NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20806109|ref|NP_031441|]
View 

poly [ADP-ribose] polymerase 1 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN03123 super family cl33639
poly [ADP-ribose] polymerase; Provisional
 9-1010 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: 825.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109     9 YRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRQPDvEVDGFSELRWDDQQKVKKT 88
Cdd:PLN03123    8 WKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSID-DVEGIDSLRWEDQQKIRKY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    89 AEAGGVA-GKGQDGSGGKAEKTLgdflaEYAKSNRSMCKGCLEKIEKGQMRLSKKmVDPEKPQLGMidrWYHPTCFVKkr 167
Cdd:PLN03123   87 VESGGTGtGTASDAAASSFEYGI-----EVAKTSRATCRRCSEKILKGEVRISSK-PEGQGYKGLA---WHHAKCFLE-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   168 delgFRPEYSASQLKGFSLLSAEDKEAL----KKQLPAIKNE------------GKRKGDEVDGTD------EVAKKKSK 225
Cdd:PLN03123  156 ----MSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEkaeerkqeskkgAKRKKDASGDDKskkaktDRDVSTST 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   226 KGKDKDSSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVF 305
Cdd:PLN03123  232 AASQKKSSDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPLLY 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   306 KSDAYYCTGDVTAWTKCMVKTQNPSR--KEWVTPKEFRE---ISYLKKLKVKKQDRIFPPESSAPAplalplsvTSAPTA 380
Cdd:PLN03123  312 SGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPDETDNqylRKWFKSQKSKKPERLLPPSSSNES--------SGKQAQ 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   381 VNSSAPADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAANVRVVCEDFL 460
Cdd:PLN03123  384 SNSSDSESEFLGDLKVSIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVREDYL 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   461 QDVSASTKSLqellsahslsswgaevkaepgevvapkgksaaPSKKskgaVKEEGVNKSEKRMKLTLKGGAAVDPDSGLE 540
Cdd:PLN03123  464 VDCFKKKKKL--------------------------------PFDK----YKLEASGTSSSMVTVKVKGRSAVHEASGLQ 507

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   541 HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGT-VIGSNKLEQMpSKEDAVEHFMKLYE 619
Cdd:PLN03123  508 DTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEM-SKSDAIHEFKRLFL 586

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   620 EKTGNAWHS----KNFTKYPKKFYPLEIDYGQDEEAVKKLTVkpGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQK 695
Cdd:PLN03123  587 EKTGNPWESweqkTNFQKQPGKFYPLDIDYGVNEQPKKKAAS--GSKSNLAPRLVELMKMLFDVETYRAAMMEFEINMSE 664

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   696 MPLGKLSRRQIQAAYSILSEVQQAVSQGS-----SESQILDLSNRFYTLIP--HdfgmkkPPLLNNADSVQAKVEMLDNL 768
Cdd:PLN03123  665 MPLGKLSKANIQKGFEALTEIQNLLKENDqdpsiRESLLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKMLEAL 738

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   769 LDIEVAYSLLrgGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRY 848
Cdd:PLN03123  739 QDIEIASRLV--GFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKY 816

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   849 KPFRQ-LHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALG 927
Cdd:PLN03123  817 APYKEkLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALG 896

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   928 NMYELKHASHISKLPKGKHSVKGLGKTTPDPSASITLEG-VEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLK 1006
Cdd:PLN03123  897 EIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDdVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVR 976


