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Conserved domains on  [gi|1953009792|ref|XP_038422212|]
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protein mono-ADP-ribosyltransferase PARP3 [Canis lupus familiaris]

Protein Classification

WGR_PARP3_like and parp_like domain-containing protein( domain architecture ID 10168760)

WGR_PARP3_like 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 ...
 181-530 1.13e-130

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: 383.93  E-value: 1.13e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 181 PCSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALELALKAPTDGGPNLEELSSHFYTVI 260
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 261 PHNFSRNRPPPINSPELLQAKKDMLLVLADIELAQTLQASpeeeKVEEVPHPLDRDYQLLKCQLQLLDPEEPEYKVIHTY 340
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD----DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 341 LEKTGG--TYRCPALQHIWKVNREGEGDRFQAHSKLSNRKLLWHGTNVAVVAAILASGLRIMPHS----GGRVGKGIYFA 414
Cdd:cd01437   157 LKNTHAptTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIYFA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 415 SENSKSAGYvtgisCGAHQ---IGYMFLGEVALGREHHITIDDPSLKQPPPGFDSVIARGSTEPDPSqDTELELDGqrVV 491
Cdd:cd01437   237 DMFSKSANY-----CHASAsdpTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPS-EFEIDLDG--VV 308

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1953009792 492 VPQGQPVPCAEFSSSRFFQSEYLIYQESQCHLRYLLEVH 530
Cdd:cd01437   309 VPLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 58-156 1.22e-56

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: 184.15  E-value: 1.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  58 PQTQVHEDYACTLNQTNIGRNNNKFYIIQLLEEGDRFACWNRWGRVGEVGQSKLS-YFVLLEDAKKDFEKKFQDKTKNRW 136
Cdd:cd08002     1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKgPWDSLEGAIKDFEKKFKDKTKNNW 80

                          90       100
                  ....*....|....*....|
gi 1953009792 137 VERDHFVAHPGKYTLIEVQG 156
Cdd:cd08002    81 EDRENFVPHPGKYTLIEMDY 100
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 181-530 1.13e-130

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: 383.93  E-value: 1.13e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 181 PCSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALELALKAPTDGGPNLEELSSHFYTVI 260
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 261 PHNFSRNRPPPINSPELLQAKKDMLLVLADIELAQTLQASpeeeKVEEVPHPLDRDYQLLKCQLQLLDPEEPEYKVIHTY 340
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD----DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 341 LEKTGG--TYRCPALQHIWKVNREGEGDRFQAHSKLSNRKLLWHGTNVAVVAAILASGLRIMPHS----GGRVGKGIYFA 414
Cdd:cd01437   157 LKNTHAptTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIYFA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 415 SENSKSAGYvtgisCGAHQ---IGYMFLGEVALGREHHITIDDPSLKQPPPGFDSVIARGSTEPDPSqDTELELDGqrVV 491
Cdd:cd01437   237 DMFSKSANY-----CHASAsdpTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPS-EFEIDLDG--VV 308

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1953009792 492 VPQGQPVPCAEFSSSRFFQSEYLIYQESQCHLRYLLEVH 530
Cdd:cd01437   309 VPLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 2-529 1.61e-106

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 332.19  E-value: 1.61e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792   2 APKRKPQVQQEGPEKKKGRQGAEEEdsfrstaEALRAApTEKHVVRVDPACPLSHNPQTQVHED----YACTLNQTNIGR 77
Cdd:PLN03124  117 VKVGSANGTGEDEKEKGGDEEREKE-------EKIVTA-TKKGRAVLDQWLPDHIKSNYHVLEEgddvYDAMLNQTNVGD 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  78 NNNKFYIIQLLE--EGDRFACWNRWGRVGEVGQSKL-SYFVLLEDAKKDFEKKFQDKTKNRWVERDHFVAHPGKYTLIEV 154
Cdd:PLN03124  189 NNNKFYVLQVLEsdDGSKYMVYTRWGRVGVKGQDKLhGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEM 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 155 QGEDEAQeavvKVDGGSVRNIVQRVRPCSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEA 234
Cdd:PLN03124  269 DYEDEEE----SKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKR 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 235 -LELALKAPTDggpNLEELSSHFYTVIPHNFSRN--RPPPINSPELLQAKKDMLLVLADIELAQTLQASPEEEKVEevph 311
Cdd:PLN03124  345 iAEVISRSDRE---TLEELSGEFYTVIPHDFGFKkmRQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDD---- 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 312 PLDRDYQLLKCQLQLLDPEEPEYKVIHTYLEKTGG----TYRCPALQhIWKVNREGEGDRFQAHSKLSNRKLLWHGTNVA 387
Cdd:PLN03124  418 PLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHGqthsGYTLEIVQ-IFKVSREGEDERFQKFSSTKNRMLLWHGSRLT 496

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 388 VVAAILASGLRI----MPHSGGRVGKGIYFASENSKSAGYvtgisCGAH---QIGYMFLGEVALGREHHITIDDPSLKQP 460
Cdd:PLN03124  497 NWTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANY-----CYASaanPDGVLLLCEVALGDMNELLQADYNANKL 571

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953009792 461 PPGFDSVIARGSTEPDPSQDTELElDGqrVVVPQGQPV--PCAEFSSSRffqSEYLIYQESQCHLRYLLEV 529
Cdd:PLN03124  572 PPGKLSTKGVGRTVPDPSEAKTLE-DG--VVVPLGKPVesPYSKGSLEY---NEYIVYNVDQIRMRYVLQV 636
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 58-156 1.22e-56

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: 184.15  E-value: 1.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  58 PQTQVHEDYACTLNQTNIGRNNNKFYIIQLLEEGDRFACWNRWGRVGEVGQSKLS-YFVLLEDAKKDFEKKFQDKTKNRW 136
Cdd:cd08002     1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKgPWDSLEGAIKDFEKKFKDKTKNNW 80

                          90       100
                  ....*....|....*....|
gi 1953009792 137 VERDHFVAHPGKYTLIEVQG 156
Cdd:cd08002    81 EDRENFVPHPGKYTLIEMDY 100
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 333-529 4.18e-51

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: 173.29  E-value: 4.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 333 EYKVIHTYLEKTGG---TYRcPALQHIWKVNREGEGDRFQAHSKLSNRKLLWHGTNVAVVAAILASGLRI----MPHSGG 405
Cdd:pfam00644   3 EYQIIEKYFLSTHDpthGYP-LFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIappeAPVTGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 406 RVGKGIYFASENSKSAGYVTgiSCGAHQIGYMFLGEVALGREHHITIDDPsLKQPPPGFDSVIARGSTEPDPSQDteleL 485
Cdd:pfam00644  82 MFGKGIYFADDASKSANYCP--PSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPESFVD----L 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953009792 486 DGqrvvVPQGQPVPcAEFSSSRFFQSEYLIYQESQCHLRYLLEV 529
Cdd:pfam00644 155 DG----VPLGKLVA-TGYDSSVLLYNEYVVYNVNQVRPKYLLEV 193
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 62-143 2.66e-31

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: 115.85  E-value: 2.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792   62 VHEDYACTLNQTNIGRNNNKFYIIQLLEEGD-RFACWNRWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTKNRWVERD 140
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDDFgGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 1953009792  141 HFV 143
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 ...
 66-143 1.25e-30

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: 113.88  E-value: 1.25e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLLE-EGDRFACWNRWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTKNRWVERDHFV 143
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDdLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
66-133 1.41e-09

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 54.61  E-value: 1.41e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLleEGDRFACWN---RWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTK 133
Cdd:COG3831     1 MRLYLERIDPAGNSARFYELEV--EPDLFGGWSltrRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKLR 69
 
Name Accession Description Interval E-value
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 181-530 1.13e-130

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: 383.93  E-value: 1.13e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 181 PCSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALELALKAPTDGGPNLEELSSHFYTVI 260
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSQGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 261 PHNFSRNRPPPINSPELLQAKKDMLLVLADIELAQTLQASpeeeKVEEVPHPLDRDYQLLKCQLQLLDPEEPEYKVIHTY 340
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKD----DEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 341 LEKTGG--TYRCPALQHIWKVNREGEGDRFQAHSKLSNRKLLWHGTNVAVVAAILASGLRIMPHS----GGRVGKGIYFA 414
Cdd:cd01437   157 LKNTHAptTEYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEapvtGYMFGKGIYFA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 415 SENSKSAGYvtgisCGAHQ---IGYMFLGEVALGREHHITIDDPSLKQPPPGFDSVIARGSTEPDPSqDTELELDGqrVV 491
Cdd:cd01437   237 DMFSKSANY-----CHASAsdpTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDPS-EFEIDLDG--VV 308

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1953009792 492 VPQGQPVPCAEFSSSRFFQSEYLIYQESQCHLRYLLEVH 530
Cdd:cd01437   309 VPLGKPVPSGHKTDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 2-529 1.61e-106

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 332.19  E-value: 1.61e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792   2 APKRKPQVQQEGPEKKKGRQGAEEEdsfrstaEALRAApTEKHVVRVDPACPLSHNPQTQVHED----YACTLNQTNIGR 77
Cdd:PLN03124  117 VKVGSANGTGEDEKEKGGDEEREKE-------EKIVTA-TKKGRAVLDQWLPDHIKSNYHVLEEgddvYDAMLNQTNVGD 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  78 NNNKFYIIQLLE--EGDRFACWNRWGRVGEVGQSKL-SYFVLLEDAKKDFEKKFQDKTKNRWVERDHFVAHPGKYTLIEV 154
Cdd:PLN03124  189 NNNKFYVLQVLEsdDGSKYMVYTRWGRVGVKGQDKLhGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEM 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 155 QGEDEAQeavvKVDGGSVRNIVQRVRPCSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEA 234
Cdd:PLN03124  269 DYEDEEE----SKKDKPSVSSEDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKR 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 235 -LELALKAPTDggpNLEELSSHFYTVIPHNFSRN--RPPPINSPELLQAKKDMLLVLADIELAQTLQASPEEEKVEevph 311
Cdd:PLN03124  345 iAEVISRSDRE---TLEELSGEFYTVIPHDFGFKkmRQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDD---- 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 312 PLDRDYQLLKCQLQLLDPEEPEYKVIHTYLEKTGG----TYRCPALQhIWKVNREGEGDRFQAHSKLSNRKLLWHGTNVA 387
Cdd:PLN03124  418 PLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHGqthsGYTLEIVQ-IFKVSREGEDERFQKFSSTKNRMLLWHGSRLT 496

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 388 VVAAILASGLRI----MPHSGGRVGKGIYFASENSKSAGYvtgisCGAH---QIGYMFLGEVALGREHHITIDDPSLKQP 460
Cdd:PLN03124  497 NWTGILSQGLRIappeAPSTGYMFGKGVYFADMFSKSANY-----CYASaanPDGVLLLCEVALGDMNELLQADYNANKL 571

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953009792 461 PPGFDSVIARGSTEPDPSQDTELElDGqrVVVPQGQPV--PCAEFSSSRffqSEYLIYQESQCHLRYLLEV 529
Cdd:PLN03124  572 PPGKLSTKGVGRTVPDPSEAKTLE-DG--VVVPLGKPVesPYSKGSLEY---NEYIVYNVDQIRMRYVLQV 636
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 66-529 1.45e-63

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 223.90  E-value: 1.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLLEEGDRFACW--NRWGRVG--EVGQSKLSYFVLLeDAKKDFEKKFQDKTKN---RWVE 138
Cdd:PLN03123  520 YNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYvfRKWGRVGneKIGGNKLEEMSKS-DAIHEFKRLFLEKTGNpweSWEQ 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 139 RDHFVAHPGKYTLIEVQ-GEDEAQEAVVKVDGGSvrnivqrvrpcSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPL 217
Cdd:PLN03123  599 KTNFQKQPGKFYPLDIDyGVNEQPKKKAASGSKS-----------NLAPRLVELMKMLFDVETYRAAMMEFEINMSEMPL 667

