NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|67463999|pdb|1ZM2|F]
View 

Chain F, Exotoxin A

Protein Classification

poly(ADP-ribose) polymerase family protein( domain architecture ID 2436)

poly(ADP-ribose) polymerase family protein similar to Oncorhynchus masou poly [ADP-ribose] polymerase 1, which acts as Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair

EC:  2.4.2.-
Gene Ontology:  GO:0003950|GO:0003684|GO:0006281

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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. ...
 24-195 2.88e-110

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 pfam09009:

Pssm-ID: 444809  Cd Length: 177  Bit Score: 313.13  E-value: 2.88e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F         24 LLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRV 103
Cdd:pfam09009   1 LLAAHQQLEDQGYVFAGYHGGFLAAAQSIVFGGIRARSQDLDAIWRGFYIAGDPALAYGYALDNDPDARGRIRNGALLRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F        104 YVPRSSLPGFYRTSLTLAAPEAA-GEVERLIGHPLPLR----LDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPR 178
Cdd:pfam09009  81 YVPRAALPGFFRTSLPLAAEAAAlGEIERLIGHNLPLNsvlgLDAITGPEDEGEPDETILGWDLAEHAVAIPSAIPGDPR 160

                         170
                  ....*....|....*..
1ZM2_F        179 NVGGDLDPSSIPDKEQA 195
Cdd:pfam09009 161 NVGGDLDPINIPDKEKA 177
 
Name Accession Description Interval E-value
Exotox-A_cataly pfam09009
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, ...
 24-195 2.88e-110

Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, catalyze the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, with subsequent inhibition of protein synthesis.


Pssm-ID: 430368  Cd Length: 177  Bit Score: 313.13  E-value: 2.88e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F         24 LLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRV 103
Cdd:pfam09009   1 LLAAHQQLEDQGYVFAGYHGGFLAAAQSIVFGGIRARSQDLDAIWRGFYIAGDPALAYGYALDNDPDARGRIRNGALLRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F        104 YVPRSSLPGFYRTSLTLAAPEAA-GEVERLIGHPLPLR----LDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPR 178
Cdd:pfam09009  81 YVPRAALPGFFRTSLPLAAEAAAlGEIERLIGHNLPLNsvlgLDAITGPEDEGEPDETILGWDLAEHAVAIPSAIPGDPR 160

                         170
                  ....*....|....*..
1ZM2_F        179 NVGGDLDPSSIPDKEQA 195
Cdd:pfam09009 161 NVGGDLDPINIPDKEKA 177
Dipth_tox_like cd01436
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic ...
 39-171 5.69e-67

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: 202.49  E-value: 5.69e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F       39 VGYHGTFLEAAQSIVFGgVRARSQ----DLDAIWRGFYIAGDPALAYGYAQDQEPDarGRIRNGALLRVYVPRSslPGFY 114
Cdd:cd01436   1 SSYHGTKPGYVDSIQKG-IQKPKSgtqgNYDDDWKGFYSTDNKYDAAGYSVDNENP--LSGKAGGVVKVTYPGL--TKVL 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZM2_F      115 RTSLTlaapeAAGEVERLIGHPLP-------------------LRLDAITGPEEE-GGRLETILGWPLAERTVVIPS 171
Cdd:cd01436  76 ALKVD-----NAETIKKELGLSLTeplmeqvgteefikrfgdgASRVVLSLPFAEgSSSVEYINNWEQAKALSVELE 147
 
Name Accession Description Interval E-value
Exotox-A_cataly pfam09009
Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, ...
 24-195 2.88e-110

Exotoxin A catalytic; Members of this family, which are found in prokaryotic exotoxin A, catalyze the transfer of ADP ribose from nicotinamide adenine dinucleotide (NAD) to elongation factor-2 in eukaryotic cells, with subsequent inhibition of protein synthesis.


Pssm-ID: 430368  Cd Length: 177  Bit Score: 313.13  E-value: 2.88e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F         24 LLQAHRQLEERGYVFVGYHGTFLEAAQSIVFGGVRARSQDLDAIWRGFYIAGDPALAYGYAQDQEPDARGRIRNGALLRV 103
Cdd:pfam09009   1 LLAAHQQLEDQGYVFAGYHGGFLAAAQSIVFGGIRARSQDLDAIWRGFYIAGDPALAYGYALDNDPDARGRIRNGALLRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F        104 YVPRSSLPGFYRTSLTLAAPEAA-GEVERLIGHPLPLR----LDAITGPEEEGGRLETILGWPLAERTVVIPSAIPTDPR 178
Cdd:pfam09009  81 YVPRAALPGFFRTSLPLAAEAAAlGEIERLIGHNLPLNsvlgLDAITGPEDEGEPDETILGWDLAEHAVAIPSAIPGDPR 160

                         170
                  ....*....|....*..
1ZM2_F        179 NVGGDLDPSSIPDKEQA 195
Cdd:pfam09009 161 NVGGDLDPINIPDKEKA 177
Dipth_tox_like cd01436
Mono-ADP-ribosylating toxins catalyze the transfer of ADP_ribose from NAD+ to eukaryotic ...
 39-171 5.69e-67

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: 202.49  E-value: 5.69e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1ZM2_F       39 VGYHGTFLEAAQSIVFGgVRARSQ----DLDAIWRGFYIAGDPALAYGYAQDQEPDarGRIRNGALLRVYVPRSslPGFY 114
Cdd:cd01436   1 SSYHGTKPGYVDSIQKG-IQKPKSgtqgNYDDDWKGFYSTDNKYDAAGYSVDNENP--LSGKAGGVVKVTYPGL--TKVL 75

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1ZM2_F      115 RTSLTlaapeAAGEVERLIGHPLP-------------------LRLDAITGPEEE-GGRLETILGWPLAERTVVIPS 171
Cdd:cd01436  76 ALKVD-----NAETIKKELGLSLTeplmeqvgteefikrfgdgASRVVLSLPFAEgSSSVEYINNWEQAKALSVELE 147
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH