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Conserved domains on  [gi|729042217|ref|NP_005476|]
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protein mono-ADP-ribosyltransferase PARP3 isoform a [Homo sapiens]

Protein Classification

poly(ADP-ribose) polymerase family protein( domain architecture ID 10168760)

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 ...
 182-532 1.24e-139

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: 407.04  E-value: 1.24e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 182 PCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVI 261
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 262 PHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEqektvEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQT 341
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDE-----DDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 342 YLEQTG--SNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHS----GGRVGKGIYF 415
Cdd:cd01437  156 YLKNTHapTTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIYF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 416 ASENSKSAGYVIGMKcgAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTElelDGQQVVVP 495
Cdd:cd01437  236 ADMFSKSANYCHASA--SDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVVP 310

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 729042217 496 QGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVH 532
Cdd:cd01437  311 LGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 58-157 9.31e-50

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: 166.43  E-value: 9.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  58 PGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQdSNRFFTCWNRWGRVGEVGQSKINHFTR-LEDAKKDFEKKFREKTKNN 136
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLE-SGKEYYVWNRWGRVGEKGQNKLKGPWDsLEGAIKDFEKKFKDKTKNN 79

                         90       100
                 ....*....|....*....|.
gi 729042217 137 WAERDHFVSHPGKYTLIEVQA 157
Cdd:cd08002   80 WEDRENFVPHPGKYTLIEMDY 100
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 182-532 1.24e-139

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: 407.04  E-value: 1.24e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 182 PCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVI 261
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 262 PHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEqektvEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQT 341
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDE-----DDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 342 YLEQTG--SNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHS----GGRVGKGIYF 415
Cdd:cd01437  156 YLKNTHapTTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIYF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 416 ASENSKSAGYVIGMKcgAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTElelDGQQVVVP 495
Cdd:cd01437  236 ADMFSKSANYCHASA--SDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVVP 310

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 729042217 496 QGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVH 532
Cdd:cd01437  311 LGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 81-531 4.50e-103

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 323.33  E-value: 4.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  81 KFYIIQLLQ-DSNRFFTCWNRWGRVGEVGQSKINH-FTRLEDAKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAE 158
Cdd:PLN03124 192 KFYVLQVLEsDDGSKYMVYTRWGRVGVKGQDKLHGpYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDYE 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 159 DEAQeavvKVDRGPVRTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEA-LE 237
Cdd:PLN03124 272 DEEE----SKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRiAE 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 238 EALKGPTdggQSLEELSSHFYTVIPHNFGHS--QPPPINSPELLQAKKDMLLVLADIELAQAL--QAVSEQEKtveevph 313
Cdd:PLN03124 348 VISRSDR---ETLEELSGEFYTVIPHDFGFKkmRQFTIDTPQKLKHKLEMVEALGEIEIATKLlkDDIGEQDD------- 417

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 314 PLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQT-GSNHRCPTL--QHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAV 390
Cdd:PLN03124 418 PLYAHYKRLNCELEPLDTDSEEFSMIAKYLENThGQTHSGYTLeiVQIFKVSREGEDERFQKFSSTKNRMLLWHGSRLTN 497

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 391 VAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYvigmkCGAH---HVGYMFLGEVALGREHHINTDNPSLKSPP 463
Cdd:PLN03124 498 WTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANY-----CYASaanPDGVLLLCEVALGDMNELLQADYNANKLP 572

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729042217 464 PGFDSVIARGHTEPDPTQDTELElDGqqVVVPQGQPVPCPeFSSSTFSQSEYLIYQESQCRLRYLLEV 531
Cdd:PLN03124 573 PGKLSTKGVGRTVPDPSEAKTLE-DG--VVVPLGKPVESP-YSKGSLEYNEYIVYNVDQIRMRYVLQV 636
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 335-531 7.08e-53

