NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|110825963|ref|NP_001036083|]
View 

poly [ADP-ribose] polymerase 2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN03124 super family cl33640
poly [ADP-ribose] polymerase; Provisional
 52-566 0e+00

poly [ADP-ribose] polymerase; Provisional


The actual alignment was detected with superfamily member PLN03124:

Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 554.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  52 VAGGKANKDRTEDKQDESVKALLlKGKAPVDPECTAKVgKA--HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQ 129
Cdd:PLN03124 127 EDEKEKGGDEEREKEEKIVTATK-KGRAVLDQWLPDHI-KSnyHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 130 RNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYatntQDEEETKKE- 208
Cdd:PLN03124 205 SKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDY----EDEEESKKDk 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 209 ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALME 287
Cdd:PLN03124 281 PSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEE 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 288 ACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYE 365
Cdd:PLN03124 360 LSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEE 439

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 366 FKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYM 443
Cdd:PLN03124 440 FSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYM 519

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 444 FGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTL-NGST 522
Cdd:PLN03124 520 FGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGDMNELLQADYNANKLPPGKLSTKGVGRTVPDPSEAKTLeDGVV 599

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 110825963 523 VPLG-----PASDTGilnpdgytLNYNEYIVYNPNQVRMRYLLKVQFNF 566
Cdd:PLN03124 600 VPLGkpvesPYSKGS--------LEYNEYIVYNVDQIRMRYVLQVKFNY 640
PARP2_NTR cd22252
NTR (N-terminal region) domain of poly [ADP-ribose] polymerase 2 (PARP-2) and similar proteins; ...
 19-78 7.57e-30

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: 111.53  E-value: 7.57e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  19 ESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQdESVKALLLKGK 78
Cdd:cd22252    1 ESKRVNNGNTATEDSPPAKKTRRCQRKEVKKEPVAGGKADKDRTEDKQ-ESVKALLLKGK 59
 
Name Accession Description Interval E-value
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 52-566 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 554.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  52 VAGGKANKDRTEDKQDESVKALLlKGKAPVDPECTAKVgKA--HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQ 129
Cdd:PLN03124 127 EDEKEKGGDEEREKEEKIVTATK-KGRAVLDQWLPDHI-KSnyHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 130 RNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYatntQDEEETKKE- 208
Cdd:PLN03124 205 SKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDY----EDEEESKKDk 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 209 ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALME 287
Cdd:PLN03124 281 PSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEE 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 288 ACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYE 365
Cdd:PLN03124 360 LSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEE 439

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 366 FKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYM 443
Cdd:PLN03124 440 FSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYM 519

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 444 FGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTL-NGST 522
Cdd:PLN03124 520 FGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGDMNELLQADYNANKLPPGKLSTKGVGRTVPDPSEAKTLeDGVV 599

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 110825963 523 VPLG-----PASDTGilnpdgytLNYNEYIVYNPNQVRMRYLLKVQFNF 566
Cdd:PLN03124 600 VPLGkpvesPYSKGS--------LEYNEYIVYNVDQIRMRYVLQVKFNY 640
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 218-563 8.45e-172

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: 490.24  E-value: 8.45e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 218 ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQH-GRALMEACNEFYTRI 296
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 297 PHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQST 376
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 377 HAPTHsDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMS 454
Cdd:cd01437  161 HAPTT-EYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 455 SKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPS-SAHFVTLNGSTVPLGPASDTGI 533
Cdd:cd01437  240 SKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDpSEFEIDLDGVVVPLGKPVPSGH 319

                        330       340       350
                 ....*....|....*....|....*....|
gi 110825963 534 LNpdGYTLNYNEYIVYNPNQVRMRYLLKVQ 563
Cdd:cd01437  320 KT--DTSLLYNEYIVYDVAQVRLKYLLEVK 347
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 363-564 2.33e-94

