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Conserved domains on  [gi|255560005|ref|XP_002521021|]
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poly [ADP-ribose] polymerase 1 [Ricinus communis]

Protein Classification

PLN03123 family protein( domain architecture ID 11477448)

PLN03123 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 1-982 0e+00

poly [ADP-ribose] polymerase; Provisional


:

Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 1952.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005   1 MAAPPKPWKAEYAKSGRSSCKTCKKPIDKEKLRLGKMVQATQFDGFMPMWNHESCVLKKAKQIKSIDDVEGIDSLRWEDQ 80
Cdd:PLN03123   1 MAAPPKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSIDDVEGIDSLRWEDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  81 QKIRKCVEGGGIATQDANANALNVMEYGIEVSQTSRATCRRCSQKILKGQVRISSKPDEPRAKALAWHHADCFIDLHPSV 160
Cdd:PLN03123  81 QKIRKYVESGGTGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSKPEGQGYKGLAWHHAKCFLEMSPST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 161 QVEKMSGWESLPPSDQEAVRALIKEVPSTAKAGIVEERKSTSAVGAKRKKDGGGDQKPKITRTDGDVSTSRNASAKNSND 240
Cdd:PLN03123 161 PVEKLSGWDTLSDSDQEAVLPLVKKSPSEAKEEKAEERKQESKKGAKRKKDASGDDKSKKAKTDRDVSTSTAASQKKSSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 241 LESTLEAQSKGLWSLKDDLKKQVTTVELRQMLEANGQDNSGSELDLRDRCADGMIFGALGLCPTCSGFLRYSGGMYRCTG 320
Cdd:PLN03123 241 LESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPLLYSGGMYRCQG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 321 FLSEWSKCSYSTCEPERKKGKWKVPEDTDNQFLRNWFKTQKSKKPIRALPSPSFDNPSGSKAASGQSPSsEGESLGDLKV 400
Cdd:PLN03123 321 YLSEWSKCSYSTLEPERIKKKWKIPDETDNQYLRKWFKSQKSKKPERLLPPSSSNESSGKQAQSNSSDS-ESEFLGDLKV 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 401 AFSGLSKESVEEWKGKIEGAGGQVHAKIKKDTNCYIVSGALDHDDVEMRKARRMKLPVVREDYLVDCFKKHKKLPFSFYK 480
Cdd:PLN03123 400 SIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVREDYLVDCFKKKKKLPFDKYK 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 481 VEAVSGASSVITVKVKGRSAVHEASGLQDTGHILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSDCHVFRKWGRV 560
Cdd:PLN03123 480 LEASGTSSSMVTVKVKGRSAVHEASGLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRV 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 561 GNEKIGGKKLDEMSKLDAICEFKRLFLEKTGNSWEAWEQKQNFQKRPGKFFPLDIDYGVNKQLTRKPRNDANSQLAQPLV 640
Cdd:PLN03123 560 GNEKIGGNKLEEMSKSDAIHEFKRLFLEKTGNPWESWEQKTNFQKQPGKFYPLDIDYGVNEQPKKKAASGSKSNLAPRLV 639

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 641 ELMKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLNSNSHDPSIRENLIVDASNRFFTVIPSIHP 720
Cdd:PLN03123 640 ELMKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSIRESLLVDASNRFFTLIPSIHP 719

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 721 HVIRDEYDFKSKVKMLEALQDIEIASRFLGFDADNDDSFDDKYRKLRCDITPLSHDSEDYQLIEKYLHTTHAPTHTDWSL 800
Cdd:PLN03123 720 HIIRDEDDLKSKVKMLEALQDIEIASRLVGFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSL 799

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 801 ELEEVFSLEREGEIDKFAPYRRKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPATGYMFGKGIYFADLVSKSAQYCYT 880
Cdd:PLN03123 800 ELEEVFSLEREGEFDKYAPYKEKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYT 879

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 881 DKKNPVGLMLLSEVALGEVYELKNAMYMDKPPEGKHSTKGLGKKVPQESEFVKWRDEVTVPCGRPVPSKVKASELMYNEY 960
Cdd:PLN03123 880 DRKNPVGLMLLSEVALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEY 959

