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Conserved domains on  [gi|1958643949|ref|XP_038961911|]
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probable dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase isoform X3 [Rattus norvegicus]

Protein Classification

glycosyltransferase family protein( domain architecture ID 229536)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Alg6_Alg8 super family cl46505
ALG6, ALG8 glycosyltransferase family; N-linked (asparagine-linked) glycosylation of proteins ...
74-267 3.04e-69

ALG6, ALG8 glycosyltransferase family; N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147.


The actual alignment was detected with superfamily member pfam03155:

Pssm-ID: 480845  Cd Length: 477  Bit Score: 221.60  E-value: 3.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643949  74 TSGLVQQSQHTVLPSVSPSATLICTLIAILPSVFCLWFKPQgPRGFLRCLVLCALSSFMFGWHVHEKAILLAILPMSLLA 153
Cdd:pfam03155 280 TRGLVGDTSFAVLPQILPKLTLILTLLAQLPSLIKLFLRPS-KRLFLLALTLCSLSFFLFSWHVHEKAILLVLLPLSLLA 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643949 154 VEKAGDATIFLILTTTGHYSLFPLLFTAPELPIKILLMSLFTVYSISSLRTLFRKEKP-----LFNWMETLYLLGLGPLE 228
Cdd:pfam03155 359 LEDPRDLSLFRWLSNVGTFSLFPLLFKDGLLLIKVVLTLLWNILFGLALRKLARLPFPslrvfLLDRLELLYLLSLIGML 438
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958643949 229 VCCEFLFPFTSWKLKYPFIPLLLTSVYCAVGITYAWIRL 267
Cdd:pfam03155 439 VLHCLLHLLVPPPARYPFLPLMLTSVYCSFGVFYSFLLY 477
 
Name Accession Description Interval E-value
Alg6_Alg8 pfam03155
ALG6, ALG8 glycosyltransferase family; N-linked (asparagine-linked) glycosylation of proteins ...
74-267 3.04e-69

ALG6, ALG8 glycosyltransferase family; N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147.


Pssm-ID: 460831  Cd Length: 477  Bit Score: 221.60  E-value: 3.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643949  74 TSGLVQQSQHTVLPSVSPSATLICTLIAILPSVFCLWFKPQgPRGFLRCLVLCALSSFMFGWHVHEKAILLAILPMSLLA 153
Cdd:pfam03155 280 TRGLVGDTSFAVLPQILPKLTLILTLLAQLPSLIKLFLRPS-KRLFLLALTLCSLSFFLFSWHVHEKAILLVLLPLSLLA 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643949 154 VEKAGDATIFLILTTTGHYSLFPLLFTAPELPIKILLMSLFTVYSISSLRTLFRKEKP-----LFNWMETLYLLGLGPLE 228
Cdd:pfam03155 359 LEDPRDLSLFRWLSNVGTFSLFPLLFKDGLLLIKVVLTLLWNILFGLALRKLARLPFPslrvfLLDRLELLYLLSLIGML 438
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958643949 229 VCCEFLFPFTSWKLKYPFIPLLLTSVYCAVGITYAWIRL 267
Cdd:pfam03155 439 VLHCLLHLLVPPPARYPFLPLMLTSVYCSFGVFYSFLLY 477
 
Name Accession Description Interval E-value
Alg6_Alg8 pfam03155
ALG6, ALG8 glycosyltransferase family; N-linked (asparagine-linked) glycosylation of proteins ...
74-267 3.04e-69

ALG6, ALG8 glycosyltransferase family; N-linked (asparagine-linked) glycosylation of proteins is mediated by a highly conserved pathway in eukaryotes, in which a lipid (dolichol phosphate)-linked oligosaccharide is assembled at the endoplasmic reticulum membrane prior to the transfer of the oligosaccharide moiety to the target asparagine residues. This oligosaccharide is composed of Glc(3)Man(9)GlcNAc(2). The addition of the three glucose residues is the final series of steps in the synthesis of the oligosaccharide precursor. Alg6 transfers the first glucose residue, and Alg8 transfers the second one. In the human alg6 gene, a C->T transition, which causes Ala333 to be replaced with Val, has been identified as the cause of a congenital disorder of glycosylation, designated as type Ic OMIM:603147.


Pssm-ID: 460831  Cd Length: 477  Bit Score: 221.60  E-value: 3.04e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643949  74 TSGLVQQSQHTVLPSVSPSATLICTLIAILPSVFCLWFKPQgPRGFLRCLVLCALSSFMFGWHVHEKAILLAILPMSLLA 153
Cdd:pfam03155 280 TRGLVGDTSFAVLPQILPKLTLILTLLAQLPSLIKLFLRPS-KRLFLLALTLCSLSFFLFSWHVHEKAILLVLLPLSLLA 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958643949 154 VEKAGDATIFLILTTTGHYSLFPLLFTAPELPIKILLMSLFTVYSISSLRTLFRKEKP-----LFNWMETLYLLGLGPLE 228
Cdd:pfam03155 359 LEDPRDLSLFRWLSNVGTFSLFPLLFKDGLLLIKVVLTLLWNILFGLALRKLARLPFPslrvfLLDRLELLYLLSLIGML 438
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958643949 229 VCCEFLFPFTSWKLKYPFIPLLLTSVYCAVGITYAWIRL 267
Cdd:pfam03155 439 VLHCLLHLLVPPPARYPFLPLMLTSVYCSFGVFYSFLLY 477
 
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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