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: 177.91  E-value: 7.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  335 EYKVIQTYLEQT-GSNHRCP-TLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRI----MPHSGGR 408
Cdd:pfam00644   3 EYQIIEKYFLSThDPTHGYPlFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIappeAPVTGYM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  409 VGKGIYFASENSKSAGYviGMKCGAHHVGYMFLGEVALGREHHINTDNPsLKSPPPGFDSVIARGHTEPDPTQDteleLD 488
Cdd:pfam00644  83 FGKGIYFADDASKSANY--CPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPESFVD----LD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 729042217  489 GqqvvVPQGQPVPcPEFSSSTFSQSEYLIYQESQCRLRYLLEV 531
Cdd:pfam00644 156 G----VPLGKLVA-TGYDSSVLLYNEYVVYNVNQVRPKYLLEV 193
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 58-157 9.31e-50

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: 166.43  E-value: 9.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  58 PGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQdSNRFFTCWNRWGRVGEVGQSKINHFTR-LEDAKKDFEKKFREKTKNN 136
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLE-SGKEYYVWNRWGRVGEKGQNKLKGPWDsLEGAIKDFEKKFKDKTKNN 79

                         90       100
                 ....*....|....*....|.
gi 729042217 137 WAERDHFVSHPGKYTLIEVQA 157
Cdd:cd08002   80 WEDRENFVPHPGKYTLIEMDY 100
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 62-144 9.75e-28

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: 106.22  E-value: 9.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217    62 VYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERD 141
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDDFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 729042217   142 HFV 144
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 ...
 66-144 1.41e-26

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: 102.70  E-value: 1.41e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729042217   66 YNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERDHFV 144
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDDLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
81-134 1.28e-09

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 54.99  E-value: 1.28e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 729042217  81 KFYIIQLLQDsnrFFTCWN---RWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTK 134
Cdd:COG3831   16 RFYELEVEPD---LFGGWSltrRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKLR 69
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 182-532 1.24e-139

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: 407.04  E-value: 1.24e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 182 PCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLEELSSHFYTVI 261
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 262 PHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEqektvEEVPHPLDRDYQLLKCQLQLLDSGAPEYKVIQT 341
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDE-----DDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEK 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 342 YLEQTG--SNHRCPTLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRIMPHS----GGRVGKGIYF 415
Cdd:cd01437  156 YLKNTHapTTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIYF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 416 ASENSKSAGYVIGMKcgAHHVGYMFLGEVALGREHHINTDNPSLKSPPPGFDSVIARGHTEPDPTQDTElelDGQQVVVP 495
Cdd:cd01437  236 ADMFSKSANYCHASA--SDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPSEFEI---DLDGVVVP 310

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 729042217 496 QGQPVPCPEFSSSTFSQSEYLIYQESQCRLRYLLEVH 532
Cdd:cd01437  311 LGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 81-531 4.50e-103

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 323.33  E-value: 4.50e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  81 KFYIIQLLQ-DSNRFFTCWNRWGRVGEVGQSKINH-FTRLEDAKKDFEKKFREKTKNNWAERDHFVSHPGKYTLIEVQAE 158
Cdd:PLN03124 192 KFYVLQVLEsDDGSKYMVYTRWGRVGVKGQDKLHGpYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDYE 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 159 DEAQeavvKVDRGPVRTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEA-LE 237
Cdd:PLN03124 272 DEEE----SKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRiAE 347

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 238 EALKGPTdggQSLEELSSHFYTVIPHNFGHS--QPPPINSPELLQAKKDMLLVLADIELAQAL--QAVSEQEKtveevph 313
Cdd:PLN03124 348 VISRSDR---ETLEELSGEFYTVIPHDFGFKkmRQFTIDTPQKLKHKLEMVEALGEIEIATKLlkDDIGEQDD------- 417

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 314 PLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQT-GSNHRCPTL--QHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAV 390
Cdd:PLN03124 418 PLYAHYKRLNCELEPLDTDSEEFSMIAKYLENThGQTHSGYTLeiVQIFKVSREGEDERFQKFSSTKNRMLLWHGSRLTN 497

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 391 VAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYvigmkCGAH---HVGYMFLGEVALGREHHINTDNPSLKSPP 463
Cdd:PLN03124 498 WTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANY-----CYASaanPDGVLLLCEVALGDMNELLQADYNANKLP 572

