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Conserved domains on  [gi|296080691|ref|NP_001171647|]
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protein mono-ADP-ribosyltransferase TIPARP [Homo sapiens]

Protein Classification

WWE and TCCD_inducible_PARP_like domain-containing protein( domain architecture ID 11137801)

WWE and 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 ...
 529-648 5.91e-62

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: 201.78  E-value: 5.91e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691 529 HLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSK--GVHFMFLAKVLTGRYTMGSHGMRRp 606
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadGLKEMFLARVLTGDYTQGHPGYRR- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 296080691 607 PPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQY 648
Cdd:cd01439   80 PPLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 346-401 1.48e-04

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: 40.36  E-value: 1.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296080691  346 VWkFFCRDHFGWREYPESVIRLIEEANSRGLK--EVRFMMWNNHYILH---------NSFFRREIKR 401
Cdd:pfam02825   1 VW-EWEDDNGGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDfksmtqtnkDTGTTRPVRR 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 ...
 529-648 5.91e-62

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: 201.78  E-value: 5.91e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691 529 HLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSK--GVHFMFLAKVLTGRYTMGSHGMRRp 606
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadGLKEMFLARVLTGDYTQGHPGYRR- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 296080691 607 PPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQY 648
Cdd:cd01439   80 PPLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 474-648 2.28e-33

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: 126.68  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691  474 YRIIYNLFHKT---VPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMfgrdriinerhLFHGTSQDVVDGICKHNF--D 548
Cdd:pfam00644   4 YQIIEKYFLSThdpTHGYPLFILEIFRVQRDGEWERFQPKKKLRNRRL-----------LWHGSRLTNFLGILSQGLriA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691  549 PRVCGKHATMFGQGSYFAKKASYSHNFSKKS-SKGVHFMFLAKVLTG---------------RYTMGSHGMRRPPPV--- 609
Cdd:pfam00644  73 PPEAPVTGYMFGKGIYFADDASKSANYCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklpPGKHSVKGLGKTAPEsfv 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 296080691  610 ----NP-GSVTSDLYDSCVdnfFEPQIFVIFNDDQSYPYFVIQY 648
Cdd:pfam00644 153 dldgVPlGKLVATGYDSSV---LLYNEYVVYNVNQVRPKYLLEV 193
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 346-401 1.48e-04

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: 40.36  E-value: 1.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296080691  346 VWkFFCRDHFGWREYPESVIRLIEEANSRGLK--EVRFMMWNNHYILH---------NSFFRREIKR 401
Cdd:pfam02825   1 VW-EWEDDNGGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDfksmtqtnkDTGTTRPVRR 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 ...
 529-648 5.91e-62

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: 201.78  E-value: 5.91e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691 529 HLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSK--GVHFMFLAKVLTGRYTMGSHGMRRp 606
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadGLKEMFLARVLTGDYTQGHPGYRR- 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 296080691 607 PPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQY 648
Cdd:cd01439   80 PPLKPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 474-648 2.28e-33

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: 126.68  E-value: 2.28e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691  474 YRIIYNLFHKT---VPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMfgrdriinerhLFHGTSQDVVDGICKHNF--D 548
Cdd:pfam00644   4 YQIIEKYFLSThdpTHGYPLFILEIFRVQRDGEWERFQPKKKLRNRRL-----------LWHGSRLTNFLGILSQGLriA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691  549 PRVCGKHATMFGQGSYFAKKASYSHNFSKKS-SKGVHFMFLAKVLTG---------------RYTMGSHGMRRPPPV--- 609
Cdd:pfam00644  73 PPEAPVTGYMFGKGIYFADDASKSANYCPPSeAHGNGLMLLSEVALGdmnelkkadyaeklpPGKHSVKGLGKTAPEsfv 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 296080691  610 ----NP-GSVTSDLYDSCVdnfFEPQIFVIFNDDQSYPYFVIQY 648
Cdd:pfam00644 153 dldgVPlGKLVATGYDSSV---LLYNEYVVYNVNQVRPKYLLEV 193
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 529-644 1.79e-22

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: 93.78  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691 529 HLFHGTSQDVVDGICKHNFDPRVCGK--HATMFGQGSYFAKKASYSHNFSKKSS---------------KGVHFMFLAKV 591
Cdd:cd01341    1 FLFHGSPPGNVISILKLGLRPASYGVllNGGMFGKGIYSAPNISKSNGYSVGCDgqhvfqngkpkvcgrELCVFGFLTLG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 296080691 592 LTGRYTMGSHGMrRPPPVNPGSVTSDLYDSCV----DNFFEPQIFVIFND-DQSYPYF 644
Cdd:cd01341   81 VMSGATEESSRV-LFPRNFRGATGAEVVDLLVamcrDALLLPREYIIFEPySQVSIRY 137
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 489-649 4.33e-07

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: 51.44  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691 489 KYRILQILRVQNQFLWEKYKRKKEYMNRKMFgrdRIINERHLFHGTSqdVVDGICKHNFDPRvcgkHA---TMFGQGSYF 565
Cdd:cd01438   54 RYNIIRIQKVVNKKLRERYCHRQKEIAEENH---NHHNERMLFHGSP--FINAIIHKGFDER----HAyigGMFGAGIYF 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691 566 AKKASYSHNFSKKSSKGV----H-----FMFLAKVLTGRYTMG-------SHGMRRPPP-----VNPGSVTSDLYDScvd 624
Cdd:cd01438  125 AENSSKSNQYVYGIGGGTgcptHkdrscYVCHRQMLFCRVTLGksflqfsAMKMAHAPPghhsvIGRPSVNGLAYAE--- 201

                        170       180
                 ....*....|....*....|....*
gi 296080691 625 nffepqiFVIFNDDQSYPYFVIQYE 649
Cdd:cd01438  202 -------YVIYRGEQAYPEYLITYQ 219
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 346-401 1.48e-04

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: 40.36  E-value: 1.48e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296080691  346 VWkFFCRDHFGWREYPESVIRLIEEANSRGLK--EVRFMMWNNHYILH---------NSFFRREIKR 401
Cdd:pfam02825   1 VW-EWEDDNGGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDfksmtqtnkDTGTTRPVRR 66
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 466-595 2.43e-04

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: 43.80  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296080691 466 PVSAEDKSYRIIYNLFHKT---VPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMfgrdriinerhLFHGTSQDVVDGI 542
Cdd:cd01437  142 PLDKDSEEYKIIEKYLKNThapTTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKL-----------LWHGSRLTNFVGI 210

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296080691 543 CKHNFDPRVCGKHAT--MFGQGSYFA----KKASYSHnfsKKSSKGVHFMFLAKVLTGR 595
Cdd:cd01437  211 LSQGLRIAPPEAPVTgyMFGKGIYFAdmfsKSANYCH---ASASDPTGLLLLCEVALGK 266
 
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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