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Conserved domains on  [gi|1709741|sp|Q11208|]
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RecName: Full=Poly [ADP-ribose] polymerase; Short=PARP; AltName: Full=NAD(+) ADP-ribosyltransferase; Short=ADPRT; AltName: Full=Poly[ADP-ribose] synthase; AltName: Full=Protein ADP-ribosyltransferase

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03123 super family cl33639
poly [ADP-ribose] polymerase; Provisional
 1-996 0e+00

poly [ADP-ribose] polymerase; Provisional


The actual alignment was detected with superfamily member PLN03123:

Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 734.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741     1 MEIDLPFKVEYSKSSRASCKGCKNKIEAGILRIAAMVQSAFHDGKQPNWFHEQCFFQKQRP-TSAGDIENFENIRFEDQE 79
Cdd:PLN03123   2 AAPPKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQiKSIDDVEGIDSLRWEDQQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    80 RIKKAIdncttvisaGGSKKGAKRSKGENNAIKDFGIEYAKSGRASCRGCEQKILKDQIRIRKTVfdteVGMKYGGqPLW 159
Cdd:PLN03123  82 KIRKYV---------ESGGTGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSKP----EGQGYKG-LAW 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   160 HHVECFAqlrgELGWLDTGENLPGFQTLKSDDKADV----KKALPVIKDEGV-----SSAKKAK---------------- 214
Cdd:PLN03123 148 HHAKCFL----EMSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEKAeerkqESKKGAKrkkdasgddkskkakt 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   215 IEKIDEEDAASIK---ELTEKIKKQSKRLFKFRDEIKNEMSKDDMVALLEANNMEPVKGDSEkLLDQVADLLTFGALLPC 291
Cdd:PLN03123 224 DRDVSTSTAASQKkssDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELD-LRDRCADGMMFGALGPC 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   292 TDCKGrQLLFHKSGYLCNGDLTEWTKCTKLLKEPER--KSCKIP-----GYLKYKFLKDVRKNPEvraiRYIPPSTStil 364
Cdd:PLN03123 303 PLCSG-PLLYSGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPdetdnQYLRKWFKSQKSKKPE----RLLPPSSS--- 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   365 kNISLKKGDELDGPKVKRERppLYNIEIALI-APKEREGIVKDRISKLGGTVSTKITEKTTVvLSTPEEVERMSSRMKKA 443
Cdd:PLN03123 375 -NESSGKQAQSNSSDSESEF--LGDLKVSIVgASKEKVTEWKAKIEEAGGVFHATVKKDTNC-LVVCGELDDEDAEMRKA 450

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   444 KTLGLHVIPEDYL-EAVEQngagainyissmslcdwgtdpatritQEESKSSKSKSIYTKSVPKSMTLKIKDGLAVDPDS 522
Cdd:PLN03123 451 RRMKIPIVREDYLvDCFKK--------------------------KKKLPFDKYKLEASGTSSSMVTVKVKGRSAVHEAS 504

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   523 GLEDVAHVyVSRNKEKYNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSWGRIGT-TIGGNKLDNFSNLvDAIVQFK 601
Cdd:PLN03123 505 GLQDTGHI-LEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEMSKS-DAIHEFK 582

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   602 ELYLEKSGNHFE---NRENFVKVAGRMYPIDIDYAEDSKIDLSAEHDIKSKLPLSVQDIIKLMFDVDSMKRTMMEFDLDM 678
Cdd:PLN03123 583 RLFLEKTGNPWEsweQKTNFQKQPGKFYPLDIDYGVNEQPKKKAASGSKSNLAPRLVELMKMLFDVETYRAAMMEFEINM 662

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   679 EKMPLGKLSQKQIQSAYKVLTEIYELIQGGGTNAKF-----IDATNRFYTLIPhnfgTQSPPLLDTTEQVEQLRQMLDSL 753
Cdd:PLN03123 663 SEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSIresllVDASNRFFTLIP----SIHPHIIRDEDDLKSKVKMLEAL 738

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   754 IEIECAYSLLQTEDSKADinPIDKHYEQLKTKLEPLDKNSEEYILLQKYVKNTHAETHKLYDLEVVDIFKVARQGEARRY 833
Cdd:PLN03123 739 QDIEIASRLVGFDVDEDD--SLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKY 816

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   834 KPFK-KLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADMVSKSANYCCTSHHNSTGLMLLSEVALG 912
Cdd:PLN03123 817 APYKeKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALG 896

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   913 DMMECTAAKYVTKLPNDKHSCFGRGRTMPNPSESIIREDGVEIPLGKPITNDSLKSSLLYNEFIIYDIAQVNIQYMLRMN 992
Cdd:PLN03123 897 EIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVR 976


