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Conserved domains on  [gi|2462615753|ref|XP_054214812|]
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protein mono-ADP-ribosyltransferase PARP12 isoform X1 [Homo sapiens]

Protein Classification

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 ...
 596-712 6.20e-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: 200.24  E-value: 6.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 596 QLFHGTSAIFVDAICQQNFDWRVCGVHGTSYGKGSYFARDAAYSHHYSKSDTQ---THTMFLARVLVGEFVRGNASFVRP 672
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadgLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462615753 673 PAK-EGWSNAFYDSCVNSVSDPSIFVIFEKHQVYPEYVIQY 712
Cdd:cd01439    81 PLKpSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 299-372 2.52e-14

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


:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 68.14  E-value: 2.52e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615753  299 YRWQFLDR-GKWEDLD--NMELIEEAYC--NPKIERILCSesastfHSHCLNFNAMTYGATQARRLSTASSVTKPPHFI 372
Cdd:smart00678   1 YVWEYEGRnGKWWPYDprVSEDIEEAYAagKKLCELSICG------FPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE super family cl46925
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 429-501 1.93e-10

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


The actual alignment was detected with superfamily member smart00678:

Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 57.35  E-value: 1.93e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615753  429 QGTVHPVTTVSSSDVEKAYLAyctpgsDGQAATLKFQAgkHNYELDFKAFVQKNLVYGTTKKVcRRPKYVSPQ 501
Cdd:smart00678   9 NGKWWPYDPRVSEDIEEAYAA------GKKLCELSICG--FPYTIDFNAMTQYNQATGTTRKV-RRVTYSPYS 72
ZnF_C3H1 smart00356
zinc finger;
177-200 2.64e-03

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.68  E-value: 2.64e-03
                           10        20
                   ....*....|....*....|....
gi 2462615753  177 KLHICQYFLQGECKFGTSCKRSHD 200
Cdd:smart00356   3 KTELCKFFKRGYCPRGDRCKFAHP 26
 
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 ...
 596-712 6.20e-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: 200.24  E-value: 6.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 596 QLFHGTSAIFVDAICQQNFDWRVCGVHGTSYGKGSYFARDAAYSHHYSKSDTQ---THTMFLARVLVGEFVRGNASFVRP 672
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadgLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462615753 673 PAK-EGWSNAFYDSCVNSVSDPSIFVIFEKHQVYPEYVIQY 712
Cdd:cd01439    81 PLKpSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 542-712 3.52e-38

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: 140.55  E-value: 3.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 542 SEEYQKVWNLFNRTLP-----FYFVQKIERVQNLALWEVYQWQKGQMqkqnggkavDERQLFHGTSAIFVDAICQQNF-- 614
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKLR---------NRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 615 DWRVCGVHGTSYGKGSYFARDAAYSHHYSKSDTQTHT--MFLARVLVGE------------------FVRGNASFVR--- 671
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPSEAHGNglMLLSEVALGDmnelkkadyaeklppgkhSVKGLGKTAPesf 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462615753 672 -----PPAKEGwSNAFYDSCvnsVSDPSIFVIFEKHQVYPEYVIQY 712
Cdd:pfam00644 152 vdldgVPLGKL-VATGYDSS---VLLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 299-372 2.52e-14

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 68.14  E-value: 2.52e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615753  299 YRWQFLDR-GKWEDLD--NMELIEEAYC--NPKIERILCSesastfHSHCLNFNAMTYGATQARRLSTASSVTKPPHFI 372
Cdd:smart00678   1 YVWEYEGRnGKWWPYDprVSEDIEEAYAagKKLCELSICG------FPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 429-501 1.93e-10

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 57.35  E-value: 1.93e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615753  429 QGTVHPVTTVSSSDVEKAYLAyctpgsDGQAATLKFQAgkHNYELDFKAFVQKNLVYGTTKKVcRRPKYVSPQ 501
Cdd:smart00678   9 NGKWWPYDPRVSEDIEEAYAA------GKKLCELSICG--FPYTIDFNAMTQYNQATGTTRKV-RRVTYSPYS 72
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 378-493 4.08e-08

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: 50.37  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 378 IWYWSDEFGSWQEYGRQDcppgaplkcgvgatsvfphhavsclhkvsgfpsqgtvhpvttvsSSDVEKAYLayctpgSDG 457
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEV--------------------------------------------SSLIEEAYQ------KGK 30

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462615753 458 QAATLKFQAGKHNYELDFKAFVQKNLVYGTTKKVCR 493
Cdd:pfam02825  31 PSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
ZnF_C3H1 smart00356
zinc finger;
177-200 2.64e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.68  E-value: 2.64e-03
                           10        20
                   ....*....|....*....|....
gi 2462615753  177 KLHICQYFLQGECKFGTSCKRSHD 200
Cdd:smart00356   3 KTELCKFFKRGYCPRGDRCKFAHP 26
 
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 ...
 596-712 6.20e-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: 200.24  E-value: 6.20e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 596 QLFHGTSAIFVDAICQQNFDWRVCGVHGTSYGKGSYFARDAAYSHHYSKSDTQ---THTMFLARVLVGEFVRGNASFVRP 672
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCGKHGTMYGKGSYFAKNASYSHQYSKKSPKadgLKEMFLARVLTGDYTQGHPGYRRP 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2462615753 673 PAK-EGWSNAFYDSCVNSVSDPSIFVIFEKHQVYPEYVIQY 712
Cdd:cd01439    81 PLKpSGVELDRYDSCVDNVSNPSIFVIFSDVQAYPEYLITY 121
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 542-712 3.52e-38