                  ....
gi 20806109  1007 FNFK 1010
Cdd:PLN03123  977 FKHK 980
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 9-1010 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 825.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109     9 YRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRQPDvEVDGFSELRWDDQQKVKKT 88
Cdd:PLN03123    8 WKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSID-DVEGIDSLRWEDQQKIRKY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    89 AEAGGVA-GKGQDGSGGKAEKTLgdflaEYAKSNRSMCKGCLEKIEKGQMRLSKKmVDPEKPQLGMidrWYHPTCFVKkr 167
Cdd:PLN03123   87 VESGGTGtGTASDAAASSFEYGI-----EVAKTSRATCRRCSEKILKGEVRISSK-PEGQGYKGLA---WHHAKCFLE-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   168 delgFRPEYSASQLKGFSLLSAEDKEAL----KKQLPAIKNE------------GKRKGDEVDGTD------EVAKKKSK 225
Cdd:PLN03123  156 ----MSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEkaeerkqeskkgAKRKKDASGDDKskkaktDRDVSTST 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   226 KGKDKDSSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVF 305
Cdd:PLN03123  232 AASQKKSSDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPLLY 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   306 KSDAYYCTGDVTAWTKCMVKTQNPSR--KEWVTPKEFRE---ISYLKKLKVKKQDRIFPPESSAPAplalplsvTSAPTA 380
Cdd:PLN03123  312 SGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPDETDNqylRKWFKSQKSKKPERLLPPSSSNES--------SGKQAQ 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   381 VNSSAPADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAANVRVVCEDFL 460
Cdd:PLN03123  384 SNSSDSESEFLGDLKVSIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVREDYL 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   461 QDVSASTKSLqellsahslsswgaevkaepgevvapkgksaaPSKKskgaVKEEGVNKSEKRMKLTLKGGAAVDPDSGLE 540
Cdd:PLN03123  464 VDCFKKKKKL--------------------------------PFDK----YKLEASGTSSSMVTVKVKGRSAVHEASGLQ 507

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   541 HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGT-VIGSNKLEQMpSKEDAVEHFMKLYE 619
Cdd:PLN03123  508 DTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEM-SKSDAIHEFKRLFL 586

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   620 EKTGNAWHS----KNFTKYPKKFYPLEIDYGQDEEAVKKLTVkpGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQK 695
Cdd:PLN03123  587 EKTGNPWESweqkTNFQKQPGKFYPLDIDYGVNEQPKKKAAS--GSKSNLAPRLVELMKMLFDVETYRAAMMEFEINMSE 664

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   696 MPLGKLSRRQIQAAYSILSEVQQAVSQGS-----SESQILDLSNRFYTLIP--HdfgmkkPPLLNNADSVQAKVEMLDNL 768
Cdd:PLN03123  665 MPLGKLSKANIQKGFEALTEIQNLLKENDqdpsiRESLLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKMLEAL 738

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   769 LDIEVAYSLLrgGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRY 848
Cdd:PLN03123  739 QDIEIASRLV--GFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKY 816

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   849 KPFRQ-LHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALG 927
Cdd:PLN03123  817 APYKEkLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALG 896

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   928 NMYELKHASHISKLPKGKHSVKGLGKTTPDPSASITLEG-VEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLK 1006
Cdd:PLN03123  897 EIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDdVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVR 976


                  ....
gi 20806109  1007 FNFK 1010
Cdd:PLN03123  977 FKHK 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: 565.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  662 KSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQAVSQGSS-ESQILDLSNRFYTLI 740
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  741 PHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSsKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKN 820
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDS-DDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  821 THATTHnAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM 900
Cdd:cd01437  160 THAPTT-EYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADM 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  901 VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISK-LPKGKHSVKGLGKTTPDPSAS-ITLEGVEVPLGTGIPSG 978
Cdd:cd01437  239 FSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFeIDLDGVVVPLGKPVPSG 318

                        330       340
                 ....*....|....*....|....*....
gi 20806109  979 VN-DTCLLYNEYIVYDIAQVNLKYLLKLK 1006
Cdd:cd01437  319 HKtDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 808-1007 1.96e-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: 302.72  E-value: 1.96e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    808 SEEAEVIRKYVKNTHATTHnAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVT 887
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPTH-GYPLFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    888 GYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPsaSITLEGv 967
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAPES--FVDLDG- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 20806109    968 eVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLKF 1007
Cdd:pfam00644  157 -VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 548-633 1.17e-24

