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Conserved domains on  [gi|530402916|ref|XP_005267304|]
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poly [ADP-ribose] polymerase 2 isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03124 super family cl33640
poly [ADP-ribose] polymerase; Provisional
 32-489 8.57e-156

poly [ADP-ribose] polymerase; Provisional


The actual alignment was detected with superfamily member PLN03124:

Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 457.76  E-value: 8.57e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  32 DSSPAKKTRRCQRQESKKMPVAGGKAN-KDRTEDKQDGMPGRSWASKRVSeSVKalllKGKAPVDPECTAKVgKA--HVY 108
Cdd:PLN03124  97 ATTGRKKDLLERLCAALESDVKVGSANgTGEDEKEKGGDEEREKEEKIVT-ATK----KGRAVLDQWLPDHI-KSnyHVL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 109 CEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNW 188
Cdd:PLN03124 171 EEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHW 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 189 EDREKFEKVPGKYDMLQMDYatntQDEEETKKE-ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAP 266
Cdd:PLN03124 251 SDRKNFISHPKKYTWLEMDY----EDEEESKKDkPSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLP 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 267 LGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALMEACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAI 344
Cdd:PLN03124 327 LGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEELSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIAT 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 345 KLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHN 422
Cdd:PLN03124 406 KLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKN 485

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530402916 423 RMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 489
Cdd:PLN03124 486 RMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCE 552
 
Name Accession Description Interval E-value
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 32-489 8.57e-156

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 457.76  E-value: 8.57e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  32 DSSPAKKTRRCQRQESKKMPVAGGKAN-KDRTEDKQDGMPGRSWASKRVSeSVKalllKGKAPVDPECTAKVgKA--HVY 108
Cdd:PLN03124  97 ATTGRKKDLLERLCAALESDVKVGSANgTGEDEKEKGGDEEREKEEKIVT-ATK----KGRAVLDQWLPDHI-KSnyHVL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 109 CEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNW 188
Cdd:PLN03124 171 EEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHW 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 189 EDREKFEKVPGKYDMLQMDYatntQDEEETKKE-ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAP 266
Cdd:PLN03124 251 SDRKNFISHPKKYTWLEMDY----EDEEESKKDkPSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLP 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 267 LGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALMEACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAI 344
Cdd:PLN03124 327 LGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEELSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIAT 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 345 KLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHN 422
Cdd:PLN03124 406 KLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKN 485

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530402916 423 RMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 489
Cdd:PLN03124 486 RMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCE 552
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 231-489 1.20e-128

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: 377.77  E-value: 1.20e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 231 ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQH-GRALMEACNEFYTRI 309
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 310 PHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQST 389
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 390 HAPTHsDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMS 467
Cdd:cd01437  161 HAPTT-EYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMF 239

                        250       260
                 ....*....|....*....|..
gi 530402916 468 SKSANYCFASRLKNTGLLLLSE 489
Cdd:cd01437  240 SKSANYCHASASDPTGLLLLCE 261
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 376-489 8.47e-60

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: 195.25  E-value: 8.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  376 SYEFKVISQYLQSTHAPTHSdYTMTLLDLFEVEKDGEKEAFRED--LHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPIT 453
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKkkLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530402916  454 GYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 489
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSE 115
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 110-195 4.10e-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: 115.08  E-value: 4.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916   110 EGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWE 189
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTKGQTKLKTF-DSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 530402916   190 DREKFE 195
Cdd:smart00773  79 ERGKFV 84
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
127-185 3.64e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 36.50  E-value: 3.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402916 127 NNNKYYLIQLlEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 185
Cdd:COG3831   13 NSARFYELEV-EPDLFGGWSLTRRWGRIGTKGQTKTKTF-ASEEEALAALEKLVAEKLR 69
 
Name Accession Description Interval E-value
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 32-489 8.57e-156

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 457.76  E-value: 8.57e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  32 DSSPAKKTRRCQRQESKKMPVAGGKAN-KDRTEDKQDGMPGRSWASKRVSeSVKalllKGKAPVDPECTAKVgKA--HVY 108
Cdd:PLN03124  97 ATTGRKKDLLERLCAALESDVKVGSANgTGEDEKEKGGDEEREKEEKIVT-ATK----KGRAVLDQWLPDHI-KSnyHVL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 109 CEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNW 188
Cdd:PLN03124 171 EEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDGSKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHW 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 189 EDREKFEKVPGKYDMLQMDYatntQDEEETKKE-ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAP 266
Cdd:PLN03124 251 SDRKNFISHPKKYTWLEMDY----EDEEESKKDkPSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLP 326

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 267 LGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALMEACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAI 344
Cdd:PLN03124 327 LGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEELSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIAT 405

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 345 KLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHN 422
Cdd:PLN03124 406 KLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKN 485

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530402916 423 RMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 489
Cdd:PLN03124 486 RMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCE 552
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 231-489 1.20e-128

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: 377.77  E-value: 1.20e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 231 ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQH-GRALMEACNEFYTRI 309
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 310 PHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQST 389
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 390 HAPTHsDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMS 467
Cdd:cd01437  161 HAPTT-EYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMF 239