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: 286.54  E-value: 2.33e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  363 SYEFKVISQYLQSTHAPTHSdYTMTLLDLFEVEKDGEKEAFRED--LHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPIT 440
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKkkLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  441 GYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPkAEGLLQGKHSTKGLGKMAPssAHFVTLNG 520
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAP--ESFVDLDG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 110825963  521 stVPLGPASDTGIlnpDGYTLNYNEYIVYNPNQVRMRYLLKVQF 564
Cdd:pfam00644 157 --VPLGKLVATGY---DSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR smart00773
Proposed nucleic acid binding domain; This domain is named after its most conserved central ...
 97-182 2.01e-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: 116.62  E-value: 2.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963    97 EGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWE 176
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTKGQTKLKTF-DSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 110825963   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 7.57e-30

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: 111.53  E-value: 7.57e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  19 ESKRVNNGNTAPEDSSPAKKTRRCQRQESKKMPVAGGKANKDRTEDKQdESVKALLLKGK 78
Cdd:cd22252    1 ESKRVNNGNTATEDSPPAKKTRRCQRKEVKKEPVAGGKADKDRTEDKQ-ESVKALLLKGK 59
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
114-172 2.56e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 37.27  E-value: 2.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 110825963 114 NNNKYYLIQLlEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 172
Cdd:COG3831   13 NSARFYELEV-EPDLFGGWSLTRRWGRIGTKGQTKTKTF-ASEEEALAALEKLVAEKLR 69
 
Name Accession Description Interval E-value
PLN03124 PLN03124
poly [ADP-ribose] polymerase; Provisional
 52-566 0e+00

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215591 [Multi-domain]  Cd Length: 643  Bit Score: 554.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  52 VAGGKANKDRTEDKQDESVKALLlKGKAPVDPECTAKVgKA--HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQ 129
Cdd:PLN03124 127 EDEKEKGGDEEREKEEKIVTATK-KGRAVLDQWLPDHI-KSnyHVLEEGDDVYDAMLNQTNVGDNNNKFYVLQVLESDDG 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 130 RNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWEDREKFEKVPGKYDMLQMDYatntQDEEETKKE- 208
Cdd:PLN03124 205 SKYMVYTRWGRVGVKGQDKLHGPYDSREPAIREFEKKFYDKTKNHWSDRKNFISHPKKYTWLEMDY----EDEEESKKDk 280

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 209 ESLKSPLKP-ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQHgRALME 287
Cdd:PLN03124 281 PSVSSEDKNkQSKLDPRVAQFISLICDVSMMKQQMMEIGYNARKLPLGKLSKSTILKGYEVLKRIAEVISRSDR-ETLEE 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 288 ACNEFYTRIPHDFGLRT--PPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYE 365
Cdd:PLN03124 360 LSGEFYTVIPHDFGFKKmrQFTIDTPQKLKHKLEMVEALGEIEIATKLLKDDIGEQDDPLYAHYKRLNCELEPLDTDSEE 439

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 366 FKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYM 443
Cdd:PLN03124 440 FSMIAKYLENTHGQTHSGYTLEIVQIFKVSREGEDERFQkfSSTKNRMLLWHGSRLTNWTGILSQGLRIAPPEAPSTGYM 519

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 444 FGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAHFVTL-NGST 522
Cdd:PLN03124 520 FGKGVYFADMFSKSANYCYASAANPDGVLLLCEVALGDMNELLQADYNANKLPPGKLSTKGVGRTVPDPSEAKTLeDGVV 599

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 110825963 523 VPLG-----PASDTGilnpdgytLNYNEYIVYNPNQVRMRYLLKVQFNF 566
Cdd:PLN03124 600 VPLGkpvesPYSKGS--------LEYNEYIVYNVDQIRMRYVLQVKFNY 640
parp_like cd01437
Poly(ADP-ribose) polymerase (parp) catalytic domain catalyses the covalent attachment of ...
 218-563 8.45e-172

