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Conserved domains on  [gi|568962932|ref|XP_006511781|]
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protein mono-ADP-ribosyltransferase PARP3 isoform X1 [Mus musculus]

Protein Classification

poly(ADP-ribose) polymerase family protein( domain architecture ID 10236928)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 181-532 1.50e-123

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: 365.82  E-value: 1.50e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 181 PCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVI 260
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 261 PHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAApgeeeeKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQ 340
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD------DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 341 TYLKQTGNSY--RCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHS----GGRVGKGIY 414
Cdd:cd01437  155 KYLKNTHAPTteYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIY 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 415 FASENSKSAGYVTTMHCGGhqVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIElelDGQPVVV 494
Cdd:cd01437  235 FADMFSKSANYCHASASDP--TGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVV 309

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568962932 495 PQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIH 532
Cdd:cd01437  310 PLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
WGR super family cl01581
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 56-154 8.28e-35

WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs) as well as the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, a small family of bacterial DNA ligases, and various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain occurs in single-domain proteins and in a variety of domain architectures, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain.


The actual alignment was detected with superfamily member cd08002:

Pssm-ID: 445480  Cd Length: 100  Bit Score: 126.37  E-value: 8.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  56 PGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFT-CLEDAKKDFKKKFWEKTKNKW 134
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKGPWdSLEGAIKDFEKKFKDKTKNNW 80

                         90       100
                 ....*....|....*....|
gi 568962932 135 EERDRFVAQPNKYTLIEVQG 154
Cdd:cd08002   81 EDRENFVPHPGKYTLIEMDY 100
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 181-532 1.50e-123

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: 365.82  E-value: 1.50e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 181 PCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVI 260
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 261 PHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAApgeeeeKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQ 340
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD------DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 341 TYLKQTGNSY--RCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHS----GGRVGKGIY 414
Cdd:cd01437  155 KYLKNTHAPTteYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIY 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 415 FASENSKSAGYVTTMHCGGhqVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIElelDGQPVVV 494
Cdd:cd01437  235 FADMFSKSANYCHASASDP--TGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVV 309

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568962932 495 PQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIH 532
Cdd:cd01437  310 PLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 64-531 8.05e-83

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 270.17  E-value: 8.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  64 YDCTLNQTNIGNNNNKFYIIQLLE--EGSRFFCWNRWGRVGEVGQSKMNH-FTCLEDAKKDFKKKFWEKTKNKWEERDRF 140
Cdd:PLN03124 177 YDAMLNQTNVGDNNNKFYVLQVLEsdDGSKYMVYTRWGRVGVKGQDKLHGpYDSREPAIREFEKKFYDKTKNHWSDRKNF 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 141 VAQPNKYTLIEVQGEAESQEavvkalSPQVYSGPVRTVVKPCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKL 220
Cdd:PLN03124 257 ISHPKKYTWLEMDYEDEEES------KKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKL 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 221 TKQQIARGFEALEALEEAMKNptGDGQSLEELSSCFYTVIPHNFG--RSRPPPINSPDVLQAKKDMLLVLADIELA-QTL 297
Cdd:PLN03124 331 SKSTILKGYEVLKRIAEVISR--SDRETLEELSGEFYTVIPHDFGfkKMRQFTIDTPQKLKHKLEMVEALGEIEIAtKLL 408

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 298 QAAPGEEEEkveevphPLDRDYQLLRCQLQLLDSGESEYKAIQTYLK----QTGNSYRCpDLRHVWKVNREGEGDRFQAH 373
Cdd:PLN03124 409 KDDIGEQDD-------PLYAHYKRLNCELEPLDTDSEEFSMIAKYLEnthgQTHSGYTL-EIVQIFKVSREGEDERFQKF 480

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 374 SKLGNRRLLWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYVTTmHCgGHQVGYMFLGEVALGKE 449
Cdd:PLN03124 481 SSTKNRMLLWHGSRLTNWTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANYCYA-SA-ANPDGVLLLCEVALGDM 558

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 450 HHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIELElDGQPVVVPQGPPVQCPsfkSSSFSQSEYLIYKESQCRLRYLL 529
Cdd:PLN03124 559 NELLQADYNANKLPPGKLSTKGVGRTVPDPSEAKTLE-DGVVVPLGKPVESPYS---KGSLEYNEYIVYNVDQIRMRYVL 634


                 ..
gi 568962932 530 EI 531
Cdd:PLN03124 635 QV 636
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 182-319 1.95e-56

Poly(ADP-ribose) polymerase, regulatory 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: 460732 [Multi-domain]  Cd Length: 135  Bit Score: 185.04  E-value: 1.95e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  182 CSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGD--GQSLEELSSCFYTV 259
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAkaKAKLEDLSNRFYTL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  260 IPHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAApgeeeEKVEEVPHPLDRDY 319
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKD-----SKSDDDEHPLDRHY 135
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 56-154 8.28e-35

WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage.


Pssm-ID: 153429  Cd Length: 100  Bit Score: 126.37  E-value: 8.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  56 PGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFT-CLEDAKKDFKKKFWEKTKNKW 134
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKGPWdSLEGAIKDFEKKFKDKTKNNW 80

                         90       100
                 ....*....|....*....|
gi 568962932 135 EERDRFVAQPNKYTLIEVQG 154
Cdd:cd08002   81 EDRENFVPHPGKYTLIEMDY 100
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 60-141 1.59e-15

Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.


Pssm-ID: 214814  Cd Length: 84  Bit Score: 71.55  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932    60 VHEDYDCTLNQTNIGNNNNKFYIIQLLEE-GSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERD 138
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDdFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 568962932   139 RFV 141
Cdd:smart00773  82 KFV 84
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 64-141 1.41e-10

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


Pssm-ID: 398851  Cd Length: 79  Bit Score: 57.25  E-value: 1.41e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568962932   64 YDCTLNQTNIGNNNNKFYIIQLLE-EGSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFV 141
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDdLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 181-532 1.50e-123

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: 365.82  E-value: 1.50e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 181 PCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVI 260
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 261 PHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAApgeeeeKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQ 340
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD------DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 341 TYLKQTGNSY--RCPDLRHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHS----GGRVGKGIY 414
Cdd:cd01437  155 KYLKNTHAPTteYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIY 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 415 FASENSKSAGYVTTMHCGGhqVGYMFLGEVALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIElelDGQPVVV 494
Cdd:cd01437  235 FADMFSKSANYCHASASDP--TGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVV 309

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 568962932 495 PQGPPVQCPSFKSSSFSQSEYLIYKESQCRLRYLLEIH 532
Cdd:cd01437  310 PLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 64-531 8.05e-83

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 270.17  E-value: 8.05e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  64 YDCTLNQTNIGNNNNKFYIIQLLE--EGSRFFCWNRWGRVGEVGQSKMNH-FTCLEDAKKDFKKKFWEKTKNKWEERDRF 140
Cdd:PLN03124 177 YDAMLNQTNVGDNNNKFYVLQVLEsdDGSKYMVYTRWGRVGVKGQDKLHGpYDSREPAIREFEKKFYDKTKNHWSDRKNF 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 141 VAQPNKYTLIEVQGEAESQEavvkalSPQVYSGPVRTVVKPCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKL 220
Cdd:PLN03124 257 ISHPKKYTWLEMDYEDEEES------KKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKL 330

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 221 TKQQIARGFEALEALEEAMKNptGDGQSLEELSSCFYTVIPHNFG--RSRPPPINSPDVLQAKKDMLLVLADIELA-QTL 297
Cdd:PLN03124 331 SKSTILKGYEVLKRIAEVISR--SDRETLEELSGEFYTVIPHDFGfkKMRQFTIDTPQKLKHKLEMVEALGEIEIAtKLL 408

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 298 QAAPGEEEEkveevphPLDRDYQLLRCQLQLLDSGESEYKAIQTYLK----QTGNSYRCpDLRHVWKVNREGEGDRFQAH 373
Cdd:PLN03124 409 KDDIGEQDD-------PLYAHYKRLNCELEPLDTDSEEFSMIAKYLEnthgQTHSGYTL-EIVQIFKVSREGEDERFQKF 480

