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Conserved domains on  [gi|1816721222|ref|WP_163647419|]
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glycosyltransferase [Mycolicibacterium monacense]

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 ...
 1-172 6.34e-22

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 cd03809:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 362  Bit Score: 92.43  E-value: 6.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   1 MVHDLGSLDRPQEYPKLLLRE-----RTAVSRAHAVFAVSDFTASSIKRHFPrVNP---VPLHLGAINPVHSRPAH---- 68
Cdd:cd03809   107 TIHDLIPLRYPEFFPKRFRLYyrlllPISLRRADAIITVSEATRDDIIKFYG-VPPekiVVIPLGVDPSFFPPESAavli 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  69 ------DKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNFTPERLPPRTEIRSA-----------VSDEVLAA 131
Cdd:cd03809   186 akyllpEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLglggrvrflgyVSDEDLPA 265

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1816721222 132 LFECCSGFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGE 172
Cdd:cd03809   266 LYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE 306
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 1-172 6.34e-22

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: 92.43  E-value: 6.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   1 MVHDLGSLDRPQEYPKLLLRE-----RTAVSRAHAVFAVSDFTASSIKRHFPrVNP---VPLHLGAINPVHSRPAH---- 68
Cdd:cd03809   107 TIHDLIPLRYPEFFPKRFRLYyrlllPISLRRADAIITVSEATRDDIIKFYG-VPPekiVVIPLGVDPSFFPPESAavli 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  69 ------DKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNFTPERLPPRTEIRSA-----------VSDEVLAA 131
Cdd:cd03809   186 akyllpEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLglggrvrflgyVSDEDLPA 265

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1816721222 132 LFECCSGFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGE 172
Cdd:cd03809   266 LYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE 306
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 69-198 2.88e-14

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: 68.07  E-value: 2.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  69 DKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNfTPERLPPRTEIRSA-----------VSDEVLAALFECCS 137
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGD-GEEEKRLKKLAEKLglgdnviflgfVSDEDLPELLKIAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816721222 138 GFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGELLAAR-AGVPIDA-SVAESADYLSNFLS 198
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGeTGFLVKPnNAEALAEAIDKLLE 143
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 126-198 8.54e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 49.60  E-value: 8.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816721222 126 DEVLAALFECCSGFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGELLA-ARAGVPIDA-SVAESADYLSNFLS 198
Cdd:COG0438    11 DLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdGETGLLVPPgDPEALAEAILRLLE 85
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 1-172 6.34e-22

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: 92.43  E-value: 6.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   1 MVHDLGSLDRPQEYPKLLLRE-----RTAVSRAHAVFAVSDFTASSIKRHFPrVNP---VPLHLGAINPVHSRPAH---- 68
Cdd:cd03809   107 TIHDLIPLRYPEFFPKRFRLYyrlllPISLRRADAIITVSEATRDDIIKFYG-VPPekiVVIPLGVDPSFFPPESAavli 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  69 ------DKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNFTPERLPPRTEIRSA-----------VSDEVLAA 131
Cdd:cd03809   186 akyllpEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLglggrvrflgyVSDEDLPA 265

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1816721222 132 LFECCSGFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGE 172
Cdd:cd03809   266 LYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPE 306
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 3-198 3.26e-16

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: 76.81  E-value: 3.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   3 HDLGSLDRPQEYPKLLLRERTAV-SRAHAVFAVSDFTASSIKRHFPRV--------NPVPLHL--GAINPVHSRPAHDKF 71
Cdd:cd03801   115 AEPGRLLLLLAAERRLLARAEALlRRADAVIAVSEALRDELRALGGIPpekivvipNGVDLERfsPPLRRKLGIPPDRPV 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  72 LLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNFTPER---------LPPRTEIRSAVSDEVLAALFECCSGFVSF 142
Cdd:cd03801   195 LLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRaeleelelgLGDRVRFLGFVPDEELPALYAAADVFVLP 274

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1816721222 143 SAYEGLGLPLYTALASGIPTIASNIPPYGELLAARAG--VPIDASVAESADYLSNFLS 198
Cdd:cd03801   275 SRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGglVVPPDDVEALADALLRLLA 332
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 69-198 2.88e-14