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 729042217 464 PGFDSVIARGHTEPDPTQDTELElDGqqVVVPQGQPVPCPeFSSSTFSQSEYLIYQESQCRLRYLLEV 531
Cdd:PLN03124 573 PGKLSTKGVGRTVPDPSEAKTLE-DG--VVVPLGKPVESP-YSKGSLEYNEYIVYNVDQIRMRYVLQV 636
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 66-531 6.61e-61

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 216.20  E-value: 6.61e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  66 YNCTLNQTNIENNNNKFYIIQLLQDSNRFfTCW--NRWGRVG--EVGQSKINHFTRLeDAKKDFEKKFREKTKNNW---A 138
Cdd:PLN03123 520 YNTTLNMSDLSTGVNSYYILQIIEEDKGS-DCYvfRKWGRVGneKIGGNKLEEMSKS-DAIHEFKRLFLEKTGNPWeswE 597

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 139 ERDHFVSHPGKYTLIEVQaedeaqeavVKVDRGPVRTVTKRVQPcSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPL 218
Cdd:PLN03123 598 QKTNFQKQPGKFYPLDID---------YGVNEQPKKKAASGSKS-NLAPRLVELMKMLFDVETYRAAMMEFEINMSEMPL 667

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 219 GKLSKQQIARGFEALEALEEALK----GPTDGGQSLEELSSHFYTVIPhnfgHSQPPPINSPELLQAKKDMLLVLADIEL 294
Cdd:PLN03123 668 GKLSKANIQKGFEALTEIQNLLKendqDPSIRESLLVDASNRFFTLIP----SIHPHIIRDEDDLKSKVKMLEALQDIEI 743

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 295 AQAL--QAVSEQEktveevphPLDRDYQLLKCQLQLLDSGAPEYKVIQTYLEQTgsnhRCPT-------LQHIWKVNQEG 365
Cdd:PLN03123 744 ASRLvgFDVDEDD--------SLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTT----HAPThtdwsleLEEVFSLEREG 811

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 366 EEDRFQAH-SKLGNRKLLWHGTNMAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYVigMKCGAHHVGYMF 440
Cdd:PLN03123 812 EFDKYAPYkEKLKNRMLLWHGSRLTNFVGILSQGLRIappeAPATGYMFGKGVYFADLVSKSAQYC--YTDRKNPVGLML 889

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 441 LGEVALGREHHInTDNPSLKSPPPGFDSVIARGHTEPDPTQDTELELDgqqVVVPQGQPVPcPEFSSSTFSQSEYLIYQE 520
Cdd:PLN03123 890 LSEVALGEIYEL-KKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDD---VVVPCGKPVP-SKVKASELMYNEYIVYNT 964

                        490
                 ....*....|.
gi 729042217 521 SQCRLRYLLEV 531
Cdd:PLN03123 965 AQVKLQFLLKV 975
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 335-531 7.08e-53

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: 177.91  E-value: 7.08e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  335 EYKVIQTYLEQT-GSNHRCP-TLQHIWKVNQEGEEDRFQAHSKLGNRKLLWHGTNMAVVAAILTSGLRI----MPHSGGR 408
Cdd:pfam00644   3 EYQIIEKYFLSThDPTHGYPlFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIappeAPVTGYM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  409 VGKGIYFASENSKSAGYviGMKCGAHHVGYMFLGEVALGREHHINTDNPsLKSPPPGFDSVIARGHTEPDPTQDteleLD 488
Cdd:pfam00644  83 FGKGIYFADDASKSANY--CPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPESFVD----LD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 729042217  489 GqqvvVPQGQPVPcPEFSSSTFSQSEYLIYQESQCRLRYLLEV 531
Cdd:pfam00644 156 G----VPLGKLVA-TGYDSSVLLYNEYVVYNVNQVRPKYLLEV 193
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 58-157 9.31e-50

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: 166.43  E-value: 9.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  58 PGTQVYEDYNCTLNQTNIENNNNKFYIIQLLQdSNRFFTCWNRWGRVGEVGQSKINHFTR-LEDAKKDFEKKFREKTKNN 136
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLE-SGKEYYVWNRWGRVGEKGQNKLKGPWDsLEGAIKDFEKKFKDKTKNN 79

                         90       100
                 ....*....|....*....|.
gi 729042217 137 WAERDHFVSHPGKYTLIEVQA 157
Cdd:cd08002   80 WEDRENFVPHPGKYTLIEMDY 100
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 183-319 3.98e-49

