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Conserved domains on  [gi|1008842576|gb|KYK25801|]
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hypothetical protein AYK26_07665 [Euryarchaeota archaeon SM23-78]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

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
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
111-339 2.09e-05

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03801:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 366  Bit Score: 45.99  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 111 YAAFSKLVEKVVCISPFHQTYFEDVYGIKN--TVAIDLPVRLQEY------KEEIEKVEYRFIYTS--VPNRGLQNLWRI 180
Cdd:cd03801   134 AEALLRRADAVIAVSEALRDELRALGGIPPekIVVIPNGVDLERFspplrrKLGIPPDRPVLLFVGrlSPRKGVDLLLEA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 181 WPMILEVIPYASLVITsdyrlwgttspGNDKDIADWLTR------DNIKFLGGVSRERLVKEQLEAEIHIYPCNYDElFC 254
Cdd:cd03801   214 LAKLLRRGPDVRLVIV-----------GGDGPLRAELEElelglgDRVRFLGFVPDEELPALYAAADVFVLPSRYEG-FG 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 255 ISVAESQVAGVFPITTAQGALK---TTNMGVYVdINANDPRQdkfFVSVVKDVVNDAAFitdRNVLTKKA----IERFNP 327
Cdd:cd03801   282 LVVLEAMAAGLPVVATDVGGLPevvEDGEGGLV-VPPDDVEA---LADALLRLLADPEL---RARLGRAArervAERFSW 354
                         250
                  ....*....|..
gi 1008842576 328 LRIVQEWDKVFN 339
Cdd:cd03801   355 ERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
111-339 2.09e-05

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 45.99  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 111 YAAFSKLVEKVVCISPFHQTYFEDVYGIKN--TVAIDLPVRLQEY------KEEIEKVEYRFIYTS--VPNRGLQNLWRI 180
Cdd:cd03801   134 AEALLRRADAVIAVSEALRDELRALGGIPPekIVVIPNGVDLERFspplrrKLGIPPDRPVLLFVGrlSPRKGVDLLLEA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 181 WPMILEVIPYASLVITsdyrlwgttspGNDKDIADWLTR------DNIKFLGGVSRERLVKEQLEAEIHIYPCNYDElFC 254
Cdd:cd03801   214 LAKLLRRGPDVRLVIV-----------GGDGPLRAELEElelglgDRVRFLGFVPDEELPALYAAADVFVLPSRYEG-FG 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 255 ISVAESQVAGVFPITTAQGALK---TTNMGVYVdINANDPRQdkfFVSVVKDVVNDAAFitdRNVLTKKA----IERFNP 327
Cdd:cd03801   282 LVVLEAMAAGLPVVATDVGGLPevvEDGEGGLV-VPPDDVEA---LADALLRLLADPEL---RARLGRAArervAERFSW 354
                         250
                  ....*....|..
gi 1008842576 328 LRIVQEWDKVFN 339
Cdd:cd03801   355 ERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
169-324 5.27e-05

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 43.03  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 169 VPNRGLQNLWRIWPMILEVIPYASLVITSDyrlwgttspGNDKD-----IADWLTRDNIKFLGGVSRERLVKEQLEAEIH 243
Cdd:pfam00534  12 EPEKGLDLLIKAFALLKEKNPNLKLVIAGD---------GEEEKrlkklAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 244 IYPCNYdELFCISVAESQVAGVFPIttaqgalkTTNMGVYVDINAN-------DPRQDKFFVSVVKDVVNDAAFitdRNV 316
Cdd:pfam00534  83 VLPSRY-EGFGIVLLEAMACGLPVI--------ASDVGGPPEVVKDgetgflvKPNNAEALAEAIDKLLEDEEL---RER 150

                  ....*...
gi 1008842576 317 LTKKAIER 324
Cdd:pfam00534 151 LGENARKR 158
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
111-339 2.09e-05

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 45.99  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 111 YAAFSKLVEKVVCISPFHQTYFEDVYGIKN--TVAIDLPVRLQEY------KEEIEKVEYRFIYTS--VPNRGLQNLWRI 180
Cdd:cd03801   134 AEALLRRADAVIAVSEALRDELRALGGIPPekIVVIPNGVDLERFspplrrKLGIPPDRPVLLFVGrlSPRKGVDLLLEA 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 181 WPMILEVIPYASLVITsdyrlwgttspGNDKDIADWLTR------DNIKFLGGVSRERLVKEQLEAEIHIYPCNYDElFC 254
Cdd:cd03801   214 LAKLLRRGPDVRLVIV-----------GGDGPLRAELEElelglgDRVRFLGFVPDEELPALYAAADVFVLPSRYEG-FG 281
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 255 ISVAESQVAGVFPITTAQGALK---TTNMGVYVdINANDPRQdkfFVSVVKDVVNDAAFitdRNVLTKKA----IERFNP 327
Cdd:cd03801   282 LVVLEAMAAGLPVVATDVGGLPevvEDGEGGLV-VPPDDVEA---LADALLRLLADPEL---RARLGRAArervAERFSW 354
                         250
                  ....*....|..
gi 1008842576 328 LRIVQEWDKVFN 339
Cdd:cd03801   355 ERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
169-324 5.27e-05

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 43.03  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 169 VPNRGLQNLWRIWPMILEVIPYASLVITSDyrlwgttspGNDKD-----IADWLTRDNIKFLGGVSRERLVKEQLEAEIH 243
Cdd:pfam00534  12 EPEKGLDLLIKAFALLKEKNPNLKLVIAGD---------GEEEKrlkklAEKLGLGDNVIFLGFVSDEDLPELLKIADVF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1008842576 244 IYPCNYdELFCISVAESQVAGVFPIttaqgalkTTNMGVYVDINAN-------DPRQDKFFVSVVKDVVNDAAFitdRNV 316
Cdd:pfam00534  83 VLPSRY-EGFGIVLLEAMACGLPVI--------ASDVGGPPEVVKDgetgflvKPNNAEALAEAIDKLLEDEEL---RER 150

                  ....*...
gi 1008842576 317 LTKKAIER 324
Cdd:pfam00534 151 LGENARKR 158
 
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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