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: 98.51  E-value: 1.17e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109     548 KGGKVFSATLGLVDIVKGTNSYYKLQLLEDDkESRYWIFRSWGRVGTViGSNKLEQMPSKEDAVEHFMKLYEEKTGNAWH 627
Cdd:smart00773    1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKNGYE 78


                    ....*.
gi 20806109     628 SKNFTK 633
Cdd:smart00773   79 ERGKFV 84
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
378-423 7.36e-04

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


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 43.47  E-value: 7.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 20806109  378 PTAVNSSAPADKPLSNMKI-LTlGKLSQ-NKDEAKAVIEKLGGKLTGS 423
Cdd:COG0272  583 MEEEEAEAAADSPLAGKTFvLT-GTLETmTRDEAKELIEALGGKVSGS 629
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 9-1010 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 825.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109     9 YRVEYAKSGRASCKKCSESIPKDSLRMAIMVQSPMFDGKVPHWYHFSCFWKVGHSIRQPDvEVDGFSELRWDDQQKVKKT 88
Cdd:PLN03123    8 WKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSID-DVEGIDSLRWEDQQKIRKY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    89 AEAGGVA-GKGQDGSGGKAEKTLgdflaEYAKSNRSMCKGCLEKIEKGQMRLSKKmVDPEKPQLGMidrWYHPTCFVKkr 167
Cdd:PLN03123   87 VESGGTGtGTASDAAASSFEYGI-----EVAKTSRATCRRCSEKILKGEVRISSK-PEGQGYKGLA---WHHAKCFLE-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   168 delgFRPEYSASQLKGFSLLSAEDKEAL----KKQLPAIKNE------------GKRKGDEVDGTD------EVAKKKSK 225
Cdd:PLN03123  156 ----MSPSTPVEKLSGWDTLSDSDQEAVlplvKKSPSEAKEEkaeerkqeskkgAKRKKDASGDDKskkaktDRDVSTST 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   226 KGKDKDSSKLEKALKAQNELIWNIKDELKKACSTNDLKELLIFNQQQVPSGESAILDRVADGMAFGALLPCKECSGQLVF 305
Cdd:PLN03123  232 AASQKKSSDLESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPLLY 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   306 KSDAYYCTGDVTAWTKCMVKTQNPSR--KEWVTPKEFRE---ISYLKKLKVKKQDRIFPPESSAPAplalplsvTSAPTA 380
Cdd:PLN03123  312 SGGMYRCQGYLSEWSKCSYSTLEPERikKKWKIPDETDNqylRKWFKSQKSKKPERLLPPSSSNES--------SGKQAQ 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   381 VNSSAPADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAANVRVVCEDFL 460
Cdd:PLN03123  384 SNSSDSESEFLGDLKVSIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVREDYL 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   461 QDVSASTKSLqellsahslsswgaevkaepgevvapkgksaaPSKKskgaVKEEGVNKSEKRMKLTLKGGAAVDPDSGLE 540
Cdd:PLN03123  464 VDCFKKKKKL--------------------------------PFDK----YKLEASGTSSSMVTVKVKGRSAVHEASGLQ 507

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   541 HSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGT-VIGSNKLEQMpSKEDAVEHFMKLYE 619
Cdd:PLN03123  508 DTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRVGNeKIGGNKLEEM-SKSDAIHEFKRLFL 586

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   620 EKTGNAWHS----KNFTKYPKKFYPLEIDYGQDEEAVKKLTVkpGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQK 695
Cdd:PLN03123  587 EKTGNPWESweqkTNFQKQPGKFYPLDIDYGVNEQPKKKAAS--GSKSNLAPRLVELMKMLFDVETYRAAMMEFEINMSE 664