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: 165.78  E-value: 3.98e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  183 CSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDG--GQSLEELSSHFYTV 260
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAkaKAKLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 729042217  261 IPHNFGHSQPPPINSPELLQAKKDMLLVLADIELAQALQAVSEQEKTVeevpHPLDRDY 319
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKDSKSDDDE----HPLDRHY 135
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 61-156 1.20e-33

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: 123.18  E-value: 1.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  61 QVYED----YNCTLNQTNIENNNNKFYIIQLL-QDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKN 135
Cdd:cd07997    1 HVYGDiatvYDATLNQTDISNNNNKFYKIQILeSKGPNTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGN 80

                         90       100
                 ....*....|....*....|.
gi 729042217 136 NWAERDHFVSHPGKYTLIEVQ 156
Cdd:cd07997   81 EWENRPLFKKQPGKYALVELD 101
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 62-155 2.27e-31

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: 117.04  E-value: 2.27e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  62 VYED----YNCTLNQTNIENNNNKFYIIQLLQDSNR-FFTCWNRWGRVGEVGQSKINHF-TRLEDAKKDFEKKFREKTKN 135
Cdd:cd08003    2 VYEEgddvYDAMLNQTNIQQNNNKYYIIQLLEDDAEkIYSVWFRWGRVGKKGQSSLVPCgSDLEQAKSLFEKKFLDKTKN 81

                         90       100
                 ....*....|....*....|
gi 729042217 136 NWAERDHFVSHPGKYTLIEV 155
Cdd:cd08003   82 EWEDRANFEKVAGKYDLLEM 101
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 62-144 9.75e-28

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: 106.22  E-value: 9.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217    62 VYEDYNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERD 141
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDDFGGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 729042217   142 HFV 144
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 ...
 66-144 1.41e-26

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: 102.70  E-value: 1.41e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729042217   66 YNCTLNQTNIENNNNKFYIIQLLQDSNRFFTCWNRWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTKNNWAERDHFV 144
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDDLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 32-531 1.80e-19

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 92.17  E-value: 1.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  32 TAEALKAIPAE-----KRIIRVDPTCplsSNPGTQVYED----YNCTLNQTNIENNNNKFYIIQLLQ--DSNRFFtcWNR 100
Cdd:PLN03122 296 SEEAIESLSAElklygKRGVYKDSKL---QEEGGKIFEKdgilYNCAFSICDLGRGLNEYCIMQLITvpDSNLHL--YYK 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 101 WGRVGE--VGQSKINHFTRLEDAKKDFEKKFREKTKNN---WAERDHFVSHPGKYTLIEVqaedeaqEAVVKVDRG--PV 173
Cdd:PLN03122 371 KGRVGDdpNAEERLEEWEDVDAAIKEFVRLFEEITGNEfepWEREKKFEKKRLKFYPIDM-------DDGVDVRAGglGL 443

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 174 RTVTKRVQPCSLDPATQKLITNIFSKEMFKNTMALMDLDVKKMPLGKLSKQQIARGFEALEALEEALKGPTDGGQSLE-- 251
Cdd:PLN03122 444 RQLGVAAAHCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKAEam 523

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 252 --ELSSHFYTVIphnfgHSQPPpinspellqakkdmlLVLADI-ELAQALQAVSEQEKTVEEVPH------------PLD 316
Cdd:PLN03122 524 wlDFSNKWFSLV-----HSTRP---------------FVIRDIdELADHAASALETVRDINVASRligdmtgstlddPLS 583

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 317 RDYQLLKCQLQLLDSGAPEYKVIQTYLEQT------GSNHRCPTLQHIWKVNQEGEEDrFQAHSKLGNRKLLWHGTNMAV 390
Cdd:PLN03122 584 DRYKKLGCSISPVDKESDDYKMIVKYLEKTyepvkvGDVSYSVSVENIFAVESSAGPS-LDEIKKLPNKVLLWCGTRSSN 662

