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Conserved domains on  [gi|1937906948|ref|NP_112629|]
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poly(ADP-ribose) glycohydrolase [Rattus norvegicus]

Protein Classification

poly(ADP-ribose) glycohydrolase( domain architecture ID 10523475)

poly(ADP-ribose) glycohydrolase hydrolyzes poly(ADP-D-ribose) at glycosidic (1''-2') linkages of ribose-ribose bonds to produce free ADP-D-ribose

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PARG_cat pfam05028
Poly (ADP-ribose) glycohydrolase (PARG); Poly(ADP-ribose) glycohydrolase (PARG), is a ...
577-905 4.12e-176

Poly (ADP-ribose) glycohydrolase (PARG); Poly(ADP-ribose) glycohydrolase (PARG), is a ubiquitously expressed exo- and endoglycohydrolase which mediates oxidative and excitotoxic neuronal death.


:

Pssm-ID: 461528  Cd Length: 329  Bit Score: 514.42  E-value: 4.12e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 577 LEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNakmkSEYSSYPDIN 656
Cdd:pfam05028   1 LDEEESQVFFSETLPKIARLALRLPSLFPAPIPLLKQGENGSVTLSQEQIACLLANAFFCTFPRQR----REYKNFPSIN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 657 FNRLFE--GRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSL--EDFPEWERCDKPLTRLHVTYEGTIEGNGRGMLQV 732
Cdd:pfam05028  77 FDRLFNsnSRSKVRCEKLKCLLHYFERVTSSMPTGLVTFERRVLsdPDIPDWSKSTKPLSSVHVTSDGTIEDQGVGALQV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 733 DFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQR 812
Cdd:pfam05028 157 DFANKYIGGGVLGEGCVQEEIRFLINPELIVSRLFTEVLEDNEALIITGAERFSNYSGYASSFRFAGDYIDTTPRDSTGR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 813 RCTEIVAIDALHFrRYLDQFVPEKVRRELNKAYCGFLRPGV-PPENLSAVATGNWGCGAFGGD----------ARlkali 881
Cdd:pfam05028 237 RKTDIVAIDALYF-PSSSQYKPENILRELNKAYCGFSSQYVsLFVSTSPIATGNWGCGAFGGDpelkaliqwlAA----- 310
                         330       340
                  ....*....|....*....|....
gi 1937906948 882 qllaaAAAERDVVYFTFGDSELMR 905
Cdd:pfam05028 311 -----SQAGRPLIYYTFGDEELQT 329
 
Name Accession Description Interval E-value
PARG_cat pfam05028
Poly (ADP-ribose) glycohydrolase (PARG); Poly(ADP-ribose) glycohydrolase (PARG), is a ...
577-905 4.12e-176

Poly (ADP-ribose) glycohydrolase (PARG); Poly(ADP-ribose) glycohydrolase (PARG), is a ubiquitously expressed exo- and endoglycohydrolase which mediates oxidative and excitotoxic neuronal death.


Pssm-ID: 461528  Cd Length: 329  Bit Score: 514.42  E-value: 4.12e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 577 LEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNakmkSEYSSYPDIN 656
Cdd:pfam05028   1 LDEEESQVFFSETLPKIARLALRLPSLFPAPIPLLKQGENGSVTLSQEQIACLLANAFFCTFPRQR----REYKNFPSIN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 657 FNRLFE--GRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSL--EDFPEWERCDKPLTRLHVTYEGTIEGNGRGMLQV 732
Cdd:pfam05028  77 FDRLFNsnSRSKVRCEKLKCLLHYFERVTSSMPTGLVTFERRVLsdPDIPDWSKSTKPLSSVHVTSDGTIEDQGVGALQV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 733 DFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQR 812
Cdd:pfam05028 157 DFANKYIGGGVLGEGCVQEEIRFLINPELIVSRLFTEVLEDNEALIITGAERFSNYSGYASSFRFAGDYIDTTPRDSTGR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 813 RCTEIVAIDALHFrRYLDQFVPEKVRRELNKAYCGFLRPGV-PPENLSAVATGNWGCGAFGGD----------ARlkali 881
Cdd:pfam05028 237 RKTDIVAIDALYF-PSSSQYKPENILRELNKAYCGFSSQYVsLFVSTSPIATGNWGCGAFGGDpelkaliqwlAA----- 310
                         330       340
                  ....*....|....*....|....
gi 1937906948 882 qllaaAAAERDVVYFTFGDSELMR 905
Cdd:pfam05028 311 -----SQAGRPLIYYTFGDEELQT 329
 
Name Accession Description Interval E-value
PARG_cat pfam05028
Poly (ADP-ribose) glycohydrolase (PARG); Poly(ADP-ribose) glycohydrolase (PARG), is a ...
577-905 4.12e-176

Poly (ADP-ribose) glycohydrolase (PARG); Poly(ADP-ribose) glycohydrolase (PARG), is a ubiquitously expressed exo- and endoglycohydrolase which mediates oxidative and excitotoxic neuronal death.


Pssm-ID: 461528  Cd Length: 329  Bit Score: 514.42  E-value: 4.12e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 577 LEEAEAQHLYQSILPDMVKIALCLPNICTQPIPLLKQKMNHSVTMSQEQIASLLANAFFCTFPRRNakmkSEYSSYPDIN 656
Cdd:pfam05028   1 LDEEESQVFFSETLPKIARLALRLPSLFPAPIPLLKQGENGSVTLSQEQIACLLANAFFCTFPRQR----REYKNFPSIN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 657 FNRLFE--GRSSRKPEKLKTLFCYFRRVTEKKPTGLVTFTRQSL--EDFPEWERCDKPLTRLHVTYEGTIEGNGRGMLQV 732
Cdd:pfam05028  77 FDRLFNsnSRSKVRCEKLKCLLHYFERVTSSMPTGLVTFERRVLsdPDIPDWSKSTKPLSSVHVTSDGTIEDQGVGALQV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 733 DFANRFVGGGVTGAGLVQEEIRFLINPELIVSRLFTEVLDHNECLIITGTEQYSEYTGYAETYRWARSHEDGSEKDDWQR 812
Cdd:pfam05028 157 DFANKYIGGGVLGEGCVQEEIRFLINPELIVSRLFTEVLEDNEALIITGAERFSNYSGYASSFRFAGDYIDTTPRDSTGR 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937906948 813 RCTEIVAIDALHFrRYLDQFVPEKVRRELNKAYCGFLRPGV-PPENLSAVATGNWGCGAFGGD----------ARlkali 881
Cdd:pfam05028 237 RKTDIVAIDALYF-PSSSQYKPENILRELNKAYCGFSSQYVsLFVSTSPIATGNWGCGAFGGDpelkaliqwlAA----- 310
                         330       340
                  ....*....|....*....|....
gi 1937906948 882 qllaaAAAERDVVYFTFGDSELMR 905
Cdd:pfam05028 311 -----SQAGRPLIYYTFGDEELQT 329
 
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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