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Conserved domains on  [gi|1958795548|ref|XP_038937138|]
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protein mono-ADP-ribosyltransferase PARP3 isoform X2 [Rattus norvegicus]

Protein Classification

WGR and parp_like domain-containing protein( domain architecture ID 10236928)

WGR and parp_like domain-containing protein

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 ...
 175-525 9.71e-137

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: 399.34  E-value: 9.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 175 PCSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVI 254
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 255 PHNFGRSRPPPINSPDILQAKKDMLLVLADIELAQTLQAApgeeeKVEEVPHPLDRDYQLLKCQLQLLDPGESEYKAIQT 334
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD-----DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 335 YLEQTG---NGYrRPDLQHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHS----GGRVGKGIY 407
Cdd:cd01437   156 YLKNTHaptTEY-TVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 408 FASENSKSASYVTAMRcgSHQVGYMFLGEVALGKVHHITMDDPSLKSPPPGFDSVIARGQTEPDPAQDIElqlDGQPVVV 487
Cdd:cd01437   235 FADMFSKSANYCHASA--SDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVV 309

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958795548 488 PQGRPVACPSFKSSSFSQSEYLIYKESQCRLRYLLEIH 525
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 1.43e-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: 128.29  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  56 PGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGGRFSCWNRWGRVGEVGQSKMNHF-GCLEDAKKDFKKKFWEKTKNKW 134
Cdd:cd08002     1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKGPwDSLEGAIKDFEKKFKDKTKNNW 80

                          90       100
                  ....*....|....*....|
gi 1958795548 135 EERDHFVAHPNKYTLIEVQG 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 ...
 175-525 9.71e-137

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: 399.34  E-value: 9.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 175 PCSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVI 254
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 255 PHNFGRSRPPPINSPDILQAKKDMLLVLADIELAQTLQAApgeeeKVEEVPHPLDRDYQLLKCQLQLLDPGESEYKAIQT 334
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD-----DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 335 YLEQTG---NGYrRPDLQHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHS----GGRVGKGIY 407
Cdd:cd01437   156 YLKNTHaptTEY-TVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 408 FASENSKSASYVTAMRcgSHQVGYMFLGEVALGKVHHITMDDPSLKSPPPGFDSVIARGQTEPDPAQDIElqlDGQPVVV 487
Cdd:cd01437   235 FADMFSKSANYCHASA--SDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVV 309

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958795548 488 PQGRPVACPSFKSSSFSQSEYLIYKESQCRLRYLLEIH 525
Cdd:cd01437   310 PLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 64-524 4.27e-95

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 302.14  E-value: 4.27e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  64 YDCTLNQTNIGNNNNKFYIIQLLE--EGGRFSCWNRWGRVGEVGQSKMNH-FGCLEDAKKDFKKKFWEKTKNKWEERDHF 140
Cdd:PLN03124  177 YDAMLNQTNVGDNNNKFYVLQVLEsdDGSKYMVYTRWGRVGVKGQDKLHGpYDSREPAIREFEKKFYDKTKNHWSDRKNF 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 141 VAHPNKYTLIEVQGEAETQEAVVKVDGPVRTVFKPCSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIA 220
Cdd:PLN03124  257 ISHPKKYTWLEMDYEDEEESKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTIL 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 221 RGFEALEALEEAMKNptGDGQSLEELSSCFYTVIPHNFG--RSRPPPINSPDILQAKKDMLLVLADIELA-QTLQAAPGE 297
Cdd:PLN03124  337 KGYEVLKRIAEVISR--SDRETLEELSGEFYTVIPHDFGfkKMRQFTIDTPQKLKHKLEMVEALGEIEIAtKLLKDDIGE 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 298 EEKveevphPLDRDYQLLKCQLQLLDPGESEYKAIQTYLE----QTGNGYRRpDLQHVWKVNREGEGDRFQAHSKLGNRR 373
Cdd:PLN03124  415 QDD------PLYAHYKRLNCELEPLDTDSEEFSMIAKYLEnthgQTHSGYTL-EIVQIFKVSREGEDERFQKFSSTKNRM 487

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 374 LLWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSASYVTAMrcGSHQVGYMFLGEVALGKVHHITMDD 449
Cdd:PLN03124  488 LLWHGSRLTNWTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANYCYAS--AANPDGVLLLCEVALGDMNELLQAD 565