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 218 GKLSKQQIARGFEALEALELALKApTDGGPNLEEL-----SSHFYTVIP--HnfsrnrPPPINSPELLQAKKDMLLVLAD 290
Cdd:PLN03123  668 GKLSKANIQKGFEALTEIQNLLKE-NDQDPSIRESllvdaSNRFFTLIPsiH------PHIIRDEDDLKSKVKMLEALQD 740

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 291 IELAQTLQASPEEEKVeevphPLDRDYQLLKCQLQLLDPEEPEYKVIHTYLEKTGG---TYRCPALQHIWKVNREGEGDR 367
Cdd:PLN03123  741 IEIASRLVGFDVDEDD-----SLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHApthTDWSLELEEVFSLEREGEFDK 815

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 368 FQAH-SKLSNRKLLWHGTNVAVVAAILASGLRI----MPHSGGRVGKGIYFASENSKSAGYVtgISCGAHQIGYMFLGEV 442
Cdd:PLN03123  816 YAPYkEKLKNRMLLWHGSRLTNFVGILSQGLRIappeAPATGYMFGKGVYFADLVSKSAQYC--YTDRKNPVGLMLLSEV 893

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 443 ALGREHHITiDDPSLKQPPPGFDSVIARGSTEPDPSQDTELELDgqrVVVPQGQPVPcAEFSSSRFFQSEYLIYQESQCH 522
Cdd:PLN03123  894 ALGEIYELK-KAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDD---VVVPCGKPVP-SKVKASELMYNEYIVYNTAQVK 968


                  ....*..
gi 1953009792 523 LRYLLEV 529
Cdd:PLN03123  969 LQFLLKV 975
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 58-156 1.22e-56

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: 184.15  E-value: 1.22e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  58 PQTQVHEDYACTLNQTNIGRNNNKFYIIQLLEEGDRFACWNRWGRVGEVGQSKLS-YFVLLEDAKKDFEKKFQDKTKNRW 136
Cdd:cd08002     1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESGKEYYVWNRWGRVGEKGQNKLKgPWDSLEGAIKDFEKKFKDKTKNNW 80

                          90       100
                  ....*....|....*....|
gi 1953009792 137 VERDHFVAHPGKYTLIEVQG 156
Cdd:cd08002    81 EDRENFVPHPGKYTLIEMDY 100
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 333-529 4.18e-51

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: 173.29  E-value: 4.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 333 EYKVIHTYLEKTGG---TYRcPALQHIWKVNREGEGDRFQAHSKLSNRKLLWHGTNVAVVAAILASGLRI----MPHSGG 405
Cdd:pfam00644   3 EYQIIEKYFLSTHDpthGYP-LFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIappeAPVTGY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 406 RVGKGIYFASENSKSAGYVTgiSCGAHQIGYMFLGEVALGREHHITIDDPsLKQPPPGFDSVIARGSTEPDPSQDteleL 485
Cdd:pfam00644  82 MFGKGIYFADDASKSANYCP--PSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAPESFVD----L 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953009792 486 DGqrvvVPQGQPVPcAEFSSSRFFQSEYLIYQESQCHLRYLLEV 529
Cdd:pfam00644 155 DG----VPLGKLVA-TGYDSSVLLYNEYVVYNVNQVRPKYLLEV 193
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 182-317 1.55e-48

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: 164.23  E-value: 1.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 182 CSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPLGKLSKQQIARGFEALEALELALKAPTDGGPN--LEELSSHFYTV 259
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAKAKakLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953009792 260 IPHNFSRNRPPPINSPELLQAKKDMLLVLADIELAQTLQASpeeEKVEEVPHPLDRDY 317
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKD---SKSDDDEHPLDRHY 135
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 66-154 1.75e-40