                        970       980
                 ....*....|....*....|..
gi 255560005 961 IVYNTAQVKMQFLLKVRFRHKR 982
Cdd:PLN03123 960 IVYNTAQVKLQFLLKVRFKHKR 981
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 1-982 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 1952.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005   1 MAAPPKPWKAEYAKSGRSSCKTCKKPIDKEKLRLGKMVQATQFDGFMPMWNHESCVLKKAKQIKSIDDVEGIDSLRWEDQ 80
Cdd:PLN03123   1 MAAPPKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSIDDVEGIDSLRWEDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  81 QKIRKCVEGGGIATQDANANALNVMEYGIEVSQTSRATCRRCSQKILKGQVRISSKPDEPRAKALAWHHADCFIDLHPSV 160
Cdd:PLN03123  81 QKIRKYVESGGTGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSKPEGQGYKGLAWHHAKCFLEMSPST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 161 QVEKMSGWESLPPSDQEAVRALIKEVPSTAKAGIVEERKSTSAVGAKRKKDGGGDQKPKITRTDGDVSTSRNASAKNSND 240
Cdd:PLN03123 161 PVEKLSGWDTLSDSDQEAVLPLVKKSPSEAKEEKAEERKQESKKGAKRKKDASGDDKSKKAKTDRDVSTSTAASQKKSSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 241 LESTLEAQSKGLWSLKDDLKKQVTTVELRQMLEANGQDNSGSELDLRDRCADGMIFGALGLCPTCSGFLRYSGGMYRCTG 320
Cdd:PLN03123 241 LESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPLLYSGGMYRCQG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 321 FLSEWSKCSYSTCEPERKKGKWKVPEDTDNQFLRNWFKTQKSKKPIRALPSPSFDNPSGSKAASGQSPSsEGESLGDLKV 400
Cdd:PLN03123 321 YLSEWSKCSYSTLEPERIKKKWKIPDETDNQYLRKWFKSQKSKKPERLLPPSSSNESSGKQAQSNSSDS-ESEFLGDLKV 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 401 AFSGLSKESVEEWKGKIEGAGGQVHAKIKKDTNCYIVSGALDHDDVEMRKARRMKLPVVREDYLVDCFKKHKKLPFSFYK 480
Cdd:PLN03123 400 SIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVREDYLVDCFKKKKKLPFDKYK 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 481 VEAVSGASSVITVKVKGRSAVHEASGLQDTGHILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSDCHVFRKWGRV 560
Cdd:PLN03123 480 LEASGTSSSMVTVKVKGRSAVHEASGLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRV 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 561 GNEKIGGKKLDEMSKLDAICEFKRLFLEKTGNSWEAWEQKQNFQKRPGKFFPLDIDYGVNKQLTRKPRNDANSQLAQPLV 640
Cdd:PLN03123 560 GNEKIGGNKLEEMSKSDAIHEFKRLFLEKTGNPWESWEQKTNFQKQPGKFYPLDIDYGVNEQPKKKAASGSKSNLAPRLV 639

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 641 ELMKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLNSNSHDPSIRENLIVDASNRFFTVIPSIHP 720
Cdd:PLN03123 640 ELMKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSIRESLLVDASNRFFTLIPSIHP 719

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 721 HVIRDEYDFKSKVKMLEALQDIEIASRFLGFDADNDDSFDDKYRKLRCDITPLSHDSEDYQLIEKYLHTTHAPTHTDWSL 800
Cdd:PLN03123 720 HIIRDEDDLKSKVKMLEALQDIEIASRLVGFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSL 799

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 801 ELEEVFSLEREGEIDKFAPYRRKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPATGYMFGKGIYFADLVSKSAQYCYT 880
Cdd:PLN03123 800 ELEEVFSLEREGEFDKYAPYKEKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYT 879

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 881 DKKNPVGLMLLSEVALGEVYELKNAMYMDKPPEGKHSTKGLGKKVPQESEFVKWRDEVTVPCGRPVPSKVKASELMYNEY 960
Cdd:PLN03123 880 DRKNPVGLMLLSEVALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEY 959

                        970       980
                 ....*....|....*....|..
gi 255560005 961 IVYNTAQVKMQFLLKVRFRHKR 982
Cdd:PLN03123 960 IVYNTAQVKLQFLLKVRFKHKR 981
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 633-977 1.63e-169

