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Conserved domains on  [gi|61556810|ref|NP_001013072|]
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inactive ADP-ribosyltransferase ARH2 isoform 1 [Rattus norvegicus]

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 ...
6-327 1.14e-28

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: 109.97  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810     6 AAMLLGTVGDALGYGNvcrENSASGSIQEEL----QKTRGLDSLVLSPGKWpvSDNTIMHMATAEALTT-DYWCLDDLYR 80
Cdd:pfam03747   1 GALLGLAVGDALGAPV---EFWSYDEIRREYggigTPMPGGGHLGLPPGEW--TDDTQMALALLESLLEaGGFDPEDLAR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810    81 EMVKRyvetveklsehrpdpstiegcsqlkpdnyllawhtpfsekgsgfgaatkAMCIGMRYwkPERLETLIEVSIECGR 160
Cdd:pfam03747  76 RLAMR-------------------------------------------------IAPLGLLY--PGDPEEAAELARESAR 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   161 MTHNHPTGFLGSLCTALFASYAIQGKSLVQWGRdmlkvlplaeeycrksirhmaeyqehwfyfeakwqfyleerkireds 240
Cdd:pfam03747 105 LTHGHPRAVAGAVAYAAAIAAALRGADLEEALE----------------------------------------------- 137
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   241 evtavfpdnydaeerdktykkwssEGRGGRRGHDAPMIAYDALLASGSSWTELCQRAMFHRGESGATGTIAGCLFGLLHG 320
Cdd:pfam03747 138 ------------------------AIGGGGYVVEALPAALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYG 193

                  ....*..
gi 61556810   321 LATVPPG 327
Cdd:pfam03747 194 LEAIPEE 200
 
Name Accession Description Interval E-value
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
6-327 1.14e-28

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: 109.97  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810     6 AAMLLGTVGDALGYGNvcrENSASGSIQEEL----QKTRGLDSLVLSPGKWpvSDNTIMHMATAEALTT-DYWCLDDLYR 80
Cdd:pfam03747   1 GALLGLAVGDALGAPV---EFWSYDEIRREYggigTPMPGGGHLGLPPGEW--TDDTQMALALLESLLEaGGFDPEDLAR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810    81 EMVKRyvetveklsehrpdpstiegcsqlkpdnyllawhtpfsekgsgfgaatkAMCIGMRYwkPERLETLIEVSIECGR 160
Cdd:pfam03747  76 RLAMR-------------------------------------------------IAPLGLLY--PGDPEEAAELARESAR 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   161 MTHNHPTGFLGSLCTALFASYAIQGKSLVQWGRdmlkvlplaeeycrksirhmaeyqehwfyfeakwqfyleerkireds 240
Cdd:pfam03747 105 LTHGHPRAVAGAVAYAAAIAAALRGADLEEALE----------------------------------------------- 137
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   241 evtavfpdnydaeerdktykkwssEGRGGRRGHDAPMIAYDALLASGSSWTELCQRAMFHRGESGATGTIAGCLFGLLHG 320
Cdd:pfam03747 138 ------------------------AIGGGGYVVEALPAALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYG 193

                  ....*..
gi 61556810   321 LATVPPG 327
Cdd:pfam03747 194 LEAIPEE 200
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
1-349 1.94e-17

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 80.68  E-value: 1.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   1 MEKFKAAMLLGTVGDALGYGNvcrENSASGSIQEELQKTRGLdslvLSPGKWP---VSDNTIMHMATAEALTtDYWCLDd 77
Cdd:COG1397   2 LDRARGALLGLAIGDALGAPV---EFYSREEIRARYGPITDY----VGGGNLPpgeWTDDTQMALALAESLL-EAGGFD- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810  78 lYREMVKRYVETVEKLSEHRPDPSTIEGCSqlkpdNYLLAWHTPFSEKGSGFGAATKAMCIGMRYwkPERLETLIEVSIE 157
Cdd:COG1397  73 -PEDLARRFLRWLRTGPGRDIGPTTRRALR-----NLRRGGAGESGEGSAGNGAAMRIAPLGLAY--AGDPEEAAELARA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810 158 CGRMTHNHPTGFLGSLCTALFASYAIQGKSLVQWgrDMLKVLPLAeeycrksirhmaeyqehwfyfeakwqFYLeerkir 237
Cdd:COG1397 145 SAALTHGHPRAIAGAVAYAAAVAAALRGADLEEG--YVVETLPAA--------------------------LWA------ 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810 238 edsevtAVFPDNYDaeerdktykkwssegrggrrghdapmiayDALLAsgsswtelcqrAMFHRGESGATGTIAGCLFGL 317
Cdd:COG1397 191 ------LLRADDFE-----------------------------EALLL-----------AVNLGGDTDTTAAIAGALAGA 224
                       330       340       350
                ....*....|....*....|....*....|..
gi 61556810 318 LHGLATVPPGLYQELEHKGRLEDLGTALHRLS 349
Cdd:COG1397 225 LYGLEAIPERWLEPLERRDRLEELAERLAALA 256
 
