NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568937824|ref|XP_006504372|]
View 

glycosyltransferase 1 domain-containing protein 1 isoform X1 [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 2-260 5.89e-10

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: 59.47  E-value: 5.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824   2 RLLFLA--VLRPHTGNAVTAGRLRDHLEAAGH--MCVLRDAFDFESPSEIANLIMDENLEAALALHLYR----------- 66
Cdd:cd03801    1 KILLLSpeLPPPVGGAERHVRELARALAARGHdvTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelrpllrl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824  67 -GGRLLQGHSIPFGVIF----------------GGTDLNEDANHKEKKEVMGKVLEEARFA---VAFTEAMKDTAQVQWP 126
Cdd:cd03801   81 rKFDVVHAHGLLAALLAallalllgaplvvtlhGAEPGRLLLLLAAERRLLARAEALLRRAdavIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 127 HATGKIFVqsqgiatIPNA---NFNWNTFLQQSEIDQSAdnlYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG 203
Cdd:cd03801  161 IPPEKIVV-------IPNGvdlERFSPPLRRKLGIPPDR---PVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937824 204 PEvDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGMSAAILE 260
Cdd:cd03801  231 GD-GPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLE 286
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-260 5.89e-10

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: 59.47  E-value: 5.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824   2 RLLFLA--VLRPHTGNAVTAGRLRDHLEAAGH--MCVLRDAFDFESPSEIANLIMDENLEAALALHLYR----------- 66
Cdd:cd03801    1 KILLLSpeLPPPVGGAERHVRELARALAARGHdvTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelrpllrl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824  67 -GGRLLQGHSIPFGVIF----------------GGTDLNEDANHKEKKEVMGKVLEEARFA---VAFTEAMKDTAQVQWP 126
Cdd:cd03801   81 rKFDVVHAHGLLAALLAallalllgaplvvtlhGAEPGRLLLLLAAERRLLARAEALLRRAdavIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 127 HATGKIFVqsqgiatIPNA---NFNWNTFLQQSEIDQSAdnlYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG 203
Cdd:cd03801  161 IPPEKIVV-------IPNGvdlERFSPPLRRKLGIPPDR---PVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937824 204 PEvDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGMSAAILE 260
Cdd:cd03801  231 GD-GPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLE 286
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
175-260 9.99e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 38.65  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824  175 RPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDpvftREVKERVRR-AAGVRLIREMcqEDLHAVVKSCFALVNSSVSEG 253
Cdd:pfam13692  12 PNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----EELEELAAGlEDRVIFTGFV--EDLAELLAAADVFVLPSLYEG 85


                  ....*..
gi 568937824  254 MSAAILE 260
Cdd:pfam13692  86 FGLKLLE 92
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-260 5.89e-10

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: 59.47  E-value: 5.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824   2 RLLFLA--VLRPHTGNAVTAGRLRDHLEAAGH--MCVLRDAFDFESPSEIANLIMDENLEAALALHLYR----------- 66
Cdd:cd03801    1 KILLLSpeLPPPVGGAERHVRELARALAARGHdvTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRllrelrpllrl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824  67 -GGRLLQGHSIPFGVIF----------------GGTDLNEDANHKEKKEVMGKVLEEARFA---VAFTEAMKDTAQVQWP 126
Cdd:cd03801   81 rKFDVVHAHGLLAALLAallalllgaplvvtlhGAEPGRLLLLLAAERRLLARAEALLRRAdavIAVSEALRDELRALGG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 127 HATGKIFVqsqgiatIPNA---NFNWNTFLQQSEIDQSAdnlYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG 203
Cdd:cd03801  161 IPPEKIVV-------IPNGvdlERFSPPLRRKLGIPPDR---PVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVG 230

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937824 204 PEvDPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGMSAAILE 260
Cdd:cd03801  231 GD-GPLRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLE 286
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 76-260 1.54e-08

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 55.08  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824  76 IPFGVIFGGTDLNEDANHKEKKEVMGKVLEEARFAVAFTEAMKDTAQVQWPHAtGKIFVqsqgiatIPNAnFNWNTFlqq 155
Cdd:cd03798  120 VPYVVTEHGSDINVFPPRSLLRKLLRWALRRAARVIAVSKALAEELVALGVPR-DRVDV-------IPNG-VDPARF--- 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 156 SEIDQSAD-NLYIFLIIC--GLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDPVFTREVKERVRRAAGVRLIREMCQ 232
Cdd:cd03798  188 QPEDRGLGlPLDAFVILFvgRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPH 267