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: 498.72  E-value: 1.63e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 633 SQLAQPLVELMKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLNsnshDPSIRENLIVDASNRFF 712
Cdd:cd01437    2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALK----RGSSQGSQLEELSNEFY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 713 TVIP----SIHPHVIRDEYDFKSKVKMLEALQDIEIASRFLGFDADNDD-SFDDKYRKLRCDITPLSHDSEDYQLIEKYL 787
Cdd:cd01437   78 TLIPhdfgMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDdPLDANYEKLKCKIEPLDKDSEEYKIIEKYL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 788 HTTHAPTHtDWSLELEEVFSLEREGEIDKFAPyRRKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPATGYMFGKGIYF 867
Cdd:cd01437  158 KNTHAPTT-EYTVEVQEIFRVEREGETDRFKP-FKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 868 ADLVSKSAQYCYTDKKNPVGLMLLSEVALGEVYELKNAMYMDK-PPEGKHSTKGLGKKVPQESEFVKWRDEVTVPCGRPV 946
Cdd:cd01437  236 ADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPV 315

                        330       340       350
                 ....*....|....*....|....*....|..
gi 255560005 947 PSKVK-ASELMYNEYIVYNTAQVKMQFLLKVR 977
Cdd:cd01437  316 PSGHKtDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 777-978 1.38e-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: 1.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  777 SEDYQLIEKYLHTTHAPTHTdWSLELEEVFSLEREGEIDKFAPyRRKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPA 856
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQP-KKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  857 TGYMFGKGIYFADLVSKSAQYCYTDKKNPVGLMLLSEVALGEVYELKNAMYMDKPPEGKHSTKGLGKKVPqesEFVKWRD 936
Cdd:pfam00644  79 TGYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAP---ESFVDLD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 255560005  937 EvtVPCGRPVPSKVKASELMYNEYIVYNTAQVKMQFLLKVRF 978
Cdd:pfam00644 156 G--VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 516-595 8.40e-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: 96.20  E-value: 8.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005   516 DGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGsDCHVFRKWGRVGneKIGGKKLDEMSKL-DAICEFKRLFLEKTGNSW 594
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDDFG-GYSVYRRWGRIG--TKGQTKLKTFDSLeDAIKEFEKLFKEKTKNGY 77


                   .
gi 255560005   595 E 595
Cdd:smart00773  78 E 78
 
Name Accession Description Interval E-value
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 1-982 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 1952.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005   1 MAAPPKPWKAEYAKSGRSSCKTCKKPIDKEKLRLGKMVQATQFDGFMPMWNHESCVLKKAKQIKSIDDVEGIDSLRWEDQ 80
Cdd:PLN03123   1 MAAPPKPWKAEYAKSSRSSCKTCKSPIDKDELRLGKMVQSTQFDGFMPMWNHASCILKKKNQIKSIDDVEGIDSLRWEDQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  81 QKIRKCVEGGGIATQDANANALNVMEYGIEVSQTSRATCRRCSQKILKGQVRISSKPDEPRAKALAWHHADCFIDLHPSV 160
Cdd:PLN03123  81 QKIRKYVESGGTGTGTASDAAASSFEYGIEVAKTSRATCRRCSEKILKGEVRISSKPEGQGYKGLAWHHAKCFLEMSPST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 161 QVEKMSGWESLPPSDQEAVRALIKEVPSTAKAGIVEERKSTSAVGAKRKKDGGGDQKPKITRTDGDVSTSRNASAKNSND 240
Cdd:PLN03123 161 PVEKLSGWDTLSDSDQEAVLPLVKKSPSEAKEEKAEERKQESKKGAKRKKDASGDDKSKKAKTDRDVSTSTAASQKKSSD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 241 LESTLEAQSKGLWSLKDDLKKQVTTVELRQMLEANGQDNSGSELDLRDRCADGMIFGALGLCPTCSGFLRYSGGMYRCTG 320
Cdd:PLN03123 241 LESKLEAQSKELWSLKDDLKKHVSTAELREMLEANGQDTSGSELDLRDRCADGMMFGALGPCPLCSGPLLYSGGMYRCQG 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 321 FLSEWSKCSYSTCEPERKKGKWKVPEDTDNQFLRNWFKTQKSKKPIRALPSPSFDNPSGSKAASGQSPSsEGESLGDLKV 400
Cdd:PLN03123 321 YLSEWSKCSYSTLEPERIKKKWKIPDETDNQYLRKWFKSQKSKKPERLLPPSSSNESSGKQAQSNSSDS-ESEFLGDLKV 399

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 401 AFSGLSKESVEEWKGKIEGAGGQVHAKIKKDTNCYIVSGALDHDDVEMRKARRMKLPVVREDYLVDCFKKHKKLPFSFYK 480
Cdd:PLN03123 400 SIVGASKEKVTEWKAKIEEAGGVFHATVKKDTNCLVVCGELDDEDAEMRKARRMKIPIVREDYLVDCFKKKKKLPFDKYK 479

