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Conserved domains on  [gi|1958659347|ref|XP_038942186|]
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N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase isoform X1 [Rattus norvegicus]

Protein Classification

phosphodiester glycosidase family protein( domain architecture ID 10561816)

phosphodiester glycosidase family protein such as mammalian N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase, which catalyzes the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides by removing GlcNAc residues from GlcNAc-alpha-P-mannose moieties, which are formed in the first step

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NAGPA pfam09992
Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure ...
 131-306 2.05e-34

Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure of a member from Bacteroides has been crystallized and modelled onto the luminal region of the human member of the family, the transmembrane glycoprotein N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. There is some conservation of potentially functional residues, implying that in the bacterial members this family acts in some way as a phosphodiester glycosidase. The human protein is also present, so the eukaryotic members are likely to be catalysing the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides.


:

Pssm-ID: 430971  Cd Length: 169  Bit Score: 124.74  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 131 AGCRVAQNGGFFRMGTGECLGNVVSDGRLVS-SSGGLQNAQFGIRRDGTLVTGYLSEEDvldtvNPFVQLLSGVVWLIRN 209
Cdd:pfam09992   1 SGAVAAVNGGFFDPGSGGPLGLVISNGKVLGlLNGGRAVGAFALTPDGVLVITLNPLDF-----YDLSEAVGAGPLLVKD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 210 GSIYINesqitecdetqetgsFSKFVNVMSARTAVGHDRKGQLILFHADGqTEQRGLNLWEMAEFLLKQDVVNAINLDGG 289
Cdd:pfam09992  76 GKIVPT---------------SSDGGWGRAPRTAIGITADGTILLVVVDG-RQSIGATLKELAQLLKRLGAVNALNLDGG 139

                         170
                  ....*....|....*..
gi 1958659347 290 GSATFVLNGTLASYPSD 306
Cdd:pfam09992 140 GSTTLVVEGKVLNNPSG 156
 
Name Accession Description Interval E-value
NAGPA pfam09992
Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure ...
 131-306 2.05e-34

Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure of a member from Bacteroides has been crystallized and modelled onto the luminal region of the human member of the family, the transmembrane glycoprotein N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. There is some conservation of potentially functional residues, implying that in the bacterial members this family acts in some way as a phosphodiester glycosidase. The human protein is also present, so the eukaryotic members are likely to be catalysing the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides.


Pssm-ID: 430971  Cd Length: 169  Bit Score: 124.74  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 131 AGCRVAQNGGFFRMGTGECLGNVVSDGRLVS-SSGGLQNAQFGIRRDGTLVTGYLSEEDvldtvNPFVQLLSGVVWLIRN 209
Cdd:pfam09992   1 SGAVAAVNGGFFDPGSGGPLGLVISNGKVLGlLNGGRAVGAFALTPDGVLVITLNPLDF-----YDLSEAVGAGPLLVKD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 210 GSIYINesqitecdetqetgsFSKFVNVMSARTAVGHDRKGQLILFHADGqTEQRGLNLWEMAEFLLKQDVVNAINLDGG 289
Cdd:pfam09992  76 GKIVPT---------------SSDGGWGRAPRTAIGITADGTILLVVVDG-RQSIGATLKELAQLLKRLGAVNALNLDGG 139

                         170
                  ....*....|....*..
gi 1958659347 290 GSATFVLNGTLASYPSD 306
Cdd:pfam09992 140 GSTTLVVEGKVLNNPSG 156
NAGPA COG4632
Sugar-P-sugar glycosidase (uncovering enzyme, UCE), NAGPA superfamily [Carbohydrate transport ...
 121-306 2.42e-31

Sugar-P-sugar glycosidase (uncovering enzyme, UCE), NAGPA superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 443670 [Multi-domain]  Cd Length: 310  Bit Score: 120.69  E-value: 2.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 121 RATVEDTAVPAGCRVAQNGGFFRMGtGECLGNVVSDGRLVSSSGGLQNAQ-FGIRRDGTLVTGYLSEEDVLDTVNPFVQL 199
Cdd:COG4632   122 DVLTLVTTPARGNRPVAPGGLFDPG-GKPTGIIISNGKVISPNKDGPARDvLGIDKDGKLIVGDPVTIDLEKLPAGVEEA 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 200 LSGVVWLIRNGSIYINESQitecdetqetgsfSKFVNVMSARTAVGHDRKGQLILFHADG-QTEQRGLNLWEMAEFLLKQ 278
Cdd:COG4632   201 VGGGPLLVKNGKVVVDADE-------------AAFGNGRAPRTAIGITADGTLLLVVVDGrQPGSIGATLAELAQLLKEL 267

                         170       180
                  ....*....|....*....|....*...
gi 1958659347 279 DVVNAINLDGGGSATFVLNGTLASYPSD 306
Cdd:COG4632   268 GAVDALNLDGGGSTTLVYNGKVVNRPSD 295
 
Name Accession Description Interval E-value
NAGPA pfam09992
Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure ...
 131-306 2.05e-34

Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure of a member from Bacteroides has been crystallized and modelled onto the luminal region of the human member of the family, the transmembrane glycoprotein N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. There is some conservation of potentially functional residues, implying that in the bacterial members this family acts in some way as a phosphodiester glycosidase. The human protein is also present, so the eukaryotic members are likely to be catalysing the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides.


Pssm-ID: 430971  Cd Length: 169  Bit Score: 124.74  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 131 AGCRVAQNGGFFRMGTGECLGNVVSDGRLVS-SSGGLQNAQFGIRRDGTLVTGYLSEEDvldtvNPFVQLLSGVVWLIRN 209
Cdd:pfam09992   1 SGAVAAVNGGFFDPGSGGPLGLVISNGKVLGlLNGGRAVGAFALTPDGVLVITLNPLDF-----YDLSEAVGAGPLLVKD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 210 GSIYINesqitecdetqetgsFSKFVNVMSARTAVGHDRKGQLILFHADGqTEQRGLNLWEMAEFLLKQDVVNAINLDGG 289
Cdd:pfam09992  76 GKIVPT---------------SSDGGWGRAPRTAIGITADGTILLVVVDG-RQSIGATLKELAQLLKRLGAVNALNLDGG 139

                         170
                  ....*....|....*..
gi 1958659347 290 GSATFVLNGTLASYPSD 306
Cdd:pfam09992 140 GSTTLVVEGKVLNNPSG 156
NAGPA COG4632
Sugar-P-sugar glycosidase (uncovering enzyme, UCE), NAGPA superfamily [Carbohydrate transport ...
 121-306 2.42e-31

Sugar-P-sugar glycosidase (uncovering enzyme, UCE), NAGPA superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 443670 [Multi-domain]  Cd Length: 310  Bit Score: 120.69  E-value: 2.42e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 121 RATVEDTAVPAGCRVAQNGGFFRMGtGECLGNVVSDGRLVSSSGGLQNAQ-FGIRRDGTLVTGYLSEEDVLDTVNPFVQL 199
Cdd:COG4632   122 DVLTLVTTPARGNRPVAPGGLFDPG-GKPTGIIISNGKVISPNKDGPARDvLGIDKDGKLIVGDPVTIDLEKLPAGVEEA 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958659347 200 LSGVVWLIRNGSIYINESQitecdetqetgsfSKFVNVMSARTAVGHDRKGQLILFHADG-QTEQRGLNLWEMAEFLLKQ 278
Cdd:COG4632   201 VGGGPLLVKNGKVVVDADE-------------AAFGNGRAPRTAIGITADGTLLLVVVDGrQPGSIGATLAELAQLLKEL 267

                         170       180
                  ....*....|....*....|....*...
gi 1958659347 279 DVVNAINLDGGGSATFVLNGTLASYPSD 306
Cdd:COG4632   268 GAVDALNLDGGGSTTLVYNGKVVNRPSD 295
 
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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