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Conserved domains on  [gi|14249738|ref|NP_115909|]
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N-acetylglucosamine-1-phosphotransferase subunit gamma precursor [Homo sapiens]

Protein Classification

PRKCSH domain-containing protein( domain architecture ID 10546062)

PRKCSH domain-containing protein similar to Homo sapiens N-acetylglucosamine-1-phosphotransferase subunit gamma, which is non-catalytic subunit of the N-acetylglucosamine-1-phosphotransferase complex, an enzyme that catalyzes the formation of mannose 6-phosphate (M6P) markers on high mannose type oligosaccharides in the Golgi apparatus

CATH:  2.70.130.10

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 69-129 2.31e-12

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.


:

Pssm-ID: 400321  Cd Length: 72  Bit Score: 61.40  E-value: 2.31e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14249738    69 GKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIANNT-----------FTGMWMRDGDAC 129
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKGQEKGGSSFSLGRFSESSWAESTyddewtkgsnrYISMIYGNGTKC 72
 
Name Accession Description Interval E-value
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 69-129 2.31e-12

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.


Pssm-ID: 400321  Cd Length: 72  Bit Score: 61.40  E-value: 2.31e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14249738    69 GKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIANNT-----------FTGMWMRDGDAC 129
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKGQEKGGSSFSLGRFSESSWAESTyddewtkgsnrYISMIYGNGTKC 72
 
Name Accession Description Interval E-value
PRKCSH pfam07915
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 69-129 2.31e-12

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. Mutations in the gene coding for PRKCSH have been found to be involved in the development of autosomal dominant polycystic liver disease (ADPLD), but the precise role the protein has in the pathogenesis of this disease is unknown. This family also includes an ER sensor for misfolded glycoproteins and is therefore likely to be a generic sugar binding domain.


Pssm-ID: 400321  Cd Length: 72  Bit Score: 61.40  E-value: 2.31e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14249738    69 GKCFSLVESTYKYEFCPFHNVTQHEQTFRWNAYSGILGIWHEWEIANNT-----------FTGMWMRDGDAC 129
Cdd:pfam07915   1 GKCFYYDEGEWTYEFCFGKHVRQFHKGQEKGGSSFSLGRFSESSWAESTyddewtkgsnrYISMIYGNGTKC 72
PRKCSH_1 pfam13015
Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a ...
 60-174 1.66e-06

Glucosidase II beta subunit-like protein; The sequences found in this family are similar to a region found in the beta-subunit of glucosidase II, which is also known as protein kinase C substrate 80K-H (PRKCSH). The enzyme catalyzes the sequential removal of two alpha-1,3-linked glucose residues in the second step of N-linked oligosaccharide processing. The beta subunit is required for the solubility and stability of the heterodimeric enzyme, and is involved in retaining the enzyme within the endoplasmic reticulum. The beta-subunit confers substrate specificity for di- and monoglucosylated glycans on the glucose-trimming activity of the alpha-subunit.


Pssm-ID: 404038  Cd Length: 154  Bit Score: 47.13  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14249738    60 GPVHLFR-LSGKCFSLVESTYKYEFCPFHNVTQHeqtfrwnaySGILGIWHEWEianntFTGMWMRDGDACRSRSRQSK- 137
Cdd:pfam13015  31 GPDDILRaYEGRETKEKIGGYTYKVCFLGSIFQD---------DISIGNFKKQE-----GNKLYYENGAKCWNGPHRSAi 96

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 14249738   138 VELACGKSNRLAHVSEPSTCVYALTFETPLVCHPHAL 174
Cdd:pfam13015  97 VEVECGDVNELVSVSEPEKCEYLFVVKSPAACSNVYL 133
 
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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