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Conserved domains on  [gi|2029080357|ref|XP_040902124|]
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protein mono-ADP-ribosyltransferase TIPARP [Toxotes jaculatrix]

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 ...
 604-723 1.53e-63

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: 207.17  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 604 HLFHGTSADVVEGICKHNFDPRVCGKHATMFGQGSYFARKAVYSHNFSKRSPK--GVHCMFLAKVLTGRFTVGNPSMRRP 681
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2029080357 682 PPiNPRDPSSDLYDSCVDNWVDPQIYVIFNDDQSYPYFIIHY 723
Cdd:cd01439    81 PL-KPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 390-453 4.69e-12

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: 61.54  E-value: 4.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2029080357 390 VWkYYCRDNFGWREYSEPVVKLIEEASSRGLK--EVRFITLQNQYILNIREGFQQNAIFGFRRQIK 453
Cdd:pfam02825   1 VW-EWEDDNGGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65
 
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 ...
 604-723 1.53e-63

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: 207.17  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 604 HLFHGTSADVVEGICKHNFDPRVCGKHATMFGQGSYFARKAVYSHNFSKRSPK--GVHCMFLAKVLTGRFTVGNPSMRRP 681
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2029080357 682 PPiNPRDPSSDLYDSCVDNWVDPQIYVIFNDDQSYPYFIIHY 723
Cdd:cd01439    81 PL-KPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 549-723 6.22e-28

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: 111.27  E-value: 6.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 549 YRTVYSLFHKTVSETK---FRIIKILRVQNPFLWEKYKRKKEYMSRRMsemdrllserhLFHGTSADVVEGICKHNF--D 623
Cdd:pfam00644   4 YQIIEKYFLSTHDPTHgypLFILEIFRVQRDGEWERFQPKKKLRNRRL-----------LWHGSRLTNFLGILSQGLriA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 624 PRVCGKHATMFGQGSYFARKAVYSHNFSKRSP-KGVHCMFLAKVLTGRFTV--GNPSMRRPPP----------------- 683
Cdd:pfam00644  73 PPEAPVTGYMFGKGIYFADDASKSANYCPPSEaHGNGLMLLSEVALGDMNElkKADYAEKLPPgkhsvkglgktapesfv 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2029080357 684 ---INPRD-PSSDLYDSCVdnwVDPQIYVIFNDDQSYPYFIIHY 723
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 ...
 390-453 4.69e-12

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: 61.54  E-value: 4.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2029080357 390 VWkYYCRDNFGWREYSEPVVKLIEEASSRGLK--EVRFITLQNQYILNIREGFQQNAIFGFRRQIK 453
Cdd:pfam02825   1 VW-EWEDDNGGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 390-456 5.15e-07

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 47.72  E-value: 5.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029080357  390 VWKYYCRdNFGWREYSEPVVKLIEEASSRGLKEVRFITLQNQYILNIREGFQQNAIFGFRRQIKKRP 456
Cdd:smart00678   2 VWEYEGR-NGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVT 67
 
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 ...
 604-723 1.53e-63

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: 207.17  E-value: 1.53e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 604 HLFHGTSADVVEGICKHNFDPRVCGKHATMFGQGSYFARKAVYSHNFSKRSPK--GVHCMFLAKVLTGRFTVGNPSMRRP 681
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadGLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2029080357 682 PPiNPRDPSSDLYDSCVDNWVDPQIYVIFNDDQSYPYFIIHY 723
Cdd:cd01439    81 PL-KPSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 549-723 6.22e-28

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: 111.27  E-value: 6.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 549 YRTVYSLFHKTVSETK---FRIIKILRVQNPFLWEKYKRKKEYMSRRMsemdrllserhLFHGTSADVVEGICKHNF--D 623
Cdd:pfam00644   4 YQIIEKYFLSTHDPTHgypLFILEIFRVQRDGEWERFQPKKKLRNRRL-----------LWHGSRLTNFLGILSQGLriA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 624 PRVCGKHATMFGQGSYFARKAVYSHNFSKRSP-KGVHCMFLAKVLTGRFTV--GNPSMRRPPP----------------- 683
Cdd:pfam00644  73 PPEAPVTGYMFGKGIYFADDASKSANYCPPSEaHGNGLMLLSEVALGDMNElkKADYAEKLPPgkhsvkglgktapesfv 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2029080357 684 ---INPRD-PSSDLYDSCVdnwVDPQIYVIFNDDQSYPYFIIHY 723
Cdd:pfam00644 153 dldGVPLGkLVATGYDSSV---LLYNEYVVYNVNQVRPKYLLEV 193
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 604-719 5.67e-18

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: 81.07  E-value: 5.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 604 HLFHGTSADVVEGICKHNFDPRVCGK--HATMFGQGSYFARKAVYSHNFSKR---------------SPKGVHCMFLAKV 666
Cdd:cd01341     1 FLFHGSPPGNVISILKLGLRPASYGVllNGGMFGKGIYSAPNISKSNGYSVGcdgqhvfqngkpkvcGRELCVFGFLTLG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2029080357 667 LTGRFTVGNPSMrRPPPINPRDPSSDLYDSCVDNWVD----PQIYVIFND-DQSYPYF 719
Cdd:cd01341    81 VMSGATEESSRV-LFPRNFRGATGAEVVDLLVAMCRDalllPREYIIFEPySQVSIRY 137
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 390-453 4.69e-12

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: 61.54  E-value: 4.69e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2029080357 390 VWkYYCRDNFGWREYSEPVVKLIEEASSRGLK--EVRFITLQNQYILNIREGFQQNAIFGFRRQIK 453
Cdd:pfam02825   1 VW-EWEDDNGGWHPYDPEVSSLIEEAYQKGKPsvDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVR 65
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 545-724 3.42e-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: 51.82  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 545 EDRSYRTVYSLFHKTVSE-----------TKFRIIKILRVQNPFLWEKYKRKKEYMSrrmSEMDRLLSERHLFHGTSadV 613
Cdd:cd01438    24 DDKEYQSVEEEMQSTIREhrdggnaggifNRYNIIRIQKVVNKKLRERYCHRQKEIA---EENHNHHNERMLFHGSP--F 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2029080357 614 VEGICKHNFDPRvcgkHA---TMFGQGSYFARKAVYSHNFSKRSPKGVHC--------------MFLAKVLTGRFTVGNP 676
Cdd:cd01438    99 INAIIHKGFDER----HAyigGMFGAGIYFAENSSKSNQYVYGIGGGTGCpthkdrscyvchrqMLFCRVTLGKSFLQFS 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2029080357 677 SMR--RPPPINPR---DPSSdlydscvdNWVDPQIYVIFNDDQSYPYFIIHYE 724
Cdd:cd01438   175 AMKmaHAPPGHHSvigRPSV--------NGLAYAEYVIYRGEQAYPEYLITYQ 219
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 390-456 5.15e-07

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 47.72  E-value: 5.15e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2029080357  390 VWKYYCRdNFGWREYSEPVVKLIEEASSRGLKEVRFITLQNQYILNIREGFQQNAIFGFRRQIKKRP 456
Cdd:smart00678   2 VWEYEGR-NGKWWPYDPRVSEDIEEAYAAGKKLCELSICGFPYTIDFNAMTQYNQATGTTRKVRRVT 67
 
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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