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: 490.24  E-value: 8.45e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 218 ESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQH-GRALMEACNEFYTRI 296
Cdd:cd01437    1 KSKLDKPVQELIKLIFDVEMMKKAMTELKIDASKMPLGKLSKNQIQKGYEVLKEIEEALKRGSSqGSQLEELSNEFYTLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 297 PHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEHPLDQHYRNLHCALRPLDHESYEFKVISQYLQST 376
Cdd:cd01437   81 PHDFGMSKPPVIDNEELLKAKRELLEALRDIEIASKLLKDDEDDSDDPLDANYEKLKCKIEPLDKDSEEYKIIEKYLKNT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 377 HAPTHsDYTMTLLDLFEVEKDGEKEAFR--EDLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMS 454
Cdd:cd01437  161 HAPTT-EYTVEVQEIFRVEREGETDRFKpfKKLGNRKLLWHGSRLTNFVGILSQGLRIAPPEAPVTGYMFGKGIYFADMF 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 455 SKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPS-SAHFVTLNGSTVPLGPASDTGI 533
Cdd:cd01437  240 SKSANYCHASASDPTGLLLLCEVALGKMNELKKADYMAKELPKGKHSVKGLGKTAPDpSEFEIDLDGVVVPLGKPVPSGH 319

                        330       340       350
                 ....*....|....*....|....*....|
gi 110825963 534 LNpdGYTLNYNEYIVYNPNQVRMRYLLKVQ 563
Cdd:cd01437  320 KT--DTSLLYNEYIVYDVAQVRLKYLLEVK 347
PLN03123 PLN03123
poly [ADP-ribose] polymerase; Provisional
 48-564 1.32e-145

poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 215590 [Multi-domain]  Cd Length: 981  Bit Score: 444.62  E-value: 1.32e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  48 KKMPVAGGKANKDRTEdkqdESVKALLLKGKAPVDpECTAKVGKAHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDD 127
Cdd:PLN03123 471 KKLPFDKYKLEASGTS----SSMVTVKVKGRSAVH-EASGLQDTGHILEDGKSIYNTTLNMSDLSTGVNSYYILQIIEED 545

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 128 AQRNFSVWMRWGRVG--KMGQHSLVACSgnlnKAKEI--FQKKFLDKTKNNWE---DREKFEKVPGKYDMLQMDYATNtq 200
Cdd:PLN03123 546 KGSDCYVFRKWGRVGneKIGGNKLEEMS----KSDAIheFKRLFLEKTGNPWEsweQKTNFQKQPGKFYPLDIDYGVN-- 619

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 201 dEEETKKEESlksplKPESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAGQ 280
Cdd:PLN03123 620 -EQPKKKAAS-----GSKSNLAPRLVELMKMLFDVETYRAAMMEFEINMSEMPLGKLSKANIQKGFEALTEIQNLLKEND 693

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 281 HGRA-----LMEACNEFYTRIP--HdfglrtPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSPEhPLDQHYRNLH 353
Cdd:PLN03123 694 QDPSireslLVDASNRFFTLIPsiH------PHIIRDEDDLKSKVKMLEALQDIEIASRLVGFDVDEDD-SLDDKYKKLH 766

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 354 CALRPLDHESYEFKVISQYLQSTHAPTHSDYTMTLLDLFEVEKDGEKEAF---REDLHNRMLLWHGSRMSNWVGILSHGL 430
Cdd:PLN03123 767 CDISPLPHDSEDYKLIEKYLLTTHAPTHTDWSLELEEVFSLEREGEFDKYapyKEKLKNRMLLWHGSRLTNFVGILSQGL 846

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 431 RIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANpKAEGLLQGKHSTKGLGKMAP 510
Cdd:PLN03123 847 RIAPPEAPATGYMFGKGVYFADLVSKSAQYCYTDRKNPVGLMLLSEVALGEIYELKKAK-YMDKPPRGKHSTKGLGKTVP 925

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 110825963 511 SSAHFVTL-NGSTVPLGPASDTGILNPDgytLNYNEYIVYNPNQVRMRYLLKVQF 564
Cdd:PLN03123 926 QESEFVKWrDDVVVPCGKPVPSKVKASE---LMYNEYIVYNTAQVKLQFLLKVRF 977
PARP pfam00644
Poly(ADP-ribose) polymerase catalytic domain; Poly(ADP-ribose) polymerase catalyzes the ...
 363-564 2.33e-94

