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Conserved domains on  [gi|2486190711|ref|WP_278938430|]
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ADP-ribosylglycohydrolase family protein [Barnesiella intestinihominis]

Protein Classification

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 ...
33-315 2.45e-13

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: 68.75  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711  33 GGWAGKMIGVSYGLPTEF-------KALGKMYEDSIHWTPVRVKDALWEDDLYVQLTLMDVMDKHGmqaeqkkyqealat 105
Cdd:pfam03747   1 GALLGLAVGDALGAPVEFwsydeirREYGGIGTPMPGGGHLGLPPGEWTDDTQMALALLESLLEAG-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 106 agfrlwhanvqtrknyfdsifppqsgqpefNLHADDI--DFQIEADYIGFMCPGMPQTANKMADYMGHIMNYGD-GVYGG 182
Cdd:pfam03747  67 ------------------------------GFDPEDLarRLAMRIAPLGLLYPGDPEEAAELARESARLTHGHPrAVAGA 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 183 AFVASLYSEAYLQNDIRSIIEkallslpaESGYRRIIEDVIAFhqenpddwtkcwqmledkwaranicnpgtkynidakl 262
Cdd:pfam03747 117 VAYAAAIAAALRGADLEEALE--------AIGGGGYVVEALPA------------------------------------- 151
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2486190711 263 ngayIVIGLLYGEGDINKTLEISTRCGQDSDCNPSNALAVLGIIKGFSAFPQE 315
Cdd:pfam03747 152 ----ALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPEE 200
CE2_N super family cl40254
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll ...
418-514 3.41e-03

Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.


The actual alignment was detected with superfamily member pfam17996:

Pssm-ID: 465608  Cd Length: 108  Bit Score: 37.26  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 418 AGDEITFTFEGTGASIEgwwVKNGGK---ADVYVDGIFKRTIDcfyyyAKQEHRNINIFHilNLEEGKHTINIVvkgeKR 494
Cdd:pfam17996  18 PGTYVEFRFTGTSLSVV---LKDSYGnnyLNVIIDGKQPVRLK-----LDGTGRTYTLAE--GLPPGEHTVRLF----KR 83
                          90       100
                  ....*....|....*....|
gi 2486190711 495 EESEGCAIGVRGAVVYKNGT 514
Cdd:pfam17996  84 TEAQCGYTEFLGFVLDDGGK 103
 
Name Accession Description Interval E-value
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
33-315 2.45e-13

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: 68.75  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711  33 GGWAGKMIGVSYGLPTEF-------KALGKMYEDSIHWTPVRVKDALWEDDLYVQLTLMDVMDKHGmqaeqkkyqealat 105
Cdd:pfam03747   1 GALLGLAVGDALGAPVEFwsydeirREYGGIGTPMPGGGHLGLPPGEWTDDTQMALALLESLLEAG-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 106 agfrlwhanvqtrknyfdsifppqsgqpefNLHADDI--DFQIEADYIGFMCPGMPQTANKMADYMGHIMNYGD-GVYGG 182
Cdd:pfam03747  67 ------------------------------GFDPEDLarRLAMRIAPLGLLYPGDPEEAAELARESARLTHGHPrAVAGA 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 183 AFVASLYSEAYLQNDIRSIIEkallslpaESGYRRIIEDVIAFhqenpddwtkcwqmledkwaranicnpgtkynidakl 262
Cdd:pfam03747 117 VAYAAAIAAALRGADLEEALE--------AIGGGGYVVEALPA------------------------------------- 151
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2486190711 263 ngayIVIGLLYGEGDINKTLEISTRCGQDSDCNPSNALAVLGIIKGFSAFPQE 315
Cdd:pfam03747 152 ----ALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPEE 200
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
27-322 1.51e-05

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 46.39  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711  27 LKDKIAGGWAGKMIGVSYGLPTEFKALGKMYEDSIHWT----PVRVKDALWEDDLyvQLTL--MDVMDKHG--MQAEQ-K 97
Cdd:COG1397     1 LLDRARGALLGLAIGDALGAPVEFYSREEIRARYGPITdyvgGGNLPPGEWTDDT--QMALalAESLLEAGgfDPEDLaR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711  98 KYQEALAT-AGFRLWHAnvqTRK---NYfdsifppQSGQPEF-NLHADDIDFQIEADYIGFMCPGMPQTANKMAD---YM 169
Cdd:COG1397    79 RFLRWLRTgPGRDIGPT---TRRalrNL-------RRGGAGEsGEGSAGNGAAMRIAPLGLAYAGDPEEAAELARasaAL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 170 GHimNYGDGVYGGAFVAslyseaylqndirsiiekALLSLpaesgyrriiedviAFHQENPDDWtkcwqmledkWARANI 249
Cdd:COG1397   149 TH--GHPRAIAGAVAYA------------------AAVAA--------------ALRGADLEEG----------YVVETL 184
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486190711 250 CnpgtkynidaklngayIVIGLLYGEGDINKTLEISTRCGQDSDCNPSNALAVLGIIKGFSAFPQEYREAIEK 322
Cdd:COG1397   185 P----------------AALWALLRADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLER 241
CE2_N pfam17996
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll ...
418-514 3.41e-03

Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.