                 ....
gi 1709741   993 FKYK 996
Cdd:PLN03123 977 FKHK 980
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 1-996 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 734.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741     1 MEIDLPFKVEYSKSSRASCKGCKNKIEAGILRIAAMVQSAFHDGKQPNWFHEQCFFQKQRP-TSAGDIENFENIRFEDQE 79
Cdd:PLN03123   2 AAPPKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQiKSIDDVEGIDSLRWEDQQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    80 RIKKAIdncttvisaGGSKKGAKRSKGENNAIKDFGIEYAKSGRASCRGCEQKILKDQIRIRKTVfdteVGMKYGGqPLW 159
Cdd:PLN03123  82 KIRKYV---------ESGGTGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSKP----EGQGYKG-LAW 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   160 HHVECFAqlrgELGWLDTGENLPGFQTLKSDDKADV----KKALPVIKDEGV-----SSAKKAK---------------- 214
Cdd:PLN03123 148 HHAKCFL----EMSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEKAeerkqESKKGAKrkkdasgddkskkakt 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   215 IEKIDEEDAASIK---ELTEKIKKQSKRLFKFRDEIKNEMSKDDMVALLEANNMEPVKGDSEkLLDQVADLLTFGALLPC 291
Cdd:PLN03123 224 DRDVSTSTAASQKkssDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELD-LRDRCADGMMFGALGPC 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   292 TDCKGrQLLFHKSGYLCNGDLTEWTKCTKLLKEPER--KSCKIP-----GYLKYKFLKDVRKNPEvraiRYIPPSTStil 364
Cdd:PLN03123 303 PLCSG-PLLYSGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPdetdnQYLRKWFKSQKSKKPE----RLLPPSSS--- 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   365 kNISLKKGDELDGPKVKRERppLYNIEIALI-APKEREGIVKDRISKLGGTVSTKITEKTTVvLSTPEEVERMSSRMKKA 443
Cdd:PLN03123 375 -NESSGKQAQSNSSDSESEF--LGDLKVSIVgASKEKVTEWKAKIEEAGGVFHATVKKDTNC-LVVCGELDDEDAEMRKA 450

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   444 KTLGLHVIPEDYL-EAVEQngagainyissmslcdwgtdpatritQEESKSSKSKSIYTKSVPKSMTLKIKDGLAVDPDS 522
Cdd:PLN03123 451 RRMKIPIVREDYLvDCFKK--------------------------KKKLPFDKYKLEASGTSSSMVTVKVKGRSAVHEAS 504

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   523 GLEDVAHVyVSRNKEKYNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSWGRIGT-TIGGNKLDNFSNLvDAIVQFK 601
Cdd:PLN03123 505 GLQDTGHI-LEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEMSKS-DAIHEFK 582

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   602 ELYLEKSGNHFE---NRENFVKVAGRMYPIDIDYAEDSKIDLSAEHDIKSKLPLSVQDIIKLMFDVDSMKRTMMEFDLDM 678
Cdd:PLN03123 583 RLFLEKTGNPWEsweQKTNFQKQPGKFYPLDIDYGVNEQPKKKAASGSKSNLAPRLVELMKMLFDVETYRAAMMEFEINM 662

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   679 EKMPLGKLSQKQIQSAYKVLTEIYELIQGGGTNAKF-----IDATNRFYTLIPhnfgTQSPPLLDTTEQVEQLRQMLDSL 753
Cdd:PLN03123 663 SEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSIresllVDASNRFFTLIP----SIHPHIIRDEDDLKSKVKMLEAL 738

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   754 IEIECAYSLLQTEDSKADinPIDKHYEQLKTKLEPLDKNSEEYILLQKYVKNTHAETHKLYDLEVVDIFKVARQGEARRY 833
Cdd:PLN03123 739 QDIEIASRLVGFDVDEDD--SLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKY 816

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   834 KPFK-KLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADMVSKSANYCCTSHHNSTGLMLLSEVALG 912
Cdd:PLN03123 817 APYKeKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALG 896

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   913 DMMECTAAKYVTKLPNDKHSCFGRGRTMPNPSESIIREDGVEIPLGKPITNDSLKSSLLYNEFIIYDIAQVNIQYMLRMN 992
Cdd:PLN03123 897 EIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVR 976


                 ....
gi 1709741   993 FKYK 996
Cdd:PLN03123 977 FKHK 980
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 647-991 4.12e-170

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: 500.64  E-value: 4.12e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  647 KSKLPLSVQDIIKLMFDVDSMKRTMMEFDLDMEKMPLGKLSQKQIQSAYKVLTEIYELI-QGGGTNAKFIDATNRFYTLI 725
Cdd:cd01437   1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALkRGSSQGSQLEELSNEFYTLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  726 PHNFGTQSPPLLDTTEQVEQLRQMLDSLIEIECAYSLLQtEDSKADINPIDKHYEQLKTKLEPLDKNSEEYILLQKYVKN 805
Cdd:cd01437  81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLK-DDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKN 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  806 THAETHKlYDLEVVDIFKVARQGEARRYKPFKKLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADM 885
Cdd:cd01437 160 THAPTTE-YTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADM 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  886 VSKSANYCCTSHHNSTGLMLLSEVALGDMMECTAAKYVTK-LPNDKHSCFGRGRTMPNPSESIIREDGVEIPLGKPITND 964
Cdd:cd01437 239 FSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPVPSG 318

                       330       340
                ....*....|....*....|....*...
gi 1709741  965 SLK-SSLLYNEFIIYDIAQVNIQYMLRM 991
Cdd:cd01437 319 HKTdTSLLYNEYIVYDVAQVRLKYLLEV 346
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 793-993 7.20e-99

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: 308.88  E-value: 7.20e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    793 SEEYILLQKYVKNTHAETHKlYDLEVVDIFKVARQGEARRYKPFKKLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVT 872
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    873 GYMFGKGIYFADMVSKSANYCCTSHHNSTGLMLLSEVALGDMMECTAAKYVTKLPNDKHSCFGRGRTMPnpsESIIREDG 952
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAP---ESFVDLDG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1709741    953 VeiPLGKPITNDSLKSSLLYNEFIIYDIAQVNIQYMLRMNF 993
Cdd:pfam00644 157 V--PLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 534-619 1.18e-27

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


Pssm-ID: 214814  Cd Length: 84  Bit Score: 106.99  E-value: 1.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741     534 RNKEKYNVVLGITDIQKNKNSFYKLQLLESDmKNRFWVFRSWGRIGTTiGGNKLDNFSNLVDAIVQFKELYLEKSGNHFE 613
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 1709741     614 NRENFV 619
Cdd:smart00773  79 ERGKFV 84
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
546-607 4.21e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 37.27  E-value: 4.21e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709741  546 TDIQKNKNSFYKLQLlESDMKNRFWVFRSWGRIGTTiGGNKLDNFSNLVDAIVQFKELYLEK 607
Cdd:COG3831   8 IDPAGNSARFYELEV-EPDLFGGWSLTRRWGRIGTK-GQTKTKTFASEEEALAALEKLVAEK 67
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 1-996 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 734.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741     1 MEIDLPFKVEYSKSSRASCKGCKNKIEAGILRIAAMVQSAFHDGKQPNWFHEQCFFQKQRP-TSAGDIENFENIRFEDQE 79
Cdd:PLN03123   2 AAPPKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQiKSIDDVEGIDSLRWEDQQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    80 RIKKAIdncttvisaGGSKKGAKRSKGENNAIKDFGIEYAKSGRASCRGCEQKILKDQIRIRKTVfdteVGMKYGGqPLW 159
Cdd:PLN03123  82 KIRKYV---------ESGGTGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSKP----EGQGYKG-LAW 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   160 HHVECFAqlrgELGWLDTGENLPGFQTLKSDDKADV----KKALPVIKDEGV-----SSAKKAK---------------- 214
Cdd:PLN03123 148 HHAKCFL----EMSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEKAeerkqESKKGAKrkkdasgddkskkakt 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   215 IEKIDEEDAASIK---ELTEKIKKQSKRLFKFRDEIKNEMSKDDMVALLEANNMEPVKGDSEkLLDQVADLLTFGALLPC 291
Cdd:PLN03123 224 DRDVSTSTAASQKkssDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELD-LRDRCADGMMFGALGPC 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   292 TDCKGrQLLFHKSGYLCNGDLTEWTKCTKLLKEPER--KSCKIP-----GYLKYKFLKDVRKNPEvraiRYIPPSTStil 364
Cdd:PLN03123 303 PLCSG-PLLYSGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPdetdnQYLRKWFKSQKSKKPE----RLLPPSSS--- 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   365 kNISLKKGDELDGPKVKRERppLYNIEIALI-APKEREGIVKDRISKLGGTVSTKITEKTTVvLSTPEEVERMSSRMKKA 443
Cdd:PLN03123 375 -NESSGKQAQSNSSDSESEF--LGDLKVSIVgASKEKVTEWKAKIEEAGGVFHATVKKDTNC-LVVCGELDDEDAEMRKA 450

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   444 KTLGLHVIPEDYL-EAVEQngagainyissmslcdwgtdpatritQEESKSSKSKSIYTKSVPKSMTLKIKDGLAVDPDS 522
Cdd:PLN03123 451 RRMKIPIVREDYLvDCFKK--------------------------KKKLPFDKYKLEASGTSSSMVTVKVKGRSAVHEAS 504

