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Conserved domains on  [gi|1021311823|ref|NP_001310450|]
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protein mono-ADP-ribosyltransferase PARP6 isoform 3 [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

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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. ...
 450-574 8.30e-35

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: 128.45  E-value: 8.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311823 450 FAFHGSHIENWHSILRNGLVNASYTKlQLHGAAYGKGIYLSPISSISFGYSGMGKGQHRM-------PSKDELVQRYNRM 522
Cdd:cd01341     1 FLFHGSPPGNVISILKLGLRPASYGV-LLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFqngkpkvCGRELCVFGFLTL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1021311823 523 NTIPQTRSIQSRFLQSRNLNCIALCEVITSKD------LQKHGNIWVCPVSDHVCTRF 574
Cdd:cd01341    80 GVMSGATEESSRVLFPRNFRGATGAEVVDLLVamcrdaLLLPREYIIFEPYSQVSIRY 137
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 225-338 1.45e-29

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: 113.81  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311823 225 FGYPPSPQVSGHCknIPTLEYGFLVQimkyaeQRIPTLNEYCVVCDEQHVFQNGsmlKPAVCTRELCVFSFYTLGVMSGA 304
Cdd:cd01341    17 LGLRPASYGVLLN--GGMFGKGIYSA------PNISKSNGYSVGCDGQHVFQNG---KPKVCGRELCVFGFLTLGVMSGA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1021311823 305 AEE-----------VATGAEVVDLLVAMCRAALESPRKSIIFEPY 338
Cdd:cd01341    86 TEEssrvlfprnfrGATGAEVVDLLVAMCRDALLLPREYIIFEPY 130
 
Name Accession Description Interval E-value
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 450-574 8.30e-35

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: 128.45  E-value: 8.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311823 450 FAFHGSHIENWHSILRNGLVNASYTKlQLHGAAYGKGIYLSPISSISFGYSGMGKGQHRM-------PSKDELVQRYNRM 522
Cdd:cd01341     1 FLFHGSPPGNVISILKLGLRPASYGV-LLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFqngkpkvCGRELCVFGFLTL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1021311823 523 NTIPQTRSIQSRFLQSRNLNCIALCEVITSKD------LQKHGNIWVCPVSDHVCTRF 574
Cdd:cd01341    80 GVMSGATEESSRVLFPRNFRGATGAEVVDLLVamcrdaLLLPREYIIFEPYSQVSIRY 137
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 225-338 1.45e-29

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: 113.81  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311823 225 FGYPPSPQVSGHCknIPTLEYGFLVQimkyaeQRIPTLNEYCVVCDEQHVFQNGsmlKPAVCTRELCVFSFYTLGVMSGA 304
Cdd:cd01341    17 LGLRPASYGVLLN--GGMFGKGIYSA------PNISKSNGYSVGCDGQHVFQNG---KPKVCGRELCVFGFLTLGVMSGA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1021311823 305 AEE-----------VATGAEVVDLLVAMCRAALESPRKSIIFEPY 338
Cdd:cd01341    86 TEEssrvlfprnfrGATGAEVVDLLVAMCRDALLLPREYIIFEPY 130
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 438-509 4.24e-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: 62.35  E-value: 4.24e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021311823 438 RFRTAKKLYGSTFAFHGSHIENWHSILRNGLVNASYtKLQLHGAAYGKGIYLSPISSISFGYS--GMGKGQHRM 509
Cdd:pfam00644  39 RFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPP-EAPVTGYMFGKGIYFADDASKSANYCppSEAHGNGLM 111
 
Name Accession Description Interval E-value
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 450-574 8.30e-35

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: 128.45  E-value: 8.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311823 450 FAFHGSHIENWHSILRNGLVNASYTKlQLHGAAYGKGIYLSPISSISFGYSGMGKGQHRM-------PSKDELVQRYNRM 522
Cdd:cd01341     1 FLFHGSPPGNVISILKLGLRPASYGV-LLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFqngkpkvCGRELCVFGFLTL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1021311823 523 NTIPQTRSIQSRFLQSRNLNCIALCEVITSKD------LQKHGNIWVCPVSDHVCTRF 574
Cdd:cd01341    80 GVMSGATEESSRVLFPRNFRGATGAEVVDLLVamcrdaLLLPREYIIFEPYSQVSIRY 137
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 225-338 1.45e-29

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: 113.81  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1021311823 225 FGYPPSPQVSGHCknIPTLEYGFLVQimkyaeQRIPTLNEYCVVCDEQHVFQNGsmlKPAVCTRELCVFSFYTLGVMSGA 304
Cdd:cd01341    17 LGLRPASYGVLLN--GGMFGKGIYSA------PNISKSNGYSVGCDGQHVFQNG---KPKVCGRELCVFGFLTLGVMSGA 85

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1021311823 305 AEE-----------VATGAEVVDLLVAMCRAALESPRKSIIFEPY 338
Cdd:cd01341    86 TEEssrvlfprnfrGATGAEVVDLLVAMCRDALLLPREYIIFEPY 130
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 438-509 4.24e-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: 62.35  E-value: 4.24e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1021311823 438 RFRTAKKLYGSTFAFHGSHIENWHSILRNGLVNASYtKLQLHGAAYGKGIYLSPISSISFGYS--GMGKGQHRM 509
Cdd:pfam00644  39 RFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPP-EAPVTGYMFGKGIYFADDASKSANYCppSEAHGNGLM 111
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 438-508 1.32e-05

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: 47.65  E-value: 1.32e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1021311823 438 RFRTAKKLYGSTFAFHGSHIENWHSILRNGL----VNASYTklqlhGAAYGKGIYLSPISSISFGYSGMGKGQHR 508
Cdd:cd01437   185 RFKPFKKLGNRKLLWHGSRLTNFVGILSQGLriapPEAPVT-----GYMFGKGIYFADMFSKSANYCHASASDPT 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.
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