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   696 MPLGKLSRRQIQAAYSILSEVQQAVSQGS-----SESQILDLSNRFYTLIP--HdfgmkkPPLLNNADSVQAKVEMLDNL 768
Cdd:PLN03123  665 MPLGKLSKANIQKGFEALTEIQNLLKENDqdpsiRESLLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKMLEAL 738

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   769 LDIEVAYSLLrgGSDDSSKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRY 848
Cdd:PLN03123  739 QDIEIASRLV--GFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKY 816

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   849 KPFRQ-LHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALG 927
Cdd:PLN03123  817 APYKEkLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALG 896

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   928 NMYELKHASHISKLPKGKHSVKGLGKTTPDPSASITLEG-VEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLK 1006
Cdd:PLN03123  897 EIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDdVVVPCGKPVPSKVKASELMYNEYIVYNTAQVKLQFLLKVR 976


                  ....
gi 20806109  1007 FNFK 1010
Cdd:PLN03123  977 FKHK 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: 565.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  662 KSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQAVSQGSS-ESQILDLSNRFYTLI 740
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  741 PHDFGMKKPPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSsKDPIDVNYEKLKTDIKVVDRDSEEAEVIRKYVKN 820
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDS-DDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKN 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  821 THATTHnAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADM 900
Cdd:cd01437  160 THAPTT-EYTVEVQEIFRVEREGETDRFKPFKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADM 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  901 VSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISK-LPKGKHSVKGLGKTTPDPSAS-ITLEGVEVPLGTGIPSG 978
Cdd:cd01437  239 FSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFeIDLDGVVVPLGKPVPSG 318

                        330       340
                 ....*....|....*....|....*....
gi 20806109  979 VN-DTCLLYNEYIVYDIAQVNLKYLLKLK 1006
Cdd:cd01437  319 HKtDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 406-1011 1.12e-176

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 529.41  E-value: 1.12e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   406 KDEAKAVIEKLGGKLTGSANKASLCISTKKEVEKMSKKMEEVKAANVRVVCEdflqdvSASTKSLQELLSAHSLSSWGAE 485
Cdd:PLN03124   38 EDAKTASKSGTKSSAGRKKRRERQDDGDDEPVSPKRIAIDEVKGMTVRELRE------AASERGLATTGRKKDLLERLCA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   486 VKAEPGEVVAPKGKSAAPSKKSKGAVKEegvnKSEKRMKLTLKGGAAVD---PDSgLEHSAHVLEKGGKVFSATLGLVDI 562
Cdd:PLN03124  112 ALESDVKVGSANGTGEDEKEKGGDEERE----KEEKIVTATKKGRAVLDqwlPDH-IKSNYHVLEEGDDVYDAMLNQTNV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   563 VKGTNSYYKLQLLEDDKESRYWIFRSWGRVGtVIGSNKLE-QMPSKEDAVEHFMKLYEEKTGNAWHS-KNFTKYPKKFYP 640
Cdd:PLN03124  187 GDNNNKFYVLQVLESDDGSKYMVYTRWGRVG-VKGQDKLHgPYDSREPAIREFEKKFYDKTKNHWSDrKNFISHPKKYTW 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   641 LEIDYGQDEEAVKKLTV----KPGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEV 716
Cdd:PLN03124  266 LEMDYEDEEESKKDKPSvsseDKNKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRI 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   717 QQAVSQGSSEsQILDLSNRFYTLIPHDFGMKK--PPLLNNADSVQAKVEMLDNLLDIEVAYSLLRGGSDDSsKDPIDVNY 794
Cdd:PLN03124  346 AEVISRSDRE-TLEELSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQ-DDPLYAHY 423

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   795 EKLKTDIKVVDRDSEEAEVIRKYVKNTHATTHNAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILS 874
Cdd:PLN03124  424 KRLNCELEPLDTDSEEFSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQKFSSTKNRMLLWHGSRLTNWTGILS 503

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   875 QGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHAS-HISKLPKGKHSVKGLGK 953
Cdd:PLN03124  504 QGLRIAPPEAPSTGYMFGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGDMNELLQADyNANKLPPGKLSTKGVGR 583

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 20806109   954 TTPDPSASITLE-GVEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLKFNFKT 1011
Cdd:PLN03124  584 TVPDPSEAKTLEdGVVVPLGKPVESPYSKGSLEYNEYIVYNVDQIRMRYVLQVKFNYKR 642
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 190-1010 6.97e-102

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 338.31  E-value: 6.97e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   190 EDKEALKKQlpaiKNEGKRKGDEVDGTDEVAKKKSKKGKDKDSSKLEKALKAQNELIWNIKDElkkaCSTNDLKELLIFN 269
Cdd:PLN03122   16 EGKGGTRKQ----KAENKEHEGEQSPKKAKKEKKQDDSGNGNGKSAEDAVKEFEEFCKAIEEH----LSIEQMREILEEN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   270 QQQVPSGESAILDRVADGMAFGALLPCKECSGQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRKE--WVTPKEFREiSYLK 347
Cdd:PLN03122   88 GQDSSGSDDAVLPRCQDQLFYGPLEKCPLCGGALECDGHRYTCTGFISEWSSCTFSTKNPPRKEepLKIPDSVKN-SFIT 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   348 KLKVKKQDrifppessapaPLALPLSVTSAPtavnssapaDKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKA 427
Cdd:PLN03122  167 KLLKKHQD-----------PSKRPKRELGAP---------GKPFSGMMISLSGRLSRTHQYWKKDIEKHGGKVANSVEGV 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   428 SLCISTKKEVEK-MSKKMEEVKAANVRVVCEDFLQDvSASTKSLQELlsahslsswgaevkaEPGEVVA---PKGKSAAP 503
Cdd:PLN03122  227 TCLVVSPAERERgGSSKIAEAMERGIPVVREAWLID-SIEKQEAQPL---------------EAYDVVSdlsVEGRGIPW 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   504 SKKSKgavKEEGVNKSEKRMKLTLKGGaaVDPDSGL-EHSAHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESR 582
Cdd:PLN03122  291 DKQDP---SEEAIESLSAELKLYGKRG--VYKDSKLqEEGGKIFEKDGILYNCAFSICDLGRGLNEYCIMQLITVPDSNL 365

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   583 YWIFRSwGRVGTVIGSN-KLEQMPSKEDAVEHFMKLYEEKTGN---AWH-SKNFTKYPKKFYPLEIDYGQDEEA----VK 653
Cdd:PLN03122  366 HLYYKK-GRVGDDPNAEeRLEEWEDVDAAIKEFVRLFEEITGNefePWErEKKFEKKRLKFYPIDMDDGVDVRAgglgLR 444

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   654 KLTVKpGTKSKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQAV-----SQGSSESQ 728
Cdd:PLN03122  445 QLGVA-AAHCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVksekeTGQKAEAM 523

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   729 ILDLSNRFYTLIP--HDFGMKKPPLLnnADSVQAKVEMLDnllDIEVAYSLLRGGSDDSSKDPIDVNYEKLKTDIKVVDR 806
Cdd:PLN03122  524 WLDFSNKWFSLVHstRPFVIRDIDEL--ADHAASALETVR---DINVASRLIGDMTGSTLDDPLSDRYKKLGCSISPVDK 598

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   807 DSEEAEVIRKYVKNTHATTH---NAYDLEVIDIFKIEREGeSQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPE 883
Cdd:PLN03122  599 ESDDYKMIVKYLEKTYEPVKvgdVSYSVSVENIFAVESSA-GPSLDEIKKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCS 677

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109   884 APVTGYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALG-NMYELKHASH-ISKLPKGKHSVKGLGKTTPDPSAS 961
Cdd:PLN03122  678 LPVPGYMFGKAIVCSDAAAEAARYGFTAVDRPEGFLVLAVASLGdEVLELTKPPEdVKSYEEKKVGVKGLGRKKTDESEH 757