                        250       260
                 ....*....|....*....|..
gi 530402916 468 SKSANYCFASRLKNTGLLLLSE 489
Cdd:cd01437  240 SKSANYCHASASDPTGLLLLCE 261
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 76-489 5.00e-115

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 362.19  E-value: 5.00e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  76 SKRVSESVKALLLKGKAPVDpECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVG 155
Cdd:PLN03123 482 ASGTSSSMVTVKVKGRSAVH-EASGLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVG 560

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 156 --KMGQHSLVACSgnlnKAKEI--FQKKFLDKTKNNWE---DREKFEKVPGKYDMLQMDYATNtqdEEETKKEESlkspl 228
Cdd:PLN03123 561 neKIGGNKLEEMS----KSDAIheFKRLFLEKTGNPWEsweQKTNFQKQPGKFYPLDIDYGVN---EQPKKKAAS----- 628

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 229 KPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHGRA-----LMEACN 303
Cdd:PLN03123 629 GSKSNLAPRLVELMKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSireslLVDASN 708

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 304 EFYTRIP--HdfglrtPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEhPLDQHYRNLHCALRPLDHESYEFKV 381
Cdd:PLN03123 709 RFFTLIPsiH------PHIIRDEDDLKSKVKMLEALQDIEIASRLVGFDVDEDD-SLDDKYKKLHCDISPLPHDSEDYKL 781

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 382 ISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAF---REDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFG 458
Cdd:PLN03123 782 IEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKYapyKEKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFG 861

                        410       420       430
                 ....*....|....*....|....*....|.
gi 530402916 459 KGIYFADMSSKSANYCFASRLKNTGLLLLSE 489
Cdd:PLN03123 862 KGVYFADLVSKSAQYCYTDRKNPVGLMLLSE 892
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 106-208 1.96e-71

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: 222.20  E-value: 1.96e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 106 HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTK 185
Cdd:cd08003    1 HVYEEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKKGQSSLVPCGSDLEQAKSLFEKKFLDKTK 80

                         90       100
                 ....*....|....*....|...
gi 530402916 186 NNWEDREKFEKVPGKYDMLQMDY 208
Cdd:cd08003   81 NEWEDRANFEKVAGKYDLLEMDY 103
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 376-489 8.47e-60

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: 195.25  E-value: 8.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  376 SYEFKVISQYLQSTHAPTHSdYTMTLLDLFEVEKDGEKEAFRED--LHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPIT 453
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKkkLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530402916  454 GYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 489
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSE 115
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 232-362 9.56e-52

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: 171.94  E-value: 9.56e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  232 SQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAG---QHGRALMEACNEFYTR 308
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPslaKAKAKLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530402916  309 IPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSP-EHPLDQHY 362
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKDSKSDDdEHPLDRHY 135
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 106-208 1.85e-43

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: 148.99  E-value: 1.85e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 106 HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 185
Cdd:cd07997    1 HVYGDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPF-GSLESAIKEFEKKFKDKTG 79

                         90       100
                 ....*....|....*....|...
gi 530402916 186 NNWEDREKFEKVPGKYDMLQMDY 208
Cdd:cd07997   80 NEWENRPLFKKQPGKYALVELDY 102
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 107-208 3.54e-41

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: 142.93  E-value: 3.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 107 VYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaqRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKN 186
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESG--KEYYVWNRWGRVGEKGQNKLKGPWDSLEGAIKDFEKKFKDKTKN 78

                         90       100
                 ....*....|....*....|..
gi 530402916 187 NWEDREKFEKVPGKYDMLQMDY 208
Cdd:cd08002   79 NWEDRENFVPHPGKYTLIEMDY 100
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 110-195 4.10e-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: 115.08  E-value: 4.10e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916   110 EGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWE 189
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTKGQTKLKTF-DSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 530402916   190 DREKFE 195
Cdd:smart00773  79 ERGKFV 84
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 115-195 8.19e-29

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: 108.48  E-value: 8.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916  115 YDVMLNQTNLQFNNNKYYLIQlLEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWEDREKF 194
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQ-VEDDLFGGYSLFRRWGRIGTRGQTKLKSF-DSLEEAIKEFEKLFAEKTKKGYRERGEF 78


                  .
gi 530402916  195 E 195
Cdd:pfam05406  79 E 79
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 129-488 1.47e-28

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 119.90  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 129 NKYYLIQLLEDdAQRNFSVWMRWGRVG-KMGQHSLVACSGNLNKAKEIFQKKFLDKTKNN---WEDREKFEKVPGKYDML 204
Cdd:PLN03122 350 NEYCIMQLITV-PDSNLHLYYKKGRVGdDPNAEERLEEWEDVDAAIKEFVRLFEEITGNEfepWEREKKFEKKRLKFYPI 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 205 QMDYATNTQDEEETKKEESLKSPlkpESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKK 284
Cdd:PLN03122 429 DMDDGVDVRAGGLGLRQLGVAAA---HCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLE 505