Pssm-ID: 465608  Cd Length: 108  Bit Score: 37.26  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 418 AGDEITFTFEGTGASIEgwwVKNGGK---ADVYVDGIFKRTIDcfyyyAKQEHRNINIFHilNLEEGKHTINIVvkgeKR 494
Cdd:pfam17996  18 PGTYVEFRFTGTSLSVV---LKDSYGnnyLNVIIDGKQPVRLK-----LDGTGRTYTLAE--GLPPGEHTVRLF----KR 83
                          90       100
                  ....*....|....*....|
gi 2486190711 495 EESEGCAIGVRGAVVYKNGT 514
Cdd:pfam17996  84 TEAQCGYTEFLGFVLDDGGK 103
 
Name Accession Description Interval E-value
ADP_ribosyl_GH pfam03747
ADP-ribosylglycohydrolase; This family includes enzymes that ADP-ribosylations, for example ...
33-315 2.45e-13

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: 68.75  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711  33 GGWAGKMIGVSYGLPTEF-------KALGKMYEDSIHWTPVRVKDALWEDDLYVQLTLMDVMDKHGmqaeqkkyqealat 105
Cdd:pfam03747   1 GALLGLAVGDALGAPVEFwsydeirREYGGIGTPMPGGGHLGLPPGEWTDDTQMALALLESLLEAG-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 106 agfrlwhanvqtrknyfdsifppqsgqpefNLHADDI--DFQIEADYIGFMCPGMPQTANKMADYMGHIMNYGD-GVYGG 182
Cdd:pfam03747  67 ------------------------------GFDPEDLarRLAMRIAPLGLLYPGDPEEAAELARESARLTHGHPrAVAGA 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 183 AFVASLYSEAYLQNDIRSIIEkallslpaESGYRRIIEDVIAFhqenpddwtkcwqmledkwaranicnpgtkynidakl 262
Cdd:pfam03747 117 VAYAAAIAAALRGADLEEALE--------AIGGGGYVVEALPA------------------------------------- 151
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2486190711 263 ngayIVIGLLYGEGDINKTLEISTRCGQDSDCNPSNALAVLGIIKGFSAFPQE 315
Cdd:pfam03747 152 ----ALYALLRAGDDFEEALLAAVNLGGDTDTTAAIAGALLGAYYGLEAIPEE 200
DraG COG1397
ADP-ribosylglycohydrolase [Posttranslational modification, protein turnover, chaperones];
27-322 1.51e-05

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


Pssm-ID: 441007  Cd Length: 256  Bit Score: 46.39  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711  27 LKDKIAGGWAGKMIGVSYGLPTEFKALGKMYEDSIHWT----PVRVKDALWEDDLyvQLTL--MDVMDKHG--MQAEQ-K 97
Cdd:COG1397     1 LLDRARGALLGLAIGDALGAPVEFYSREEIRARYGPITdyvgGGNLPPGEWTDDT--QMALalAESLLEAGgfDPEDLaR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711  98 KYQEALAT-AGFRLWHAnvqTRK---NYfdsifppQSGQPEF-NLHADDIDFQIEADYIGFMCPGMPQTANKMAD---YM 169
Cdd:COG1397    79 RFLRWLRTgPGRDIGPT---TRRalrNL-------RRGGAGEsGEGSAGNGAAMRIAPLGLAYAGDPEEAAELARasaAL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 170 GHimNYGDGVYGGAFVAslyseaylqndirsiiekALLSLpaesgyrriiedviAFHQENPDDWtkcwqmledkWARANI 249
Cdd:COG1397   149 TH--GHPRAIAGAVAYA------------------AAVAA--------------ALRGADLEEG----------YVVETL 184
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2486190711 250 CnpgtkynidaklngayIVIGLLYGEGDINKTLEISTRCGQDSDCNPSNALAVLGIIKGFSAFPQEYREAIEK 322
Cdd:COG1397   185 P----------------AALWALLRADDFEEALLLAVNLGGDTDTTAAIAGALAGALYGLEAIPERWLEPLER 241
CE2_N pfam17996
Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll ...
418-514 3.41e-03

Carbohydrate esterase 2 N-terminal; This is the N-terminal beta-sheet domain with jelly roll topology found in CE2 acetyl-esterase from the bacterium Clostridium thermocellum. This enzyme displays dual activities, it catalyzes the deacetylation of plant polysaccharides and also potentiates the activity of its appended cellulase catalytic module through its noncatalytic cellulose binding function. This N-terminal jelly-roll domain appears to extend the substrate/cellulose binding cleft of the catalytic domain in C.thermocellum.


Pssm-ID: 465608  Cd Length: 108  Bit Score: 37.26  E-value: 3.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2486190711 418 AGDEITFTFEGTGASIEgwwVKNGGK---ADVYVDGIFKRTIDcfyyyAKQEHRNINIFHilNLEEGKHTINIVvkgeKR 494
Cdd:pfam17996  18 PGTYVEFRFTGTSLSVV---LKDSYGnnyLNVIIDGKQPVRLK-----LDGTGRTYTLAE--GLPPGEHTVRLF----KR 83
                          90       100
                  ....*....|....*....|
gi 2486190711 495 EESEGCAIGVRGAVVYKNGT 514
Cdd:pfam17996  84 TEAQCGYTEFLGFVLDDGGK 103
 
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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