                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|
gi 20806109   962 ITLE-GVEVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLKFNFK 1010
Cdd:PLN03122  758 FKWRdDITVPCGRLIPSEHKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEK 807
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 808-1007 1.96e-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: 302.72  E-value: 1.96e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    808 SEEAEVIRKYVKNTHATTHnAYDLEVIDIFKIEREGESQRYKPFRQLHNRRLLWHGSRTTNFAGILSQGLRIAPPEAPVT 887
Cdd:pfam00644    1 SEEYQIIEKYFLSTHDPTH-GYPLFILEIFRVQRDGEWERFQPKKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    888 GYMFGKGIYFADMVSKSANYCHTSQGDPIGLILLGEVALGNMYELKHASHISKLPKGKHSVKGLGKTTPDPsaSITLEGv 967
Cdd:pfam00644   80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAPES--FVDLDG- 156

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 20806109    968 eVPLGTGIPSGVNDTCLLYNEYIVYDIAQVNLKYLLKLKF 1007
Cdd:pfam00644  157 -VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 663-794 5.20e-60

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: 201.21  E-value: 5.20e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    663 SKLPKPVQELVGMIFDVESMKKALVEYEIDLQKMPLGKLSRRQIQAAYSILSEVQQAVSQGSS---ESQILDLSNRFYTL 739
Cdd:pfam02877    1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLakaKAKLEDLSNRFYTL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 20806109    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 3.59e-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: 183.57  E-value: 3.59e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  543 AHVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGSNKLEQMPSKEDAVEHFMKLYEEKT 622
Cdd:cd08001    1 AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGTTIGGNKLEEFSSLEEAKMAFEELYEEKT 80

                         90       100
                 ....*....|....*....|....
gi 20806109  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 3.40e-31

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins 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: 117.79  E-value: 3.40e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  544 HVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTViGSNKLEQMPSKEDAVEHFMKLYEEKTG 623
Cdd:cd07997    1 HVYGDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGER-GQSQLTPFGSLESAIKEFEKKFKDKTG 79

                         90       100
                 ....*....|....*....|...
gi 20806109  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 5.27e-29

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: 110.44  E-value: 5.27e-29
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20806109  554 SATLGLVDIvkGTNSYYKLQLLEDDKESRYWIFRSWGRVGTVIGSNKLEQMPSKEDAVEHFMKLYEEKTGNAWH 627
Cdd:cd07994    1 KATLGFQDI--GSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYY 72
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 12-87 4.41e-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: 105.48  E-value: 4.41e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109     12 EYAKSGRASCKKCSESIPKDSLRMAIMV---QSPMFDGKVPHWYHFSCFWKVGHSIRQPDVE------VDGFSELRWDDQ 82
Cdd:pfam00645    1 EYAKSGRAKCKGCKKKIEKGELRIGKVVdfvPSPFFDGGSKRWYHWGCFTKKQLKNRKETKEiddaddLDGFDELKDEDQ 80


                   ....*
gi 20806109     83 QKVKK 87
Cdd:pfam00645   81 EKIRK 85
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 391-463 2.29e-26

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: 102.99  E-value: 2.29e-26
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20806109  391 LSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSAN-KASLCISTKKEVEKMSKKMEEVKAANVRVVCEDFLQDV 463
Cdd:cd17747    1 LTGMKFALIGKLSKSKDELKKLIEKLGGKVASKVTkKVTLCISTKAEVEKMSKKMKEAKEAGVPVVSEDFLEDC 74
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 860-1001 4.39e-25

