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Conserved domains on  [gi|156523968|ref|NP_001609|]
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poly [ADP-ribose] polymerase 1 [Homo sapiens]

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
 6-1010 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: 848.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968    6 DKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDvEVDGFSELRWDDQQKV 85
Cdd:PLN03123    5 PKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSID-DVEGIDSLRWEDQQKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   86 KKTAEAGGvtgkGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKmVDPEKPQLGMidrWYHPGCFVK 165
Cdd:PLN03123   84 RKYVESGG----TGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSK-PEGQGYKGLA---WHHAKCFLE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  166 nreelgFRPEYSASQLKGFSLLATEDKEAL----KKQLPGVKSE------------GKRKGDEVD-------GVDEVAKK 222
Cdd:PLN03123  156 ------MSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEkaeerkqeskkgAKRKKDASGddkskkaKTDRDVST 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  223 KSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQL 302
Cdd:PLN03123  230 STAASQKKSSDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  303 VFKSDAYYCTGDVTAWTKCMVKTQTPNR--KEWVTPKEFRE---ISYLKKLKVKKQDRIFPPETSASvaatpppsTASAP 377
Cdd:PLN03123  310 LYSGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPDETDNqylRKWFKSQKSKKPERLLPPSSSNE--------SSGKQ 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  378 AAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSED 457
Cdd:PLN03123  382 AQSNSSDSESEFLGDLKVSIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVRED 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  458 FLQDVSASTKSLqelflahilspwgaevkaePVEvvaprgksgaalskkskgQVKEEGINKSEKRMKLTLKGGAAVDPDS 537
Cdd:PLN03123  462 YLVDCFKKKKKL-------------------PFD------------------KYKLEASGTSSSMVTVKVKGRSAVHEAS 504

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  538 GLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGT-VIGSNKLEQMpSKEDAIEHFMK 616
Cdd:PLN03123  505 GLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEM-SKSDAIHEFKR 583

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  617 LYEEKTGNAWHS----KNFTKYPKKFYPLEIDYGQDEEAVKKLTVnpGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEID 692
Cdd:PLN03123  584 LFLEKTGNPWESweqkTNFQKQPGKFYPLDIDYGVNEQPKKKAAS--GSKSNLAPRLVELMKMLFDVETYRAAMMEFEIN 661

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  693 LQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSD-----SQILDLSNRFYTLIP--HdfgmkkPPLLNNADSVQAKVEML 765
Cdd:PLN03123  662 MSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDpsireSLLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKML 735

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  766 DNLLDIEVAYSLLrgGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGEC 845
Cdd:PLN03123  736 EALQDIEIASRLV--GFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEF 813

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  846 QRYKPFKQ-LHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEV 924
Cdd:PLN03123  814 DKYAPYKEkLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEV 893

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  925 ALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISL-DGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLL 1003
Cdd:PLN03123  894 ALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWrDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLL 973


                  ....*..
gi 156523968 1004 KLKFNFK 1010
Cdd:PLN03123  974 KVRFKHK 980
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 6-1010 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 848.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968    6 DKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDvEVDGFSELRWDDQQKV 85
Cdd:PLN03123    5 PKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSID-DVEGIDSLRWEDQQKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   86 KKTAEAGGvtgkGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKmVDPEKPQLGMidrWYHPGCFVK 165
Cdd:PLN03123   84 RKYVESGG----TGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSK-PEGQGYKGLA---WHHAKCFLE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  166 nreelgFRPEYSASQLKGFSLLATEDKEAL----KKQLPGVKSE------------GKRKGDEVD-------GVDEVAKK 222
Cdd:PLN03123  156 ------MSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEkaeerkqeskkgAKRKKDASGddkskkaKTDRDVST 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  223 KSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQL 302
Cdd:PLN03123  230 STAASQKKSSDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  303 VFKSDAYYCTGDVTAWTKCMVKTQTPNR--KEWVTPKEFRE---ISYLKKLKVKKQDRIFPPETSASvaatpppsTASAP 377
Cdd:PLN03123  310 LYSGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPDETDNqylRKWFKSQKSKKPERLLPPSSSNE--------SSGKQ 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  378 AAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSED 457
Cdd:PLN03123  382 AQSNSSDSESEFLGDLKVSIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVRED 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  458 FLQDVSASTKSLqelflahilspwgaevkaePVEvvaprgksgaalskkskgQVKEEGINKSEKRMKLTLKGGAAVDPDS 537
Cdd:PLN03123  462 YLVDCFKKKKKL-------------------PFD------------------KYKLEASGTSSSMVTVKVKGRSAVHEAS 504