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   523 GLEDVAHVyVSRNKEKYNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSWGRIGT-TIGGNKLDNFSNLvDAIVQFK 601
Cdd:PLN03123 505 GLQDTGHI-LEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEMSKS-DAIHEFK 582

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   602 ELYLEKSGNHFE---NRENFVKVAGRMYPIDIDYAEDSKIDLSAEHDIKSKLPLSVQDIIKLMFDVDSMKRTMMEFDLDM 678
Cdd:PLN03123 583 RLFLEKTGNPWEsweQKTNFQKQPGKFYPLDIDYGVNEQPKKKAASGSKSNLAPRLVELMKMLFDVETYRAAMMEFEINM 662

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   679 EKMPLGKLSQKQIQSAYKVLTEIYELIQGGGTNAKF-----IDATNRFYTLIPhnfgTQSPPLLDTTEQVEQLRQMLDSL 753
Cdd:PLN03123 663 SEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSIresllVDASNRFFTLIP----SIHPHIIRDEDDLKSKVKMLEAL 738

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   754 IEIECAYSLLQTEDSKADinPIDKHYEQLKTKLEPLDKNSEEYILLQKYVKNTHAETHKLYDLEVVDIFKVARQGEARRY 833
Cdd:PLN03123 739 QDIEIASRLVGFDVDEDD--SLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKY 816

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   834 KPFK-KLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADMVSKSANYCCTSHHNSTGLMLLSEVALG 912
Cdd:PLN03123 817 APYKeKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALG 896

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   913 DMMECTAAKYVTKLPNDKHSCFGRGRTMPNPSESIIREDGVEIPLGKPITNDSLKSSLLYNEFIIYDIAQVNIQYMLRMN 992
Cdd:PLN03123 897 EIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVR 976


                 ....
gi 1709741   993 FKYK 996
Cdd:PLN03123 977 FKHK 980
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 647-991 4.12e-170

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: 500.64  E-value: 4.12e-170
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  647 KSKLPLSVQDIIKLMFDVDSMKRTMMEFDLDMEKMPLGKLSQKQIQSAYKVLTEIYELI-QGGGTNAKFIDATNRFYTLI 725
Cdd:cd01437   1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALkRGSSQGSQLEELSNEFYTLI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  726 PHNFGTQSPPLLDTTEQVEQLRQMLDSLIEIECAYSLLQtEDSKADINPIDKHYEQLKTKLEPLDKNSEEYILLQKYVKN 805
Cdd:cd01437  81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLK-DDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKN 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  806 THAETHKlYDLEVVDIFKVARQGEARRYKPFKKLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADM 885
Cdd:cd01437 160 THAPTTE-YTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADM 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  886 VSKSANYCCTSHHNSTGLMLLSEVALGDMMECTAAKYVTK-LPNDKHSCFGRGRTMPNPSESIIREDGVEIPLGKPITND 964
Cdd:cd01437 239 FSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPVPSG 318

                       330       340
                ....*....|....*....|....*...
gi 1709741  965 SLK-SSLLYNEFIIYDIAQVNIQYMLRM 991
Cdd:cd01437 319 HKTdTSLLYNEYIVYDVAQVRLKYLLEV 346
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 506-996 2.49e-160

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 486.65  E-value: 2.49e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   506 KSMTLKIKDGLAVdPDSGLED---VAHVYVSRNKEKYNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSWGRIGTTi 582
Cdd:PLN03124 142 EKIVTATKKGRAV-LDQWLPDhikSNYHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDGSKYMVYTRWGRVGVK- 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   583 GGNKLDN-FSNLVDAIVQFKELYLEKSGNHFENRENFVKVAGRMYPIDIDYAEDS-----KIDLSAEHDIK-SKLPLSVQ 655
Cdd:PLN03124 220 GQDKLHGpYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDYEDEEeskkdKPSVSSEDKNKqSKLDPRVA 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   656 DIIKLMFDVDSMKRTMMEFDLDMEKMPLGKLSQKQIQSAYKVLTEIYELIQGGGTNaKFIDATNRFYTLIPHNFGTQS-- 733
Cdd:PLN03124 300 QFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISRSDRE-TLEELSGEFYTVIPHDFGFKKmr 378

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   734 PPLLDTTEQVEQLRQMLDSLIEIECAYSLLQtEDSKADINPIDKHYEQLKTKLEPLDKNSEEYILLQKYVKNTHAETHKL 813
Cdd:PLN03124 379 QFTIDTPQKLKHKLEMVEALGEIEIATKLLK-DDIGEQDDPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHGQTHSG 457

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   814 YDLEVVDIFKVARQGEARRYKPFKKLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADMVSKSANYC 893
Cdd:PLN03124 458 YTLEIVQIFKVSREGEDERFQKFSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYC 537