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: 141.70  E-value: 1.75e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLLEE--GDRFACWNRWGRVGEVGQSKLSYFVL-LEDAKKDFEKKFQDKTKNRWVERDHF 142
Cdd:cd08003    10 YDAMLNQTNIQQNNNKYYIIQLLEDdaEKIYSVWFRWGRVGKKGQSSLVPCGSdLEQAKSLFEKKFLDKTKNEWEDRANF 89

                          90
                  ....*....|..
gi 1953009792 143 VAHPGKYTLIEV 154
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 ...
 66-156 4.89e-40

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: 140.52  E-value: 4.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLLEEGD--RFACWNRWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTKNRWVERDHFV 143
Cdd:cd07997    10 YDATLNQTDISNNNNKFYKIQILESKGpnTYALFTRWGRVGERGQSQLTPFGSLESAIKEFEKKFKDKTGNEWENRPLFK 89

                          90
                  ....*....|...
gi 1953009792 144 AHPGKYTLIEVQG 156
Cdd:cd07997    90 KQPGKYALVELDY 102
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 62-143 2.66e-31

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: 115.85  E-value: 2.66e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792   62 VHEDYACTLNQTNIGRNNNKFYIIQLLEEGD-RFACWNRWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTKNRWVERD 140
Cdd:smart00773   2 GGEIYDVYLNFTDLASNNNKFYIIQLLEDDFgGYSVYRRWGRIGTKGQTKLKTFDSLEDAIKEFEKLFKEKTKNGYEERG 81


                   ...
gi 1953009792  141 HFV 143
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 ...
 66-143 1.25e-30

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: 113.88  E-value: 1.25e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLLE-EGDRFACWNRWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTKNRWVERDHFV 143
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQVEDdLFGGYSLFRRWGRIGTRGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEFE 79
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 63-155 3.67e-22

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: 91.12  E-value: 3.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  63 HEDYACTLNQTNIGRNNNKFYIIQLLEEGDRFACW--NRWGRVG-EVGQSKLSYFVLLEDAKKDFEKKFQDKTKNRWVER 139
Cdd:cd08001     8 GNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWvfRSWGRVGtTIGGNKLEEFSSLEEAKMAFEELYEEKTGNDFENR 87

                          90
                  ....*....|....*.
gi 1953009792 140 DHFVAHPGKYTLIEVQ 155
Cdd:cd08001    88 KNFKKKPGKFYPLDID 103
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 66-529 4.35e-18

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 87.93  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLLEEGDR-FACWNRWGRVGE--VGQSKLSYFVLLEDAKKDFEKKFQDKTKNR---WVER 139
Cdd:PLN03122  336 YNCAFSICDLGRGLNEYCIMQLITVPDSnLHLYYKKGRVGDdpNAEERLEEWEDVDAAIKEFVRLFEEITGNEfepWERE 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 140 DHFVAHPGKYTLIEVqgeDEAQEavVKVDGGSVRNIVQRVRPCSLDAPTQKLITNIFSKDMFKNAMTLMNLDVKKMPLGK 219
Cdd:PLN03122  416 KKFEKKRLKFYPIDM---DDGVD--VRAGGLGLRQLGVAAAHCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGM 490

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 220 LSKQQIARGFEALEALELALKAPTDGGPNLE----ELSSHFYTVIPhnfsRNRPPPINS-PELLQAKKDMLLVLADIELA 294
Cdd:PLN03122  491 LSDFHLKRCEEVLLEFAEFVKSEKETGQKAEamwlDFSNKWFSLVH----STRPFVIRDiDELADHAASALETVRDINVA 566

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 295 QTLQASPEEEKVEEvphPLDRDYQLLKCQLQLLDPEEPEYKVIHTYLEKT------GGTYRCPALQHIWKVNREGeGDRF 368
Cdd:PLN03122  567 SRLIGDMTGSTLDD---PLSDRYKKLGCSISPVDKESDDYKMIVKYLEKTyepvkvGDVSYSVSVENIFAVESSA-GPSL 642