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  538 GLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGT-VIGSNKLEQMpSKEDAIEHFMK 616
Cdd:PLN03123  505 GLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEM-SKSDAIHEFKR 583

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  617 LYEEKTGNAWHS----KNFTKYPKKFYPLEIDYGQDEEAVKKLTVnpGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEID 692
Cdd:PLN03123  584 LFLEKTGNPWESweqkTNFQKQPGKFYPLDIDYGVNEQPKKKAAS--GSKSNLAPRLVELMKMLFDVETYRAAMMEFEIN 661

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  693 LQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSD-----SQILDLSNRFYTLIP--HdfgmkkPPLLNNADSVQAKVEML 765
Cdd:PLN03123  662 MSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDpsireSLLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKML 735

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  766 DNLLDIEVAYSLLrgGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGEC 845
Cdd:PLN03123  736 EALQDIEIASRLV--GFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEF 813

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  846 QRYKPFKQ-LHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEV 924
Cdd:PLN03123  814 DKYAPYKEkLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEV 893

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  925 ALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISL-DGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLL 1003
Cdd:PLN03123  894 ALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWrDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLL 973


                  ....*..
gi 156523968 1004 KLKFNFK 1010
Cdd:PLN03123  974 KVRFKHK 980
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 662-1006 0e+00

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: 575.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  662 KSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSS-DSQILDLSNRFYTLI 740
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  741 PHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSsKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKN 820
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDS-DDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  821 THATTHnAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM 900
Cdd:cd01437   160 THAPTT-EYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  901 VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISK-LPKGKHSVKGLGKTTPDPSAN-ISLDGVDVPLGTGISSG 978
Cdd:cd01437   239 FSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFeIDLDGVVVPLGKPVPSG 318

                         330       340
                  ....*....|....*....|....*....
gi 156523968  979 VN-DTSLLYNEYIVYDIAQVNLKYLLKLK 1006
Cdd:cd01437   319 HKtDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 808-1007 1.14e-96

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: 303.49  E-value: 1.14e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   808 SEEAEIIRKYVKNTHATTHnAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVT 887
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPTH-GYPLFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   888 GYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPsaNISLDGv 967
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAPES--FVDLDG- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 156523968   968 dVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKF 1007
Cdd:pfam00644  157 -VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 548-633 5.38e-25

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: 99.28  E-value: 5.38e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968    548 KGGKVFSATLGLVDIVKGTNSYYKLQLLEDDkENRYWIFRSWGRVGTViGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWH 627
Cdd:smart00773    1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKNGYE 78


                    ....*.
gi 156523968    628 SKNFTK 633
Cdd:smart00773   79 ERGKFV 84
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
559-622 5.22e-04

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 39.97  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156523968  559 LVDIVKGTNSYYKLQLLEDDKENryWIF-RSWGRVGTvIGSNKLEQMPSKEDAIEHFMKLYEEKT 622
Cdd:COG3831     7 RIDPAGNSARFYELEVEPDLFGG--WSLtRRWGRIGT-KGQTKTKTFASEEEALAALEKLVAEKL 68
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 6-1010 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 848.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968    6 DKLYRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRHPDvEVDGFSELRWDDQQKV 85
Cdd:PLN03123    5 PKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSID-DVEGIDSLRWEDQQKI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   86 KKTAEAGGvtgkGQDGIGSKAEKTLGDFAAEYAKSNRSTCKGCMEKIEKGQVRLSKKmVDPEKPQLGMidrWYHPGCFVK 165
Cdd:PLN03123   84 RKYVESGG----TGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSK-PEGQGYKGLA---WHHAKCFLE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  166 nreelgFRPEYSASQLKGFSLLATEDKEAL----KKQLPGVKSE------------GKRKGDEVD-------GVDEVAKK 222
Cdd:PLN03123  156 ------MSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEkaeerkqeskkgAKRKKDASGddkskkaKTDRDVST 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  223 KSKKEKDKDSKLEKALKAQNDLIWNIKDELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQL 302
Cdd:PLN03123  230 STAASQKKSSDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  303 VFKSDAYYCTGDVTAWTKCMVKTQTPNR--KEWVTPKEFRE---ISYLKKLKVKKQDRIFPPETSASvaatpppsTASAP 377
Cdd:PLN03123  310 LYSGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPDETDNqylRKWFKSQKSKKPERLLPPSSSNE--------SSGKQ 381

