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Conserved domains on  [gi|1720416523|ref|XP_030110897|]
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protein mono-ADP-ribosyltransferase PARP11 isoform X4 [Mus musculus]

Protein Classification

TCCD_inducible_PARP_like domain-containing protein( domain architecture ID 10106618)

TCCD_inducible_PARP_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 77-213 5.28e-61

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: 186.37  E-value: 5.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  77 MLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHgntfqihgvslqqrhlfRTYKSMFLA 156
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKA-----------------DGLKEMFLA 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416523 157 RVLIGDYINGDSKYMRPP-SKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDF 213
Cdd:cd01439    64 RVLTGDYTQGHPGYRRPPlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 77-213 5.28e-61

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: 186.37  E-value: 5.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  77 MLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHgntfqihgvslqqrhlfRTYKSMFLA 156
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKA-----------------DGLKEMFLA 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416523 157 RVLIGDYINGDSKYMRPP-SKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDF 213
Cdd:cd01439    64 RVLTGDYTQGHPGYRRPPlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 23-213 1.03e-44

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: 147.48  E-value: 1.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  23 THEYNEVASLFGKTMD-----RNRIKRIQRIQNLDLWEFFCRKKAQlkkkrgvpqINEQMLFHGTSSEFVEAICIHNF-- 95
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKL---------RNRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  96 DWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFqihgvslqqrhlfrtyksMFLARVLIGD------------- 162
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPSEAHGNGL------------------MLLSEVALGDmnelkkadyaekl 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416523 163 -----YINGDSKYMR--------PPSKDGSyVNLYDSCVddtWNPKIFVVFDANQIYPEYLIDF 213
Cdd:pfam00644 134 ppgkhSVKGLGKTAPesfvdldgVPLGKLV-ATGYDSSV---LLYNEYVVYNVNQVRPKYLLEV 193
 
Name Accession Description Interval E-value
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 77-213 5.28e-61

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: 186.37  E-value: 5.28e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  77 MLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHgntfqihgvslqqrhlfRTYKSMFLA 156
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKA-----------------DGLKEMFLA 63

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720416523 157 RVLIGDYINGDSKYMRPP-SKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDF 213
Cdd:cd01439    64 RVLTGDYTQGHPGYRRPPlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 23-213 1.03e-44

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: 147.48  E-value: 1.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  23 THEYNEVASLFGKTMD-----RNRIKRIQRIQNLDLWEFFCRKKAQlkkkrgvpqINEQMLFHGTSSEFVEAICIHNF-- 95
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKL---------RNRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  96 DWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFqihgvslqqrhlfrtyksMFLARVLIGD------------- 162
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPSEAHGNGL------------------MLLSEVALGDmnelkkadyaekl 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720416523 163 -----YINGDSKYMR--------PPSKDGSyVNLYDSCVddtWNPKIFVVFDANQIYPEYLIDF 213
Cdd:pfam00644 134 ppgkhSVKGLGKTAPesfvdldgVPLGKLV-ATGYDSSV---LLYNEYVVYNVNQVRPKYLLEV 193
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 34-214 1.23e-11

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: 61.45  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  34 GKTMDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRgVPQINEQMLFHGtsSEFVEAICIHNFDWRiNGVHGAVFGKGTYF 113
Cdd:cd01438    49 GGIFNRYNIIRIQKVVNKKLRERYCHRQKEIAEEN-HNHHNERMLFHG--SPFINAIIHKGFDER-HAYIGGMFGAGIYF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523 114 ARDAAYSSRFCKdDIKHGNTFQIHgvslQQRHLFRTYKSMFLARVLIGDYI------------NGDSKYMRPPSKDGSYV 181
Cdd:cd01438   125 AENSSKSNQYVY-GIGGGTGCPTH----KDRSCYVCHRQMLFCRVTLGKSFlqfsamkmahapPGHHSVIGRPSVNGLAY 199

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720416523 182 NLYdscvddtwnpkifVVFDANQIYPEYLIDFH 214
Cdd:cd01438   200 AEY-------------VIYRGEQAYPEYLITYQ 219
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 77-209 2.19e-05

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: 42.93  E-value: 2.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720416523  77 MLFHGTSSEFVEAICIHNFDWR--INGVHGAVFGKGTYFARDAAYSSRFCKDDiKHGNTFQIHGVSLQQRHLFrtyKSMF 154
Cdd:cd01341     1 FLFHGSPPGNVISILKLGLRPAsyGVLLNGGMFGKGIYSAPNISKSNGYSVGC-DGQHVFQNGKPKVCGRELC---VFGF 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720416523 155 LARVLIGDYiNGDSKYMRPPSKDGSYV--NLYDSCVDDT-WN---PKIFVVFDAN-QIYPEY 209
Cdd:cd01341    77 LTLGVMSGA-TEESSRVLFPRNFRGATgaEVVDLLVAMCrDAlllPREYIIFEPYsQVSIRY 137
 
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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