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: 101.87  E-value: 4.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  860 LWHGSRTTNFAGILSQGLRIAPPEAPVTGYMFGKGIYFADMVSKSANYCHTSQGD----------------PIGLILLGE 923
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQhvfqngkpkvcgrelcVFGFLTLGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  924 VALGNMYELKHA-SHISKLPKGKHSVKGLGKTTPdpsasitlegvevplgtgipsgvnDTCLLYNEYIVYD-IAQVNLKY 1001
Cdd:cd01341   82 MSGATEESSRVLfPRNFRGATGAEVVDLLVAMCR------------------------DALLLPREYIIFEpYSQVSIRY 137
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 116-199 7.69e-25

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: 99.31  E-value: 7.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    116 EYAKSNRSMCKGCLEKIEKGQMRLSKKMVDPEKPQ-LGMIDRWYHPTCFVKKR--DELGFRPEYSASQLKGFSLLSAEDK 192
Cdd:pfam00645    1 EYAKSGRAKCKGCKKKIEKGELRIGKVVDFVPSPFfDGGSKRWYHWGCFTKKQlkNRKETKEIDDADDLDGFDELKDEDQ 80


                   ....*..
gi 20806109    193 EALKKQL 199
Cdd:pfam00645   81 EKIRKAI 87
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 548-633 1.17e-24

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: 98.51  E-value: 1.17e-24
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109     548 KGGKVFSATLGLVDIVKGTNSYYKLQLLEDDkESRYWIFRSWGRVGTViGSNKLEQMPSKEDAVEHFMKLYEEKTGNAWH 627
Cdd:smart00773    1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTK-GQTKLKTFDSLEDAIKEFEKLFKEKTKNGYE 78


                    ....*.
gi 20806109     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 ...
 281-332 2.12e-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: 96.87  E-value: 2.12e-24
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 20806109    281 LDRVADGMAFGALLPCKECS-GQLVFKSDAYYCTGDVTAWTKCMVKTQNPSRK 332
Cdd:pfam08063    1 LDRCADGMLFGALEPCPECKnGQLVFNGSGYKCTGYVSEWTKCTYSTKDPKRK 53
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 553-633 5.55e-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: 90.76  E-value: 5.55e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109    553 FSATLGLVDIVKGTNSYYKLQLlEDDKESRYWIFRSWGRVGTvIGSNKLEQMPSKEDAVEHFMKLYEEKTGNAWHSKNFT 632
Cdd:pfam05406    1 YDLYLEQTDAARNSNKFYEIQV-EDDLFGGYSLFRRWGRIGT-RGQTKLKSFDSLEEAIKEFEKLFAEKTKKGYRERGEF 78


                   .
gi 20806109    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 7.85e-22

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: 91.23  E-value: 7.85e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  544 HVLEKGGKVFSATLGLVDIVKGTNSYYKLQLLEDDKESRYWIFRSWGRVGTViGSNKLEQMPSK-EDAVEHFMKLYEEKT 622
Cdd:cd08003    1 HVYEEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKK-GQSSLVPCGSDlEQAKSLFEKKFLDKT 79

                         90       100
                 ....*....|....*....|....
gi 20806109  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 9.32e-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: 68.20  E-value: 9.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  552 VFSATLGLVDIVKGTNSYYKLQLLEDDKEsrYWIFRSWGRVGtVIGSNKL-EQMPSKEDAVEHFMKLYEEKTGNAWHSK- 629
Cdd:cd08002    8 DYDCMLNQTNIGHNNNKFYVIQLLESGKE--YYVWNRWGRVG-EKGQNKLkGPWDSLEGAIKDFEKKFKDKTKNNWEDRe 84

                         90
                 ....*....|....*.
gi 20806109  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 ...
 386-462 5.66e-09

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: 53.45  E-value: 5.66e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20806109    386 PADKPLSNMKILTLGKLSQNKDEAKAVIEKLGGKLTGSANKASLCIStkkeVEKMSKKMEEVKAANVRVVCEDFLQD 462
Cdd:pfam00533    1 PKEKLFSGKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVI----VEARTKKYLKAKELGIPIVTEEWLLD 73
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 20806109  859 LLWHGSRTTNFAGILSQGLRIAPpeAPVTGYMFGKGIYFADMVSKSANYCH-TSQGDPIGLILLGEVALGNmYELKHASH 937
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRF--CGKHGTMYGKGSYFAKNASYSHQYSKkSPKADGLKEMFLARVLTGD-YTQGHPGY 77

