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Conserved domains on  [gi|1774959466|ref|NP_001363258|]
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glycosyltransferase-like domain-containing protein 1 isoform g [Homo sapiens]

Protein Classification

glycosyltransferase( domain architecture ID 11546995)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 135-247 2.23e-11

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.


:

Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.42  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 135 VWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVIS 214
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1774959466 215 TAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIF 247
Cdd:cd01635   194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 206-298 7.45e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 206 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 276
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1774959466 277 LYKG-EIA--PFSWAALHGKFRSLL 298
Cdd:COG0438    94 GEAArERAeeRFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 135-247 2.23e-11

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.42  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 135 VWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVIS 214
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1774959466 215 TAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIF 247
Cdd:cd01635   194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 134-306 1.47e-04

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: 41.49  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 134 IVWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETfTDVPDIFSEAKKALGSSVLHW-GYLPSKD--DYFQvlcMAD 210
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 211 VVISTAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFpaeylystpeqlskrlqnfckrpdiirKHLYKGE-IAPFSWAA 289
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---------------------------KDGETGFlVKPNNAEA 133

                         170
                  ....*....|....*...
gi 1774959466 290 LHGKFRSLLT-TEPREDL 306
Cdd:pfam00534 134 LAEAIDKLLEdEELRERL 151
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 206-298 7.45e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 206 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 276
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1774959466 277 LYKG-EIA--PFSWAALHGKFRSLL 298
Cdd:COG0438    94 GEAArERAeeRFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 135-247 2.23e-11

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 62.42  E-value: 2.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 135 VWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVIS 214
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVL 193

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1774959466 215 TAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIF 247
Cdd:cd01635   194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 136-289 4.00e-06

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 47.74  E-value: 4.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 136 WPHrwehdKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHW-GYLPsKDDYFQVLCMADVVIS 214
Cdd:cd03809   202 EPR-----KNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFlGYVS-DEDLPALYRGARAFVF 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 215 TAKHEFFGVAMLEAVYCGCyP-LCPKDLVYPEIFPAEYLY---STPEQLSKRLQNFCKRPDIIRKHLYKG--EIAPFSWA 288
Cdd:cd03809   276 PSLYEGFGLPVLEAMACGT-PvIASNISVLPEVAGDAALYfdpLDPESIADAILRLLEDPSLREELIRKGleRAKKFSWE 354


                  .
gi 1774959466 289 A 289
Cdd:cd03809   355 K 355
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 142-233 7.78e-06

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 46.82  E-value: 7.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 142 HDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYlpsKDDYFQVLCMADVVISTAKHEFF 221
Cdd:cd03808   200 KDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGF---RSDVPELLAESDVFVLPSYREGL 276

                          90
                  ....*....|..
gi 1774959466 222 GVAMLEAVYCGC 233
Cdd:cd03808   277 PRSLLEAMAAGR 288
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 134-298 2.16e-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: 45.61  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 134 IVWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIfSEAKKALGSSVLHWGYLPsKDDYFQVLCMADVVI 213
Cdd:cd03801   195 LLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAEL-EELELGLGDRVRFLGFVP-DEELPALYAAADVFV 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 214 STAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFPAEYLY-----STPEQLSKRLQNFCKRPDI---IRKHLYKGEIAPF 285
Cdd:cd03801   273 LPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGlvvppDDVEALADALLRLLADPELrarLGRAARERVAERF 352

                         170
                  ....*....|...
gi 1774959466 286 SWAALHGKFRSLL 298
Cdd:cd03801   353 SWERVAERLLDLY 365
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 134-306 1.47e-04

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: 41.49  E-value: 1.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 134 IVWPHRWEHDKDPESFFKVLMHLKDLGLNFHVSVLGETfTDVPDIFSEAKKALGSSVLHW-GYLPSKD--DYFQvlcMAD 210
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IAD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 211 VVISTAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFpaeylystpeqlskrlqnfckrpdiirKHLYKGE-IAPFSWAA 289
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---------------------------KDGETGFlVKPNNAEA 133

                         170
                  ....*....|....*...
gi 1774959466 290 LHGKFRSLLT-TEPREDL 306
Cdd:pfam00534 134 LAEAIDKLLEdEELRERL 151
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 206-298 7.45e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 7.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959466 206 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 276
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1774959466 277 LYKG-EIA--PFSWAALHGKFRSLL 298
Cdd:COG0438    94 GEAArERAeeRFSWEAIAERLLALY 118
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 195-232 8.31e-03

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. 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 bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 37.33  E-value: 8.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1774959466 195 YLPSKDDYFQVLCMADVVISTAKHEFFGVAMLEAVYCG 232
Cdd:cd04962   256 FLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACG 293
 
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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