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Conserved domains on  [gi|4557263|ref|NP_001116|]
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ADP-ribosylarginine hydrolase isoform 1 [Homo sapiens]

Protein Classification

ADP-ribosylglycohydrolase family protein( domain architecture ID 10509975)

ADP-ribosylglycohydrolase family protein similar to vertebrate [protein ADP-ribosylarginine] hydrolase, which catalyzes the reverse reaction of mono-ADP-ribosylation

CATH:  1.10.4080.10
EC:  3.2.2.-
Gene Ontology:  GO:0016799|GO:0046872

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
6-323 7.62e-36

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: 129.23  E-value: 7.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263      6 AAMVLSAAGDALGYYngkWEFLqDGEKIHRQLAQLG----GLDALDVGRWRVSDDTVMHLATAEALVEAGKAPkltqlYY 81
Cdd:pfam03747   1 GALLGLAVGDALGAP---VEFW-SYDEIRREYGGIGtpmpGGGHLGLPPGEWTDDTQMALALLESLLEAGGFD-----PE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263     82 LLAKHYqdcmedmdgrapggasvhnamqlkpgkpngwripfnsheggcgaAMRAMCIGLRFPHhsQLDTLIQVSIESGRM 161
Cdd:pfam03747  72 DLARRL--------------------------------------------AMRIAPLGLLYPG--DPEEAAELARESARL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    162 THHHPTGYLGALASALFTAYAVNSRPPlqwgkglmellPEAKKYIVQSGYfveenlqhwsyfqtkwenylklrgildges 241
Cdd:pfam03747 106 THGHPRAVAGAVAYAAAIAAALRGADL-----------EEALEAIGGGGY------------------------------ 144
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    242 aptfpesfgvkerdqfytslsysgwggssGHDAPMIAYDAVLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFK 321
Cdd:pfam03747 145 -----------------------------VVEALPAALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLE 195

                  ..
gi 4557263    322 GV 323
Cdd:pfam03747 196 AI 197
 
Name Accession Description Interval E-value
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
6-323 7.62e-36

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: 129.23  E-value: 7.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263      6 AAMVLSAAGDALGYYngkWEFLqDGEKIHRQLAQLG----GLDALDVGRWRVSDDTVMHLATAEALVEAGKAPkltqlYY 81
Cdd:pfam03747   1 GALLGLAVGDALGAP---VEFW-SYDEIRREYGGIGtpmpGGGHLGLPPGEWTDDTQMALALLESLLEAGGFD-----PE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263     82 LLAKHYqdcmedmdgrapggasvhnamqlkpgkpngwripfnsheggcgaAMRAMCIGLRFPHhsQLDTLIQVSIESGRM 161
Cdd:pfam03747  72 DLARRL--------------------------------------------AMRIAPLGLLYPG--DPEEAAELARESARL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    162 THHHPTGYLGALASALFTAYAVNSRPPlqwgkglmellPEAKKYIVQSGYfveenlqhwsyfqtkwenylklrgildges 241
Cdd:pfam03747 106 THGHPRAVAGAVAYAAAIAAALRGADL-----------EEALEAIGGGGY------------------------------ 144
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    242 aptfpesfgvkerdqfytslsysgwggssGHDAPMIAYDAVLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFK 321
Cdd:pfam03747 145 -----------------------------VVEALPAALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLE 195

                  ..
gi 4557263    322 GV 323
Cdd:pfam03747 196 AI 197
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
1-347 1.43e-33

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 124.97  E-value: 1.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    1 MEKYVAAMVLSAAGDALGYyngKWEFLqDGEKIHRQLAQLGGL-DALDVGRWRVSDDTVMHLATAEALVEAGKapkLTQl 79
Cdd:COG1397   2 LDRARGALLGLAIGDALGA---PVEFY-SREEIRARYGPITDYvGGGNLPPGEWTDDTQMALALAESLLEAGG---FDP- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263   80 yYLLAKHYQDCMEDMDGRAPGGASVHNAMQLKpgkpNGWRIPFNSHEGGCGAAMRAMCIGLRFPHhsQLDTLIQVSIESG 159
Cdd:COG1397  74 -EDLARRFLRWLRTGPGRDIGPTTRRALRNLR----RGGAGESGEGSAGNGAAMRIAPLGLAYAG--DPEEAAELARASA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263  160 RMTHHHPTGYLGALASALFTAYAVNSRPPLQWgkglmellpeakkyivqsgyFVEENLQhwsyfqtkwenylklrgildg 239
Cdd:COG1397 147 ALTHGHPRAIAGAVAYAAAVAAALRGADLEEG--------------------YVVETLP--------------------- 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263  240 esaptfpesfgvkerdqfytslsysgwggssghdapmIAYdAVLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYG 319
Cdd:COG1397 186 -------------------------------------AAL-WALLRADDFEEALLLAVNLGGDTDTTAAIAGALAGALYG 227
                       330       340
                ....*....|....*....|....*....
gi 4557263  320 FKGVsPSNY-EKLEYRNRLEETARALYSL 347
Cdd:COG1397 228 LEAI-PERWlEPLERRDRLEELAERLAAL 255
 
Name Accession Description Interval E-value
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
6-323 7.62e-36

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: 129.23  E-value: 7.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263      6 AAMVLSAAGDALGYYngkWEFLqDGEKIHRQLAQLG----GLDALDVGRWRVSDDTVMHLATAEALVEAGKAPkltqlYY 81
Cdd:pfam03747   1 GALLGLAVGDALGAP---VEFW-SYDEIRREYGGIGtpmpGGGHLGLPPGEWTDDTQMALALLESLLEAGGFD-----PE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263     82 LLAKHYqdcmedmdgrapggasvhnamqlkpgkpngwripfnsheggcgaAMRAMCIGLRFPHhsQLDTLIQVSIESGRM 161
Cdd:pfam03747  72 DLARRL--------------------------------------------AMRIAPLGLLYPG--DPEEAAELARESARL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    162 THHHPTGYLGALASALFTAYAVNSRPPlqwgkglmellPEAKKYIVQSGYfveenlqhwsyfqtkwenylklrgildges 241
Cdd:pfam03747 106 THGHPRAVAGAVAYAAAIAAALRGADL-----------EEALEAIGGGGY------------------------------ 144
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    242 aptfpesfgvkerdqfytslsysgwggssGHDAPMIAYDAVLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYGFK 321
Cdd:pfam03747 145 -----------------------------VVEALPAALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLE 195

                  ..
gi 4557263    322 GV 323
Cdd:pfam03747 196 AI 197
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
1-347 1.43e-33

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 124.97  E-value: 1.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263    1 MEKYVAAMVLSAAGDALGYyngKWEFLqDGEKIHRQLAQLGGL-DALDVGRWRVSDDTVMHLATAEALVEAGKapkLTQl 79
Cdd:COG1397   2 LDRARGALLGLAIGDALGA---PVEFY-SREEIRARYGPITDYvGGGNLPPGEWTDDTQMALALAESLLEAGG---FDP- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263   80 yYLLAKHYQDCMEDMDGRAPGGASVHNAMQLKpgkpNGWRIPFNSHEGGCGAAMRAMCIGLRFPHhsQLDTLIQVSIESG 159
Cdd:COG1397  74 -EDLARRFLRWLRTGPGRDIGPTTRRALRNLR----RGGAGESGEGSAGNGAAMRIAPLGLAYAG--DPEEAAELARASA 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263  160 RMTHHHPTGYLGALASALFTAYAVNSRPPLQWgkglmellpeakkyivqsgyFVEENLQhwsyfqtkwenylklrgildg 239
Cdd:COG1397 147 ALTHGHPRAIAGAVAYAAAVAAALRGADLEEG--------------------YVVETLP--------------------- 185
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4557263  240 esaptfpesfgvkerdqfytslsysgwggssghdapmIAYdAVLAAGDSWKELAHRAFFHGGDSDSTAAIAGCWWGVMYG 319
Cdd:COG1397 186 -------------------------------------AAL-WALLRADDFEEALLLAVNLGGDTDTTAAIAGALAGALYG 227
                       330       340
                ....*....|....*....|....*....
gi 4557263  320 FKGVsPSNY-EKLEYRNRLEETARALYSL 347
Cdd:COG1397 228 LEAI-PERWlEPLERRDRLEELAERLAAL 255
 
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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