-terminal catalytic (C) domain - blocks protein synthesis by transfer of ADP-ribose from NAD to a diphthamide residue of EF-2.


Pssm-ID: 397059  Cd Length: 187  Bit Score: 404.16  E-value: 4.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417    2 GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGV 81
Cdd:pfam02763   1 GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKEFYSTDNKYDAAGYSVDNENPLSGKAGGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417   82 VKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALS 161
Cdd:pfam02763  81 VKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALS 160

                         170       180
                  ....*....|....*....|....*..
gi 310909417  162 VELEINFETRGKRGQDAMYEYMAQACA 188
Cdd:pfam02763 161 VELEINFETRGKRGQDAMYEYMAQACA 187
Diphtheria_T pfam02764
Diphtheria toxin, T domain; Central domain of diphtheria toxin is the translocation (T) domain. ...
 205-370 9.76e-79

Diphtheria toxin, T domain; Central domain of diphtheria toxin is the translocation (T) domain. pH induced conformational change in this domain triggers insertion into the endosomal membrane and facilitates the transfer of the catalytic domain into the cytoplasm.


Pssm-ID: 460683  Cd Length: 161  Bit Score: 239.72  E-value: 9.76e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  205 LDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALehpelSELKTVTGTNPVFAGANYAAWAV 284
Cdd:pfam02764   1 LDWDKVRDKAQTIVKSLKEHGPIKNKMSRSPNKPVSEEKAKSTLEEFHDTAL-----AALKEVTGTNPAFSAANLAAWAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  285 NVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVES 364
Cdd:pfam02764  76 DVAQTFSSENADGLDKTAAVTAIVPGLGQALGIADGIVHHDPEAIAVNSIALSALMVAQAIPVVGELADIGFAAYNLVES 155


                  ....*.
gi 310909417  365 IINLFQ 370
Cdd:pfam02764 156 LAQLFQ 161
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 19-157 3.87e-17

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 77.21  E-value: 3.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  19 SSYHGTKPGYVDSIQK-GIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENP-------------LSGKAGGVVKV 84
Cdd:cd01341    1 FLFHGSPPGNVISILKlGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQhvfqngkpkvcgrELCVFGFLTLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310909417  85 TYPGLTKVLALKVdnaetikkelglslteplmeqvgteeFIKRFGDGASRVVLSLPFA----EGSSSVEYINNWEQA 157
Cdd:cd01341   81 VMSGATEESSRVL--------------------------FPRNFRGATGAEVVDLLVAmcrdALLLPREYIIFEPYS 131
 
Name Accession Description Interval E-value
Diphtheria_C pfam02763
Diphtheria toxin, C domain; N-terminal catalytic (C) domain - blocks protein synthesis by ...
 2-188 4.38e-143

Diphtheria toxin, C domain; N-terminal catalytic (C) domain - blocks protein synthesis by transfer of ADP-ribose from NAD to a diphthamide residue of EF-2.


Pssm-ID: 397059  Cd Length: 187  Bit Score: 404.16  E-value: 4.38e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417    2 GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGV 81
Cdd:pfam02763   1 GADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKEFYSTDNKYDAAGYSVDNENPLSGKAGGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417   82 VKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALS 161
Cdd:pfam02763  81 VKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALS 160

                         170       180
                  ....*....|....*....|....*..
gi 310909417  162 VELEINFETRGKRGQDAMYEYMAQACA 188
Cdd:pfam02763 161 VELEINFETRGKRGQDAMYEYMAQACA 187
Diphtheria_T pfam02764
Diphtheria toxin, T domain; Central domain of diphtheria toxin is the translocation (T) domain. ...
 205-370 9.76e-79

Diphtheria toxin, T domain; Central domain of diphtheria toxin is the translocation (T) domain. pH induced conformational change in this domain triggers insertion into the endosomal membrane and facilitates the transfer of the catalytic domain into the cytoplasm.


Pssm-ID: 460683  Cd Length: 161  Bit Score: 239.72  E-value: 9.76e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  205 LDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVSEEKAKQYLEEFHQTALehpelSELKTVTGTNPVFAGANYAAWAV 284
Cdd:pfam02764   1 LDWDKVRDKAQTIVKSLKEHGPIKNKMSRSPNKPVSEEKAKSTLEEFHDTAL-----AALKEVTGTNPAFSAANLAAWAY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  285 NVAQVIDSETADNLEKTTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYNFVES 364
Cdd:pfam02764  76 DVAQTFSSENADGLDKTAAVTAIVPGLGQALGIADGIVHHDPEAIAVNSIALSALMVAQAIPVVGELADIGFAAYNLVES 155


                  ....*.
gi 310909417  365 IINLFQ 370
Cdd:pfam02764 156 LAQLFQ 161
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 19-157 3.87e-17

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 77.21  E-value: 3.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  19 SSYHGTKPGYVDSIQK-GIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENP-------------LSGKAGGVVKV 84
Cdd:cd01341    1 FLFHGSPPGNVISILKlGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQhvfqngkpkvcgrELCVFGFLTLG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 310909417  85 TYPGLTKVLALKVdnaetikkelglslteplmeqvgteeFIKRFGDGASRVVLSLPFA----EGSSSVEYINNWEQA 157
Cdd:cd01341   81 VMSGATEESSRVL--------------------------FPRNFRGATGAEVVDLLVAmcrdALLLPREYIIFEPYS 131
Dipth_tox_like cd01436
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic ...
 21-158 9.67e-05

Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic Elongation Factor 2, halting protein synthesis. A single molecule of delivered toxin is sufficient to kill a cell. These toxins share mono-ADP-ribosylating activity with a variety of bacterial toxins, such as cholera toxin and pertussis toxin. The structural core is homologous to the poly-ADP ribosylating enzymes such as the PARP enzymes and Tankyrase. Diphtheria toxin is encoded by a lysogenic bacteriophage. Both diphtheria toxin and Pseudomonas aeruginosa exotoxin A are multi-domain proteins. These domains provide a EF2 ADP_ribosylating, receptor-binding, and intracellular trafficking/transmembrane functions .


Pssm-ID: 238716  Cd Length: 147  Bit Score: 42.25  E-value: 9.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 310909417  21 YHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNA 100
Cdd:cd01436    3 YHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNKYDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNA 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 310909417 101 ETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAK 158
Cdd:cd01436   83 ETIKKELGLSLTEPLMEQVGTEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAK 140
 
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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