Name Accession Description Interval E-value
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
6-327 1.14e-28

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: 109.97  E-value: 1.14e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810     6 AAMLLGTVGDALGYGNvcrENSASGSIQEEL----QKTRGLDSLVLSPGKWpvSDNTIMHMATAEALTT-DYWCLDDLYR 80
Cdd:pfam03747   1 GALLGLAVGDALGAPV---EFWSYDEIRREYggigTPMPGGGHLGLPPGEW--TDDTQMALALLESLLEaGGFDPEDLAR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810    81 EMVKRyvetveklsehrpdpstiegcsqlkpdnyllawhtpfsekgsgfgaatkAMCIGMRYwkPERLETLIEVSIECGR 160
Cdd:pfam03747  76 RLAMR-------------------------------------------------IAPLGLLY--PGDPEEAAELARESAR 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   161 MTHNHPTGFLGSLCTALFASYAIQGKSLVQWGRdmlkvlplaeeycrksirhmaeyqehwfyfeakwqfyleerkireds 240
Cdd:pfam03747 105 LTHGHPRAVAGAVAYAAAIAAALRGADLEEALE----------------------------------------------- 137
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   241 evtavfpdnydaeerdktykkwssEGRGGRRGHDAPMIAYDALLASGSSWTELCQRAMFHRGESGATGTIAGCLFGLLHG 320
Cdd:pfam03747 138 ------------------------AIGGGGYVVEALPAALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYG 193

                  ....*..
gi 61556810   321 LATVPPG 327
Cdd:pfam03747 194 LEAIPEE 200
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
1-349 1.94e-17

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 80.68  E-value: 1.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810   1 MEKFKAAMLLGTVGDALGYGNvcrENSASGSIQEELQKTRGLdslvLSPGKWP---VSDNTIMHMATAEALTtDYWCLDd 77
Cdd:COG1397   2 LDRARGALLGLAIGDALGAPV---EFYSREEIRARYGPITDY----VGGGNLPpgeWTDDTQMALALAESLL-EAGGFD- 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810  78 lYREMVKRYVETVEKLSEHRPDPSTIEGCSqlkpdNYLLAWHTPFSEKGSGFGAATKAMCIGMRYwkPERLETLIEVSIE 157
Cdd:COG1397  73 -PEDLARRFLRWLRTGPGRDIGPTTRRALR-----NLRRGGAGESGEGSAGNGAAMRIAPLGLAY--AGDPEEAAELARA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810 158 CGRMTHNHPTGFLGSLCTALFASYAIQGKSLVQWgrDMLKVLPLAeeycrksirhmaeyqehwfyfeakwqFYLeerkir 237
Cdd:COG1397 145 SAALTHGHPRAIAGAVAYAAAVAAALRGADLEEG--YVVETLPAA--------------------------LWA------ 190
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61556810 238 edsevtAVFPDNYDaeerdktykkwssegrggrrghdapmiayDALLAsgsswtelcqrAMFHRGESGATGTIAGCLFGL 317
Cdd:COG1397 191 ------LLRADDFE-----------------------------EALLL-----------AVNLGGDTDTTAAIAGALAGA 224
                       330       340       350
                ....*....|....*....|....*....|..
gi 61556810 318 LHGLATVPPGLYQELEHKGRLEDLGTALHRLS 349
Cdd:COG1397 225 LYGLEAIPERWLEPLERRDRLEELAERLAALA 256
 
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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