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 481 VEAVSGASSVITVKVKGRSAVHEASGLQDTGHILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSDCHVFRKWGRV 560
Cdd:PLN03123 480 LEASGTSSSMVTVKVKGRSAVHEASGLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEEDKGSDCYVFRKWGRV 559

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 561 GNEKIGGKKLDEMSKLDAICEFKRLFLEKTGNSWEAWEQKQNFQKRPGKFFPLDIDYGVNKQLTRKPRNDANSQLAQPLV 640
Cdd:PLN03123 560 GNEKIGGNKLEEMSKSDAIHEFKRLFLEKTGNPWESWEQKTNFQKQPGKFYPLDIDYGVNEQPKKKAASGSKSNLAPRLV 639

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 641 ELMKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLNSNSHDPSIRENLIVDASNRFFTVIPSIHP 720
Cdd:PLN03123 640 ELMKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKENDQDPSIRESLLVDASNRFFTLIPSIHP 719

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 721 HVIRDEYDFKSKVKMLEALQDIEIASRFLGFDADNDDSFDDKYRKLRCDITPLSHDSEDYQLIEKYLHTTHAPTHTDWSL 800
Cdd:PLN03123 720 HIIRDEDDLKSKVKMLEALQDIEIASRLVGFDVDEDDSLDDKYKKLHCDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSL 799

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 801 ELEEVFSLEREGEIDKFAPYRRKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPATGYMFGKGIYFADLVSKSAQYCYT 880
Cdd:PLN03123 800 ELEEVFSLEREGEFDKYAPYKEKLKNRMLLWHGSRLTNFVGILSQGLRIAPPEAPATGYMFGKGVYFADLVSKSAQYCYT 879

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 881 DKKNPVGLMLLSEVALGEVYELKNAMYMDKPPEGKHSTKGLGKKVPQESEFVKWRDEVTVPCGRPVPSKVKASELMYNEY 960
Cdd:PLN03123 880 DRKNPVGLMLLSEVALGEIYELKKAKYMDKPPRGKHSTKGLGKTVPQESEFVKWRDDVVVPCGKPVPSKVKASELMYNEY 959

                        970       980
                 ....*....|....*....|..
gi 255560005 961 IVYNTAQVKMQFLLKVRFRHKR 982
Cdd:PLN03123 960 IVYNTAQVKLQFLLKVRFKHKR 981
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 633-977 1.63e-169

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: 498.72  E-value: 1.63e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 633 SQLAQPLVELMKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLNsnshDPSIRENLIVDASNRFF 712
Cdd:cd01437    2 SKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALK----RGSSQGSQLEELSNEFY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 713 TVIP----SIHPHVIRDEYDFKSKVKMLEALQDIEIASRFLGFDADNDD-SFDDKYRKLRCDITPLSHDSEDYQLIEKYL 787
Cdd:cd01437   78 TLIPhdfgMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDdPLDANYEKLKCKIEPLDKDSEEYKIIEKYL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 788 HTTHAPTHtDWSLELEEVFSLEREGEIDKFAPyRRKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPATGYMFGKGIYF 867
Cdd:cd01437  158 KNTHAPTT-EYTVEVQEIFRVEREGETDRFKP-FKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYF 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 868 ADLVSKSAQYCYTDKKNPVGLMLLSEVALGEVYELKNAMYMDK-PPEGKHSTKGLGKKVPQESEFVKWRDEVTVPCGRPV 946
Cdd:cd01437  236 ADMFSKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKeLPKGKHSVKGLGKTAPDPSEFEIDLDGVVVPLGKPV 315

                        330       340       350
                 ....*....|....*....|....*....|..
gi 255560005 947 PSKVK-ASELMYNEYIVYNTAQVKMQFLLKVR 977
Cdd:cd01437  316 PSGHKtDTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 196-981 5.37e-168

