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Conserved domains on  [gi|1062692902|ref|WP_069332948|]
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glycosyltransferase [Cereibacter johrii]

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 ...
36-265 2.52e-64

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 cd02520:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 196  Bit Score: 202.83  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  36 PFVCLLRPVCGQDRFDRETLGSSFGLDWPDYEIVFCAAREEDAAVPLVRELIRLHPGARARLMIGEERITANPKLNNLAK 115
Cdd:cd02520     1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 116 GWAGTRARMIAIADANLLLPRDYLEQLAS-EWRPGVALVSSPpaggraeglwgaleagflnglqgrwqlaaarlglgFAQ 194
Cdd:cd02520    81 GYEEARYDILVISDSDISVPPDYLRRMVApLMDPGVGLVTCL-----------------------------------CAF 125
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062692902 195 GKTMYLDRALLDRQGGLAALGAELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWSRIR 265
Cdd:cd02520   126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSRTR 196
 
Name Accession Description Interval E-value
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
36-265 2.52e-64

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 202.83  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  36 PFVCLLRPVCGQDRFDRETLGSSFGLDWPDYEIVFCAAREEDAAVPLVRELIRLHPGARARLMIGEERITANPKLNNLAK 115
Cdd:cd02520     1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 116 GWAGTRARMIAIADANLLLPRDYLEQLAS-EWRPGVALVSSPpaggraeglwgaleagflnglqgrwqlaaarlglgFAQ 194
Cdd:cd02520    81 GYEEARYDILVISDSDISVPPDYLRRMVApLMDPGVGLVTCL-----------------------------------CAF 125
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062692902 195 GKTMYLDRALLDRQGGLAALGAELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWSRIR 265
Cdd:cd02520   126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSRTR 196
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
91-263 5.98e-56

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 180.56  E-value: 5.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  91 PGARARLmIGEERITANPKLNNLAKGWAGTRARMIAIADANLLLPRDYLEQLASEWR-PGVALVSSPPAGGRAEGLWGAL 169
Cdd:pfam13506   1 PSVRALV-VGGPPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLAdPKVGLVTSPPVGSDPKGLAAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 170 EAGFLNGLQGRWQlaAARLGLGFAQGKTMYLDRALLDRQGGLAALGAELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRR 249
Cdd:pfam13506  80 EAAFFNTLAGVLQ--AALSGIGFAVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPR 157
                         170
                  ....*....|....*.
gi 1062692902 250 R--LRDVWARQLRWSR 263
Cdd:pfam13506 158 RtsFRAFMARQLRWAR 173
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
26-352 1.78e-23

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 98.66  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  26 RRRPTPPATRPFVCLLRPVCGQDRFDRETLGSSFGLDWP--DYEIVFCAAREEDAAVPLVRELIRLHPgaRARLMIGEER 103
Cdd:COG1215    19 ARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPEN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 104 ITanpKLNNLAKGWAGTRARMIAIADANLLLPRDYLEQLASEWR-PGVAlvssppaggraeglwgaleagflnglqgrwq 182
Cdd:COG1215    97 GG---KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAdPGVG------------------------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 183 laaarlglgfAQGKTMYLDRALLDRQGGLAALgaELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWS 262
Cdd:COG1215   143 ----------ASGANLAFRREALEEVGGFDED--TLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 263 RIRRQGFpaLFALEPLLSPVLPLLMLAPTAPLLIPLFLALWYGGEALLCRAMGW----PAGRRDLAAWVLRDLMLPVLWA 338
Cdd:COG1215   211 RGGLQLL--LKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLalllALRRRRLLLPLLHLLYGLLLLL 288
                         330
                  ....*....|....
gi 1062692902 339 ATFARQGFEWRGTA 352
Cdd:COG1215   289 AALRGKKVVWKKTP 302
 
Name Accession Description Interval E-value
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
36-265 2.52e-64

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 202.83  E-value: 2.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  36 PFVCLLRPVCGQDRFDRETLGSSFGLDWPDYEIVFCAAREEDAAVPLVRELIRLHPGARARLMIGEERITANPKLNNLAK 115
Cdd:cd02520     1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 116 GWAGTRARMIAIADANLLLPRDYLEQLAS-EWRPGVALVSSPpaggraeglwgaleagflnglqgrwqlaaarlglgFAQ 194
Cdd:cd02520    81 GYEEARYDILVISDSDISVPPDYLRRMVApLMDPGVGLVTCL-----------------------------------CAF 125
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1062692902 195 GKTMYLDRALLDRQGGLAALGAELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWSRIR 265
Cdd:cd02520   126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSRTR 196
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
91-263 5.98e-56