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 374 SKLGNRRLLWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYVTTmHCgGHQVGYMFLGEVALGKE 449
Cdd:PLN03124 481 SSTKNRMLLWHGSRLTNWTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANYCYA-SA-ANPDGVLLLCEVALGDM 558

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 450 HHITIDDPSLKSPPSGFDSVIARGQTEPDPAQDIELElDGQPVVVPQGPPVQCPsfkSSSFSQSEYLIYKESQCRLRYLL 529
Cdd:PLN03124 559 NELLQADYNANKLPPGKLSTKGVGRTVPDPSEAKTLE-DGVVVPLGKPVESPYS---KGSLEYNEYIVYNVDQIRMRYVL 634


                 ..
gi 568962932 530 EI 531
Cdd:PLN03124 635 QV 636
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 182-319 1.95e-56

Poly(ADP-ribose) polymerase, regulatory 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: 460732 [Multi-domain]  Cd Length: 135  Bit Score: 185.04  E-value: 1.95e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  182 CSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGD--GQSLEELSSCFYTV 259
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAkaKAKLEDLSNRFYTL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  260 IPHNFGRSRPPPINSPDVLQAKKDMLLVLADIELAQTLQAApgeeeEKVEEVPHPLDRDY 319
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKD-----SKSDDDEHPLDRHY 135
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 64-531 8.06e-49

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 181.53  E-value: 8.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  64 YDCTLNQTNIGNNNNKFYIIQLLEE--GSRFFCWNRWGRVG--EVGQSKMNHFTCLEDAKKDFKKKFWEkTKNKWE---E 136
Cdd:PLN03123 520 YNTTLNMSDLSTGVNSYYILQIIEEdkGSDCYVFRKWGRVGneKIGGNKLEEMSKSDAIHEFKRLFLEK-TGNPWEsweQ 598

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 137 RDRFVAQPNKYTLIEVQ---GEAESQEAVVKALSpqvysgpvrtvvkpcSLDPATQNLITNIFSKEMFKNAMTLMNLDVK 213
Cdd:PLN03123 599 KTNFQKQPGKFYPLDIDygvNEQPKKKAASGSKS---------------NLAPRLVELMKMLFDVETYRAAMMEFEINMS 663

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 214 KMPLGKLTKQQIARGFEAL----EALEEAMKNPTGDGQSLEELSSCFYTVIPhnfgRSRPPPINSPDVLQAKKDMLLVLA 289
Cdd:PLN03123 664 EMPLGKLSKANIQKGFEALteiqNLLKENDQDPSIRESLLVDASNRFFTLIP----SIHPHIIRDEDDLKSKVKMLEALQ 739

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 290 DIELAQTLqaapgeeEEKVEEVPHPLDRDYQLLRCQLQLLDSGESEYKAIQTYLKQTgnsyRCP-------DLRHVWKVN 362
Cdd:PLN03123 740 DIEIASRL-------VGFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTT----HAPthtdwslELEEVFSLE 808

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 363 REGEGDRFQAH-SKLGNRRLLWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYVTTmhCGGHQVG 437
Cdd:PLN03123 809 REGEFDKYAPYkEKLKNRMLLWHGSRLTNFVGILSQGLRIappeAPATGYMFGKGVYFADLVSKSAQYCYT--DRKNPVG 886

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 438 YMFLGEVALGKEHHITiDDPSLKSPPSGFDSVIARGQTEPDPAQDIELELDgqpvvvpqgPPVQC--PSFKSSSFSQ--- 512
Cdd:PLN03123 887 LMLLSEVALGEIYELK-KAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDD---------VVVPCgkPVPSKVKASElmy 956

                        490
                 ....*....|....*....
gi 568962932 513 SEYLIYKESQCRLRYLLEI 531
Cdd:PLN03123 957 NEYIVYNTAQVKLQFLLKV 975
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 335-530 2.65e-47