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 512.04  E-value: 5.37e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 196 EERKSTSAVGAKRKKDGGGDQKPKITRTDGDVSTSRNASAK----NSNDLESTLEAQSKGLWSLKDDLKKQVTTVELRQM 271
Cdd:PLN03122   4 ETRSQAHAPAAEEGKGGTRKQKAENKEHEGEQSPKKAKKEKkqddSGNGNGKSAEDAVKEFEEFCKAIEEHLSIEQMREI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 272 LEANGQDNSGSELDLRDRCADGMIFGALGLCPTCSGFLRYSGGMYRCTGFLSEWSKCSYSTCEPERKKGKWKVPEDTDNQ 351
Cdd:PLN03122  84 LEENGQDSSGSDDAVLPRCQDQLFYGPLEKCPLCGGALECDGHRYTCTGFISEWSSCTFSTKNPPRKEEPLKIPDSVKNS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 352 FLRNWFKTQK--SKKPIRALPSPsfdnpsgskaasgqspsseGESLGDLKVAFSGLSKESVEEWKGKIEGAGGQVHAKIK 429
Cdd:PLN03122 164 FITKLLKKHQdpSKRPKRELGAP-------------------GKPFSGMMISLSGRLSRTHQYWKKDIEKHGGKVANSVE 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 430 KDTnCYIVSGALDHDDV--EMRKARRMKLPVVREDYLVDCFKKHKKLPFSFY----------------KVEAVSGASSVI 491
Cdd:PLN03122 225 GVT-CLVVSPAERERGGssKIAEAMERGIPVVREAWLIDSIEKQEAQPLEAYdvvsdlsvegrgipwdKQDPSEEAIESL 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 492 TVKVK--GRSAVHEASGLQ-DTGHILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSdCHVFRKWGRVGNEKIGGK 568
Cdd:PLN03122 304 SAELKlyGKRGVYKDSKLQeEGGKIFEKDGILYNCAFSICDLGRGLNEYCIMQLITVPDSN-LHLYYKKGRVGDDPNAEE 382

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 569 KLDEMSKLD-AICEFKRLFLEKTGNSWEAWEQKQNFQKRPGKFFPLDIDYGVNK-----QLTRKPRNDANSQLAQPLVEL 642
Cdd:PLN03122 383 RLEEWEDVDaAIKEFVRLFEEITGNEFEPWEREKKFEKKRLKFYPIDMDDGVDVragglGLRQLGVAAAHCKLDPKVANF 462

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 643 MKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLNSNSHDPSIRENLIVDASNRFFTVIPSIHPHV 722
Cdd:PLN03122 463 MKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSEKETGQKAEAMWLDFSNKWFSLVHSTRPFV 542

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 723 IRDEYDFKSKV-KMLEALQDIEIASRFLG--FDADNDDSFDDKYRKLRCDITPLSHDSEDYQLIEKYLHTTHAPTH---T 796
Cdd:PLN03122 543 IRDIDELADHAaSALETVRDINVASRLIGdmTGSTLDDPLSDRYKKLGCSISPVDKESDDYKMIVKYLEKTYEPVKvgdV 622

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 797 DWSLELEEVFSLEREG-----EIDkfapyrrKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPATGYMFGKGIYFADLV 871
Cdd:PLN03122 623 SYSVSVENIFAVESSAgpsldEIK-------KLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVPGYMFGKAIVCSDAA 695

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 872 SKSAQYCYTDKKNPVGLMLLSEVALG-EVYELKnamymdKPPEG-------KHSTKGLGKKVPQESEFVKWRDEVTVPCG 943
Cdd:PLN03122 696 AEAARYGFTAVDRPEGFLVLAVASLGdEVLELT------KPPEDvksyeekKVGVKGLGRKKTDESEHFKWRDDITVPCG 769

                        810       820       830
                 ....*....|....*....|....*....|....*...
gi 255560005 944 RPVPSKVKASELMYNEYIVYNTAQVKMQFLLKVRFRHK 981
Cdd:PLN03122 770 RLIPSEHKDSPLEYNEYAVYDPKQVSIRFLVGVKYEEK 807
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 480-982 2.11e-148

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 455.07  E-value: 2.11e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 480 KVEAVSGASSVITVKvKGRSAVHE--ASGLQDTGHILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSDCHVFRKW 557
Cdd:PLN03124 135 DEEREKEEKIVTATK-KGRAVLDQwlPDHIKSNYHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDGSKYMVYTRW 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 558 GRVGNEkiGGKKLD--EMSKLDAICEFKRLFLEKTGNSWEaweQKQNFQKRPGKFFPLDIDYGVNKQL------TRKPRN 629
Cdd:PLN03124 214 GRVGVK--GQDKLHgpYDSREPAIREFEKKFYDKTKNHWS---DRKNFISHPKKYTWLEMDYEDEEESkkdkpsVSSEDK 288