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 180.56  E-value: 5.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  91 PGARARLmIGEERITANPKLNNLAKGWAGTRARMIAIADANLLLPRDYLEQLASEWR-PGVALVSSPPAGGRAEGLWGAL 169
Cdd:pfam13506   1 PSVRALV-VGGPPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLAdPKVGLVTSPPVGSDPKGLAAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 170 EAGFLNGLQGRWQlaAARLGLGFAQGKTMYLDRALLDRQGGLAALGAELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRR 249
Cdd:pfam13506  80 EAAFFNTLAGVLQ--AALSGIGFAVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPR 157
                         170
                  ....*....|....*.
gi 1062692902 250 R--LRDVWARQLRWSR 263
Cdd:pfam13506 158 RtsFRAFMARQLRWAR 173
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
26-352 1.78e-23

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 98.66  E-value: 1.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  26 RRRPTPPATRPFVCLLRPVCGQDRFDRETLGSSFGLDWP--DYEIVFCAAREEDAAVPLVRELIRLHPgaRARLMIGEER 103
Cdd:COG1215    19 ARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPEN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 104 ITanpKLNNLAKGWAGTRARMIAIADANLLLPRDYLEQLASEWR-PGVAlvssppaggraeglwgaleagflnglqgrwq 182
Cdd:COG1215    97 GG---KAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAdPGVG------------------------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 183 laaarlglgfAQGKTMYLDRALLDRQGGLAALgaELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWS 262
Cdd:COG1215   143 ----------ASGANLAFRREALEEVGGFDED--TLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWA 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 263 RIRRQGFpaLFALEPLLSPVLPLLMLAPTAPLLIPLFLALWYGGEALLCRAMGW----PAGRRDLAAWVLRDLMLPVLWA 338
Cdd:COG1215   211 RGGLQLL--LKHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLalllALRRRRLLLPLLHLLYGLLLLL 288
                         330
                  ....*....|....
gi 1062692902 339 ATFARQGFEWRGTA 352
Cdd:COG1215   289 AALRGKKVVWKKTP 302
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
36-263 2.65e-10

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 59.69  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902  36 PFVCLLRPVCGQDRFDRETLGSSFGLDWPDYEIVFCAAREEDAAVPLVRELIRLHPGARARLMIGEERITANPKLNNLAK 115
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGKSRGLNH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 116 GWAGTRARMIAIADANLLLPRDYLEQLASEWR-PGVALVSSPPAGGRAEGLWGALEAGFLNGLQGRWQLAAARLGLGFAQ 194
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDsPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRLALGVLPLS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1062692902 195 GKTMYLDRALLDRQGGLAALGAeLAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWSR 263
Cdd:pfam13641 162 GAGSAIRREVLKELGLFDPFFL-LGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVY 229
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
125-304 4.15e-04

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 40.78  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 125 IAIADANLLLPRDYLEQLASEW-RPGVALVSSPPAGGRAEGLWGALEAGFLNGLQGRWQLAAARLG--LGFAqGKTMYLD 201
Cdd:pfam13632   2 ILLLDADTVLPPDCLLGIANEMaSPEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGrvLPFV-GSGAFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 202 RALLDRQGGLAalGAELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWSR---IRRQGFPALFALEPL 278
Cdd:pfam13632  81 RSALQEVGGWD--DGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYgclLILLIRLLGYLGTLL 158
                         170       180
                  ....*....|....*....|....*.
gi 1062692902 279 LSPVLPLLMLAPTAPLLIPLFLALWY 304
Cdd:pfam13632 159 WSGLPLALLLLLLFSISSLALVLLLL 184
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
112-263 5.81e-04

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 41.02  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 112 NLAKGWAGTRARMIAIADANLLLPRDYLEQLASEWR--PGVALVSSP------PAGGRAEGLWGALEAGFLnglqGRWQL 183
Cdd:cd06421    75 NLNNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLddPKVALVQTPqffynpDPFDWLADGAPNEQELFY----GVIQP 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1062692902 184 AAARLGLGFAQGKTMYLDRALLDRQGGLAalGAELAEDVAATRLVRAAGGTVRLVPRPFTQPIGRRRLRDVWARQLRWSR 263
Cdd:cd06421   151 GRDRWGAAFCCGSGAVVRREALDEIGGFP--TDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWAR 228
 
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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