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: 163.27  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  335 EYKAIQTYLKQTGNSYRCPDLR--HVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRI----MPHSGGR 408
Cdd:pfam00644   3 EYQIIEKYFLSTHDPTHGYPLFilEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIappeAPVTGYM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  409 VGKGIYFASENSKSAGYVTTmhCGGHQVGYMFLGEVALGKEHHITIDDPsLKSPPSGFDSVIARGQTEPDPAQDIElELD 488
Cdd:pfam00644  83 FGKGIYFADDASKSANYCPP--SEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPESFVDLD-GVP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568962932  489 GQPVVVPQGPPVQCPsfksssfsQSEYLIYKESQCRLRYLLE 530
Cdd:pfam00644 159 LGKLVATGYDSSVLL--------YNEYVVYNVNQVRPKYLLE 192
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 56-154 8.28e-35

WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage.


Pssm-ID: 153429  Cd Length: 100  Bit Score: 126.37  E-value: 8.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  56 PGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGSRFFCWNRWGRVGEVGQSKMNHFT-CLEDAKKDFKKKFWEKTKNKW 134
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKGPWdSLEGAIKDFEKKFKDKTKNNW 80

                         90       100
                 ....*....|....*....|
gi 568962932 135 EERDRFVAQPNKYTLIEVQG 154
Cdd:cd08002   81 EDRENFVPHPGKYTLIEMDY 100
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 64-154 6.91e-20

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.


Pssm-ID: 153426  Cd Length: 102  Bit Score: 84.66  E-value: 6.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  64 YDCTLNQTNIGNNNNKFYIIQLLEEGS--RFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFV 141
Cdd:cd07997   10 YDATLNQTDISNNNNKFYKIQILESKGpnTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEWENRPLFK 89

                         90
                 ....*....|...
gi 568962932 142 AQPNKYTLIEVQG 154
Cdd:cd07997   90 KQPGKYALVELDY 102
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 64-152 8.42e-20

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-2 and similar proteins. Similar to PARP-1, PARP-2 is ubiquitously expressed and its activity is induced by DNA strand breaks. It also plays a role in cell differentiation, cell death, and maintaining genomic stability. Studies on mice deficient with PARP-2 shows that it is important in fat storage, T cell maturation, and spermatogenesis.


Pssm-ID: 153430  Cd Length: 103  Bit Score: 84.30  E-value: 8.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  64 YDCTLNQTNIGNNNNKFYIIQLLEE--GSRFFCWNRWGRVGEVGQSKMNHFTC-LEDAKKDFKKKFWEKTKNKWEERDRF 140
Cdd:cd08003   10 YDAMLNQTNIQQNNNKYYIIQLLEDdaEKIYSVWFRWGRVGKKGQSSLVPCGSdLEQAKSLFEKKFLDKTKNEWEDRANF 89

                         90
                 ....*....|..
gi 568962932 141 VAQPNKYTLIEV 152
Cdd:cd08003   90 EKVAGKYDLLEM 101
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 60-141 1.59e-15

Proposed nucleic acid binding domain; This domain is named after its most conserved central motif. It is found in a variety of polyA polymerases as well as in molybdate metabolism regulators (e.g. in E.coli) and other proteins of unknown function. The domain is found in isolation in some proteins and is between 70 and 80 residues in length. It is proposed that it may be a nucleic acid binding domain.


Pssm-ID: 214814  Cd Length: 84  Bit Score: 71.55  E-value: 1.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932    60 VHEDYDCTLNQTNIGNNNNKFYIIQLLEE-GSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERD 138
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDdFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 568962932   139 RFV 141
Cdd:smart00773  82 KFV 84
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 177-531 2.60e-13

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 72.91  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 177 TVVKPCSLDPATQNLITNIFSKEMFKNAMTLMNLDVKKMPLGKLTKQQIARGFEALEALEEAMKNPTGDGQSLE----EL 252
Cdd:PLN03122 448 VAAAHCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKAEamwlDF 527