                         90
                 ....*....|.
gi 20806109  938 ISKLPKGKHSV 948
Cdd:cd01439   78 RRPPLKPSGVE 88
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 800-1003 1.28e-05

Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 poly-ADP-ribosylates Telomere Repeat Binding Factor 1 (TRF1) while Tankyrase 2 can poly-ADP-ribosylate itself or TRF1. The tankyrases also contain multiple ankyrin repeats that mediate protein-protein interaction (binding TRF1 and insulin-responsive aminopeptidase) and may function as a complex. Overexpression of Tank1 promotes increased telomere length when overexpressed, while overexpressed Tank2 has been shown to promote PARP cleavage- independent cell death (necrosis).


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 47.59  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  800 DIKVVDRDSEEAEVIRKYVKNTHAT-THNAYDleVIDIFKIEREGESQRYKpFRQ---------LHNRRLLWHGSRTTNf 869
Cdd:cd01438   25 DKEYQSVEEEMQSTIREHRDGGNAGgIFNRYN--IIRIQKVVNKKLRERYC-HRQkeiaeenhnHHNERMLFHGSPFIN- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  870 aGILSQGL--RIAppeapVTGYMFGKGIYFADMVSKSANYCHtSQGDPIGL--------------ILLGEVALGNMYELK 933
Cdd:cd01438  101 -AIIHKGFdeRHA-----YIGGMFGAGIYFAENSSKSNQYVY-GIGGGTGCpthkdrscyvchrqMLFCRVTLGKSFLQF 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20806109  934 HASHISKLPKGKHSVKGlgkttpDPSASitlegvevplgtgipsgvndtCLLYNEYIVYDIAQVNLKYLL 1003
Cdd:cd01438  174 SAMKMAHAPPGHHSVIG------RPSVN---------------------GLAYAEYVIYRGEQAYPEYLI 216
BRCT smart00292
breast cancer carboxy-terminal domain;
389-462 2.01e-05

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 43.52  E-value: 2.01e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20806109     389 KPLSNMKILTLGKLSQN-KDEAKAVIEKLGGKLTGSANK--ASLCISTKKEVEKmsKKMEEVKAANVRVVCEDFLQD 462
Cdd:smart00292    2 KLFKGKTFYITGSFDKEeRDELKELIEALGGKVTSSLSSktTTHVIVGSPEGGK--LELLKAIALGIPIVKEEWLLD 76
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 569-622 3.98e-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: 39.89  E-value: 3.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 20806109  569 YYKLQLlEDDKESRYWIFRSWGRVGTvIGSNKLEQMPSKEDAVEHFMKLYEEKT 622
Cdd:cd07996   16 FYEIEL-EGDLFGEWSLVRRWGRIGT-KGQSRTKTFDSEEEALKAAEKLIREKL 67
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
378-423 7.36e-04

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


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 43.47  E-value: 7.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 20806109  378 PTAVNSSAPADKPLSNMKI-LTlGKLSQ-NKDEAKAVIEKLGGKLTGS 423
Cdd:COG0272  583 MEEEEAEAAADSPLAGKTFvLT-GTLETmTRDEAKELIEALGGKVSGS 629
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
559-622 1.29e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 38.81  E-value: 1.29e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20806109  559 LVDIVKGTNSYYKLQLLEDDKESryWIF-RSWGRVGTvIGSNKLEQMPSKEDAVEHFMKLYEEKT 622
Cdd:COG3831    7 RIDPAGNSARFYELEVEPDLFGG--WSLtRRWGRIGT-KGQTKTKTFASEEEALAALEKLVAEKL 68
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH