NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767936521|ref|XP_011541945|]
View 

protein mono-ADP-ribosyltransferase PARP8 isoform X8 [Homo sapiens]

Protein Classification

poly(ADP-ribose) polymerase family protein( domain architecture ID 10102014)

poly(ADP-ribose) polymerase family protein such as protein mono-ADP-ribosyltransferase PARP6 that mediates mono-ADP-ribosylation of target proteins

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 cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 500-624 3.09e-26

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: 104.56  E-value: 3.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936521 500 FAFHGSHIENWHSILRNGLVVASNTRlQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKVSAKDEPASSSKSSNTSQ---- 575
Cdd:cd01341    1 FLFHGSPPGNVISILKLGLRPASYGV-LLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKVCGRELCVFGfltl 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767936521 576 ---SQKKGQQSQFLQSRNLKCIALCEVITSSD------LHKHGEIWVVPNTDHVCTRF 624
Cdd:cd01341   80 gvmSGATEESSRVLFPRNFRGATGAEVVDLLVamcrdaLLLPREYIIFEPYSQVSIRY 137
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 288-387 1.25e-23

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: 96.86  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936521 288 CIPVRDRGFLVQtiefaeQRIPVLNEYCVVCDEPHVFQNGpmlRPTVCERELCVFAFQTLGVMNEAADE----------- 356
Cdd:cd01341   29 NGGMFGKGIYSA------PNISKSNGYSVGCDGQHVFQNG---KPKVCGRELCVFGFLTLGVMSGATEEssrvlfprnfr 99

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767936521 357 IATGAQVVDLLVSMCRSALESPRKVVIFEPY 387
Cdd:cd01341  100 GATGAEVVDLLVAMCRDALLLPREYIIFEPY 130
 
Name Accession Description Interval E-value
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 500-624 3.09e-26

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: 104.56  E-value: 3.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936521 500 FAFHGSHIENWHSILRNGLVVASNTRlQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKVSAKDEPASSSKSSNTSQ---- 575
Cdd:cd01341    1 FLFHGSPPGNVISILKLGLRPASYGV-LLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKVCGRELCVFGfltl 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767936521 576 ---SQKKGQQSQFLQSRNLKCIALCEVITSSD------LHKHGEIWVVPNTDHVCTRF 624
Cdd:cd01341   80 gvmSGATEESSRVLFPRNFRGATGAEVVDLLVamcrdaLLLPREYIIFEPYSQVSIRY 137
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 288-387 1.25e-23

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: 96.86  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936521 288 CIPVRDRGFLVQtiefaeQRIPVLNEYCVVCDEPHVFQNGpmlRPTVCERELCVFAFQTLGVMNEAADE----------- 356
Cdd:cd01341   29 NGGMFGKGIYSA------PNISKSNGYSVGCDGQHVFQNG---KPKVCGRELCVFGFLTLGVMSGATEEssrvlfprnfr 99

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767936521 357 IATGAQVVDLLVSMCRSALESPRKVVIFEPY 387
Cdd:cd01341  100 GATGAEVVDLLVAMCRDALLLPREYIIFEPY 130
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 488-558 1.04e-11

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes 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: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 64.28  E-value: 1.04e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767936521  488 NFRAAKKLFGSTFAFHGSHIENWHSILRNGLVVASNtRLQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKV 558
Cdd:pfam00644  39 RFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPP-EAPVTGYMFGKGIYFADDASKSANYCPPSEAHGN 108
 
Name Accession Description Interval E-value
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 500-624 3.09e-26

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: 104.56  E-value: 3.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936521 500 FAFHGSHIENWHSILRNGLVVASNTRlQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKVSAKDEPASSSKSSNTSQ---- 575
Cdd:cd01341    1 FLFHGSPPGNVISILKLGLRPASYGV-LLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKVCGRELCVFGfltl 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767936521 576 ---SQKKGQQSQFLQSRNLKCIALCEVITSSD------LHKHGEIWVVPNTDHVCTRF 624
Cdd:cd01341   80 gvmSGATEESSRVLFPRNFRGATGAEVVDLLVamcrdaLLLPREYIIFEPYSQVSIRY 137
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 288-387 1.25e-23

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: 96.86  E-value: 1.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936521 288 CIPVRDRGFLVQtiefaeQRIPVLNEYCVVCDEPHVFQNGpmlRPTVCERELCVFAFQTLGVMNEAADE----------- 356
Cdd:cd01341   29 NGGMFGKGIYSA------PNISKSNGYSVGCDGQHVFQNG---KPKVCGRELCVFGFLTLGVMSGATEEssrvlfprnfr 99

                         90       100       110
                 ....*....|....*....|....*....|.
gi 767936521 357 IATGAQVVDLLVSMCRSALESPRKVVIFEPY 387
Cdd:cd01341  100 GATGAEVVDLLVAMCRDALLLPREYIIFEPY 130
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 488-558 1.04e-11

Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes 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: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 64.28  E-value: 1.04e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767936521  488 NFRAAKKLFGSTFAFHGSHIENWHSILRNGLVVASNtRLQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKV 558
Cdd:pfam00644  39 RFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPP-EAPVTGYMFGKGIYFADDASKSANYCPPSEAHGN 108
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 489-558 5.47e-07

Poly(ADP-ribose) polymerase (parp) catalytic domain 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. Poly(ADP-ribose)-like 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 through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 52.27  E-value: 5.47e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936521 489 FRAAKKLFGSTFAFHGSHIENWHSILRNGLVVASnTRLQLHGAMYGSGIYLSPMSSISFGYSGMNKKQKV 558
Cdd:cd01437  186 FKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAP-PEAPVTGYMFGKGIYFADMFSKSANYCHASASDPT 254
 
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