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958795548 450 PSLKSPPPGFDSVIARGQTEPDPAQDIELQlDGqpVVVPQGRPVACPsFKSSSFSQSEYLIYKESQCRLRYLLEI 524
Cdd:PLN03124  566 YNANKLPPGKLSTKGVGRTVPDPSEAKTLE-DG--VVVPLGKPVESP-YSKGSLEYNEYIVYNVDQIRMRYVLQV 636
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 176-312 4.22e-59

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: 191.97  E-value: 4.22e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 176 CSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALEEAMKNPTGD--GQSLEELSSCFYTV 253
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAkaKAKLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795548 254 IPHNFGRSRPPPINSPDILQAKKDMLLVLADIELAQTLQaapgEEEKVEEVPHPLDRDY 312
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLL----KDSKSDDDEHPLDRHY 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 1.43e-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: 128.29  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  56 PGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGGRFSCWNRWGRVGEVGQSKMNHF-GCLEDAKKDFKKKFWEKTKNKW 134
Cdd:cd08002     1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKGPwDSLEGAIKDFEKKFKDKTKNNW 80

                          90       100
                  ....*....|....*....|
gi 1958795548 135 EERDHFVAHPNKYTLIEVQG 154
Cdd:cd08002    81 EDRENFVPHPGKYTLIEMDY 100
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 60-141 2.42e-16

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: 73.86  E-value: 2.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548   60 VHEDYDCTLNQTNIGNNNNKFYIIQLLEE-GGRFSCWNRWGRVGEVGQSKMNHFGCLEDAKKDFKKKFWEKTKNKWEERD 138
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDdFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 1958795548  139 HFV 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 1.74e-11

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: 59.95  E-value: 1.74e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795548  64 YDCTLNQTNIGNNNNKFYIIQLLE-EGGRFSCWNRWGRVGEVGQSKMNHFGCLEDAKKDFKKKFWEKTKNKWEERDHFV 141
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDdLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
79-113 8.92e-03

WGR domain, predicted DNA-binding domain in MolR [Transcription];


Pssm-ID: 443043  Cd Length: 83  Bit Score: 35.35  E-value: 8.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958795548  79 KFYIIQLleEGGRFSCWN---RWGRVGEVGQSKMNHFG 113
Cdd:COG3831    16 RFYELEV--EPDLFGGWSltrRWGRIGTKGQTKTKTFA 51
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 175-525 9.71e-137

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: 399.34  E-value: 9.71e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 175 PCSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALEEAMKNPTGDGQSLEELSSCFYTVI 254
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 255 PHNFGRSRPPPINSPDILQAKKDMLLVLADIELAQTLQAApgeeeKVEEVPHPLDRDYQLLKCQLQLLDPGESEYKAIQT 334
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD-----DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 335 YLEQTG---NGYrRPDLQHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRIMPHS----GGRVGKGIY 407
Cdd:cd01437   156 YLKNTHaptTEY-TVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIY 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 408 FASENSKSASYVTAMRcgSHQVGYMFLGEVALGKVHHITMDDPSLKSPPPGFDSVIARGQTEPDPAQDIElqlDGQPVVV 487
Cdd:cd01437   235 FADMFSKSANYCHASA--SDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVV 309

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1958795548 488 PQGRPVACPSFKSSSFSQSEYLIYKESQCRLRYLLEIH 525
Cdd:cd01437   310 PLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 64-524 4.27e-95

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 302.14  E-value: 4.27e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  64 YDCTLNQTNIGNNNNKFYIIQLLE--EGGRFSCWNRWGRVGEVGQSKMNH-FGCLEDAKKDFKKKFWEKTKNKWEERDHF 140
Cdd:PLN03124  177 YDAMLNQTNVGDNNNKFYVLQVLEsdDGSKYMVYTRWGRVGVKGQDKLHGpYDSREPAIREFEKKFYDKTKNHWSDRKNF 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 141 VAHPNKYTLIEVQGEAETQEAVVKVDGPVRTVFKPCSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIA 220
Cdd:PLN03124  257 ISHPKKYTWLEMDYEDEEESKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTIL 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 221 RGFEALEALEEAMKNptGDGQSLEELSSCFYTVIPHNFG--RSRPPPINSPDILQAKKDMLLVLADIELA-QTLQAAPGE 297
Cdd:PLN03124  337 KGYEVLKRIAEVISR--SDRETLEELSGEFYTVIPHDFGfkKMRQFTIDTPQKLKHKLEMVEALGEIEIAtKLLKDDIGE 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 298 EEKveevphPLDRDYQLLKCQLQLLDPGESEYKAIQTYLE----QTGNGYRRpDLQHVWKVNREGEGDRFQAHSKLGNRR 373
Cdd:PLN03124  415 QDD------PLYAHYKRLNCELEPLDTDSEEFSMIAKYLEnthgQTHSGYTL-EIVQIFKVSREGEDERFQKFSSTKNRM 487

