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Conserved domains on  [gi|2038648774|pdb|7CE4|A]
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Chain A, Poly [ADP-ribose] polymerase tankyrase-2

Protein Classification

poly(ADP-ribose) polymerase family protein( domain architecture ID 2436)

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

EC:  2.4.2.-
Gene Ontology:  GO:0003950|GO:0003684|GO:0006281

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADP_ribosyl super family cl00283
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 30-191 1.46e-114

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.


The actual alignment was detected with superfamily member cd01438:

Pssm-ID: 444809 [Multi-domain]  Cd Length: 223  Bit Score: 324.93  E-value: 1.46e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A       30 GTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFH 109
Cdd:cd01438  15 GTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFH 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A      110 GSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFS 189
Cdd:cd01438  95 GSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQMLFCRVTLGKSFLQFS 174


                ..
7CE4_A      190 AM 191
Cdd:cd01438 175 AM 176
 
Name Accession Description Interval E-value
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 30-191 1.46e-114

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: 324.93  E-value: 1.46e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A       30 GTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFH 109
Cdd:cd01438  15 GTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFH 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A      110 GSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFS 189
Cdd:cd01438  95 GSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQMLFCRVTLGKSFLQFS 174


                ..
7CE4_A      190 AM 191
Cdd:cd01438 175 AM 176
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 41-183 9.24e-18

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: 76.99  E-value: 9.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A         41 KEFQSVEEEMQSTvrehRDGGHAGGIFnrynILKIQKVCNKKLWERYTHRRKevseenhnHANERMLFHGSP--FVNAII 118
Cdd:pfam00644   2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQPKKK--------LRNRRLLWHGSRltNFLGIL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
7CE4_A        119 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPVHKDRScyicHRQLLFCRVTLGK 183
Cdd:pfam00644  66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGD 120
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 33-182 7.28e-05

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 42.52  E-value: 7.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A        33 LIDLSPDDKEFQSVEEEMQSTvrehRDGGHAGGIFNRYNILKIQKvcnkklwERYTHRRKEVSEeNHNhaneRML-FHGS 111
Cdd:PLN03124 430 LEPLDTDSEEFSMIAKYLENT----HGQTHSGYTLEIVQIFKVSR-------EGEDERFQKFSS-TKN----RMLlWHGS 493

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7CE4_A       112 PFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYVYgigGGTGCPVHkdrscyichrQLLFCRVTLG 182
Cdd:PLN03124 494 RLTNwtGILSQGL--RIAppeapSTGYMFGKGVYFADMFSKSANYCY---ASAANPDG----------VLLLCEVALG 556
 
Name Accession Description Interval E-value
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 30-191 1.46e-114

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: 324.93  E-value: 1.46e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A       30 GTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFH 109
Cdd:cd01438  15 GTILLDLAPDDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNIIRIQKVVNKKLRERYCHRQKEIAEENHNHHNERMLFH 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A      110 GSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFS 189
Cdd:cd01438  95 GSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYVCHRQMLFCRVTLGKSFLQFS 174


                ..
7CE4_A      190 AM 191
Cdd:cd01438 175 AM 176
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 41-183 9.24e-18

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: 76.99  E-value: 9.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A         41 KEFQSVEEEMQSTvrehRDGGHAGGIFnrynILKIQKVCNKKLWERYTHRRKevseenhnHANERMLFHGSP--FVNAII 118
Cdd:pfam00644   2 EEYQIIEKYFLST----HDPTHGYPLF----ILEIFRVQRDGEWERFQPKKK--------LRNRRLLWHGSRltNFLGIL 65

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
7CE4_A        119 HKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPVHKDRScyicHRQLLFCRVTLGK 183
Cdd:pfam00644  66 SQGLriAPPEAPVTGyMFGKGIYFADDASKSANY---------CPPSEAHG----NGLMLLSEVALGD 120
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 106-191 2.01e-15

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: 69.51  E-value: 2.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A      106 MLFHGSPFVNAIIHKGFDERHAYIG-----GMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCyichrqllfCRVT 180
Cdd:cd01341   1 FLFHGSPPGNVISILKLGLRPASYGvllngGMFGKGIYSAPNISKSNGYSVGCDGQHVFQNGKPKVC---------GREL 71

                        90
                ....*....|.
7CE4_A      181 LGKSFLQFSAM 191
Cdd:cd01341  72 CVFGFLTLGVM 82
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 36-183 2.75e-10

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: 58.05  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A       36 LSPDDKEFQSVEEEMQSTvrehrdggHAGGIFNRYNILKIQKVCNKKLWERYTHRRKevseeNHNHaneRMLFHGSPFVN 115
Cdd:cd01437 143 LDKDSEEYKIIEKYLKNT--------HAPTTEYTVEVQEIFRVEREGETDRFKPFKK-----LGNR---KLLWHGSRLTN 206

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
7CE4_A      116 --AIIHKGF--DERHAYIGG-MFGAGIYFAENSSKSNQYVY-GIGGGTGCpvhkdrscyichrqLLFCRVTLGK 183
Cdd:cd01437 207 fvGILSQGLriAPPEAPVTGyMFGKGIYFADMFSKSANYCHaSASDPTGL--------------LLLCEVALGK 266
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 106-158 5.38e-10

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: 54.63  E-value: 5.38e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
7CE4_A      106 MLFHG--SPFVNAIIHKGFDER-HAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTG 158
Cdd:cd01439   1 LLFHGtsADAVEAICRHGFDRRfCGKHGTMYGKGSYFAKNASYSHQYSKKSPKADG 56
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 33-182 7.28e-05

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 42.52  E-value: 7.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
7CE4_A        33 LIDLSPDDKEFQSVEEEMQSTvrehRDGGHAGGIFNRYNILKIQKvcnkklwERYTHRRKEVSEeNHNhaneRML-FHGS 111
Cdd:PLN03124 430 LEPLDTDSEEFSMIAKYLENT----HGQTHSGYTLEIVQIFKVSR-------EGEDERFQKFSS-TKN----RMLlWHGS 493

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
7CE4_A       112 PFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYVYgigGGTGCPVHkdrscyichrQLLFCRVTLG 182
Cdd:PLN03124 494 RLTNwtGILSQGL--RIAppeapSTGYMFGKGVYFADMFSKSANYCY---ASAANPDG----------VLLLCEVALG 556
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 103-151 1.54e-04

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 41.70  E-value: 1.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
7CE4_A       103 NERMLFHGSPFVN--AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYVY 151
Cdd:PLN03123 825 NRMLLWHGSRLTNfvGILSQGL--RIAppeapATGYMFGKGVYFADLVSKSAQYCY 878
 
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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