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   894 CTSHHNSTGLMLLSEVALGDMMECTAAKY-VTKLPNDKHSCFGRGRTMPNPSESIIREDGVEIPLGKPITNDSLKSSLLY 972
Cdd:PLN03124 538 YASAANPDGVLLLCEVALGDMNELLQADYnANKLPPGKLSTKGVGRTVPDPSEAKTLEDGVVVPLGKPVESPYSKGSLEY 617

                        490       500
                 ....*....|....*....|....
gi 1709741   973 NEFIIYDIAQVNIQYMLRMNFKYK 996
Cdd:PLN03124 618 NEYIVYNVDQIRMRYVLQVKFNYK 641
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 793-993 7.20e-99

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: 308.88  E-value: 7.20e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    793 SEEYILLQKYVKNTHAETHKlYDLEVVDIFKVARQGEARRYKPFKKLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVT 872
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    873 GYMFGKGIYFADMVSKSANYCCTSHHNSTGLMLLSEVALGDMMECTAAKYVTKLPNDKHSCFGRGRTMPnpsESIIREDG 952
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAP---ESFVDLDG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1709741    953 VeiPLGKPITNDSLKSSLLYNEFIIYDIAQVNIQYMLRMNF 993
Cdd:pfam00644 157 V--PLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 205-996 1.23e-75

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 265.51  E-value: 1.23e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   205 EGVSSAKKAKIEKIDEEDAASIKELTEKIKKQSKrlfKFRDEIKNEMSKDDMVALLEANNMEpVKGDSEKLLDQVADLLT 284
Cdd:PLN03122  32 EGEQSPKKAKKEKKQDDSGNGNGKSAEDAVKEFE---EFCKAIEEHLSIEQMREILEENGQD-SSGSDDAVLPRCQDQLF 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   285 FGALLPCTDCKGrQLLFHKSGYLCNGDLTEWTKCTKLLKEPERKS--CKIPGYLKYKFLKDVRKnpevrairyippstst 362
Cdd:PLN03122 108 YGPLEKCPLCGG-ALECDGHRYTCTGFISEWSSCTFSTKNPPRKEepLKIPDSVKNSFITKLLK---------------- 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   363 ilknislKKGDELDGPKVKRERP--PLYNIEIALIAPKER-EGIVKDRISKLGGTVSTKITEKTTVVLStPEEVER-MSS 438
Cdd:PLN03122 171 -------KHQDPSKRPKRELGAPgkPFSGMMISLSGRLSRtHQYWKKDIEKHGGKVANSVEGVTCLVVS-PAERERgGSS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   439 RMKKAKTLGLHVIPEDYL-EAVEQNGA---GAINYISSMSLCDWGTDPATRITQEESkssksksiytkSVPKSMTLKIKD 514
Cdd:PLN03122 243 KIAEAMERGIPVVREAWLiDSIEKQEAqplEAYDVVSDLSVEGRGIPWDKQDPSEEA-----------IESLSAELKLYG 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   515 GLAVDPDSGL-EDVAHVYvsrnkEK----YNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSwGRIGTTIGGN-KLD 588
Cdd:PLN03122 312 KRGVYKDSKLqEEGGKIF-----EKdgilYNCAFSICDLGRGLNEYCIMQLITVPDSNLHLYYKK-GRVGDDPNAEeRLE 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   589 NFSNLVDAIVQFKELYLEKSGNHFE--NREN-FVKVAGRMYPIDIDYAEDSK--------IDLSAEHdikSKLPLSVQDI 657
Cdd:PLN03122 386 EWEDVDAAIKEFVRLFEEITGNEFEpwEREKkFEKKRLKFYPIDMDDGVDVRagglglrqLGVAAAH---CKLDPKVANF 462

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   658 IKLMFDVDSMKRTMMEFDLDMEKMPLGKLSQKQIQSAYKVLTEIYELIQ-----GGGTNAKFIDATNRFYTLIPhnfgTQ 732
Cdd:PLN03122 463 MKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKseketGQKAEAMWLDFSNKWFSLVH----ST 538

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   733 SPPLLDTTEQVEQL-RQMLDSLIEIECAYSLL-QTEDSKADiNPIDKHYEQLKTKLEPLDKNSEEYILLQKYVKNTHaET 810
Cdd:PLN03122 539 RPFVIRDIDELADHaASALETVRDINVASRLIgDMTGSTLD-DPLSDRYKKLGCSISPVDKESDDYKMIVKYLEKTY-EP 616

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   811 HKLYDLE----VVDIFKVaRQGEARRYKPFKKLHNRRLLWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADMV 886
Cdd:PLN03122 617 VKVGDVSysvsVENIFAV-ESSAGPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAA 695

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741   887 SKSANYCCTSHHNSTGLMLLSEVALGD-MMECTAA-KYVTKLPNDKHSCFGRGRTMPNPSESIIREDGVEIPLGKPITND 964
Cdd:PLN03122 696 AEAARYGFTAVDRPEGFLVLAVASLGDeVLELTKPpEDVKSYEEKKVGVKGLGRKKTDESEHFKWRDDITVPCGRLIPSE 775

                        810       820       830
                 ....*....|....*....|....*....|..
gi 1709741   965 SLKSSLLYNEFIIYDIAQVNIQYMLRMNFKYK 996
Cdd:PLN03122 776 HKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEK 807
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 648-779 9.27e-56

Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 460732 [Multi-domain]  Cd Length: 135  Bit Score: 188.89  E-value: 9.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    648 SKLPLSVQDIIKLMFDVDSMKRTMMEFDLDMEKMPLGKLSQKQIQSAYKVLTEIYELIQGG---GTNAKFIDATNRFYTL 724
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPslaKAKAKLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1709741    725 IPHNFGTQSPPLLDTTEQVEQLRQMLDSLIEIECAYSLLQTEDSKADINPIDKHY 779
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKDSKSDDDEHPLDRHY 135
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 528-632 1.21e-51

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: 176.25  E-value: 1.21e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  528 AHVYvSRNKEKYNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSWGRIGTTIGGNKLDNFSNLVDAIVQFKELYLEK 607
Cdd:cd08001   1 AHVL-EEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGTTIGGNKLEEFSSLEEAKMAFEELYEEK 79

                        90       100
                ....*....|....*....|....*
gi 1709741  608 SGNHFENRENFVKVAGRMYPIDIDY 632
Cdd:cd08001  80 TGNDFENRKNFKKKPGKFYPLDIDY 104
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 534-619 1.18e-27

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


Pssm-ID: 214814  Cd Length: 84  Bit Score: 106.99  E-value: 1.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741     534 RNKEKYNVVLGITDIQKNKNSFYKLQLLESDmKNRFWVFRSWGRIGTTiGGNKLDNFSNLVDAIVQFKELYLEKSGNHFE 613
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 1709741     614 NRENFV 619
Cdd:smart00773  79 ERGKFV 84
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 529-632 2.26e-25

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: 101.25  E-value: 2.26e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  529 HVYvSRNKEKYNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSWGRIGTTiGGNKLDNF-SNLVDAIVQFKELYLEK 607
Cdd:cd08003   1 HVY-EEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKK-GQSSLVPCgSDLEQAKSLFEKKFLDK 78

                        90       100
                ....*....|....*....|....*
gi 1709741  608 SGNHFENRENFVKVAGRMYPIDIDY 632
Cdd:cd08003  79 TKNEWEDRANFEKVAGKYDLLEMDY 103
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 539-632 4.76e-25

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: 100.07  E-value: 4.76e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  539 YNVVLGITDIQKNKNSFYKLQLLESDMKNRFWVFRSWGRIGtTIGGNKLDNFSNLVDAIVQFKELYLEKSGNHFENRENF 618
Cdd:cd07997  10 YDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVG-ERGQSQLTPFGSLESAIKEFEKKFKDKTGNEWENRPLF 88

                        90
                ....*....|....
gi 1709741  619 VKVAGRMYPIDIDY 632
Cdd:cd07997  89 KKQPGKYALVELDY 102
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 117-199 2.22e-24

Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an important regulatory component of the cellular response to DNA damage. The amino-terminal region of Poly(ADP-ribose) polymerase consists of two PARP-type zinc fingers. This region acts as a DNA nick sensor.


Pssm-ID: 459887 [Multi-domain]  Cd Length: 87  Bit Score: 97.77  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    117 EYAKSGRASCRGCEQKILKDQIRIRKTVFDTEVGMKYGGQPLWHHVECFAQLRGELGW----LDTGENLPGFQTLKSDDK 192
Cdd:pfam00645   1 EYAKSGRAKCKGCKKKIEKGELRIGKVVDFVPSPFFDGGSKRWYHWGCFTKKQLKNRKetkeIDDADDLDGFDELKDEDQ 80


                  ....*..
gi 1709741    193 ADVKKAL 199
Cdd:pfam00645  81 EKIRKAI 87
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 539-619 2.42e-23

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: 94.62  E-value: 2.42e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741    539 YNVVLGITDIQKNKNSFYKLQLlESDMKNRFWVFRSWGRIGTtIGGNKLDNFSNLVDAIVQFKELYLEKSGNHFENRENF 618
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQV-EDDLFGGYSLFRRWGRIGT-RGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEF 78


                  .
gi 1709741    619 V 619
Cdd:pfam05406  79 E 79
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 387-461 9.28e-23

BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.


Pssm-ID: 349378 [Multi-domain]  Cd Length: 76  Bit Score: 92.59  E-value: 9.28e-23
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709741  387 LYNIEIALIA-PKEREGIVKDRISKLGGTVSTKITEKTTVVLSTPEEVERMSSRMKKAKTLGLHVIPEDYLEAVEQ 461
Cdd:cd17747   1 LTGMKFALIGkLSKSKDELKKLIEKLGGKVASKVTKKVTLCISTKAEVEKMSKKMKEAKEAGVPVVSEDFLEDCIK 76
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 10-85 2.58e-22

Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an important regulatory component of the cellular response to DNA damage. The amino-terminal region of Poly(ADP-ribose) polymerase consists of two PARP-type zinc fingers. This region acts as a DNA nick sensor.


Pssm-ID: 459887 [Multi-domain]  Cd Length: 87  Bit Score: 92.00  E-value: 2.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741     10 EYSKSSRASCKGCKNKIEAGILRIAAMV---QSAFHDGKQPNWFHEQCFFQKQ--------RPTSAGDIENFENIRFEDQ 78
Cdd:pfam00645   1 EYAKSGRAKCKGCKKKIEKGELRIGKVVdfvPSPFFDGGSKRWYHWGCFTKKQlknrketkEIDDADDLDGFDELKDEDQ 80


                  ....*..
gi 1709741     79 ERIKKAI 85
Cdd:pfam00645  81 EKIRKAI 87
PADR1 pfam08063
PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of ...
 276-328 5.47e-21

PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of this domain is unknown.


Pssm-ID: 462349 [Multi-domain]  Cd Length: 53  Bit Score: 86.86  E-value: 5.47e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1709741    276 LDQVADLLTFGALLPCTDCKGRQLLFHKSGYLCNGDLTEWTKCTKLLKEPERK 328
Cdd:pfam08063   1 LDRCADGMLFGALEPCPECKNGQLVFNGSGYKCTGYVSEWTKCTYSTKDPKRK 53
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 845-987 5.63e-21

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: 89.93  E-value: 5.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  845 LWHGSRLTNFAGILSHGLKIAPPEAPVTGYMFGKGIYFADMVSKSANYCCTS---HHNSTGLMLLSEVALGDMMECTAAK 921
Cdd:cd01341   2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCdgqHVFQNGKPKVCGRELCVFGFLTLGV 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709741  922 YVTKLPNDKHSCFGRGRTMPNPSESIIREDgveiplgkpitNDSLKSSLLYNEFIIYD-IAQVNIQY 987
Cdd:cd01341  82 MSGATEESSRVLFPRNFRGATGAEVVDLLV-----------AMCRDALLLPREYIIFEpYSQVSIRY 137
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 542-612 1.55e-18

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: 80.78  E-value: 1.55e-18
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1709741  542 VLGITDIqkNKNSFYKLQLLESDMKNRFWVFRSWGRIGTTIGGNKLDNFSNLVDAIVQFKELYLEKSGNHF 612
Cdd:cd07994   3 TLGFQDI--GSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGY 71
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 533-632 1.75e-17

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: 78.60  E-value: 1.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  533 SRNKEKYNVVLGITDIQKNKNSFYKLQLLESDmkNRFWVFRSWGRIGTTiGGNKLDNFSNLVD-AIVQFKELYLEKSGNH 611
Cdd:cd08002   3 AEVDEDYDCMLNQTNIGHNNNKFYVIQLLESG--KEYYVWNRWGRVGEK-GQNKLKGPWDSLEgAIKDFEKKFKDKTKNN 79

                        90       100
                ....*....|....*....|.
gi 1709741  612 FENRENFVKVAGRMYPIDIDY 632
Cdd:cd08002  80 WEDRENFVPHPGKYTLIEMDY 100
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 838-936 7.72e-06

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: 48.36  E-value: 7.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  838 KLHNRRLLWHGSRLTNfaGILSHGLKiapPEAPVTGYMFGKGIYFADMVSKSANYC--------CTSHHNSTGL-----M 904
Cdd:cd01438  85 NHHNERMLFHGSPFIN--AIIHKGFD---ERHAYIGGMFGAGIYFAENSSKSNQYVygigggtgCPTHKDRSCYvchrqM 159

                        90       100       110
                ....*....|....*....|....*....|..
gi 1709741  905 LLSEVALGDMMECTAAKYVTKLPNDKHSCFGR 936
Cdd:cd01438 160 LFCRVTLGKSFLQFSAMKMAHAPPGHHSVIGR 191
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 844-990 1.57e-05

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: 45.00  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709741  844 LLWHGSRLTNFAGILSHGLKIAPpeAPVTGYMFGKGIYFADMVSKSANYC-CTSHHNSTGLMLLSEVALGDmmectaaky 922
Cdd:cd01439   1 LLFHGTSADAVEAICRHGFDRRF--CGKHGTMYGKGSYFAKNASYSHQYSkKSPKADGLKEMFLARVLTGD--------- 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709741  923 vtklpndkhscFGRGRtmPNPSESIIREDGVEIPLGKPITNDSLKSSLlyneFIIYDIAQVNIQYMLR 990
Cdd:cd01439  70 -----------YTQGH--PGYRRPPLKPSGVELDRYDSCVDNVSNPSI----FVIFSDVQAYPEYLIT 120
E_set cd02688
Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the ...
 302-367 4.42e-05

Early set domain associated with the catalytic domain of sugar utilizing enzymes at either the N or C terminus; The E or "early" set domains of sugar utilizing enzymes are associated with different types of catalytic domains at either the N-terminal or C-terminal end. These domains may be related to the immunoglobulin and/or fibronectin type III superfamilies. Members of this family include alpha amylase, sialidase, galactose oxidase, cellulase, cellulose, hyaluronate lyase, chitobiase, and chitinase. A subset of these members were recently identified as members of the CBM48 (Carbohydrate Binding Module 48) family. Members of the CBM48 family include pullulanase, maltooligosyl trehalose synthase, starch branching enzyme, glycogen branching enzyme, glycogen debranching enzyme, isoamylase, and the beta subunit of AMP-activated protein kinase.


Pssm-ID: 199878 [Multi-domain]  Cd Length: 82  Bit Score: 42.92  E-value: 4.42e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709741  302 HKSGYLCNGDLTEWtKCTKLLKEPERK---SCKIP---GYLKYKFLKDVRKNPEVRAIRYIPPSTSTILKNI 367
Cdd:cd02688  11 AKSVYLIGSFNGWW-QAQALPMTKNGGgvwSATIPlplGTYEYKYVIDGGKNVLPYFDPYYVAGDGNSGASI 81
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 395-458 1.17e-03

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 38.50  E-value: 1.17e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709741  395 IAPKEREgIVKDRISKLGGTVSTKITEKTTVVLSTPEEVERmssRMKKAKTLGLHVIPEDYLEA 458
Cdd:cd00027   8 LDDEERE-ELKKLIEALGGKVSESLSSKVTHLIAKSPSGEK---YYLAALAWGIPIVSPEWLLD 67
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 549-607 1.62e-03

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


Pssm-ID: 153425  Cd Length: 74  Bit Score: 37.97  E-value: 1.62e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 1709741  549 QKNKNSFYKLQLlESDMKNRFWVFRSWGRIGTTiGGNKLDNFSNLVDAIVQFKELYLEK 607
Cdd:cd07996  10 ERNSARFYEIEL-EGDLFGEWSLVRRWGRIGTK-GQSRTKTFDSEEEALKAAEKLIREK 66
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 384-458 2.32e-03

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 37.66  E-value: 2.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709741    384 RPPLYNIEIAL--IAPKEREgIVKDRISKLGGTVSTKITEKTTVVLstpeeVERMSSRMKKAKTLGLHVIPEDYLEA 458
Cdd:pfam00533   3 EKLFSGKTFVItgLDGLERD-ELKELIEKLGGKVTDSLSKKTTHVI-----VEARTKKYLKAKELGIPIVTEEWLLD 73
BRCT_PARP4_like cd17726
BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also ...
 398-463 2.74e-03

BRCT domain of poly [ADP-ribose] polymerase 4 (PARP-4) and similar proteins; PARP-4, also termed 193 kDa vault protein, or ADP-ribosyltransferase diphtheria toxin-like 4 (ARTD4), or PARP-related/IalphaI-related H5/proline-rich (PH5P), or vault poly(ADP-ribose) polymerase (VPARP), shows poly(ADP-ribosyl)ation activity that catalyzes the formation of ADP-ribose polymers in response to DNA damage. PARP-4 is a component of the vault ribonucleoprotein particle, at least composed of MVP, PARP4 and one or more vault RNAs (vRNAs). The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this group.


Pssm-ID: 349358 [Multi-domain]  Cd Length: 85  Bit Score: 37.65  E-value: 2.74e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709741  398 KEREGIvKDRISKLGGTVSTKITEKTT-VVLSTPEEVErmSSRMKKAKTLGLHVIPEDYLEAVEQNG 463
Cdd:cd17726  18 KEKKKL-KKKITENGGIISYIINKKCThVVVNNAKALS--SYKCRMAQKYGIPVVSLDYIWKCVEAG 81
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
546-607 4.21e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 37.27  E-value: 4.21e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709741  546 TDIQKNKNSFYKLQLlESDMKNRFWVFRSWGRIGTTiGGNKLDNFSNLVDAIVQFKELYLEK 607
Cdd:COG3831   8 IDPAGNSARFYELEV-EPDLFGGWSLTRRWGRIGTK-GQTKTKTFASEEEALAALEKLVAEK 67
 
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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