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Conserved domains on  [gi|1610576690|ref|NP_001356417|]
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hexosaminidase D isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH20_hexosaminidase super family cl02948
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ...
 1-231 4.60e-87

Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.


The actual alignment was detected with superfamily member cd06565:

Pssm-ID: 445966  Cd Length: 301  Bit Score: 265.99  E-value: 4.60e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690   1 MEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVGAMIDQVLELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGK 80
Cdd:cd06565    86 LEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690  81 LCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPEDQLAASGVPQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAA 160
Cdd:cd06565   162 LYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGA 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576690 161 SAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPTDSLQGIILTGWQRYDHYSVLCELLPAGVPSLAACLQ 231
Cdd:cd06565   240 SAWKGAT------PPNDKHLENIKSWLKAA---KKNGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 301
 
Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 1-231 4.60e-87

Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.


Pssm-ID: 119335  Cd Length: 301  Bit Score: 265.99  E-value: 4.60e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690   1 MEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVGAMIDQVLELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGK 80
Cdd:cd06565    86 LEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690  81 LCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPEDQLAASGVPQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAA 160
Cdd:cd06565   162 LYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGA 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576690 161 SAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPTDSLQGIILTGWQRYDHYSVLCELLPAGVPSLAACLQ 231
Cdd:cd06565   240 SAWKGAT------PPNDKHLENIKSWLKAA---KKNGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 301
 
Name Accession Description Interval E-value
GH20_GcnA-like cd06565
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ...
 1-231 4.60e-87

Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.


Pssm-ID: 119335  Cd Length: 301  Bit Score: 265.99  E-value: 4.60e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690   1 MEFVLKHTAFAHLREVGSFPCTLNPHEAESLALVGAMIDQVLELHPgAQRLHIGCDEVYYLGEGEASRRWlqqEQNSTGK 80
Cdd:cd06565    86 LEFILKHPEFRHLREVDDPPQTLCPGEPKTYDFIEEMIRQVLELHP-SKYIHIGMDEAYDLGRGRSLRKH---GNLGRGE 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690  81 LCLSHMRAVASGVKARRPsvTPLVWDDMLRDLPEDQLAASGVPQLVEPVLWDYTADLDVHGKVLLMQKYRRCGFPQLWAA 160
Cdd:cd06565   162 LYLEHLKKVLKIIKKRGP--KPMMWDDMLRKLSIEPEALSGLPKLVTPVVWDYYADLDEHDRPIGLWKKYGSVFAVAWGA 239

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1610576690 161 SAFKGATgpsqavPPVEHHLRNHVQWLQVAgsgPTDSLQGIILTGWQRYDHYSVLCELLPAGVPSLAACLQ 231
Cdd:cd06565   240 SAWKGAT------PPNDKHLENIKSWLKAA---KKNGVQGILLTGWGDYGHEAVLCELLPGLIPSLALALG 301
GH20_hexosaminidase cd02742
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ...
 23-206 3.34e-04

Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.


Pssm-ID: 119331 [Multi-domain]  Cd Length: 303  Bit Score: 42.04  E-value: 3.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690  23 LNPHEAESLALVGAMIDQVLELHPGaQRLHIGCDEVYYLGEGEASrrwlqqeqNSTgklclsHMRAVASGVKARrpSVTP 102
Cdd:cd02742   125 LDPTLPKGYDFLDDLFGEIAELFPD-RYLHIGGDEAHFKQDRKHL--------MSQ------FIQRVLDIVKKK--GKKV 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610576690 103 LVWDDMLRDLPEdqlaasgVPQLVEPVLWDYTADLDVHGKVLLMQKyrrcGFPQLWAASAFKGATGPSQavppveHHLRN 182
Cdd:cd02742   188 IVWQDGFDKKMK-------LKEDVIVQYWDYDGDKYNVELPEAAAK----GFPVILSNGYYLDIFIDGA------LDARK 250

                         170       180
                  ....*....|....*....|....*.
gi 1610576690 183 HVQW--LQVAGSGPTDSLQGIILTGW 206
Cdd:cd02742   251 VYKNdpLAVPTPQQKDLVLGVIACLW 276
 
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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