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  378 AAVNSSASADKPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCISTKKEVEKMNKKMEEVKEANIRVVSED 457
Cdd:PLN03123  382 AQSNSSDSESEFLGDLKVSIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVRED 461

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  458 FLQDVSASTKSLqelflahilspwgaevkaePVEvvaprgksgaalskkskgQVKEEGINKSEKRMKLTLKGGAAVDPDS 537
Cdd:PLN03123  462 YLVDCFKKKKKL-------------------PFD------------------KYKLEASGTSSSMVTVKVKGRSAVHEAS 504

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  538 GLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGT-VIGSNKLEQMpSKEDAIEHFMK 616
Cdd:PLN03123  505 GLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEM-SKSDAIHEFKR 583

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  617 LYEEKTGNAWHS----KNFTKYPKKFYPLEIDYGQDEEAVKKLTVnpGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEID 692
Cdd:PLN03123  584 LFLEKTGNPWESweqkTNFQKQPGKFYPLDIDYGVNEQPKKKAAS--GSKSNLAPRLVELMKMLFDVETYRAAMMEFEIN 661

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  693 LQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSD-----SQILDLSNRFYTLIP--HdfgmkkPPLLNNADSVQAKVEML 765
Cdd:PLN03123  662 MSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDpsireSLLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKML 735

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  766 DNLLDIEVAYSLLrgGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTHNAYDLEVIDIFKIEREGEC 845
Cdd:PLN03123  736 EALQDIEIASRLV--GFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEF 813

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  846 QRYKPFKQ-LHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEV 924
Cdd:PLN03123  814 DKYAPYKEkLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEV 893

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  925 ALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPSANISL-DGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLL 1003
Cdd:PLN03123  894 ALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWrDDVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLL 973


                  ....*..
gi 156523968 1004 KLKFNFK 1010
Cdd:PLN03123  974 KVRFKHK 980
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 662-1006 0e+00

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: 575.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  662 KSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSS-DSQILDLSNRFYTLI 740
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  741 PHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSsKDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKN 820
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDS-DDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKN 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  821 THATTHnAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM 900
Cdd:cd01437   160 THAPTT-EYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  901 VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISK-LPKGKHSVKGLGKTTPDPSAN-ISLDGVDVPLGTGISSG 978
Cdd:cd01437   239 FSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFeIDLDGVVVPLGKPVPSG 318

                         330       340
                  ....*....|....*....|....*....
gi 156523968  979 VN-DTSLLYNEYIVYDIAQVNLKYLLKLK 1006
Cdd:cd01437   319 HKtDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 436-1011 2.05e-175

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 526.33  E-value: 2.05e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  436 VEKMNKKMEEVKEANIRVVSEDFLQDVSASTKSLQELfLAHILSPWGAEVKaepvevVAPRGKSGAALSKKSKGQVKEeg 515
Cdd:PLN03124   69 VSPKRIAIDEVKGMTVRELREAASERGLATTGRKKDL-LERLCAALESDVK------VGSANGTGEDEKEKGGDEERE-- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  516 inKSEKRMKLTLKGGAAVD---PDSgLEHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRV 592
Cdd:PLN03124  140 --KEEKIVTATKKGRAVLDqwlPDH-IKSNYHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDGSKYMVYTRWGRV 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  593 GtVIGSNKLE-QMPSKEDAIEHFMKLYEEKTGNAWHS-KNFTKYPKKFYPLEIDYGQDEEAVKKLTVNPGTK----SKLP 666
Cdd:PLN03124  217 G-VKGQDKLHgPYDSREPAIREFEKKFYDKTKNHWSDrKNFISHPKKYTWLEMDYEDEEESKKDKPSVSSEDknkqSKLD 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  667 KPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQgSSDSQILDLSNRFYTLIPHDFGM 746
Cdd:PLN03124  296 PRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISR-SDRETLEELSGEFYTVIPHDFGF 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  747 KK--PPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSkDPIDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHAT 824
Cdd:PLN03124  375 KKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQD-DPLYAHYKRLNCELEPLDTDSEEFSMIAKYLENTHGQ 453