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: 68.07  E-value: 2.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  69 DKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNfTPERLPPRTEIRSA-----------VSDEVLAALFECCS 137
Cdd:pfam00534   2 KKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGD-GEEEKRLKKLAEKLglgdnviflgfVSDEDLPELLKIAD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816721222 138 GFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGELLAAR-AGVPIDA-SVAESADYLSNFLS 198
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGeTGFLVKPnNAEALAEAIDKLLE 143
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 6-190 1.02e-12

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: 66.61  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   6 GSLDRPQEYPKLLLRERTAVSRAHAVFAVSDFTASSIKRHFPRV--------NPVPLHlgAIN-----PVHSRPAHDKFL 72
Cdd:cd03811   114 SSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPpekieviyNPIDID--RIRalakePILNEPEDGPVI 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  73 LSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNftperLPPRTEIRSAV-----SDEVL--------AALFECCSGF 139
Cdd:cd03811   192 LAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGD-----GPLREELEKLAkelglAERVIflgfqsnpYPYLKKADLF 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1816721222 140 VSFSAYEGLGLPLYTALASGIPTIASNIPPYGELLAARAG---VPIDASVAESA 190
Cdd:cd03811   267 VLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENgllVPDGDAAALAG 320
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 1-168 1.38e-11

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: 63.00  E-value: 1.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   1 MVHDLGSLDRPQEYPKLLLR--ERTAVSRAHAVFAVSDF-TASSIKRHFPRVNPVPLHLGAINPVH------SRPAHDKF 71
Cdd:cd03808   111 TVHGLGFVFTEGKLLRLLYLllEKLALLFTDKVIFVNEDdRDLAIKKGIIKKKKTVLIPGSGVDLDrfqyspESLPSEKV 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  72 -LLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSnFTPERLPPRTEIRSAVSDEVL---------AALFECCSGFVS 141
Cdd:cd03808   191 vFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVG-DGELENPSEILIEKLGLEGRIeflgfrsdvPELLAESDVFVL 269

                         170       180
                  ....*....|....*....|....*..
gi 1816721222 142 FSAYEGLGLPLYTALASGIPTIASNIP 168
Cdd:cd03808   270 PSYREGLPRSLLEAMAAGRPVITTDVP 296
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 10-169 1.06e-10

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 60.71  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  10 RPQEYPKLLLRERtAVSRAHAVFAVSDFTASSI-KRHFPRV----NPVPLHLgainPVHSRPAHDKFLLSVAANRPNKRL 84
Cdd:cd03820   122 YNKGLRRLLLRRL-LYKRADKIVVLTEADKLKKyKQPNSNVvvipNPLSFPS----EEPSTNLKSKRILAVGRLTYQKGF 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  85 AYLLDTWERTGPQHPDWKLV-------------LVSNFTPE---RLPPRTeirSAVSDEVLAAlfeccSGFVSFSAYEGL 148
Cdd:cd03820   197 DLLIEAWALIAKKHPDWKLRiygdgpereelekLIDKLGLEdrvKLLGPT---KNIAEEYANS-----SIFVLSSRYEGF 268

                         170       180
                  ....*....|....*....|.
gi 1816721222 149 GLPLYTALASGIPTIASNIPP 169
Cdd:cd03820   269 PMVLLEAMAYGLPIISFDCPT 289
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
72-180 1.70e-09

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 54.44  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  72 LLSVAANRPN-KRLAYLLDTWERTGPQHPDWKLVLVSNFTPERL-------PPRTEIRSAVSDevLAALFECCSGFVSFS 143
Cdd:pfam13692   4 ILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELeelaaglEDRVIFTGFVED--LAELLAAADVFVLPS 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1816721222 144 AYEGLGLPLYTALASGIPTIASNIPPYGELLAARAGV 180
Cdd:pfam13692  82 LYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGL 118
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 4-198 2.57e-09

