protein mono-ADP-ribosyltransferase PARP3 [Danio rerio]
Protein Classification
poly(ADP-ribose) polymerase family protein( domain architecture ID 10168760)
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
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| parp_like | cd01437 | Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
183-527 | 1.02e-149 | ||||||
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: 432.46 E-value: 1.02e-149
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| WGR_PARP3_like | cd08002 | WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ... |
59-157 | 2.86e-38 | ||||||
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage. : Pssm-ID: 153429 Cd Length: 100 Bit Score: 135.61 E-value: 2.86e-38
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| Name | Accession | Description | Interval | E-value | ||||||||
| parp_like | cd01437 | Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
183-527 | 1.02e-149 | ||||||||
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: 432.46 E-value: 1.02e-149
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| PLN03124 | PLN03124 | poly [ADP-ribose] polymerase; Provisional |
8-530 | 3.07e-109 | ||||||||
poly [ADP-ribose] polymerase; Provisional Pssm-ID: 215591 [Multi-domain] Cd Length: 643 Bit Score: 339.12 E-value: 3.07e-109
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| PARP | pfam00644 | Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
334-528 | 1.35e-66 | ||||||||
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: 213.73 E-value: 1.35e-66
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| WGR_PARP3_like | cd08002 | WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ... |
59-157 | 2.86e-38 | ||||||||
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage. Pssm-ID: 153429 Cd Length: 100 Bit Score: 135.61 E-value: 2.86e-38
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| WGR | smart00773 | Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
62-144 | 3.42e-13 | ||||||||
Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain. Pssm-ID: 214814 Cd Length: 84 Bit Score: 65.00 E-value: 3.42e-13
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| WGR | pfam05406 | WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ... |
67-144 | 3.78e-09 | ||||||||
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain. Pssm-ID: 398851 Cd Length: 79 Bit Score: 53.40 E-value: 3.78e-09
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| Name | Accession | Description | Interval | E-value | ||||||||
| parp_like | cd01437 | Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ... |
183-527 | 1.02e-149 | ||||||||
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: 432.46 E-value: 1.02e-149
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| PLN03124 | PLN03124 | poly [ADP-ribose] polymerase; Provisional |
8-530 | 3.07e-109 | ||||||||
poly [ADP-ribose] polymerase; Provisional Pssm-ID: 215591 [Multi-domain] Cd Length: 643 Bit Score: 339.12 E-value: 3.07e-109
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| PLN03123 | PLN03123 | poly [ADP-ribose] polymerase; Provisional |
83-530 | 3.04e-68 | ||||||||
poly [ADP-ribose] polymerase; Provisional Pssm-ID: 215590 [Multi-domain] Cd Length: 981 Bit Score: 237.00 E-value: 3.04e-68
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| PARP | pfam00644 | Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ... |
334-528 | 1.35e-66 | ||||||||
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: 213.73 E-value: 1.35e-66
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| PARP_reg | pfam02877 | Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ... |
184-320 | 4.54e-60 | ||||||||
Poly(ADP-ribose) polymerase, regulatory 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: 460732 [Multi-domain] Cd Length: 135 Bit Score: 194.67 E-value: 4.54e-60
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| WGR_PARP3_like | cd08002 | WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ... |
59-157 | 2.86e-38 | ||||||||
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage. Pssm-ID: 153429 Cd Length: 100 Bit Score: 135.61 E-value: 2.86e-38
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| PLN03122 | PLN03122 | Poly [ADP-ribose] polymerase; Provisional |
184-528 | 9.56e-29 | ||||||||
Poly [ADP-ribose] polymerase; Provisional Pssm-ID: 178669 [Multi-domain] Cd Length: 815 Bit Score: 121.06 E-value: 9.56e-29
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| WGR_PARP | cd07997 | WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
67-157 | 2.40e-21 | ||||||||
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others. Pssm-ID: 153426 Cd Length: 102 Bit Score: 88.90 E-value: 2.40e-21
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| WGR_PARP2_like | cd08003 | WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ... |
67-156 | 6.34e-17 | ||||||||
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-2 and similar proteins. Similar to PARP-1, PARP-2 is ubiquitously expressed and its activity is induced by DNA strand breaks. It also plays a role in cell differentiation, cell death, and maintaining genomic stability. Studies on mice deficient with PARP-2 shows that it is important in fat storage, T cell maturation, and spermatogenesis. Pssm-ID: 153430 Cd Length: 103 Bit Score: 76.21 E-value: 6.34e-17
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| WGR | smart00773 | Proposed nucleic acid binding domain; This domain is named after its most conserved central ... |
62-144 | 3.42e-13 | ||||||||
Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain. Pssm-ID: 214814 Cd Length: 84 Bit Score: 65.00 E-value: 3.42e-13
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| ADP_ribosyl | cd01341 | ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ... |
381-482 | 1.34e-09 | ||||||||
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: 56.41 E-value: 1.34e-09
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| WGR | pfam05406 | WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ... |
67-144 | 3.78e-09 | ||||||||
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain. Pssm-ID: 398851 Cd Length: 79 Bit Score: 53.40 E-value: 3.78e-09
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| TCCD_inducible_PARP_like | cd01439 | Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ... |
380-466 | 1.81e-07 | ||||||||
Poly(ADP-ribose) polymerases catalyse 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. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation Pssm-ID: 238719 [Multi-domain] Cd Length: 121 Bit Score: 50.01 E-value: 1.81e-07
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| tankyrase_like | cd01438 | Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ... |
371-524 | 4.62e-04 | ||||||||
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis). Pssm-ID: 238718 [Multi-domain] Cd Length: 223 Bit Score: 41.81 E-value: 4.62e-04
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