                        170       180
                 ....*....|....*....|....*...
gi 568937824 233 EDLHAVVKSCFALVNSSVSEGMSAAILE 260
Cdd:cd03798  268 EQVPAYYRACDVFVLPSRHEGFGLVLLE 295
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 131-271 2.11e-05

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 45.43  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 131 KIFVQSQGIA---------------TIPNAnFNWNTFLQQSEIDQSADNLYIFLIIC-G-LRPVKDPLYLVDAFSEWHQE 193
Cdd:cd03811  138 KIVCVSKGIKedlirlgpsppekieVIYNP-IDIDRIRALAKEPILNEPEDGPVILAvGrLDPQKGHDLLIEAFAKLRKK 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 194 TPNVYMVIVG--PEvdpvftREVKERVRRAAGvrlIREMC-----QEDLHAVVKSCFALVNSSVSEGMSAAILEgewsAC 266
Cdd:cd03811  217 YPDVKLVILGdgPL------REELEKLAKELG---LAERViflgfQSNPYPYLKKADLFVLSSRYEGFPNVLLE----AM 283


                 ....*
gi 568937824 267 LFRIP 271
Cdd:cd03811  284 ALGTP 288
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 133-261 1.80e-04

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 42.69  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 133 FVQSQGIA-----TIPNA----NFNwNTFLQQSEIDQS---ADNLYIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMV 200
Cdd:cd03807  147 FHQEQGYAknkivVIYNGidlfKLS-PDDASRARARRRlglAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLL 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568937824 201 IVGPEVdpvfTREVKERVRRAAG----VRLIREmcQEDLHAVVKSCFALVNSSVSEGMSAAILEG 261
Cdd:cd03807  226 LVGRGP----ERPNLERLLLELGledrVHLLGE--RSDVPALLPAMDIFVLSSRTEGFPNALLEA 284
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 134-253 2.22e-04

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: 42.35  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 134 VQSQGIATIPNANFNWNTFLQQSEIDQSADNL--YIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVG-------P 204
Cdd:cd03809  159 VPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLpePYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGgkgwedeE 238

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 568937824 205 EVDPVFTREVKERVRRAAGVRliremcQEDLHAVVKSCFALVNSSVSEG 253
Cdd:cd03809  239 LLDLVKKLGLGGRVRFLGYVS------DEDLPALYRGARAFVFPSLYEG 281
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
175-260 9.99e-04

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 38.65  E-value: 9.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824  175 RPVKDPLYLVDAFSEWHQETPNVYMVIVGPEVDpvftREVKERVRR-AAGVRLIREMcqEDLHAVVKSCFALVNSSVSEG 253
Cdd:pfam13692  12 PNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE----EELEELAAGlEDRVIFTGFV--EDLAELLAAADVFVLPSLYEG 85


                  ....*..
gi 568937824  254 MSAAILE 260
Cdd:pfam13692  86 FGLKLLE 92
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 166-260 1.24e-03

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: 38.79  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824  166 YIFLIICGLRPVKDPLYLVDAFSEWHQETPNVYMVIVGPEvdpvftrEVKERVRRAAGVRLIREMCQ-------EDLHAV 238
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-------EEEKRLKKLAEKLGLGDNVIflgfvsdEDLPEL 75

                          90       100
                  ....*....|....*....|..
gi 568937824  239 VKSCFALVNSSVSEGMSAAILE 260
Cdd:pfam00534  76 LKIADVFVLPSRYEGFGIVLLE 97
DUF2007 pfam09413
Putative prokaryotic signal transducing protein; This is a family of putative prokaryotic ...
 13-62 3.76e-03

Putative prokaryotic signal transducing protein; This is a family of putative prokaryotic signal transducing proteins of Pii-type.


Pssm-ID: 430595  Cd Length: 66  Bit Score: 35.27  E-value: 3.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568937824   13 TGNAVTAGRLRDHLEAAGHMCVLRDAFD-------FESPSEIanLIMDENLEAALAL 62
Cdd:pfam09413   7 TNDPVLASMIKALLEEAGIPCVIKDEFMsilegslGELPVRI--LVAEDDLERARRI 61
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 176-261 5.41e-03

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 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: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 38.08  E-value: 5.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568937824 176 PVKDPLYLVDAFSEWHQETPNVYMVIVGPEV-DPVFTREVKERVRRAAGVRLIREMCQEDLHAVVKSCFALVNSSVSEGM 254
Cdd:cd03813  304 PIKDVKTFIRAFKLVRRAMPDAEGWLIGPEDeDPEYAQECKRLVASLGLENKVKFLGFQNIKEYYPKLGLLVLTSISEGQ 383


                 ....*..
gi 568937824 255 SAAILEG 261
Cdd:cd03813  384 PLVILEA 390
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH