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Conserved domains on  [gi|392886182|ref|NP_001040639|]
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Nucleotide-diphospho-sugar transferase domain-containing protein [Caenorhabditis elegans]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 30-233 2.94e-25

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member pfam03407:

Pssm-ID: 472172  Cd Length: 208  Bit Score: 100.48  E-value: 2.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886182   30 GALSRLVAISFDTPSHLILKEKYPNIPSVVINLDSIKKTlPESYENRRYiiyQLVLLTRARICASLALRGISFWAMQQDT 109
Cdd:pfam03407   1 GLLDNLLVVALDEEAYERCKELGPPICYLLSDLKDFSKK-DFGFGSKTY---LKMSWRRVRLLLELLKLGYNFLFTDVDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886182  110 LWVENFDSMdleNRYPDEYMLFDtVGNEQFGEYDRMFGWICGSTFFVRGNPTTYQFFYQIDSFMRSHQ-SPDSSIMTYLC 188
Cdd:pfam03407  77 VWLRNPFPL---LRYPDADVLVS-SDNYDGTTADGLKNWPNGGFFFVRSTNATIALFKRWAESLASYPgLWDQDVFNYLL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392886182  189 GHR-----NYRCHRLPRWIIS----SSDYFRGTRETTPVMIQVDSDQTDETKME 233
Cdd:pfam03407 153 REGappllGLKCRFLDTALFGgfcqSRDENWVKTKLKPYIVHANCCSGTEGKLK 206
 
Name Accession Description Interval E-value
Nucleotid_trans pfam03407
Nucleotide-diphospho-sugar transferase; Proteins in this family have been been predicted to be ...
 30-233 2.94e-25

Nucleotide-diphospho-sugar transferase; Proteins in this family have been been predicted to be nucleotide-diphospho-sugar transferases.


Pssm-ID: 367480  Cd Length: 208  Bit Score: 100.48  E-value: 2.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886182   30 GALSRLVAISFDTPSHLILKEKYPNIPSVVINLDSIKKTlPESYENRRYiiyQLVLLTRARICASLALRGISFWAMQQDT 109
Cdd:pfam03407   1 GLLDNLLVVALDEEAYERCKELGPPICYLLSDLKDFSKK-DFGFGSKTY---LKMSWRRVRLLLELLKLGYNFLFTDVDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886182  110 LWVENFDSMdleNRYPDEYMLFDtVGNEQFGEYDRMFGWICGSTFFVRGNPTTYQFFYQIDSFMRSHQ-SPDSSIMTYLC 188
Cdd:pfam03407  77 VWLRNPFPL---LRYPDADVLVS-SDNYDGTTADGLKNWPNGGFFFVRSTNATIALFKRWAESLASYPgLWDQDVFNYLL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392886182  189 GHR-----NYRCHRLPRWIIS----SSDYFRGTRETTPVMIQVDSDQTDETKME 233
Cdd:pfam03407 153 REGappllGLKCRFLDTALFGgfcqSRDENWVKTKLKPYIVHANCCSGTEGKLK 206
 
Name Accession Description Interval E-value
Nucleotid_trans pfam03407
Nucleotide-diphospho-sugar transferase; Proteins in this family have been been predicted to be ...
 30-233 2.94e-25

Nucleotide-diphospho-sugar transferase; Proteins in this family have been been predicted to be nucleotide-diphospho-sugar transferases.


Pssm-ID: 367480  Cd Length: 208  Bit Score: 100.48  E-value: 2.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886182   30 GALSRLVAISFDTPSHLILKEKYPNIPSVVINLDSIKKTlPESYENRRYiiyQLVLLTRARICASLALRGISFWAMQQDT 109
Cdd:pfam03407   1 GLLDNLLVVALDEEAYERCKELGPPICYLLSDLKDFSKK-DFGFGSKTY---LKMSWRRVRLLLELLKLGYNFLFTDVDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392886182  110 LWVENFDSMdleNRYPDEYMLFDtVGNEQFGEYDRMFGWICGSTFFVRGNPTTYQFFYQIDSFMRSHQ-SPDSSIMTYLC 188
Cdd:pfam03407  77 VWLRNPFPL---LRYPDADVLVS-SDNYDGTTADGLKNWPNGGFFFVRSTNATIALFKRWAESLASYPgLWDQDVFNYLL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 392886182  189 GHR-----NYRCHRLPRWIIS----SSDYFRGTRETTPVMIQVDSDQTDETKME 233
Cdd:pfam03407 153 REGappllGLKCRFLDTALFGgfcqSRDENWVKTKLKPYIVHANCCSGTEGKLK 206
 
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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