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: 140.55  E-value: 3.52e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 542 SEEYQKVWNLFNRTLP-----FYFVQKIERVQNLALWEVYQWQKGQMqkqnggkavDERQLFHGTSAIFVDAICQQNF-- 614
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDpthgyPLFILEIFRVQRDGEWERFQPKKKLR---------NRRLLWHGSRLTNFLGILSQGLri 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 615 DWRVCGVHGTSYGKGSYFARDAAYSHHYSKSDTQTHT--MFLARVLVGE------------------FVRGNASFVR--- 671
Cdd:pfam00644  72 APPEAPVTGYMFGKGIYFADDASKSANYCPPSEAHGNglMLLSEVALGDmnelkkadyaeklppgkhSVKGLGKTAPesf 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2462615753 672 -----PPAKEGwSNAFYDSCvnsVSDPSIFVIFEKHQVYPEYVIQY 712
Cdd:pfam00644 152 vdldgVPLGKL-VATGYDSS---VLLYNEYVVYNVNQVRPKYLLEV 193
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 299-372 2.52e-14

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 68.14  E-value: 2.52e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462615753  299 YRWQFLDR-GKWEDLD--NMELIEEAYC--NPKIERILCSesastfHSHCLNFNAMTYGATQARRLSTASSVTKPPHFI 372
Cdd:smart00678   1 YVWEYEGRnGKWWPYDprVSEDIEEAYAagKKLCELSICG------FPYTIDFNAMTQYNQATGTTRKVRRVTYSPYSK 73
WWE smart00678
Domain in Deltex and TRIP12 homologues. Possibly involved in regulation of ubiquitin-mediated ...
 429-501 1.93e-10

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


Pssm-ID: 128922 [Multi-domain]  Cd Length: 73  Bit Score: 57.35  E-value: 1.93e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462615753  429 QGTVHPVTTVSSSDVEKAYLAyctpgsDGQAATLKFQAgkHNYELDFKAFVQKNLVYGTTKKVcRRPKYVSPQ 501
Cdd:smart00678   9 NGKWWPYDPRVSEDIEEAYAA------GKKLCELSICG--FPYTIDFNAMTQYNQATGTTRKV-RRVTYSPYS 72
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 557-712 2.07e-09

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: 58.37  E-value: 2.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 557 PFYFVQKIERVQNLALWEVYQWQKGQMQKQNGgKAVDERQLFHGTSaiFVDAICQQNFDWRVCGVHGTsYGKGSYFARDA 636
Cdd:cd01438    53 NRYNIIRIQKVVNKKLRERYCHRQKEIAEENH-NHHNERMLFHGSP--FINAIIHKGFDERHAYIGGM-FGAGIYFAENS 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 637 AYSHHY-----------SKSDTQTHT----MFLARVLVGE-FVR-----------GNASFVRPPAKEGWSNAFYdscvns 689
Cdd:cd01438   129 SKSNQYvygigggtgcpTHKDRSCYVchrqMLFCRVTLGKsFLQfsamkmahappGHHSVIGRPSVNGLAYAEY------ 202

                         170       180
                  ....*....|....*....|...
gi 2462615753 690 vsdpsifVIFEKHQVYPEYVIQY 712
Cdd:cd01438   203 -------VIYRGEQAYPEYLITY 218
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 597-708 3.51e-08

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: 52.95  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 597 LFHGTSAIFVDAICQQNFDWRVCGV--HGTSYGKGSYFARDAAYSHHYS-KSDTQTHTMFLARVLVGEF----------- 662
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPASYGVllNGGMFGKGIYSAPNISKSNGYSvGCDGQHVFQNGKPKVCGRElcvfgfltlgv 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462615753 663 ---VRGNASFVRPPAKEGWSNAF--YDSCVNSVSD----PSIFVIFEKH-QVYPEY 708
Cdd:cd01341    82 msgATEESSRVLFPRNFRGATGAevVDLLVAMCRDalllPREYIIFEPYsQVSIRY 137
WWE pfam02825
WWE domain; The WWE domain is named after three of its conserved residues and is predicted to ...
 378-493 4.08e-08

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: 50.37  E-value: 4.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462615753 378 IWYWSDEFGSWQEYGRQDcppgaplkcgvgatsvfphhavsclhkvsgfpsqgtvhpvttvsSSDVEKAYLayctpgSDG 457
Cdd:pfam02825   1 VWEWEDDNGGWHPYDPEV--------------------------------------------SSLIEEAYQ------KGK 30

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2462615753 458 QAATLKFQAGKHNYELDFKAFVQKNLVYGTTKKVCR 493
Cdd:pfam02825  31 PSVDLSITTAGFPYTIDFKSMTQTNKDTGTTRPVRR 66
ZnF_C3H1 smart00356
zinc finger;
177-200 2.64e-03

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 35.68  E-value: 2.64e-03
                           10        20
                   ....*....|....*....|....
gi 2462615753  177 KLHICQYFLQGECKFGTSCKRSHD 200
Cdd:smart00356   3 KTELCKFFKRGYCPRGDRCKFAHP 26
 
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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