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 285 IEDCIRA----GQ-HGRALMEACNEFYTRIPHDfglrTPPLIRTQKELSEKI-QLLEALGDIEIAIKLVKTELQSP-EHP 357
Cdd:PLN03122 506 FAEFVKSeketGQkAEAMWLDFSNKWFSLVHST----RPFVIRDIDELADHAaSALETVRDINVASRLIGDMTGSTlDDP 581

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 358 LDQHYRNLHCALRPLDHESYEFKVISQYLQSTHAPTH---SDYTMTLLDLFEVEKDGeKEAFRE--DLHNRMLLWHGSRM 432
Cdd:PLN03122 582 LSDRYKKLGCSISPVDKESDDYKMIVKYLEKTYEPVKvgdVSYSVSVENIFAVESSA-GPSLDEikKLPNKVLLWCGTRS 660

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530402916 433 SNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLS 488
Cdd:PLN03122 661 SNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAAAEAARYGFTAVDRPEGFLVLA 716
PARP2_NTR cd22252
NTR (N-terminal region) domain of poly [ADP-ribose] polymerase 2 (PARP-2) and similar proteins; ...
 19-91 2.92e-27

NTR (N-terminal region) domain of poly [ADP-ribose] polymerase 2 (PARP-2) and similar proteins; PARP-2 is also called ADP-ribosyltransferase diphtheria toxin-like 2 (ARTD2), DNA ADP-ribosyltransferase PARP2, NAD(+) ADP-ribosyltransferase 2 (ADPRT-2), poly[ADP-ribose] synthase 2 (pADPRT-2), or protein poly-ADP-ribosyltransferase PARP2. It is a poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. It mainly mediates glutamate and aspartate ADP-ribosylation of target proteins. PARP-2 can also ADP-ribosylate DNA; it preferentially acts on 5'-terminal phosphates at DNA strand break termini in nicked duplex. This model corresponds to the NTR (N-terminal region) domain of PARP-2, which contains a nucleolar localization sequence (NoLS) and a putative nuclear localization signal (NLS). The NTR domain has a helical SAF-A/B, Acinus, and PIAS (SAP) domain fold and may participate in protein-protein interactions.


Pssm-ID: 412075  Cd Length: 59  Bit Score: 103.82  E-value: 2.92e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530402916  19 ESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQdgmpgrswaskrvsESVKALLLKGK 91
Cdd:cd22252    1 ESKRVNNGNTATEDSPPAKKTRRCQRKEVKKEPVAGGKADKDRTEDKQ--------------ESVKALLLKGK 59
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 105-208 2.09e-23

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: 94.58  E-value: 2.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 105 AHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVG-KMGQHSLVACSgNLNKAKEIFQKKFLDK 183
Cdd:cd08001    1 AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGtTIGGNKLEEFS-SLEEAKMAFEELYEEK 79

                         90       100
                 ....*....|....*....|....*
gi 530402916 184 TKNNWEDREKFEKVPGKYDMLQMDY 208
Cdd:cd08001   80 TGNDFENRKNFKKKPGKFYPLDIDY 104
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 426-474 5.27e-17

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: 77.60  E-value: 5.27e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 530402916 426 LWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYC 474
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYS 50
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 125-190 2.88e-07

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: 47.66  E-value: 2.88e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530402916 125 QFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWED 190
Cdd:cd07994    8 DIGSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 127-185 5.46e-04

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: 38.35  E-value: 5.46e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402916 127 NNNKYYLIQLlEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 185
Cdd:cd07996   12 NSARFYEIEL-EGDLFGEWSLVRRWGRIGTKGQSRTKTF-DSEEEALKAAEKLIREKLK 68
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 425-474 1.03e-03

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: 38.84  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530402916 425 LLWHGSRMSNWVGILSHGL--RIAPPEAPitgyMFGKGIYFADMSSKSANYC 474
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFdrRFCGKHGT----MYGKGSYFAKNASYSHQYS 48
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 369-475 1.49e-03

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: 40.27  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530402916 369 LRPLDHEsyeFKVISQYLQST---------HAPTHSDYTMTLLDLFEVEKDGEKEAFRED--------LHNRMLLWHGSR 431
Cdd:cd01438   21 LAPDDKE---YQSVEEEMQSTirehrdggnAGGIFNRYNIIRIQKVVNKKLRERYCHRQKeiaeenhnHHNERMLFHGSP 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530402916 432 MSNwvGILSHGLRiaPPEAPITGyMFGKGIYFADMSSKSANYCF 475
Cdd:cd01438   98 FIN--AIIHKGFD--ERHAYIGG-MFGAGIYFAENSSKSNQYVY 136
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
127-185 3.64e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 36.50  E-value: 3.64e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530402916 127 NNNKYYLIQLlEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 185
Cdd:COG3831   13 NSARFYELEV-EPDLFGGWSLTRRWGRIGTKGQTKTKTF-ASEEEALAALEKLVAEKLR 69
 
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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