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 56.61  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   4 DLGSLDRPQEYPKLLLRERTAVSRAHAVFAVSDFTASSIKRH------------FPR-VNPVPLHLGAINPVHSRPAHD- 69
Cdd:cd03821   125 MLDPWALQQKHWKKRIALHLIERRNLNNAALVHFTSEQEADElrrfgleppiavIPNgVDIPEFDPGLRDRRKHNGLEDr 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  70 KFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLV----SNFTPER-------LPPRTEIRSAVSDEVLAALFECCSG 138
Cdd:cd03821   205 RIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAgpddGAYPAFLqlqsslgLGDRVTFTGPLYGEAKWALYASADL 284

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222 139 FVSFSAYEGLGLPLYTALASGIPTIASNIPPYGELLAARAGVPIDASVAESADYLSNFLS 198
Cdd:cd03821   285 FVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALR 344
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 45-168 2.18e-08

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: 53.18  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  45 HFPRVNPVPLHLGAINPVHSRPAHDKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLV-SNFTPERLPPRTEIRSA 123
Cdd:cd01635    86 HGPDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVgGGGEREEEEALAAALGL 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1816721222 124 VSD----------EVLAALFECCSGFVSFSAYEGLGLPLYTALASGIPTIASNIP 168
Cdd:cd01635   166 LERvviigglvddEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVG 220
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 21-167 3.22e-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: 53.15  E-value: 3.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  21 ERTAVSRAHAVFAVSDFTASSIKRHFP---RV----NPVPLHLGAINPVHSRPAHDKFL-LSVAANRPNKRLAYLLDTWE 92
Cdd:cd03798   144 LRWALRRAARVIAVSKALAEELVALGVprdRVdvipNGVDPARFQPEDRGLGLPLDAFViLFVGRLIPRKGIDLLLEAFA 223

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  93 RTGPQHPDWKLVLVSNFtPERLPPRTEIRSA-----------VSDEVLAALFECCSGFVSFSAYEGLGLPLYTALASGIP 161
Cdd:cd03798   224 RLAKARPDVVLLIVGDG-PLREALRALAEDLglgdrvtftgrLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLP 302


                  ....*.
gi 1816721222 162 TIASNI 167
Cdd:cd03798   303 VVATDV 308
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 126-198 8.54e-08

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 49.60  E-value: 8.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816721222 126 DEVLAALFECCSGFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGELLA-ARAGVPIDA-SVAESADYLSNFLS 198
Cdd:COG0438    11 DLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdGETGLLVPPgDPEALAEAILRLLE 85
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 66-179 9.70e-08

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: 51.93  E-value: 9.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  66 PAHDKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNFTPERLPPRTEIRSAVSDEVL--------AALFECCS 137
Cdd:cd03807   187 AEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDRVHllgersdvPALLPAMD 266

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1816721222 138 GFVSFSAYEGLGLPLYTALASGIPTIASNIPPYGELLAARAG 179
Cdd:cd03807   267 IFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDGTG 308
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 22-167 3.25e-06

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: 47.35  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  22 RTAVSRAHAVFAVSDFTASSIKRHFPRVNPV-------------PLHLGAINPVHSRPAHDKFLLSVAANRPNKRLAYLL 88
Cdd:cd04962   136 RFSINKSDRVTAVSSSLRQETYELFDVDKDIevihnfidedvfkRKPAGALKRRLLAPPDEKVVIHVSNFRPVKRIDDVV 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  89 DTWERTGPQHPDwKLVLVSNfTPERLPPRTEIRS-AVSDEVL-AALFECCSGFVSF-------SAYEGLGLPLYTALASG 159
Cdd:cd04962   216 RVFARVRRKIPA-KLLLVGD-GPERVPAEELARElGVEDRVLfLGKQDDVEELLSIadlfllpSEKESFGLAALEAMACG 293


                  ....*...
gi 1816721222 160 IPTIASNI 167
Cdd:cd04962   294 VPVVSSNA 301
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 18-167 1.44e-03

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 39.24  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  18 LLRERTAVSRAHAVfAVSDFTA-----SSIKRHFPRV---NPV------PLHLGAINPVHSRPAhDKFLLSVAANR---P 80
Cdd:cd03825   129 RKREALAKKRLTIV-APSRWLAdmvrrSPLLKGLPVVvipNGIdteifaPVDKAKARKRLGIPQ-DKKVILFGAESvtkP 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  81 NKRLAYLLDTWERTgPQHPDWKLVLVSNFTPERLPPRTEIRSAVS---DEVLAALFECCSGFVSFSAYEGLGLPLYTALA 157
Cdd:cd03825   207 RKGFDELIEALKLL-ATKDDLLLVVFGKNDPQIVILPFDIISLGYiddDEQLVDIYSAADLFVHPSLADNLPNTLLEAMA 285

                         170
                  ....*....|
gi 1816721222 158 SGIPTIASNI 167
Cdd:cd03825   286 CGTPVVAFDT 295
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 65-166 4.08e-03

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 37.99  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  65 RPAHDKFLLSVAANRPNKRLAYLLDTWERTGPQHPDWKLVLVSNFTPERLPPRTEIRSA----------------VSDEV 128
Cdd:cd03800   216 LPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAElaeelglidrvrfpgrVSRDD 295

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1816721222 129 LAALFECCSGFVSFSAYEGLGLPLYTALASGIPTIASN 166
Cdd:cd03800   296 LPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATA 333
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 27-165 4.58e-03

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. 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 and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 37.66  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  27 RAHAVFAVSDFTASSIKRH-FPRVNPVPL--HLGAINPVHsRPAHDKFLLSVAANR---------PNKRLAYLLDTWERt 94
Cdd:cd03814   145 PFDTTLVPSPSIARELEGHgFERVRLWPRgvDTELFHPSR-RDAALRRRLGPPGRPlllyvgrlaPEKNLEALLDADLP- 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  95 GPQHPDWKLVLV-SNftperlPPRTEIRSAVSD---------EVLAALFECCSGFVSFSAYEGLGLPLYTALASGIPTIA 164
Cdd:cd03814   223 LAASPPVRLVVVgDG------PARAELEARGPDviftgfltgEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVA 296


                  .
gi 1816721222 165 S 165
Cdd:cd03814   297 A 297
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 4-191 4.65e-03

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 37.71  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222   4 DLGSLDRPQEYPKLLLRERTAVSRAHAVFAVSDFTASSIKRHFPRVNPV-----------PLHLGAINPVHSRPAHDKFL 72
Cdd:cd03794   140 ALGVLKKGSLLKLLKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIivipnwadleeFKPPPKDELRKKLGLDDKFV 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  73 LSVAANRPNKR-LAYLLDTWERTgPQHPDWKLVLV---------SNFTPERLPPRTEIRSAVS-DEVLAALFECCSGFVS 141
Cdd:cd03794   220 VVYAGNIGKAQgLETLLEAAERL-KRRPDIRFLFVgdgdekerlKELAKARGLDNVTFLGRVPkEEVPELLSAADVGLVP 298

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1816721222 142 FS--AYEGLGLP--LYTALASGIPTIASNIPPYGEL-LAARAGVPIDA-SVAESAD 191
Cdd:cd03794   299 LKdnPANRGSSPskLFEYMAAGKPILASDDGGSDLAvEINGCGLVVEPgDPEALAD 354
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 17-165 9.17e-03

glycosyltransferase family 4 proteins; 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 glycosyltransferase family 4 (GT4). 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.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 36.66  E-value: 9.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  17 LLLRERTAVSRAHAVFAVSDFT-ASSIKRHFP----RVNPVPLHLGAINPVHSRPAHDKFLLsVAANRPNKRLAYLLDTW 91
Cdd:cd05844   133 FQRHRRALQRPAALFVAVSGFIrDRLLARGLPaeriHVHYIGIDPAKFAPRDPAERAPTILF-VGRLVEKKGCDVLIEAF 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816721222  92 ERTGPQHPDWKLVLVSNfTPERlpPRTEIRSA---------------VSDEVLAALFECCSGFVSFSA-YEGLGLPLYTA 155
Cdd:cd05844   212 RRLAARHPTARLVIAGD-GPLR--PALQALAAalgrvrflgalphaeVQDWMRRAEIFCLPSVTAASGdSEGLGIVLLEA 288

                         170
                  ....*....|
gi 1816721222 156 LASGIPTIAS 165
Cdd:cd05844   289 AACGVPVVSS 298
 
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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