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  825 THNAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKS 904
Cdd:PLN03124  454 THSGYTLEIVQIFKVSREGEDERFQKFSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFGKGVYFADMFSKS 533

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  905 ANYCHTSQGDPIGLILLGEVALGNMYELKHAS-HISKLPKGKHSVKGLGKTTPDPS-ANISLDGVDVPLGTGISSGVNDT 982
Cdd:PLN03124  534 ANYCYASAANPDGVLLLCEVALGDMNELLQADyNANKLPPGKLSTKGVGRTVPDPSeAKTLEDGVVVPLGKPVESPYSKG 613

                         570       580
                  ....*....|....*....|....*....
gi 156523968  983 SLLYNEYIVYDIAQVNLKYLLKLKFNFKT 1011
Cdd:PLN03124  614 SLEYNEYIVYNVDQIRMRYVLQVKFNYKR 642
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 250-1010 1.46e-107

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 353.72  E-value: 1.46e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  250 DELKKVCSTNDLKELLIFNKQQVPSGESAILDRVADGMVFGALLPCEECSGQLVFKSDAYYCTGDVTAWTKCMVKTQTPN 329
Cdd:PLN03122   69 KAIEEHLSIEQMREILEENGQDSSGSDDAVLPRCQDQLFYGPLEKCPLCGGALECDGHRYTCTGFISEWSSCTFSTKNPP 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  330 RKE--WVTPKEFREiSYLKKLKVKKQDrifppetsasvaatpppsTASAPaaVNSSASADKPLSNMKILTLGKLSRNKDE 407
Cdd:PLN03122  149 RKEepLKIPDSVKN-SFITKLLKKHQD------------------PSKRP--KRELGAPGKPFSGMMISLSGRLSRTHQY 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  408 VKAMIEKLGGKLTGTANKASLCISTKKEVEK-MNKKMEEVKEANIRVVSEDFLQDvSASTKSLQELflahilspwgaevk 486
Cdd:PLN03122  208 WKKDIEKHGGKVANSVEGVTCLVVSPAERERgGSSKIAEAMERGIPVVREAWLID-SIEKQEAQPL-------------- 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  487 aEPVEVVAPRGKSGAALsKKSKGQVKEEGINKSEKRMKLTLKGGaaVDPDSGL-EHSAHVLEKGGKVFSATLGLVDIVKG 565
Cdd:PLN03122  273 -EAYDVVSDLSVEGRGI-PWDKQDPSEEAIESLSAELKLYGKRG--VYKDSKLqEEGGKIFEKDGILYNCAFSICDLGRG 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  566 TNSYYKLQLLEDDKENRYWIFRSwGRVGTVIGSN-KLEQMPSKEDAIEHFMKLYEEKTGN---AWH-SKNFTKYPKKFYP 640
Cdd:PLN03122  349 LNEYCIMQLITVPDSNLHLYYKK-GRVGDDPNAEeRLEEWEDVDAAIKEFVRLFEEITGNefePWErEKKFEKKRLKFYP 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  641 LEIDYGQDEEA----VKKLTVnPGTKSKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEV 716
Cdd:PLN03122  428 IDMDDGVDVRAgglgLRQLGV-AAAHCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEF 506

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  717 QQAVSQGSSDSQ-----ILDLSNRFYTLIP--HDFGMKKPPLLnnADSVQAKVEMLDnllDIEVAYSLLRGGSDDSSKDP 789
Cdd:PLN03122  507 AEFVKSEKETGQkaeamWLDFSNKWFSLVHstRPFVIRDIDEL--ADHAASALETVR---DINVASRLIGDMTGSTLDDP 581

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  790 IDVNYEKLKTDIKVVDRDSEEAEIIRKYVKNTHATTH---NAYDLEVIDIFKIEREGeCQRYKPFKQLHNRRLLWHGSRT 866
Cdd:PLN03122  582 LSDRYKKLGCSISPVDKESDDYKMIVKYLEKTYEPVKvgdVSYSVSVENIFAVESSA-GPSLDEIKKLPNKVLLWCGTRS 660