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 369 QAHSKLSNRKLLWHGTNVAVVAAILASGLRI----MPHSGGRVGKGIYFASENSKSAGYvtGISCGAHQIGYMFLGEVAL 444
Cdd:PLN03122  643 DEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPavcsLPVPGYMFGKAIVCSDAAAEAARY--GFTAVDRPEGFLVLAVASL 720

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 445 GREhhITiddpSLKQPPPGFDS-------VIARGSTEPDPSQDTELELDgqrVVVPQGQPVPcAEFSSSRFFQSEYLIYQ 517
Cdd:PLN03122  721 GDE--VL----ELTKPPEDVKSyeekkvgVKGLGRKKTDESEHFKWRDD---ITVPCGRLIP-SEHKDSPLEYNEYAVYD 790

                         490
                  ....*....|..
gi 1953009792 518 ESQCHLRYLLEV 529
Cdd:PLN03122  791 PKQVSIRFLVGV 802
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 380-476 1.08e-10

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: 59.50  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 380 LWHGTNVAVVAAILASGLRI----MPHSGGRVGKGIYFASENSKSAGYVTGISCGAH--------------QIGYMFLGE 441
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPasygVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVfqngkpkvcgrelcVFGFLTLGV 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1953009792 442 VALGREHHITIDDPSLKQPPPGFDSVIARGSTEPD 476
Cdd:cd01341    82 MSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRD 116
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 78-138 1.12e-09

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: 54.59  E-value: 1.12e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953009792  78 NNNKFYIIQLLEEG--DRFACWNRWGRVGEV-GQSKLSYFVLLEDAKKDFEKKFQDKTKNRWVE 138
Cdd:cd07994    10 GSNKYYKLQLLEDDkeNRYWVFRSYGRVGTViGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
66-133 1.41e-09

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 54.61  E-value: 1.41e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953009792  66 YACTLNQTNIGRNNNKFYIIQLleEGDRFACWN---RWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTK 133
Cdd:COG3831     1 MRLYLERIDPAGNSARFYELEV--EPDLFGGWSltrRWGRIGTKGQTKTKTFASEEEALAALEKLVAEKLR 69
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 76-133 5.39e-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: 52.61  E-value: 5.39e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953009792  76 GRNNNKFYIIQLleEGDRFACWN---RWGRVGEVGQSKLSYFVLLEDAKKDFEKKFQDKTK 133
Cdd:cd07996    10 ERNSARFYEIEL--EGDLFGEWSlvrRWGRIGTKGQSRTKTFDSEEEALKAAEKLIREKLK 68
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 379-469 2.90e-08

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 52.32  E-value: 2.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 379 LLWHGTNVAVVAAILASGLRIMPH-SGGRV-GKGIYFASENSKSAGYvTGISCGAHQIGYMFLGEVALGR--EHHITIDD 454
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRFCgKHGTMyGKGSYFAKNASYSHQY-SKKSPKADGLKEMFLARVLTGDytQGHPGYRR 79

                          90
                  ....*....|....*...
gi 1953009792 455 PSLKQ---PPPGFDSVIA 469
Cdd:cd01439    80 PPLKPsgvELDRYDSCVD 97
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 369-472 1.61e-05

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: 46.05  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953009792 369 QAHSKLSNRKLLWHGTnvAVVAAILASGL-RIMPHSGGRVGKGIYFASENSKSAGYVTGI----SCGAHQ-------IGY 436
Cdd:cd01438    81 EENHNHHNERMLFHGS--PFINAIIHKGFdERHAYIGGMFGAGIYFAENSSKSNQYVYGIgggtGCPTHKdrscyvcHRQ 158

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1953009792 437 MFLGEVALGREhHITIDDPSLKQPPPGFDSVIARGS 472
Cdd:cd01438   159 MLFCRVTLGKS-FLQFSAMKMAHAPPGHHSVIGRPS 193
 
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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