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Conserved domains on  [gi|1034585925|ref|XP_016876401|]
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poly [ADP-ribose] polymerase 2 isoform X2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03124 super family cl33640
poly [ADP-ribose] polymerase; Provisional
 52-476 7.17e-156

poly [ADP-ribose] polymerase; Provisional


The actual alignment was detected with superfamily member PLN03124:

Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 457.38  E-value: 7.17e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  52 VAGGKANKDRTEDKQDESVKALLlKGKAPVDPECTAKVgKA--HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQ 129
Cdd:PLN03124  127 EDEKEKGGDEEREKEEKIVTATK-KGRAVLDQWLPDHI-KSnyHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 130 RNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYatntQDEEETKKE- 208
Cdd:PLN03124  205 SKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDY----EDEEESKKDk 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 209 ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALME 287
Cdd:PLN03124  281 PSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEE 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 288 ACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYE 365
Cdd:PLN03124  360 LSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEE 439

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 366 FKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYM 443
Cdd:PLN03124  440 FSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYM 519

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034585925 444 FGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 476
Cdd:PLN03124  520 FGKGVYFADMFSKSANYCYASAANPDGVLLLCE 552
PARP2_NTR cd22252
NTR (N-terminal region) domain of poly [ADP-ribose] polymerase 2 (PARP-2) and similar proteins; ...
 19-78 3.86e-29

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


:

Pssm-ID: 412075  Cd Length: 59  Bit Score: 108.83  E-value: 3.86e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  19 ESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQdESVKALLLKGK 78
Cdd:cd22252     1 ESKRVNNGNTATEDSPPAKKTRRCQRKEVKKEPVAGGKADKDRTEDKQ-ESVKALLLKGK 59
 
Name Accession Description Interval E-value
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 52-476 7.17e-156

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 457.38  E-value: 7.17e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  52 VAGGKANKDRTEDKQDESVKALLlKGKAPVDPECTAKVgKA--HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQ 129
Cdd:PLN03124  127 EDEKEKGGDEEREKEEKIVTATK-KGRAVLDQWLPDHI-KSnyHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 130 RNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYatntQDEEETKKE- 208
Cdd:PLN03124  205 SKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDY----EDEEESKKDk 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 209 ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALME 287
Cdd:PLN03124  281 PSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEE 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 288 ACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYE 365
Cdd:PLN03124  360 LSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEE 439

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 366 FKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYM 443
Cdd:PLN03124  440 FSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYM 519

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034585925 444 FGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 476
Cdd:PLN03124  520 FGKGVYFADMFSKSANYCYASAANPDGVLLLCE 552
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 218-476 1.55e-128

Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 377.00  E-value: 1.55e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 218 ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQH-GRALMEACNEFYTRI 296
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 297 PHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQST 376
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 377 HAPTHsDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMS 454
Cdd:cd01437   161 HAPTT-EYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMF 239

                         250       260
                  ....*....|....*....|..
gi 1034585925 455 SKSANYCFASRLKNTGLLLLSE 476
Cdd:cd01437   240 SKSANYCHASASDPTGLLLLCE 261
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 363-476 8.37e-60

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


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 194.86  E-value: 8.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 363 SYEFKVISQYLQSTHAPTHSdYTMTLLDLFEVEKDGEKEAFRED--LHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPIT 440
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKkkLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034585925 441 GYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 476
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSE 115
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 97-182 3.61e-31

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


Pssm-ID: 214814  Cd Length: 84  Bit Score: 115.08  E-value: 3.61e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925   97 EGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWE 176
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTKGQTKLKTF-DSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 1034585925  177 DREKFE 182
Cdd:smart00773  79 ERGKFV 84
PARP2_NTR cd22252
NTR (N-terminal region) domain of poly [ADP-ribose] polymerase 2 (PARP-2) and similar proteins; ...
 19-78 3.86e-29

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


Pssm-ID: 412075  Cd Length: 59  Bit Score: 108.83  E-value: 3.86e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  19 ESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQdESVKALLLKGK 78
Cdd:cd22252     1 ESKRVNNGNTATEDSPPAKKTRRCQRKEVKKEPVAGGKADKDRTEDKQ-ESVKALLLKGK 59
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
114-172 3.02e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 36.50  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034585925 114 NNNKYYLIQLlEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 172
Cdd:COG3831    13 NSARFYELEV-EPDLFGGWSLTRRWGRIGTKGQTKTKTF-ASEEEALAALEKLVAEKLR 69
 
Name Accession Description Interval E-value
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 52-476 7.17e-156

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 457.38  E-value: 7.17e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  52 VAGGKANKDRTEDKQDESVKALLlKGKAPVDPECTAKVgKA--HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQ 129
Cdd:PLN03124  127 EDEKEKGGDEEREKEEKIVTATK-KGRAVLDQWLPDHI-KSnyHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 130 RNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYatntQDEEETKKE- 208
Cdd:PLN03124  205 SKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDY----EDEEESKKDk 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 209 ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALME 287
Cdd:PLN03124  281 PSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEE 359

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 288 ACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYE 365
Cdd:PLN03124  360 LSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEE 439

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 366 FKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYM 443
Cdd:PLN03124  440 FSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYM 519

                         410       420       430
                  ....*....|....*....|....*....|...
gi 1034585925 444 FGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 476
Cdd:PLN03124  520 FGKGVYFADMFSKSANYCYASAANPDGVLLLCE 552
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 218-476 1.55e-128

Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active. Poly(ADP-ribose)-like polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length through interactions with telomere repeat binding factor 1.


Pssm-ID: 238717 [Multi-domain]  Cd Length: 347  Bit Score: 377.00  E-value: 1.55e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 218 ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQH-GRALMEACNEFYTRI 296
Cdd:cd01437     1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 297 PHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQST 376
Cdd:cd01437    81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 377 HAPTHsDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMS 454
Cdd:cd01437   161 HAPTT-EYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMF 239

                         250       260
                  ....*....|....*....|..
gi 1034585925 455 SKSANYCFASRLKNTGLLLLSE 476
Cdd:cd01437   240 SKSANYCHASASDPTGLLLLCE 261
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 48-476 1.33e-115

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 362.96  E-value: 1.33e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  48 KKMPVAGGKANKDRTEdkqdESVKALLLKGKAPVDpECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDD 127
Cdd:PLN03123  471 KKLPFDKYKLEASGTS----SSMVTVKVKGRSAVH-EASGLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEED 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 128 AQRNFSVWMRWGRVG--KMGQHSLVACSgnlnKAKEI--FQKKFLDKTKNNWE---DREKFEKVPGKYDMLQMDYATNtq 200
Cdd:PLN03123  546 KGSDCYVFRKWGRVGneKIGGNKLEEMS----KSDAIheFKRLFLEKTGNPWEsweQKTNFQKQPGKFYPLDIDYGVN-- 619

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 201 dEEETKKEESlksplKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQ 280
Cdd:PLN03123  620 -EQPKKKAAS-----GSKSNLAPRLVELMKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKEND 693

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 281 HGRA-----LMEACNEFYTRIP--HdfglrtPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEhPLDQHYRNLH 353
Cdd:PLN03123  694 QDPSireslLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKMLEALQDIEIASRLVGFDVDEDD-SLDDKYKKLH 766

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 354 CALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAF---REDLHNRMLLWHGSRMSNWVGILSHGL 430
Cdd:PLN03123  767 CDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKYapyKEKLKNRMLLWHGSRLTNFVGILSQGL 846

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1034585925 431 RIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 476
Cdd:PLN03123  847 RIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSE 892
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 93-195 2.59e-71

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


Pssm-ID: 153430  Cd Length: 103  Bit Score: 221.43  E-value: 2.59e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  93 HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTK 172
Cdd:cd08003     1 HVYEEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKKGQSSLVPCGSDLEQAKSLFEKKFLDKTK 80

                          90       100
                  ....*....|....*....|...
gi 1034585925 173 NNWEDREKFEKVPGKYDMLQMDY 195
Cdd:cd08003    81 NEWEDRANFEKVAGKYDLLEMDY 103
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 363-476 8.37e-60

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


Pssm-ID: 395519 [Multi-domain]  Cd Length: 195  Bit Score: 194.86  E-value: 8.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 363 SYEFKVISQYLQSTHAPTHSdYTMTLLDLFEVEKDGEKEAFRED--LHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPIT 440
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKkkLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1034585925 441 GYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSE 476
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSE 115
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 219-349 1.75e-51

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


Pssm-ID: 460732 [Multi-domain]  Cd Length: 135  Bit Score: 171.17  E-value: 1.75e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 219 SQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAG---QHGRALMEACNEFYTR 295
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPslaKAKAKLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034585925 296 IPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSP-EHPLDQHY 349
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKDSKSDDdEHPLDRHY 135
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 93-195 1.82e-43

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


Pssm-ID: 153426  Cd Length: 102  Bit Score: 148.61  E-value: 1.82e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  93 HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 172
Cdd:cd07997     1 HVYGDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPF-GSLESAIKEFEKKFKDKTG 79

                          90       100
                  ....*....|....*....|...
gi 1034585925 173 NNWEDREKFEKVPGKYDMLQMDY 195
Cdd:cd07997    80 NEWENRPLFKKQPGKYALVELDY 102
WGR_PARP3_like cd08002
WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a ...
 94-195 3.50e-41

WGR domain of poly(ADP-ribose) polymerase 3 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of human PARP-3 and similar proteins, including Arabidopsis thaliana PARP-2. PARP-3 displays a tissue-specific expression, with highest amounts found in the nuclei of epithelial cells of prostate ducts, salivary glands, liver, pancreas, and in the neurons of terminal ganglia. Unlike PARP-1 and PARP-2, PARP-3 activity is not induced by DNA strand breaks. However, it co-localizes with Polycomb group bodies and is part of complexes making up DNA-PKcs, DNA ligases III and IV, Ku70, and Ku80. PARP-3 is a nuclear protein that may be involved in transcriptional control and responses to DNA damage.


Pssm-ID: 153429  Cd Length: 100  Bit Score: 142.54  E-value: 3.50e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  94 VYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaqRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKN 173
Cdd:cd08002     1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESG--KEYYVWNRWGRVGEKGQNKLKGPWDSLEGAIKDFEKKFKDKTKN 78

                          90       100
                  ....*....|....*....|..
gi 1034585925 174 NWEDREKFEKVPGKYDMLQMDY 195
Cdd:cd08002    79 NWEDRENFVPHPGKYTLIEMDY 100
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 97-182 3.61e-31

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


Pssm-ID: 214814  Cd Length: 84  Bit Score: 115.08  E-value: 3.61e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925   97 EGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWE 176
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTKGQTKLKTF-DSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 1034585925  177 DREKFE 182
Cdd:smart00773  79 ERGKFV 84
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 64-475 8.87e-30

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 123.37  E-value: 8.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  64 DKQDESVKALL-------LKGKAPVDPECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDdAQRNFSVWM 136
Cdd:PLN03122  291 DKQDPSEEAIEslsaelkLYGKRGVYKDSKLQEEGGKIFEKDGILYNCAFSICDLGRGLNEYCIMQLITV-PDSNLHLYY 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 137 RWGRVG-KMGQHSLVACSGNLNKAKEIFQKKFLDKTKNN---WEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEESLK 212
Cdd:PLN03122  370 KKGRVGdDPNAEERLEEWEDVDAAIKEFVRLFEEITGNEfepWEREKKFEKKRLKFYPIDMDDGVDVRAGGLGLRQLGVA 449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 213 SPlkpESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRA----GQ-HGRALME 287
Cdd:PLN03122  450 AA---HCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSeketGQkAEAMWLD 526

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 288 ACNEFYTRIPHDfglrTPPLIRTQKELSEKI-QLLEALGDIEIAIKLVKTELQSP-EHPLDQHYRNLHCALRPLDHESYE 365
Cdd:PLN03122  527 FSNKWFSLVHST----RPFVIRDIDELADHAaSALETVRDINVASRLIGDMTGSTlDDPLSDRYKKLGCSISPVDKESDD 602

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 366 FKVISQYLQSTHAPTH---SDYTMTLLDLFEVEKDGeKEAFRE--DLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPIT 440
Cdd:PLN03122  603 YKMIVKYLEKTYEPVKvgdVSYSVSVENIFAVESSA-GPSLDEikKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLPVP 681

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1034585925 441 GYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLS 475
Cdd:PLN03122  682 GYMFGKAIVCSDAAAEAARYGFTAVDRPEGFLVLA 716
PARP2_NTR cd22252
NTR (N-terminal region) domain of poly [ADP-ribose] polymerase 2 (PARP-2) and similar proteins; ...
 19-78 3.86e-29

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


Pssm-ID: 412075  Cd Length: 59  Bit Score: 108.83  E-value: 3.86e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  19 ESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQdESVKALLLKGK 78
Cdd:cd22252     1 ESKRVNNGNTATEDSPPAKKTRRCQRKEVKKEPVAGGKADKDRTEDKQ-ESVKALLLKGK 59
WGR pfam05406
WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli ...
 102-182 6.72e-29

WGR domain; This domain is found in a variety of polyA polymerases as well as the E. coli molybdate metabolism regulator Swiss:P33345 and other proteins of unknown function. I have called this domain WGR after the most conserved central motif of the domain. The domain is found in isolation in proteins such as Swiss:Q9JN21 and is between 70 and 80 residues in length. I propose that this may be a nucleic acid binding domain.


Pssm-ID: 398851  Cd Length: 79  Bit Score: 108.87  E-value: 6.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 102 YDVMLNQTNLQFNNNKYYLIQlLEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWEDREKF 181
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQ-VEDDLFGGYSLFRRWGRIGTRGQTKLKSF-DSLEEAIKEFEKLFAEKTKKGYRERGEF 78


                  .
gi 1034585925 182 E 182
Cdd:pfam05406  79 E 79
WGR_PARP1_like cd08001
WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a ...
 92-195 2.51e-23

WGR domain of poly(ADP-ribose) polymerase 1 and similar proteins; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases (PARPs). It has been called WGR after the most conserved central motif of the domain. The domain typically occurs together with a catalytic PARP domain, and is between 70 and 80 residues in length. It has been proposed to function as a nucleic acid binding domain. PARPs catalyze the NAD(+)-dependent synthesis of ADP-ribose polymers and their addition to various nuclear proteins. Higher eukaryotes contain several PARPs and and there may be up to 17 human PARP-like proteins, with three of them (PARP-1, PARP-2, and PARP-3) containing a WGR domain. The synthesis of poly-ADP-ribose requires multiple enzymatic activities for initiation, trans-ADP-ribosylation, elongation, branching, and release of the polymer from the enzyme. This subfamily is composed of vertebrate PARP-1 and similar proteins, including Arabidopsis thaliana PARP-1 and PARP-3. PARP-1 is the best-studied among the PARPs. It is a widely expressed nuclear chromatin-associated enzyme that possesses auto-mono-ADP-ribosylation (initiation), elongation, and branching activities. PARP-1 is implicated in DNA damage and cell death pathways and is important in maintaining genomic stability and regulating cell proliferation, differentiation, neuronal function, inflammation, and aging.


Pssm-ID: 153428 [Multi-domain]  Cd Length: 104  Bit Score: 94.20  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925  92 AHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVG-KMGQHSLVACSgNLNKAKEIFQKKFLDK 170
Cdd:cd08001     1 AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGtTIGGNKLEEFS-SLEEAKMAFEELYEEK 79

                          90       100
                  ....*....|....*....|....*
gi 1034585925 171 TKNNWEDREKFEKVPGKYDMLQMDY 195
Cdd:cd08001    80 TGNDFENRKNFKKKPGKFYPLDIDY 104
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 413-461 5.08e-17

ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. Bacterial toxins are cytoplasmic and catalyze the transfer of a single ADP_ribose unit to eukaryotic elongation factor 2, halting protein synthesis and killing the cell. Poly(ADP-ribose) polymerases (PARPS 1-3, VPARP, tankyrase) catalyze the addition of up to 100 ADP_ribose units from NAD+. PARPs 1 and 2 are localized in the nucleaus, bind DNA, and are activated by DNA damage. VPARP is part of the vault ribonucleoprotein complex. Tankyrases regulates telomere length in part through poy(ADP_ribosylation) of telomere repeat binding factor 1 (TRF1). Poly(ADP-ribose) polymerase catalyses the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. Experiments have shown that a carboxyl 40 kDa fragment is still catalytically active.


Pssm-ID: 238651 [Multi-domain]  Cd Length: 137  Bit Score: 77.60  E-value: 5.08e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1034585925 413 LWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYC 461
Cdd:cd01341     2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYS 50
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 112-177 2.83e-07

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


Pssm-ID: 153424  Cd Length: 73  Bit Score: 47.66  E-value: 2.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034585925 112 QFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWED 177
Cdd:cd07994     8 DIGSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 114-172 4.91e-04

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


Pssm-ID: 153425  Cd Length: 74  Bit Score: 38.74  E-value: 4.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034585925 114 NNNKYYLIQLlEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 172
Cdd:cd07996    12 NSARFYEIEL-EGDLFGEWSLVRRWGRIGTKGQSRTKTF-DSEEEALKAAEKLIREKLK 68
TCCD_inducible_PARP_like cd01439
Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to ...
 412-461 9.97e-04

Poly(ADP-ribose) polymerases catalyse the covalent attachment of ADP-ribose units from NAD+ to itself and to a limited number of other DNA binding proteins, which decreases their affinity for DNA. Poly(ADP-ribose) polymerase is a regulatory component induced by DNA damage. The carboxyl-terminal region is the most highly conserved region of the protein. 2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. TCCD indicible PARP (TiPARP) is a target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation


Pssm-ID: 238719 [Multi-domain]  Cd Length: 121  Bit Score: 38.84  E-value: 9.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034585925 412 LLWHGSRMSNWVGILSHGL--RIAPPEAPitgyMFGKGIYFADMSSKSANYC 461
Cdd:cd01439     1 LLFHGTSADAVEAICRHGFdrRFCGKHGT----MYGKGSYFAKNASYSHQYS 48
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 356-462 1.45e-03

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


Pssm-ID: 238718 [Multi-domain]  Cd Length: 223  Bit Score: 40.27  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034585925 356 LRPLDHEsyeFKVISQYLQST---------HAPTHSDYTMTLLDLFEVEKDGEKEAFRED--------LHNRMLLWHGSR 418
Cdd:cd01438    21 LAPDDKE---YQSVEEEMQSTirehrdggnAGGIFNRYNIIRIQKVVNKKLRERYCHRQKeiaeenhnHHNERMLFHGSP 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1034585925 419 MSNwvGILSHGLRiaPPEAPITGyMFGKGIYFADMSSKSANYCF 462
Cdd:cd01438    98 FIN--AIIHKGFD--ERHAYIGG-MFGAGIYFAENSSKSNQYVY 136
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
114-172 3.02e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 36.50  E-value: 3.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034585925 114 NNNKYYLIQLlEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 172
Cdd:COG3831    13 NSARFYELEV-EPDLFGGWSLTRRWGRIGTKGQTKTKTF-ASEEEALAALEKLVAEKLR 69
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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