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 391 VAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYviGMKCGAHHVGYMFLGEVALGREhhINtdnpSLKSPPPGF 466
Cdd:PLN03122 663 LLRHLAKGFLPavcsLPVPGYMFGKAIVCSDAAAEAARY--GFTAVDRPEGFLVLAVASLGDE--VL----ELTKPPEDV 734

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 729042217 467 DS-------VIARGHTEPDPTQDTELELDgqqVVVPQGQPVPcPEFSSSTFSQSEYLIYQESQCRLRYLLEV 531
Cdd:PLN03122 735 KSyeekkvgVKGLGRKKTDESEHFKWRDD---ITVPCGRLIP-SEHKDSPLEYNEYAVYDPKQVSIRFLVGV 802
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 64-156 5.28e-19

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: 82.26  E-value: 5.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217  64 EDYNCTLNQTNIENNNNKFYIIQLLQ--DSNRfftCW--NRWGRVG-EVGQSKINHFTRLEDAKKDFEKKFREKTKNNWA 138
Cdd:cd08001    9 NLYSAVLGLVDIQTGTNSYYKLQLLEhdKGNR---YWvfRSWGRVGtTIGGNKLEEFSSLEEAKMAFEELYEEKTGNDFE 85

                         90
                 ....*....|....*...
gi 729042217 139 ERDHFVSHPGKYTLIEVQ 156
Cdd:cd08001   86 NRKNFKKKPGKFYPLDID 103
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
81-134 1.28e-09

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 54.99  E-value: 1.28e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 729042217  81 KFYIIQLLQDsnrFFTCWN---RWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTK 134
Cdd:COG3831   16 RFYELEVEPD---LFGGWSltrRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKLR 69
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 382-478 1.61e-09

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: 56.41  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 382 LWHGTNMAVVAAILTSGLRI----MPHSGGRVGKGIYFASENSKSAGYVIGMKCGAH--------------HVGYMFLGE 443
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRPasygVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVfqngkpkvcgrelcVFGFLTLGV 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 729042217 444 VALGREHHINTDNPSLKSPPPGFDSVIARGHTEPD 478
Cdd:cd01341   82 MSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRD 116
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 81-134 2.06e-09

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: 54.15  E-value: 2.06e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 729042217  81 KFYIIQLLQDsnrFFTCWN---RWGRVGEVGQSKINHFTRLEDAKKDFEKKFREKTK 134
Cdd:cd07996   15 RFYEIELEGD---LFGEWSlvrRWGRIGTKGQSRTKTFDSEEEALKAAEKLIREKLK 68
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 381-471 9.29e-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: 53.48  E-value: 9.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 381 LLWHGTNMAVVAAILTSGLRIMPH-SGGRV-GKGIYFASENSKSAGYVigmKCGAHHVGY--MFLGEVALGR--EHHINT 454
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCgKHGTMyGKGSYFAKNASYSHQYS---KKSPKADGLkeMFLARVLTGDytQGHPGY 77

                         90       100
                 ....*....|....*....|
gi 729042217 455 DNPSLK---SPPPGFDSVIA 471
Cdd:cd01439   78 RRPPLKpsgVELDRYDSCVD 97
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 81-139 1.08e-06

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.


Pssm-ID: 153424  Cd Length: 73  Bit Score: 46.12  E-value: 1.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 729042217  81 KFYIIQLLQDS--NRFFTCWNrWGRVGEV-GQSKINHFTRLEDAKKDFEKKFREKTKNNWAE 139
Cdd:cd07994   13 KYYKLQLLEDDkeNRYWVFRS-YGRVGTViGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 363-472 3.37e-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: 42.19  E-value: 3.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729042217 363 QEGEEDRFQAHsklgNRKLLWHGTnmAVVAAILTSGL-RIMPHSGGRVGKGIYFASENSKSAGYVIGM----KCGAHH-- 435
Cdd:cd01438   77 KEIAEENHNHH----NERMLFHGS--PFINAIIHKGFdERHAYIGGMFGAGIYFAENSSKSNQYVYGIgggtGCPTHKdr 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 729042217 436 -----VGYMFLGEVALGREhHINTDNPSLKSPPPGFDSVIAR 472
Cdd:cd01438  151 scyvcHRQMLFCRVTLGKS-FLQFSAMKMAHAPPGHHSVIGR 191
 
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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