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 253 SSCFYTVIPhnfgRSRPPPINSPDVL-QAKKDMLLVLADIELAQTLQAapgeeEEKVEEVPHPLDRDYQLLRCQLQLLDS 331
Cdd:PLN03122 528 SNKWFSLVH----STRPFVIRDIDELaDHAASALETVRDINVASRLIG-----DMTGSTLDDPLSDRYKKLGCSISPVDK 598

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 332 GESEYKAIQTYLKQTGNSYRCPDLRHVWKVNR-----EGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRI----M 402
Cdd:PLN03122 599 ESDDYKMIVKYLEKTYEPVKVGDVSYSVSVENifaveSSAGPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPavcsL 678

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 403 PHSGGRVGKGIYFASENSKSAGYVTTmhCGGHQVGYMFLGEVALGKEhhITiddpSLKSPPSGFDS-------VIARGQT 475
Cdd:PLN03122 679 PVPGYMFGKAIVCSDAAAEAARYGFT--AVDRPEGFLVLAVASLGDE--VL----ELTKPPEDVKSyeekkvgVKGLGRK 750

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568962932 476 EPDPAQDIELELDGQPV--VVPQGPPVQCPsfksssFSQSEYLIYKESQCRLRYLLEI 531
Cdd:PLN03122 751 KTDESEHFKWRDDITVPcgRLIPSEHKDSP------LEYNEYAVYDPKQVSIRFLVGV 802
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 64-141 1.41e-10

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


Pssm-ID: 398851  Cd Length: 79  Bit Score: 57.25  E-value: 1.41e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568962932   64 YDCTLNQTNIGNNNNKFYIIQLLE-EGSRFFCWNRWGRVGEVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEERDRFV 141
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDdLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 381-471 3.18e-08

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: 51.94  E-value: 3.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 381 LLWHGTNVAVVAAILTSGLRIMPH-SGGRV-GKGIYFASENSKSAGYV--TTMHCGGHqvgYMFLGEVALGK--EHHITI 454
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCgKHGTMyGKGSYFAKNASYSHQYSkkSPKADGLK---EMFLARVLTGDytQGHPGY 77

                         90       100
                 ....*....|....*....|
gi 568962932 455 DDPSLK---SPPSGFDSVIA 471
Cdd:cd01439   78 RRPPLKpsgVELDRYDSCVD 97
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 382-487 4.25e-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: 52.18  E-value: 4.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932 382 LWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYVTTMHCGGHQV--------------GYMFLGE 443
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRPasygVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVFQngkpkvcgrelcvfGFLTLGV 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 568962932 444 VALGKEHHITIDDPSLKSPPSGFDSVIARGQTEPD----PAQDIELEL 487
Cdd:cd01341   82 MSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRDalllPREYIIFEP 129
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 61-153 8.91e-08

WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of vertebrate PARP-1 and similar proteins, including Arabidopsis thaliana PARP-1 and PARP-3. PARP-1 is the best-studied among the PARPs. It is a widely expressed nuclear chromatin-associated enzyme that possesses auto-mono-ADP-ribosylation (initiation), elongation, and branching activities. PARP-1 is implicated in DNA damage and cell death pathways and is important in maintaining genomic stability and regulating cell proliferation, differentiation, neuronal function, inflammation, and aging.


Pssm-ID: 153428 [Multi-domain]  Cd Length: 104  Bit Score: 50.29  E-value: 8.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568962932  61 HEDYDCTLNQTNIGNNNNKFYIIQLLE--EGSRFFCWNRWGRVG-EVGQSKMNHFTCLEDAKKDFKKKFWEKTKNKWEER 137
Cdd:cd08001    8 GNLYSAVLGLVDIQTGTNSYYKLQLLEhdKGNRYWVFRSWGRVGtTIGGNKLEEFSSLEEAKMAFEELYEEKTGNDFENR 87

                         90
                 ....*....|....*.
gi 568962932 138 DRFVAQPNKYTLIEVQ 153
Cdd:cd08001   88 KNFKKKPGKFYPLDID 103
 
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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