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 630 DANSQLAQPLVELMKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLnsnshDPSIRENLiVDASN 709
Cdd:PLN03124 289 NKQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVI-----SRSDRETL-EELSG 362

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 710 RFFTVIP------SIHPHVIRDEYDFKSKVKMLEALQDIEIASRFLGFDADNDDS-FDDKYRKLRCDITPLSHDSEDYQL 782
Cdd:PLN03124 363 EFYTVIPhdfgfkKMRQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDpLYAHYKRLNCELEPLDTDSEEFSM 442

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 783 IEKYLHTTHAPTHTDWSLELEEVFSLEREGEIDKFAPYRrKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPATGYMFG 862
Cdd:PLN03124 443 IAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQKFS-STKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYMFG 521

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 863 KGIYFADLVSKSAQYCYTDKKNPVGLMLLSEVALGEVYELKNAMY-MDKPPEGKHSTKGLGKKVPQESEFVKWRDEVTVP 941
Cdd:PLN03124 522 KGVYFADMFSKSANYCYASAANPDGVLLLCEVALGDMNELLQADYnANKLPPGKLSTKGVGRTVPDPSEAKTLEDGVVVP 601

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|.
gi 255560005 942 CGRPVPSKVKASELMYNEYIVYNTAQVKMQFLLKVRFRHKR 982
Cdd:PLN03124 602 LGKPVESPYSKGSLEYNEYIVYNVDQIRMRYVLQVKFNYKR 642
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 777-978 1.38e-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: 1.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  777 SEDYQLIEKYLHTTHAPTHTdWSLELEEVFSLEREGEIDKFAPyRRKLKNRMLLWHGSRLTNYVGILNQGLRIAPPEAPA 856
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQP-KKKLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  857 TGYMFGKGIYFADLVSKSAQYCYTDKKNPVGLMLLSEVALGEVYELKNAMYMDKPPEGKHSTKGLGKKVPqesEFVKWRD 936
Cdd:pfam00644  79 TGYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADYAEKLPPGKHSVKGLGKTAP---ESFVDLD 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 255560005  937 EvtVPCGRPVPSKVKASELMYNEYIVYNTAQVKMQFLLKVRF 978
Cdd:pfam00644 156 G--VPLGKLVATGYDSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 511-617 1.30e-45

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: 158.91  E-value: 1.30e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 511 GHILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSDCHVFRKWGRVGNEkIGGKKLDEMSKL-DAICEFKRLFLEK 589
Cdd:cd08001    1 AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGTT-IGGNKLEEFSSLeEAKMAFEELYEEK 79

                         90       100
                 ....*....|....*....|....*...
gi 255560005 590 TGNSweaWEQKQNFQKRPGKFFPLDIDY 617
Cdd:cd08001   80 TGND---FENRKNFKKKPGKFYPLDIDY 104
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 633-750 2.96e-42

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: 150.75  E-value: 2.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  633 SQLAQPLVELMKMLFNVEAYRAAMMEFEINMSEMPLGKLSKNNIQKGFEALTEIQNLLNSNSHDPsiRENLIVDASNRFF 712
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPSLAK--AKAKLEDLSNRFY 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 255560005  713 TVIPSI----HPHVIRDEYDFKSKVKMLEALQDIEIASRFLG 750
Cdd:pfam02877  79 TLIPHDfgrnRPPVIDTEEELKEKLELLEALLDIEVASKLLK 120
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 11-87 2.81e-26

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: 103.17  E-value: 2.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005   11 EYAKSGRSSCKTCKKPIDKEKLRLGKMV---QATQFDGFMPMWNHESCV-------LKKAKQIKSIDDVEGIDSLRWEDQ 80
Cdd:pfam00645   1 EYAKSGRAKCKGCKKKIEKGELRIGKVVdfvPSPFFDGGSKRWYHWGCFtkkqlknRKETKEIDDADDLDGFDELKDEDQ 80


                  ....*..
gi 255560005   81 QKIRKCV 87
Cdd:pfam00645  81 EKIRKAI 87
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 512-617 2.54e-25

WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins and histones. Higher eukaryotes contain several PARPs and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. Poly-ADP-ribosylation was thought to be a reversible post-translational covalent modification that serves as a regulatory mechanism for protein substrates. However, it is now known that it plays important roles in many cellular processes including maintenance of genomic stability, transcriptional regulation, energy metabolism, cell death and survival, among others.


Pssm-ID: 153426  Cd Length: 102  Bit Score: 100.84  E-value: 2.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 512 HILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSDCHVFRKWGRVGneKIGGKKLDEMSKLD-AICEFKRLFLEKT 590
Cdd:cd07997    1 HVYGDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVG--ERGQSQLTPFGSLEsAIKEFEKKFKDKT 78

                         90       100
                 ....*....|....*....|....*..
gi 255560005 591 GNSweaWEQKQNFQKRPGKFFPLDIDY 617
Cdd:cd07997   79 GNE---WENRPLFKKQPGKYALVELDY 102
PADR1 pfam08063
PADR1 (NUC008) domain; This domain is found in poly(ADP-ribose)-synthetases. The function of ...
 287-338 6.69e-25

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: 98.03  E-value: 6.69e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 255560005  287 RDRCADGMIFGALGLCPTCS-GFLRYSGGMYRCTGFLSEWSKCSYSTCEPERK 338
Cdd:pfam08063   1 LDRCADGMLFGALEPCPECKnGQLVFNGSGYKCTGYVSEWTKCTYSTKDPKRK 53
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 516-595 8.40e-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: 96.20  E-value: 8.40e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005   516 DGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGsDCHVFRKWGRVGneKIGGKKLDEMSKL-DAICEFKRLFLEKTGNSW 594
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDDFG-GYSVYRRWGRIG--TKGQTKLKTFDSLeDAIKEFEKLFKEKTKNGY 77


                   .
gi 255560005   595 E 595
Cdd:smart00773  78 E 78
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 512-617 6.95e-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: 6.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 512 HILEDGNSIYNTTLNMSDLSTGVNSYYILQIIQDDKGSDCHVFRKWGRVGneKIGGKKLDEMSK-LD-AICEFKRLFLEK 589
Cdd:cd08003    1 HVYEEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVG--KKGQSSLVPCGSdLEqAKSLFEKKFLDK 78

                         90       100
                 ....*....|....*....|....*...
gi 255560005 590 TGNSWEAweqKQNFQKRPGKFFPLDIDY 617
Cdd:cd08003   79 TKNEWED---RANFEKVAGKYDLLEMDY 103
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 521-595 3.39e-17

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: 76.90  E-value: 3.39e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255560005  521 YNTTLNMSDLSTGVNSYYILQiIQDDKGSDCHVFRKWGRVGneKIGGKKLDEMSKL-DAICEFKRLFLEKTGNSWE 595
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQ-VEDDLFGGYSLFRRWGRIG--TRGQTKLKSFDSLeEAIKEFEKLFAEKTKKGYR 73
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 395-469 4.58e-16

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: 73.72  E-value: 4.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 395 LGDLKVAFSGLSKESVEEWKGKIEGAGGQVHAKIKKDTNCYIVSgaldHDDVE-----MRKARRMKLPVVREDYLVDCFK 469
Cdd:cd17747    1 LTGMKFALIGKLSKSKDELKKLIEKLGGKVASKVTKKVTLCIST----KAEVEkmskkMKEAKEAGVPVVSEDFLEDCIK 76
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 521-617 1.27e-15

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: 73.21  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 521 YNTTLNMSDLSTGVNSYYILQIIQDDKGSdcHVFRKWGRVGneKIGGKKLDEMSK--LDAICEFKRLFLEKTGNSweaWE 598
Cdd:cd08002    9 YDCMLNQTNIGHNNNKFYVIQLLESGKEY--YVWNRWGRVG--EKGQNKLKGPWDslEGAIKDFEKKFKDKTKNN---WE 81

                         90
                 ....*....|....*....
gi 255560005 599 QKQNFQKRPGKFFPLDIDY 617
Cdd:cd08002   82 DRENFVPHPGKYTLIEMDY 100
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 830-968 9.38e-15

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: 72.21  E-value: 9.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 830 LWHGSRLTNYVGILNQGLRIAPPEAPATGYMFGKGIYFADLVSKSAQYCYTDKKNPVGlmlLSEVALGEVYELKNAMYMd 909
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVF---QNGKPKVCGRELCVFGFL- 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255560005 910 kppegkhsTKGLGKKVPQESEFVKWRDEVTVPCGRPV---PSKVKASELM-YNEYIVYN-TAQV 968
Cdd:cd01341   78 --------TLGVMSGATEESSRVLFPRNFRGATGAEVvdlLVAMCRDALLlPREYIIFEpYSQV 133
zf-PARP pfam00645
Poly(ADP-ribose) polymerase and DNA-Ligase Zn-finger region; Poly(ADP-ribose) polymerase is an ...
 110-183 8.44e-14

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: 67.73  E-value: 8.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005  110 EVSQTSRATCRRCSQKILKGQVRISSKPD-----EPRAKALAWHHADCFID--------LHPSVQVEKMSGWESLPPSDQ 176
Cdd:pfam00645   1 EYAKSGRAKCKGCKKKIEKGELRIGKVVDfvpspFFDGGSKRWYHWGCFTKkqlknrkeTKEIDDADDLDGFDELKDEDQ 80


                  ....*..
gi 255560005  177 EAVRALI 183
Cdd:pfam00645  81 EKIRKAI 87
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 815-974 6.41e-09

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: 57.22  E-value: 6.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 815 DKFAPYRRKLKNRMLLWHGSRLTNyvGILNQGLriapPEAPA-TGYMFGKGIYFADLVSKSAQYCY---------TDKKN 884
Cdd:cd01438   77 KEIAEENHNHHNERMLFHGSPFIN--AIIHKGF----DERHAyIGGMFGAGIYFAENSSKSNQYVYgigggtgcpTHKDR 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 885 PVGL----MLLSEVALGEVYELKNAMYMDKPPEGKHSTkglgkkvpqesefvkwrdevtvpCGRPvpskvKASELMYNEY 960
Cdd:cd01438  151 SCYVchrqMLFCRVTLGKSFLQFSAMKMAHAPPGHHSV-----------------------IGRP-----SVNGLAYAEY 202

                        170
                 ....*....|....
gi 255560005 961 IVYNTAQVKMQFLL 974
Cdd:cd01438  203 VIYRGEQAYPEYLI 216
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 397-468 2.71e-07

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: 48.83  E-value: 2.71e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255560005  397 DLKVAFSGLSKESVEEWKGKIEGAGGQVHAKIKKDTNCYIVsgalDHDDVEMRKARRMKLPVVREDYLVDCF 468
Cdd:pfam00533   8 GKTFVITGLDGLERDELKELIEKLGGKVTDSLSKKTTHVIV----EARTKKYLKAKELGIPIVTEEWLLDCI 75
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 533-594 4.16e-07

WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs) as well as the putative Escherichia coli molybdate metabolism regulator and related bacterial proteins, a small family of bacterial DNA ligases, and various other bacterial proteins of unknown function. It has been called WGR after the most conserved central motif of the domain. The domain occurs in single-domain proteins and in a variety of domain architectures, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain.


Pssm-ID: 153424  Cd Length: 73  Bit Score: 48.43  E-value: 4.16e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255560005 533 GVNSYYILQIIQDDKGSDCHVFRKWGRVGNeKIGGKKLDEM-SKLDAICEFKRLFLEKTGNSW 594
Cdd:cd07994   10 GSNKYYKLQLLEDDKENRYWVFRSYGRVGT-VIGSTKLEQMpSKEEAEEHFMKLYEEKTGKGY 71
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 829-917 4.40e-07

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: 49.63  E-value: 4.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 829 LLWHGSRLTNYVGILNQGLRIAPPEAPATgyMFGKGIYFADLVSKSAQYCYTD-KKNPVGLMLLSEVALGEvYELKNAMY 907
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFDRRFCGKHGT--MYGKGSYFAKNASYSHQYSKKSpKADGLKEMFLARVLTGD-YTQGHPGY 77

                         90
                 ....*....|
gi 255560005 908 MDKPPEGKHS 917
Cdd:cd01439   78 RRPPLKPSGV 87
BRCT smart00292
breast cancer carboxy-terminal domain;
397-468 1.24e-06

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 46.98  E-value: 1.24e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255560005   397 DLKVAFSG-LSKESVEEWKGKIEGAGGQVHAKIKKDTNCYIVSGALDHDDVEMRKARRMKLPVVREDYLVDCF 468
Cdd:smart00292   6 GKTFYITGsFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKAIALGIPIVKEEWLLDCL 78
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 398-467 4.58e-06

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: 45.05  E-value: 4.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255560005 398 LKVAFSGLSKESVEEWKGKIEGAGGQVHAKIKKDTNcYIVSGALDHDDVEMrKARRMKLPVVREDYLVDC 467
Cdd:cd00027    1 LVICFSGLDDEEREELKKLIEALGGKVSESLSSKVT-HLIAKSPSGEKYYL-AALAWGIPIVSPEWLLDC 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.
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