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 374 LLWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSASYVTAMrcGSHQVGYMFLGEVALGKVHHITMDD 449
Cdd:PLN03124  488 LLWHGSRLTNWTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANYCYAS--AANPDGVLLLCEVALGDMNELLQAD 565

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958795548 450 PSLKSPPPGFDSVIARGQTEPDPAQDIELQlDGqpVVVPQGRPVACPsFKSSSFSQSEYLIYKESQCRLRYLLEI 524
Cdd:PLN03124  566 YNANKLPPGKLSTKGVGRTVPDPSEAKTLE-DG--VVVPLGKPVESP-YSKGSLEYNEYIVYNVDQIRMRYVLQV 636
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 176-312 4.22e-59

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: 191.97  E-value: 4.22e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 176 CSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALEEAMKNPTGD--GQSLEELSSCFYTV 253
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAkaKAKLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795548 254 IPHNFGRSRPPPINSPDILQAKKDMLLVLADIELAQTLQaapgEEEKVEEVPHPLDRDY 312
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLL----KDSKSDDDEHPLDRHY 135
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 64-524 2.73e-56

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 203.10  E-value: 2.73e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  64 YDCTLNQTNIGNNNNKFYIIQLLEEGGRFSCW--NRWGRVG--EVGQSKMNHFGCLEDAKKDFKKKFWEkTKNKWE---E 136
Cdd:PLN03123  520 YNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYvfRKWGRVGneKIGGNKLEEMSKSDAIHEFKRLFLEK-TGNPWEsweQ 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 137 RDHFVAHPNKYTLIEVQ---GEAETQEAVVKVDGpvrtvfkpcSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGK 213
Cdd:PLN03123  599 KTNFQKQPGKFYPLDIDygvNEQPKKKAASGSKS---------NLAPRLVELMKMLFDVETYRAAMMEFEINMSEMPLGK 669

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 214 LSKQQIARGFEAL----EALEEAMKNPTGDGQSLEELSSCFYTVIPhnfgRSRPPPINSPDILQAKKDMLLVLADIELAQ 289
Cdd:PLN03123  670 LSKANIQKGFEALteiqNLLKENDQDPSIRESLLVDASNRFFTLIP----SIHPHIIRDEDDLKSKVKMLEALQDIEIAS 745

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 290 TLQAAPGEEEKveevphPLDRDYQLLKCQLQLLDPGESEYKAIQTYLEQTgngyRRP-------DLQHVWKVNREGEGDR 362
Cdd:PLN03123  746 RLVGFDVDEDD------SLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTT----HAPthtdwslELEEVFSLEREGEFDK 815

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 363 FQAH-SKLGNRRLLWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSASYVTAMRcgSHQVGYMFLGEV 437
Cdd:PLN03123  816 YAPYkEKLKNRMLLWHGSRLTNFVGILSQGLRIappeAPATGYMFGKGVYFADLVSKSAQYCYTDR--KNPVGLMLLSEV 893

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 438 ALGKVHHIT----MDdpslkSPPPGFDSVIARGQTEPDPAQDIELQLDgqpVVVPQGRPVAcPSFKSSSFSQSEYLIYKE 513
Cdd:PLN03123  894 ALGEIYELKkakyMD-----KPPRGKHSTKGLGKTVPQESEFVKWRDD---VVVPCGKPVP-SKVKASELMYNEYIVYNT 964

                         490
                  ....*....|.
gi 1958795548 514 SQCRLRYLLEI 524
Cdd:PLN03123  965 AQVKLQFLLKV 975
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 328-523 6.59e-52

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: 175.21  E-value: 6.59e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 328 EYKAIQTYLEQTG---NGYRrPDLQHVWKVNREGEGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRI----MPHSGG 400
Cdd:pfam00644   3 EYQIIEKYFLSTHdptHGYP-LFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIappeAPVTGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 401 RVGKGIYFASENSKSASYVTAmrCGSHQVGYMFLGEVALGKVHHITMDDPsLKSPPPGFDSVIARGQTEPDPAQDielqL 480
Cdd:pfam00644  82 MFGKGIYFADDASKSANYCPP--SEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPESFVD----L 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958795548 481 DGqpvvVPQGRPVAcPSFKSSSFSQSEYLIYKESQCRLRYLLE 523
Cdd:pfam00644 155 DG----VPLGKLVA-TGYDSSVLLYNEYVVYNVNQVRPKYLLE 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 1.43e-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: 128.29  E-value: 1.43e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  56 PGIQVHEDYDCTLNQTNIGNNNNKFYIIQLLEEGGRFSCWNRWGRVGEVGQSKMNHF-GCLEDAKKDFKKKFWEKTKNKW 134
Cdd:cd08002     1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKGPwDSLEGAIKDFEKKFKDKTKNNW 80

                          90       100
                  ....*....|....*....|
gi 1958795548 135 EERDHFVAHPNKYTLIEVQG 154
Cdd:cd08002    81 EDRENFVPHPGKYTLIEMDY 100
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 64-152 2.26e-21

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: 88.92  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  64 YDCTLNQTNIGNNNNKFYIIQLLEE--GGRFSCWNRWGRVGEVGQSKMNHFGC-LEDAKKDFKKKFWEKTKNKWEERDHF 140
Cdd:cd08003    10 YDAMLNQTNIQQNNNKYYIIQLLEDdaEKIYSVWFRWGRVGKKGQSSLVPCGSdLEQAKSLFEKKFLDKTKNEWEDRANF 89

                          90
                  ....*....|..
gi 1958795548 141 VAHPNKYTLIEV 152
Cdd:cd08003    90 EKVAGKYDLLEM 101
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 64-154 4.72e-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: 85.05  E-value: 4.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  64 YDCTLNQTNIGNNNNKFYIIQLLEEGG--RFSCWNRWGRVGEVGQSKMNHFGCLEDAKKDFKKKFWEKTKNKWEERDHFV 141
Cdd:cd07997    10 YDATLNQTDISNNNNKFYKIQILESKGpnTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEWENRPLFK 89

                          90
                  ....*....|...
gi 1958795548 142 AHPNKYTLIEVQG 154
Cdd:cd07997    90 KQPGKYALVELDY 102
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 176-524 1.88e-16

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 82.54  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 176 CSLDPATQKLITNIFSKEMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALEEAMKNPTGDGQSLE----ELSSCFY 251
Cdd:PLN03122  453 CKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKAEamwlDFSNKWF 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 252 TVIPhnfgRSRPPPINSPD-ILQAKKDMLLVLADIELAQTLQAapgeEEKVEEVPHPLDRDYQLLKCQLQLLDPGESEYK 330
Cdd:PLN03122  533 SLVH----STRPFVIRDIDeLADHAASALETVRDINVASRLIG----DMTGSTLDDPLSDRYKKLGCSISPVDKESDDYK 604

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 331 AIQTYLEQTGNGYRRPD------LQHVWKVNREGeGDRFQAHSKLGNRRLLWHGTNVAVVAAILTSGLRI----MPHSGG 400
Cdd:PLN03122  605 MIVKYLEKTYEPVKVGDvsysvsVENIFAVESSA-GPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPavcsLPVPGY 683

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 401 RVGKGIYFASENSKSASY-VTAMrcgSHQVGYMFLGEVALGKvhHITmddpSLKSPPPGFDS-------VIARGQTEPDP 472
Cdd:PLN03122  684 MFGKAIVCSDAAAEAARYgFTAV---DRPEGFLVLAVASLGD--EVL----ELTKPPEDVKSyeekkvgVKGLGRKKTDE 754

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958795548 473 AQDIELQLDgqpVVVPQGRPVA-----CPsfksssFSQSEYLIYKESQCRLRYLLEI 524
Cdd:PLN03122  755 SEHFKWRDD---ITVPCGRLIPsehkdSP------LEYNEYAVYDPKQVSIRFLVGV 802
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 60-141 2.42e-16

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: 73.86  E-value: 2.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548   60 VHEDYDCTLNQTNIGNNNNKFYIIQLLEE-GGRFSCWNRWGRVGEVGQSKMNHFGCLEDAKKDFKKKFWEKTKNKWEERD 138
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDdFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 1958795548  139 HFV 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 1.74e-11

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: 59.95  E-value: 1.74e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958795548  64 YDCTLNQTNIGNNNNKFYIIQLLE-EGGRFSCWNRWGRVGEVGQSKMNHFGCLEDAKKDFKKKFWEKTKNKWEERDHFV 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 ...
 374-464 2.78e-09

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: 55.02  E-value: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 374 LLWHGTNVAVVAAILTSGLRIMPH-SGGRV-GKGIYFASENSKSASYV--TAMRCGSHqvgYMFLGEVALGK--VHHITM 447
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCgKHGTMyGKGSYFAKNASYSHQYSkkSPKADGLK---EMFLARVLTGDytQGHPGY 77

                          90       100
                  ....*....|....*....|
gi 1958795548 448 DDPSLK---SPPPGFDSVIA 464
Cdd:cd01439    78 RRPPLKpsgVELDRYDSCVD 97
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 61-153 3.25e-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: 51.44  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548  61 HEDYDCTLNQTNIGNNNNKFYIIQLLEEGGRFSCW--NRWGRVG-EVGQSKMNHFGCLEDAKKDFKKKFWEKTKNKWEER 137
Cdd:cd08001     8 GNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWvfRSWGRVGtTIGGNKLEEFSSLEEAKMAFEELYEEKTGNDFENR 87

                          90
                  ....*....|....*.
gi 1958795548 138 DHFVAHPNKYTLIEVQ 153
Cdd:cd08001    88 KNFKKKPGKFYPLDID 103
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 375-474 1.01e-07

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: 51.02  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 375 LWHGTNVAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSASYVT----AMRCGSHQV----------GYMFLGE 436
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPasygVLLNGGMFGKGIYSAPNISKSNGYSVgcdgQHVFQNGKPkvcgrelcvfGFLTLGV 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958795548 437 VALGKVHHITMDDPSLKSPPPGFDSVIARGQTEPDPAQ 474
Cdd:cd01341    82 MSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRDALL 119
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 324-465 1.58e-04

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: 43.35  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 324 PGESEYKAIQTYLEQT----------GNGYRRPDLQHVWKVNREGEGDRF--------QAHSKLGNRRLLWHGTnvAVVA 385
Cdd:cd01438    23 PDDKEYQSVEEEMQSTirehrdggnaGGIFNRYNIIRIQKVVNKKLRERYchrqkeiaEENHNHHNERMLFHGS--PFIN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958795548 386 AILTSGL-RIMPHSGGRVGKGIYFASENSKSASYVTAM----RCGSHQ-------VGYMFLGEVALGK--VHHITMddpS 451
Cdd:cd01438   101 AIIHKGFdERHAYIGGMFGAGIYFAENSSKSNQYVYGIgggtGCPTHKdrscyvcHRQMLFCRVTLGKsfLQFSAM---K 177

                         170
                  ....*....|....
gi 1958795548 452 LKSPPPGFDSVIAR 465
Cdd:cd01438   178 MAHAPPGHHSVIGR 191
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 79-113 6.78e-03

WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, as well as in various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain appears to occur in single-domain proteins and in a variety of domain architectures, together with ATP-dependent DNA ligase domains, WD40 repeats, leucine-rich repeats, and other domains. It has been proposed to function as a nucleic acid binding domain.


Pssm-ID: 153425  Cd Length: 74  Bit Score: 35.66  E-value: 6.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958795548  79 KFYIIQLleEGGRFSCWN---RWGRVGEVGQSKMNHFG 113
Cdd:cd07996    15 RFYEIEL--EGDLFGEWSlvrRWGRIGTKGQSRTKTFD 50
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
79-113 8.92e-03

WGR domain, predicted DNA-binding domain in MolR [Transcription];


Pssm-ID: 443043  Cd Length: 83  Bit Score: 35.35  E-value: 8.92e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1958795548  79 KFYIIQLleEGGRFSCWN---RWGRVGEVGQSKMNHFG 113
Cdd:COG3831    16 RFYELEV--EPDLFGGWSltrRWGRIGTKGQTKTKTFA 51
 
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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