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Conserved domains on  [gi|28916671|ref|NP_598644|]
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ADP-ribosylhydrolase ARH3 [Mus musculus]

Protein Classification

ADP-ribosylglycohydrolase family protein( domain architecture ID 10003641)

ADP-ribosylglycohydrolase family protein similar to vertebrate [protein ADP-ribosylarginine] hydrolase, which catalyzes the reverse reaction of mono-ADP-ribosylation, and Tripedalia cystophora major lens protein crystallin J1

CATH:  1.10.4080.10

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
27-366 1.00e-52

ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 441007  Cd Length: 256  Bit Score: 175.43  E-value: 1.00e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671  27 SRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESL-EPDPGTPGSartetlyYTDDTAMTRALVQSLLAKEAFDEVD 105
Cdd:COG1397   3 DRARGALLGLAIGDALGAPVEFYSREEIRARYGPITDYvGGGNLPPGE-------WTDDTQMALALAESLLEAGGFDPED 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 106 MAHRFAQEYKKDPDRGYGAGVITVFKKLLNPkcrdvyepaRAQFNGKGSYGNGGAMRVAGISLAYS-SVQDVQKFARLSA 184
Cdd:COG1397  76 LARRFLRWLRTGPGRDIGPTTRRALRNLRRG---------GAGESGEGSAGNGAAMRIAPLGLAYAgDPEEAAELARASA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 185 QLTHASSLGYNGAILQALAVHLALQGVSSSEhfleqllghmeelegdaqsvldakelgmeerpyssrlkkvgelldqdvv 264
Cdd:COG1397 147 ALTHGHPRAIAGAVAYAAAVAAALRGADLEE------------------------------------------------- 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 265 sreevvselgngIAAFESVPTAIYCFLRcmephpeipstFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPES 344
Cdd:COG1397 178 ------------GYVVETLPAALWALLR-----------ADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPER 234
                       330       340
                ....*....|....*....|..
gi 28916671 345 WQQSCEGFEETDVLAQSLHRVF 366
Cdd:COG1397 235 WLEPLERRDRLEELAERLAALA 256
 
Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
27-366 1.00e-52

ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441007  Cd Length: 256  Bit Score: 175.43  E-value: 1.00e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671  27 SRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESL-EPDPGTPGSartetlyYTDDTAMTRALVQSLLAKEAFDEVD 105
Cdd:COG1397   3 DRARGALLGLAIGDALGAPVEFYSREEIRARYGPITDYvGGGNLPPGE-------WTDDTQMALALAESLLEAGGFDPED 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 106 MAHRFAQEYKKDPDRGYGAGVITVFKKLLNPkcrdvyepaRAQFNGKGSYGNGGAMRVAGISLAYS-SVQDVQKFARLSA 184
Cdd:COG1397  76 LARRFLRWLRTGPGRDIGPTTRRALRNLRRG---------GAGESGEGSAGNGAAMRIAPLGLAYAgDPEEAAELARASA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 185 QLTHASSLGYNGAILQALAVHLALQGVSSSEhfleqllghmeelegdaqsvldakelgmeerpyssrlkkvgelldqdvv 264
Cdd:COG1397 147 ALTHGHPRAIAGAVAYAAAVAAALRGADLEE------------------------------------------------- 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 265 sreevvselgngIAAFESVPTAIYCFLRcmephpeipstFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPES 344
Cdd:COG1397 178 ------------GYVVETLPAALWALLR-----------ADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPER 234
                       330       340
                ....*....|....*....|..
gi 28916671 345 WQQSCEGFEETDVLAQSLHRVF 366
Cdd:COG1397 235 WLEPLERRDRLEELAERLAALA 256
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
31-343 5.87e-41

ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ADP-ribosylarginine hydrolase EC:3.2.2.19 cleaves ADP-ribose-L-arginine. The family also includes dinitrogenase reductase activating glycohydrolase. Most surprisingly the family also includes jellyfish crystallins, these proteins appear to have lost the presumed active site residues.