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: 286.54  E-value: 2.33e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  363 SYEFKVISQYLQSTHAPTHSdYTMTLLDLFEVEKDGEKEAFRED--LHNRMLLWHGSRMSNWVGILSHGLRIAPPEAPIT 440
Cdd:pfam00644   1 SEEYQIIEKYFLSTHDPTHG-YPLFILEIFRVQRDGEWERFQPKkkLRNRRLLWHGSRLTNFLGILSQGLRIAPPEAPVT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  441 GYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALGQCNELLEANPkAEGLLQGKHSTKGLGKMAPssAHFVTLNG 520
Cdd:pfam00644  80 GYMFGKGIYFADDASKSANYCPPSEAHGNGLMLLSEVALGDMNELKKADY-AEKLPPGKHSVKGLGKTAP--ESFVDLDG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 110825963  521 stVPLGPASDTGIlnpDGYTLNYNEYIVYNPNQVRMRYLLKVQF 564
Cdd:pfam00644 157 --VPLGKLVATGY---DSSVLLYNEYVVYNVNQVRPKYLLEVKF 195
WGR_PARP2_like cd08003
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 93-195 1.21e-70

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: 221.82  E-value: 1.21e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  93 HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTK 172
Cdd:cd08003    1 HVYEEGDDVYDAMLNQTNIQQNNNKYYIIQLLEDDAEKIYSVWFRWGRVGKKGQSSLVPCGSDLEQAKSLFEKKFLDKTK 80

                         90       100
                 ....*....|....*....|...
gi 110825963 173 NNWEDREKFEKVPGKYDMLQMDY 195
Cdd:cd08003   81 NEWEDRANFEKVAGKYDLLEMDY 103
PARP_reg pfam02877
Poly(ADP-ribose) polymerase, regulatory domain; Poly(ADP-ribose) polymerase catalyzes the ...
 219-349 2.48e-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: 172.32  E-value: 2.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  219 SQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRAG---QHGRALMEACNEFYTR 295
Cdd:pfam02877   1 SKLPPPVQELMKLIFNVEMMKKAMKEMKYDAKKMPLGKLSKRQIKKGYEVLKELSELLKKPslaKAKAKLEDLSNRFYTL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110825963  296 IPHDFGLRTPPLIRTQKELSEKIQLLEALGDIEIAIKLVKTELQSP-EHPLDQHY 349
Cdd:pfam02877  81 IPHDFGRNRPPVIDTEEELKEKLELLEALLDIEVASKLLKDSKSDDdEHPLDRHY 135
PLN03122 PLN03122
Poly [ADP-ribose] polymerase; Provisional
 64-564 3.89e-49

Poly [ADP-ribose] polymerase; Provisional


Pssm-ID: 178669 [Multi-domain]  Cd Length: 815  Bit Score: 182.31  E-value: 3.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  64 DKQDESVKALL-------LKGKAPV--DPECTAKVGKahVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDdAQRNFSV 134
Cdd:PLN03122 291 DKQDPSEEAIEslsaelkLYGKRGVykDSKLQEEGGK--IFEKDGILYNCAFSICDLGRGLNEYCIMQLITV-PDSNLHL 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 135 WMRWGRVG-KMGQHSLVACSGNLNKAKEIFQKKFLDKTKNN---WEDREKFEKVPGKYDMLQMDYATNTQDEEETKKEES 210
Cdd:PLN03122 368 YYKKGRVGdDPNAEERLEEWEDVDAAIKEFVRLFEEITGNEfepWEREKKFEKKRLKFYPIDMDDGVDVRAGGLGLRQLG 447

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 211 LKSPlkpESQLDLRVQELIKLICNVQAMEEMMMEMKYNTKKAPLGKLTVAQIKAGYQSLKKIEDCIRA----GQ-HGRAL 285
Cdd:PLN03122 448 VAAA---HCKLDPKVANFMKVLCSQEIYRYAMMEMGLDSPDLPMGMLSDFHLKRCEEVLLEFAEFVKSeketGQkAEAMW 524

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 286 MEACNEFYTRIPHDfglrTPPLIRTQKELSEKI-QLLEALGDIEIAIKLVKTELQSP-EHPLDQHYRNLHCALRPLDHES 363
Cdd:PLN03122 525 LDFSNKWFSLVHST----RPFVIRDIDELADHAaSALETVRDINVASRLIGDMTGSTlDDPLSDRYKKLGCSISPVDKES 600

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 364 YEFKVISQYLQSTHAPTH---SDYTMTLLDLFEVEKDGeKEAFRE--DLHNRMLLWHGSRMSNWVGILSHGLRIAPPEAP 438
Cdd:PLN03122 601 DDYKMIVKYLEKTYEPVKvgdVSYSVSVENIFAVESSA-GPSLDEikKLPNKVLLWCGTRSSNLLRHLAKGFLPAVCSLP 679

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 439 ITGYMFGKGIYFADMSSKSANYCFASRLKNTGLLLLSEVALG-QCNELLEANPKAEGLLQGKHSTKGLGKMAP-SSAHFV 516
Cdd:PLN03122 680 VPGYMFGKAIVCSDAAAEAARYGFTAVDRPEGFLVLAVASLGdEVLELTKPPEDVKSYEEKKVGVKGLGRKKTdESEHFK 759

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|.
gi 110825963 517 TLNGSTVPLGPasdtgiLNPDGY---TLNYNEYIVYNPNQVRMRYLLKVQF 564
Cdd:PLN03122 760 WRDDITVPCGR------LIPSEHkdsPLEYNEYAVYDPKQVSIRFLVGVKY 804
WGR_PARP cd07997
WGR domain of poly(ADP-ribose) polymerases; The WGR domain is found in a variety of eukaryotic ...
 93-195 2.35e-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: 149.76  E-value: 2.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  93 HVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTK 172
Cdd:cd07997    1 HVYGDIATVYDATLNQTDISNNNNKFYKIQILESKGPNTYALFTRWGRVGERGQSQLTPF-GSLESAIKEFEKKFKDKTG 79

                         90       100
                 ....*....|....*....|...
gi 110825963 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 8.22e-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: 142.93  E-value: 8.22e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  94 VYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaqRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKN 173
Cdd:cd08002    1 VGAEVDEDYDCMLNQTNIGHNNNKFYVIQLLESG--KEYYVWNRWGRVGEKGQNKLKGPWDSLEGAIKDFEKKFKDKTKN 78

                         90       100
                 ....*....|....*....|..
gi 110825963 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 2.01e-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: 116.62  E-value: 2.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963    97 EGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDaQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWE 176
Cdd:smart00773   1 EGGEIYDVYLNFTDLASNNNKFYIIQLLEDD-FGGYSVYRRWGRIGTKGQTKLKTF-DSLEDAIKEFEKLFKEKTKNGYE 78


                   ....*.
gi 110825963   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 7.57e-30

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: 111.53  E-value: 7.57e-30
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  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 3.96e-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: 110.02  E-value: 3.96e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  102 YDVMLNQTNLQFNNNKYYLIQlLEDDAQRNFSVWMRWGRVGKMGQHSLVACsGNLNKAKEIFQKKFLDKTKNNWEDREKF 181
Cdd:pfam05406   1 YDLYLEQTDAARNSNKFYEIQ-VEDDLFGGYSLFRRWGRIGTRGQTKLKSF-DSLEEAIKEFEKLFAEKTKKGYRERGEF 78


                  .
gi 110825963  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 1.89e-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: 94.97  E-value: 1.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963  92 AHVYCEGNDVYDVMLNQTNLQFNNNKYYLIQLLEDDAQRNFSVWMRWGRVG-KMGQHSLVACSgNLNKAKEIFQKKFLDK 170
Cdd:cd08001    1 AHVLEEGGNLYSAVLGLVDIQTGTNSYYKLQLLEHDKGNRYWVFRSWGRVGtTIGGNKLEEFS-SLEEAKMAFEELYEEK 79

                         90       100
                 ....*....|....*....|....*
gi 110825963 171 TKNNWEDREKFEKVPGKYDMLQMDY 195
Cdd:cd08001   80 TGNDFENRKNFKKKPGKFYPLDIDY 104
ADP_ribosyl cd01341
ADP_ribosylating enzymes catalyze the transfer of ADP_ribose from NAD+ to substrates. ...
 413-558 3.19e-19

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: 84.15  E-value: 3.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 413 LWHGSRMSNWVGILSHGLRIAPPEAPITGYMFGKGIYFADMSSKSANYCFASRLKNT----------------GLLLLSE 476
Cdd:cd01341    2 LFHGSPPGNVISILKLGLRPASYGVLLNGGMFGKGIYSAPNISKSNGYSVGCDGQHVfqngkpkvcgrelcvfGFLTLGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 477 VALGQCNELLEANPKAEGLLQGKHSTKGLGKMAPSSAhfvtlngstvplgpasdtgilnpdgytLNYNEYIVYNPN-QVR 555
Cdd:cd01341   82 MSGATEESSRVLFPRNFRGATGAEVVDLLVAMCRDAL---------------------------LLPREYIIFEPYsQVS 134


                 ...
gi 110825963 556 MRY 558
Cdd:cd01341  135 IRY 137
WGR cd07994
WGR domain; The WGR domain is found in a variety of eukaryotic poly(ADP-ribose) polymerases ...
 112-177 2.21e-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: 2.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110825963 112 QFNNNKYYLIQLLEDDAQRNFSVWMRWGRVGKMGQHSLVACSGNLNKAKEIFQKKFLDKTKNNWED 177
Cdd:cd07994    8 DIGSNKYYKLQLLEDDKENRYWVFRSYGRVGTVIGSTKLEQMPSKEEAEEHFMKLYEEKTGKGYYP 73
tankyrase_like cd01438
Tankyrases interact with the telomere reverse transcriptase complex (TERT). Tankyrase 1 ...
 356-563 2.59e-04

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: 42.58  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 356 LRPLDHEsyeFKVISQYLQST---------HAPTHSDYTMTLLDLFEVEKDGEKEAFRED--------LHNRMLLWHGSR 418
Cdd:cd01438   21 LAPDDKE---YQSVEEEMQSTirehrdggnAGGIFNRYNIIRIQKVVNKKLRERYCHRQKeiaeenhnHHNERMLFHGSP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825963 419 MSNwvGILSHGLRiaPPEAPITGyMFGKGIYFADMSSKSANY---------CFASRLKNTGL----LLLSEVALGQcnel 485
Cdd:cd01438   98 FIN--AIIHKGFD--ERHAYIGG-MFGAGIYFAENSSKSNQYvygigggtgCPTHKDRSCYVchrqMLFCRVTLGK---- 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110825963 486 leanpkaegllqgkhstkglgkmapSSAHFVTLNGSTVPLGPASDTGilNPDGYTLNYNEYIVYNPNQVRMRYLLKVQ 563
Cdd:cd01438  169 -------------------------SFLQFSAMKMAHAPPGHHSVIG--RPSVNGLAYAEYVIYRGEQAYPEYLITYQ 219
WGR_MMR_like cd07996
WGR domain of molybdate metabolism regulator and related proteins; The WGR domain is found in ...
 114-172 3.12e-04

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


Pssm-ID: 153425  Cd Length: 74  Bit Score: 39.51  E-value: 3.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 110825963 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 1.19e-03

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: 1.19e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110825963 412 LLWHGSRMSNWVGILSHGL--RIAPPEAPitgyMFGKGIYFADMSSKSANYC 461
Cdd:cd01439    1 LLFHGTSADAVEAICRHGFdrRFCGKHGT----MYGKGSYFAKNASYSHQYS 48
WGR COG3831
WGR domain, predicted DNA-binding domain in MolR [Transcription];
114-172 2.56e-03

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


Pssm-ID: 443043  Cd Length: 83  Bit Score: 37.27  E-value: 2.56e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 110825963 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH