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Conserved domains on  [gi|241982768|ref|NP_038824|]
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N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase precursor [Mus musculus]

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 ...
131-326 5.84e-38

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: 137.07  E-value: 5.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  131 AGCRIAQNGGFFRMSTGECLGNVVSDGRLVS-SSGGLQNAQFGIRRDGTIVTGYLSEEEvldpvNPFVQLLSGVVWLIRN 209
Cdd:pfam09992   1 SGAVAAVNGGFFDPGSGGPLGLVISNGKVLGlLNGGRAVGAFALTPDGVLVITLNPLDF-----YDLSEAVGAGPLLVKD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  210 GNIYINesqaiecdetqetgsFSKFVNVMSARTAVGHDREGQLILFHADGqTEQRGLNLWEMAEFLRQQDVVNAINLDGG 289
Cdd:pfam09992  76 GKIVPT---------------SSDGGWGRAPRTAIGITADGTILLVVVDG-RQSIGATLKELAQLLKRLGAVNALNLDGG 139
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 241982768  290 GSATFVLNGTLASYPSDhcqDNmwrcPRQVSTVVCVH 326
Cdd:pfam09992 140 GSTTLVVEGKVLNNPSG---AE----ERPVPNGLGVF 169
 
Name Accession Description Interval E-value
NAGPA pfam09992
Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure ...
131-326 5.84e-38

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: 137.07  E-value: 5.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  131 AGCRIAQNGGFFRMSTGECLGNVVSDGRLVS-SSGGLQNAQFGIRRDGTIVTGYLSEEEvldpvNPFVQLLSGVVWLIRN 209
Cdd:pfam09992   1 SGAVAAVNGGFFDPGSGGPLGLVISNGKVLGlLNGGRAVGAFALTPDGVLVITLNPLDF-----YDLSEAVGAGPLLVKD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  210 GNIYINesqaiecdetqetgsFSKFVNVMSARTAVGHDREGQLILFHADGqTEQRGLNLWEMAEFLRQQDVVNAINLDGG 289
Cdd:pfam09992  76 GKIVPT---------------SSDGGWGRAPRTAIGITADGTILLVVVDG-RQSIGATLKELAQLLKRLGAVNALNLDGG 139
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 241982768  290 GSATFVLNGTLASYPSDhcqDNmwrcPRQVSTVVCVH 326
Cdd:pfam09992 140 GSTTLVVEGKVLNNPSG---AE----ERPVPNGLGVF 169
NAGPA COG4632
Sugar-P-sugar glycosidase (uncovering enzyme, UCE), NAGPA superfamily [Carbohydrate transport ...
68-328 3.67e-33

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


Pssm-ID: 443670 [Multi-domain]  Cd Length: 310  Bit Score: 128.40  E-value: 3.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  68 PTNPGASHHAAVRTFVSHFEGRAVAGHLTRVADPLRTFSVLEPGGAGGCAQKRRATVEDTAVPAGCRIAQNGGFFRMsTG 147
Cdd:COG4632   69 LAGAATAAVLLAAPLLSLLAGVTAGPGAPVTGGLLVRAAAGALVGALALGRLVDVLTLVTTPARGNRPVAPGGLFDP-GG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768 148 ECLGNVVSDGRLVSSSGGLQNAQ-FGIRRDGTIVTGYLSEEEVLDPVNPFVQLLSGVVWLIRNGNIYINESQAiecdetq 226
Cdd:COG4632  148 KPTGIIISNGKVISPNKDGPARDvLGIDKDGKLIVGDPVTIDLEKLPAGVEEAVGGGPLLVKNGKVVVDADEA------- 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768 227 etgsfsKFVNVMSARTAVGHDREGQLILFHADG-QTEQRGLNLWEMAEFLRQQDVVNAINLDGGGSATFVLNGTLASYPS 305
Cdd:COG4632  221 ------AFGNGRAPRTAIGITADGTLLLVVVDGrQPGSIGATLAELAQLLKELGAVDALNLDGGGSTTLVYNGKVVNRPS 294
                        250       260
                 ....*....|....*....|...
gi 241982768 306 DHCQdnmwrcpRQVSTVVCVHEP 328
Cdd:COG4632  295 DGKE-------RPVANALGVFPK 310
 
Name Accession Description Interval E-value
NAGPA pfam09992
Phosphodiester glycosidase; This is a family conserved from bacteria to humans. The structure ...
131-326 5.84e-38

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: 137.07  E-value: 5.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  131 AGCRIAQNGGFFRMSTGECLGNVVSDGRLVS-SSGGLQNAQFGIRRDGTIVTGYLSEEEvldpvNPFVQLLSGVVWLIRN 209
Cdd:pfam09992   1 SGAVAAVNGGFFDPGSGGPLGLVISNGKVLGlLNGGRAVGAFALTPDGVLVITLNPLDF-----YDLSEAVGAGPLLVKD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  210 GNIYINesqaiecdetqetgsFSKFVNVMSARTAVGHDREGQLILFHADGqTEQRGLNLWEMAEFLRQQDVVNAINLDGG 289
Cdd:pfam09992  76 GKIVPT---------------SSDGGWGRAPRTAIGITADGTILLVVVDG-RQSIGATLKELAQLLKRLGAVNALNLDGG 139
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 241982768  290 GSATFVLNGTLASYPSDhcqDNmwrcPRQVSTVVCVH 326
Cdd:pfam09992 140 GSTTLVVEGKVLNNPSG---AE----ERPVPNGLGVF 169
NAGPA COG4632
Sugar-P-sugar glycosidase (uncovering enzyme, UCE), NAGPA superfamily [Carbohydrate transport ...
68-328 3.67e-33

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


Pssm-ID: 443670 [Multi-domain]  Cd Length: 310  Bit Score: 128.40  E-value: 3.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768  68 PTNPGASHHAAVRTFVSHFEGRAVAGHLTRVADPLRTFSVLEPGGAGGCAQKRRATVEDTAVPAGCRIAQNGGFFRMsTG 147
Cdd:COG4632   69 LAGAATAAVLLAAPLLSLLAGVTAGPGAPVTGGLLVRAAAGALVGALALGRLVDVLTLVTTPARGNRPVAPGGLFDP-GG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768 148 ECLGNVVSDGRLVSSSGGLQNAQ-FGIRRDGTIVTGYLSEEEVLDPVNPFVQLLSGVVWLIRNGNIYINESQAiecdetq 226
Cdd:COG4632  148 KPTGIIISNGKVISPNKDGPARDvLGIDKDGKLIVGDPVTIDLEKLPAGVEEAVGGGPLLVKNGKVVVDADEA------- 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 241982768 227 etgsfsKFVNVMSARTAVGHDREGQLILFHADG-QTEQRGLNLWEMAEFLRQQDVVNAINLDGGGSATFVLNGTLASYPS 305
Cdd:COG4632  221 ------AFGNGRAPRTAIGITADGTLLLVVVDGrQPGSIGATLAELAQLLKELGAVDALNLDGGGSTTLVYNGKVVNRPS 294
                        250       260
                 ....*....|....*....|...
gi 241982768 306 DHCQdnmwrcpRQVSTVVCVHEP 328
Cdd:COG4632  295 DGKE-------RPVANALGVFPK 310
 
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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