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  867 TNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALG-NMYELKHASH-ISKLPKG 944
Cdd:PLN03122  661 SNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAAAEAARYGFTAVDRPEGFLVLAVASLGdEVLELTKPPEdVKSYEEK 740

                         730       740       750       760       770       780
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156523968  945 KHSVKGLGKTTPDPSANISL-DGVDVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKFNFK 1010
Cdd:PLN03122  741 KVGVKGLGRKKTDESEHFKWrDDITVPCGRLIPSEHKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEK 807
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 808-1007 1.14e-96

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: 303.49  E-value: 1.14e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   808 SEEAEIIRKYVKNTHATTHnAYDLEVIDIFKIEREGECQRYKPFKQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVT 887
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPTH-GYPLFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   888 GYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPsaNISLDGv 967
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAPES--FVDLDG- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 156523968   968 dVPLGTGISSGVNDTSLLYNEYIVYDIAQVNLKYLLKLKF 1007
Cdd:pfam00644  157 -VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 663-794 1.47e-62

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: 208.15  E-value: 1.47e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   663 SKLPKPVQDLIKMIFDVESMKKAMVEYEIDLQKMPLGKLSKRQIQAAYSILSEVQQAVSQGSSD---SQILDLSNRFYTL 739
Cdd:pfam02877    1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAkakAKLEDLSNRFYTL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 156523968   740 IPHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSSKDPIDVNY 794
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 ...
 543-645 1.36e-54

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: 184.72  E-value: 1.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  543 AHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKT 622
Cdd:cd08001     1 AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGTTIGGNKLEEFSSLEEAKMAFEELYEEKT 80

                          90       100
                  ....*....|....*....|....
gi 156523968  623 GNAWHS-KNFTKYPKKFYPLEIDY 645
Cdd:cd08001    81 GNDFENrKNFKKKPGKFYPLDIDY 104
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 544-645 7.32e-32

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: 119.72  E-value: 7.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  544 HVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTViGSNKLEQMPSKEDAIEHFMKLYEEKTG 623
Cdd:cd07997     1 HVYGDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGER-GQSQLTPFGSLESAIKEFEKKFKDKTG 79

                          90       100
                  ....*....|....*....|...
gi 156523968  624 NAWHS-KNFTKYPKKFYPLEIDY 645
Cdd:cd07997    80 NEWENrPLFKKQPGKYALVELDY 102
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 554-627 6.03e-30

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: 113.14  E-value: 6.03e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523968  554 SATLGLVDIvkGTNSYYKLQLLEDDKENRYWIFRSWGRVGTVIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWH 627
Cdd:cd07994     1 KATLGFQDI--GSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYY 72
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 390-462 4.37e-28

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: 108.00  E-value: 4.37e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523968  390 LSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTAN-KASLCISTKKEVEKMNKKMEEVKEANIRVVSEDFLQDV 462
Cdd:cd17747     1 LTGMKFALIGKLSKSKDELKKLIEKLGGKVASKVTkKVTLCISTKAEVEKMSKKMKEAKEAGVPVVSEDFLEDC 74
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 12-87 9.14e-27

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: 104.71  E-value: 9.14e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968    12 EYAKSGRASCKKCSESIPKDSLRMAIMV---QSPMFDGKVPHWYHFSCFWKVGHSIRHPDVE------VDGFSELRWDDQ 82
Cdd:pfam00645    1 EYAKSGRAKCKGCKKKIEKGELRIGKVVdfvPSPFFDGGSKRWYHWGCFTKKQLKNRKETKEiddaddLDGFDELKDEDQ 80


                   ....*
gi 156523968    83 QKVKK 87
Cdd:pfam00645   81 EKIRK 85
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 548-633 5.38e-25

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: 99.28  E-value: 5.38e-25
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968    548 KGGKVFSATLGLVDIVKGTNSYYKLQLLEDDkENRYWIFRSWGRVGTViGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWH 627
Cdd:smart00773    1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKNGYE 78


                    ....*.
gi 156523968    628 SKNFTK 633
Cdd:smart00773   79 ERGKFV 84
PADR1 pfam08063
PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of ...
 280-331 1.19e-24

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: 97.26  E-value: 1.19e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 156523968   280 LDRVADGMVFGALLPCEECS-GQLVFKSDAYYCTGDVTAWTKCMVKTQTPNRK 331
Cdd:pfam08063    1 LDRCADGMLFGALEPCPECKnGQLVFNGSGYKCTGYVSEWTKCTYSTKDPKRK 53
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 116-199 1.22e-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: 98.54  E-value: 1.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   116 EYAKSNRSTCKGCMEKIEKGQVRLSKKMVDPEKPQ-LGMIDRWYHPGCFVK--NREELGFRPEYSASQLKGFSLLATEDK 192
Cdd:pfam00645    1 EYAKSGRAKCKGCKKKIEKGELRIGKVVDFVPSPFfDGGSKRWYHWGCFTKkqLKNRKETKEIDDADDLDGFDELKDEDQ 80


                   ....*..
gi 156523968   193 EALKKQL 199
Cdd:pfam00645   81 EKIRKAI 87
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 860-1001 2.94e-24

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: 99.17  E-value: 2.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  860 LWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGD----------------PIGLILLGE 923
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQhvfqngkpkvcgrelcVFGFLTLGV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  924 VALGNMYELKHA-SHISKLPKGKHSVKGLGKTTPdpsanisldgvdvplgtgissgvnDTSLLYNEYIVYD-IAQVNLKY 1001
Cdd:cd01341    82 MSGATEESSRVLfPRNFRGATGAEVVDLLVAMCR------------------------DALLLPREYIIFEpYSQVSIRY 137
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 553-633 3.13e-22

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: 91.53  E-value: 3.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968   553 FSATLGLVDIVKGTNSYYKLQLlEDDKENRYWIFRSWGRVGTvIGSNKLEQMPSKEDAIEHFMKLYEEKTGNAWHSKNFT 632
Cdd:pfam05406    1 YDLYLEQTDAARNSNKFYEIQV-EDDLFGGYSLFRRWGRIGT-RGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEF 78


                   .
gi 156523968   633 K 633
Cdd:pfam05406   79 E 79
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 544-645 2.09e-21

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-2 and similar proteins. Similar to PARP-1, PARP-2 is ubiquitously expressed and its activity is induced by DNA strand breaks. It also plays a role in cell differentiation, cell death, and maintaining genomic stability. Studies on mice deficient with PARP-2 shows that it is important in fat storage, T cell maturation, and spermatogenesis.


Pssm-ID: 153430  Cd Length: 103  Bit Score: 90.08  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  544 HVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKENRYWIFRSWGRVGTViGSNKLEQMPSK-EDAIEHFMKLYEEKT 622
Cdd:cd08003     1 HVYEEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKK-GQSSLVPCGSDlEQAKSLFEKKFLDKT 79

                          90       100
                  ....*....|....*....|....
gi 156523968  623 GNAWHSK-NFTKYPKKFYPLEIDY 645
Cdd:cd08003    80 KNEWEDRaNFEKVAGKYDLLEMDY 103
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 552-645 3.19e-14

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: 69.36  E-value: 3.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  552 VFSATLGLVDIVKGTNSYYKLQLLEDDKEnrYWIFRSWGRVGtVIGSNKL-EQMPSKEDAIEHFMKLYEEKTGNAWHSK- 629
Cdd:cd08002     8 DYDCMLNQTNIGHNNNKFYVIQLLESGKE--YYVWNRWGRVG-EKGQNKLkGPWDSLEGAIKDFEKKFKDKTKNNWEDRe 84

                          90
                  ....*....|....*.
gi 156523968  630 NFTKYPKKFYPLEIDY 645
Cdd:cd08002    85 NFVPHPGKYTLIEMDY 100
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 388-461 1.73e-10

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: 58.07  E-value: 1.73e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156523968   388 KPLSNMKILTLGKLSRNKDEVKAMIEKLGGKLTGTANKASLCIStkkeVEKMNKKMEEVKEANIRVVSEDFLQD 461
Cdd:pfam00533    4 KLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVI----VEARTKKYLKAKELGIPIVTEEWLLD 73
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 800-1003 8.84e-07