Pssm-ID: 461037 [Multi-domain]  Cd Length: 200  Bit Score: 142.71  E-value: 5.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671    31 GCLAGALLGDCVGAVYEAHdtvSLASVLSHVESLEPDPGTPGSARTETLYYTDDTAMTRALVQSLLAKEAFDEVDMAHRF 110
Cdd:pfam03747   1 GALLGLAVGDALGAPVEFW---SYDEIRREYGGIGTPMPGGGHLGLPPGEWTDDTQMALALLESLLEAGGFDPEDLARRL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671   111 AqeykkdpdrgygagvitvfkkllnpkcrdvyeparaqfngkgsygnggaMRVAGISLAYS-SVQDVQKFARLSAQLTHA 189
Cdd:pfam03747  78 A-------------------------------------------------MRIAPLGLLYPgDPEEAAELARESARLTHG 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671   190 SSLGYNGAILQALAVHLALQGVSssehfleqllghmeelegdaqsvldakelgmeerpyssrlkkvgelldqdvvsREEV 269
Cdd:pfam03747 109 HPRAVAGAVAYAAAIAAALRGAD-----------------------------------------------------LEEA 135
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28916671   270 VSELGNGIAAFESVPTAIYCFLRCmephpeipstFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPE 343
Cdd:pfam03747 136 LEAIGGGGYVVEALPAALYALLRA----------GDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPE 199
 
Name Accession Description Interval E-value
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
27-366 1.00e-52

ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441007  Cd Length: 256  Bit Score: 175.43  E-value: 1.00e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671  27 SRFRGCLAGALLGDCVGAVYEAHDTVSLASVLSHVESL-EPDPGTPGSartetlyYTDDTAMTRALVQSLLAKEAFDEVD 105
Cdd:COG1397   3 DRARGALLGLAIGDALGAPVEFYSREEIRARYGPITDYvGGGNLPPGE-------WTDDTQMALALAESLLEAGGFDPED 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 106 MAHRFAQEYKKDPDRGYGAGVITVFKKLLNPkcrdvyepaRAQFNGKGSYGNGGAMRVAGISLAYS-SVQDVQKFARLSA 184
Cdd:COG1397  76 LARRFLRWLRTGPGRDIGPTTRRALRNLRRG---------GAGESGEGSAGNGAAMRIAPLGLAYAgDPEEAAELARASA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 185 QLTHASSLGYNGAILQALAVHLALQGVSSSEhfleqllghmeelegdaqsvldakelgmeerpyssrlkkvgelldqdvv 264
Cdd:COG1397 147 ALTHGHPRAIAGAVAYAAAVAAALRGADLEE------------------------------------------------- 177
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671 265 sreevvselgngIAAFESVPTAIYCFLRcmephpeipstFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPES 344
Cdd:COG1397 178 ------------GYVVETLPAALWALLR-----------ADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPER 234
                       330       340
                ....*....|....*....|..
gi 28916671 345 WQQSCEGFEETDVLAQSLHRVF 366
Cdd:COG1397 235 WLEPLERRDRLEELAERLAALA 256
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
31-343 5.87e-41

ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ADP-ribosylarginine hydrolase EC:3.2.2.19 cleaves ADP-ribose-L-arginine. The family also includes dinitrogenase reductase activating glycohydrolase. Most surprisingly the family also includes jellyfish crystallins, these proteins appear to have lost the presumed active site residues.


Pssm-ID: 461037 [Multi-domain]  Cd Length: 200  Bit Score: 142.71  E-value: 5.87e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671    31 GCLAGALLGDCVGAVYEAHdtvSLASVLSHVESLEPDPGTPGSARTETLYYTDDTAMTRALVQSLLAKEAFDEVDMAHRF 110
Cdd:pfam03747   1 GALLGLAVGDALGAPVEFW---SYDEIRREYGGIGTPMPGGGHLGLPPGEWTDDTQMALALLESLLEAGGFDPEDLARRL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671   111 AqeykkdpdrgygagvitvfkkllnpkcrdvyeparaqfngkgsygnggaMRVAGISLAYS-SVQDVQKFARLSAQLTHA 189
Cdd:pfam03747  78 A-------------------------------------------------MRIAPLGLLYPgDPEEAAELARESARLTHG 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28916671   190 SSLGYNGAILQALAVHLALQGVSssehfleqllghmeelegdaqsvldakelgmeerpyssrlkkvgelldqdvvsREEV 269
Cdd:pfam03747 109 HPRAVAGAVAYAAAIAAALRGAD-----------------------------------------------------LEEA 135
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28916671   270 VSELGNGIAAFESVPTAIYCFLRCmephpeipstFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPE 343
Cdd:pfam03747 136 LEAIGGGGYVVEALPAALYALLRA----------GDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPE 199
 
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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