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Conserved domains on  [gi|31088906|ref|NP_852067|]
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protein mono-ADP-ribosyltransferase PARP11 isoform 1 [Mus musculus]

Protein Classification

E3 ubiquitin-protein ligase RNF146( domain architecture ID 10653397)

E3 ubiquitin-protein ligase RNF146 (or RING finger protein 146) is a cytoplasmic E3 ubiquitin-protein ligase responsible for PARylation-dependent ubiquitination (PARdU)

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 ...
 194-330 9.10e-60

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: 187.53  E-value: 9.10e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906 194 MLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHgntfqihgvslqqrhlfRTYKSMFLA 273
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKA-----------------DGLKEMFLA 63

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31088906 274 RVLIGDYINGDSKYMRPP-SKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDF 330
Cdd:cd01439  64 RVLTGDYTQGHPGYRRPPlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 27-107 1.71e-17

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 75.84  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906     27 WGWFYLAECGKWHMFQPDTniqcsvsSEDIEKSFKTN--PCGSISFTtskFSYKIDFAEMKQMNLVTGKQRLIKRAPFSI 104
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRV-------SEDIEEAYAAGkkLCELSICG---FPYTIDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 31088906    105 SAF 107
Cdd:smart00678  71 YSK 73
 
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 ...
 194-330 9.10e-60

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: 187.53  E-value: 9.10e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906 194 MLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHgntfqihgvslqqrhlfRTYKSMFLA 273
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKA-----------------DGLKEMFLA 63

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31088906 274 RVLIGDYINGDSKYMRPP-SKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDF 330
Cdd:cd01439  64 RVLTGDYTQGHPGYRRPPlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 140-330 6.14e-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: 149.41  E-value: 6.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906   140 THEYNEVASLFGKTMD-----RNRIKRIQRIQNLDLWEFFCRKKAQlkkkrgvpqINEQMLFHGTSSEFVEAICIHNF-- 212
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKL---------RNRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906   213 DWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFqihgvslqqrhlfrtyksMFLARVLIGD------------- 279
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPSEAHGNGL------------------MLLSEVALGDmnelkkadyaekl 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31088906   280 -----YINGDSKYMR--------PPSKDGSyVNLYDSCVddtWNPKIFVVFDANQIYPEYLIDF 330
Cdd:pfam00644 134 ppgkhSVKGLGKTAPesfvdldgVPLGKLV-ATGYDSSV---LLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 27-107 1.71e-17

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 75.84  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906     27 WGWFYLAECGKWHMFQPDTniqcsvsSEDIEKSFKTN--PCGSISFTtskFSYKIDFAEMKQMNLVTGKQRLIKRAPFSI 104
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRV-------SEDIEEAYAAGkkLCELSICG---FPYTIDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 31088906    105 SAF 107
Cdd:smart00678  71 YSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 29-99 4.97e-17

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 74.26  E-value: 4.97e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31088906    29 WFYLAECGKWHMFQPDTniqcsvsSEDIEKSF-KTNPCGSISFTTSKFSYKIDFAEMKQMNLVTGKQRLIKR 99
Cdd:pfam02825   2 WEWEDDNGGWHPYDPEV-------SSLIEEAYqKGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
 
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 ...
 194-330 9.10e-60

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: 187.53  E-value: 9.10e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906 194 MLFHGTSSEFVEAICIHNFDWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHgntfqihgvslqqrhlfRTYKSMFLA 273
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKA-----------------DGLKEMFLA 63

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 31088906 274 RVLIGDYINGDSKYMRPP-SKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDF 330
Cdd:cd01439  64 RVLTGDYTQGHPGYRRPPlKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 140-330 6.14e-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: 149.41  E-value: 6.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906   140 THEYNEVASLFGKTMD-----RNRIKRIQRIQNLDLWEFFCRKKAQlkkkrgvpqINEQMLFHGTSSEFVEAICIHNF-- 212
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKL---------RNRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906   213 DWRINGVHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFqihgvslqqrhlfrtyksMFLARVLIGD------------- 279
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPSEAHGNGL------------------MLLSEVALGDmnelkkadyaekl 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 31088906   280 -----YINGDSKYMR--------PPSKDGSyVNLYDSCVddtWNPKIFVVFDANQIYPEYLIDF 330
Cdd:pfam00644 134 ppgkhSVKGLGKTAPesfvdldgVPLGKLV-ATGYDSSV---LLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 27-107 1.71e-17

Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated proteolysis;


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 75.84  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906     27 WGWFYLAECGKWHMFQPDTniqcsvsSEDIEKSFKTN--PCGSISFTtskFSYKIDFAEMKQMNLVTGKQRLIKRAPFSI 104
Cdd:smart00678   1 YVWEYEGRNGKWWPYDPRV-------SEDIEEAYAAGkkLCELSICG---FPYTIDFNAMTQYNQATGTTRKVRRVTYSP 70


                   ...
gi 31088906    105 SAF 107
Cdd:smart00678  71 YSK 73
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 29-99 4.97e-17

WWE domain; The WWE domain is named after three of its conserved residues and is predicted to mediate specific protein- protein interactions in ubiquitin and ADP ribose conjugation systems.


Pssm-ID: 460715 [Multi-domain]  Cd Length: 66  Bit Score: 74.26  E-value: 4.97e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31088906    29 WFYLAECGKWHMFQPDTniqcsvsSEDIEKSF-KTNPCGSISFTTSKFSYKIDFAEMKQMNLVTGKQRLIKR 99
Cdd:pfam02825   2 WEWEDDNGGWHPYDPEV-------SSLIEEAYqKGKPSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 151-331 9.24e-12

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: 63.77  E-value: 9.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906 151 GKTMDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRgVPQINEQMLFHGtsSEFVEAICIHNFDWRiNGVHGAVFGKGTYF 230
Cdd:cd01438  49 GGIFNRYNIIRIQKVVNKKLRERYCHRQKEIAEEN-HNHHNERMLFHG--SPFINAIIHKGFDER-HAYIGGMFGAGIYF 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906 231 ARDAAYSSRFCKdDIKHGNTFQIHgvslQQRHLFRTYKSMFLARVLIGDYINGDS--KYMRPPSKDGSYVNlydscvddt 308
Cdd:cd01438 125 AENSSKSNQYVY-GIGGGTGCPTH----KDRSCYVCHRQMLFCRVTLGKSFLQFSamKMAHAPPGHHSVIG--------- 190

                       170       180       190
                ....*....|....*....|....*....|
gi 31088906 309 wNPKI-------FVVFDANQIYPEYLIDFH 331
Cdd:cd01438 191 -RPSVnglayaeYVIYRGEQAYPEYLITYQ 219
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 194-326 3.81e-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: 3.81e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31088906 194 MLFHGTSSEFVEAICIHNFDWR--INGVHGAVFGKGTYFARDAAYSSRFCKDDiKHGNTFQIHGVSLQQRHLFrtyKSMF 271
Cdd:cd01341   1 FLFHGSPPGNVISILKLGLRPAsyGVLLNGGMFGKGIYSAPNISKSNGYSVGC-DGQHVFQNGKPKVCGRELC---VFGF 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 31088906 272 LARVLIGDYiNGDSKYMRPPSKDGSYV--NLYDSCVDDT-WN---PKIFVVFDAN-QIYPEY 326
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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