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: 51.05  E-value: 8.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  800 DIKVVDRDSEEAEIIRKYVKNTHAT-THNAYDleVIDIFKIE----REGECQRYKPFKQ----LHNRRLLWHGSRTTNfa 870
Cdd:cd01438    25 DKEYQSVEEEMQSTIREHRDGGNAGgIFNRYN--IIRIQKVVnkklRERYCHRQKEIAEenhnHHNERMLFHGSPFIN-- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  871 GILSQGL--RIAppeapVTGYMFGKGIYFADMVSKSANYCHtSQGDPIGL--------------ILLGEVALGNMYELKH 934
Cdd:cd01438   101 AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYVY-GIGGGTGCpthkdrscyvchrqMLFCRVTLGKSFLQFS 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156523968  935 ASHISKLPKGKHSVKGlgkttpDPSANisldgvdvplgtgissgvndtSLLYNEYIVYDIAQVNLKYLL 1003
Cdd:cd01438   175 AMKMAHAPPGHHSVIG------RPSVN---------------------GLAYAEYVIYRGEQAYPEYLI 216
BRCT smart00292
breast cancer carboxy-terminal domain;
388-461 4.62e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 45.44  E-value: 4.62e-06
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156523968    388 KPLSNMKILTLGKLSRN-KDEVKAMIEKLGGKLTGTANK--ASLCISTKKEVEKmnKKMEEVKEANIRVVSEDFLQD 461
Cdd:smart00292    2 KLFKGKTFYITGSFDKEeRDELKELIEALGGKVTSSLSSktTTHVIVGSPEGGK--LELLKAIALGIPIVKEEWLLD 76
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 859-948 1.19e-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: 45.39  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  859 LLWHGSRTTNFAGILSQGLRIAPpeAPVTGYMFGKGIYFADMVSKSANYCH-TSQGDPIGLILLGEVALGNmYELKHASH 937
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFDRRF--CGKHGTMYGKGSYFAKNASYSHQYSKkSPKADGLKEMFLARVLTGD-YTQGHPGY 77

                          90
                  ....*....|.
gi 156523968  938 ISKLPKGKHSV 948
Cdd:cd01439    78 RRPPLKPSGVE 88
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 393-461 1.56e-04

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: 40.81  E-value: 1.56e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  393 MKILTLGKLSRNKDEVKAMIEKLGGKLTGTAN-KASLCISTKKEVEkmnKKMEEVKEANIRVVSEDFLQD 461
Cdd:cd00027     1 LVICFSGLDDEEREELKKLIEALGGKVSESLSsKVTHLIAKSPSGE---KYYLAALAWGIPIVSPEWLLD 67
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 576-622 2.97e-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: 40.28  E-value: 2.97e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  576 EDDKENRYW-------------IFRSWGRVGTvIGSNKLEQMPSKEDAIEHFMKLYEEKT 622
Cdd:cd07996     9 PERNSARFYeielegdlfgewsLVRRWGRIGT-KGQSRTKTFDSEEEALKAAEKLIREKL 67
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
559-622 5.22e-04

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 39.97  E-value: 5.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156523968  559 LVDIVKGTNSYYKLQLLEDDKENryWIF-RSWGRVGTvIGSNKLEQMPSKEDAIEHFMKLYEEKT 622
Cdd:COG3831     7 RIDPAGNSARFYELEVEPDLFGG--WSLtRRWGRIGT-KGQTKTKTFASEEEALAALEKLVAEKL 68
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
377-460 1.23e-03

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 42.70  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  377 PAAVNSSASADKPLSNMKIL---TLGKLSRnkDEVKAMIEKLGGKLTGTankaslcIStKKE---V--EKMNKKMEEVKE 448
Cdd:COG0272   583 MEEEEAEAAADSPLAGKTFVltgTLETMTR--DEAKELIEALGGKVSGS-------VS-KKTdyvVagENAGSKLDKAEE 652

                          90
                  ....*....|...
gi 156523968  449 ANIRVVSED-FLQ 460
Cdd:COG0272   653 LGVPILDEAeFLE 665
BRCT_DNA_ligase_like cd17748
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ...
 390-460 8.17e-03

BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also called NAD(+)-dependent polydeoxyribonucleotide synthase, catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.


Pssm-ID: 349379 [Multi-domain]  Cd Length: 76  Bit Score: 36.31  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156523968  390 LSNMKILTLGKLSR-NKDEVKAMIEKLGGKLTGTANKA-------SLCISTKKEVEKMNKkmeevKEANIRVVSE-DFLQ 460
Cdd:cd17748     1 LAGKTFVFTGTLSSmSRDEAEELIEALGGKVQSSVSKKtdylvvgDNAGSKLKKGEELKA-----KGLGIKIISEeEFLD 75
 
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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