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Conserved domains on  [gi|568926416|ref|XP_006537848|]
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ceramide glucosyltransferase isoform X1 [Mus musculus]

Protein Classification

ceramide glucosyltransferase( domain architecture ID 10118552)

ceramide glucosyltransferase catalyzes the first glycosylation step of glycosphingolipid synthesis; its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSLs), 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

CAZY:  GT2
EC:  2.4.1.80
Gene Ontology:  GO:0008120|GO:0006687
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
51-284 3.04e-90

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: 269.08  E-value: 3.04e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  51 PGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMP 130
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 131 AYEVAKYDLIWICDSGIRVIPDTLTDMVNQ-MTEKVGLVHGLpyvadrqgfaatleqvyfgtshprsyisanvtgfkCVT 209
Cdd:cd02520   81 GYEEARYDILVISDSDISVPPDYLRRMVAPlMDPGVGLVTCL-----------------------------------CAF 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926416 210 GMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRwtKLRINMLPATIIcEPISECFVASLIigwaaHHVFRW 284
Cdd:cd02520  126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRL--GYRVVLSPYVVM-QPLGSTSLASFW-----RRQLRW 192
 
Name Accession Description Interval E-value
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
51-284 3.04e-90

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: 269.08  E-value: 3.04e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  51 PGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMP 130
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 131 AYEVAKYDLIWICDSGIRVIPDTLTDMVNQ-MTEKVGLVHGLpyvadrqgfaatleqvyfgtshprsyisanvtgfkCVT 209
Cdd:cd02520   81 GYEEARYDILVISDSDISVPPDYLRRMVAPlMDPGVGLVTCL-----------------------------------CAF 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926416 210 GMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRwtKLRINMLPATIIcEPISECFVASLIigwaaHHVFRW 284
Cdd:cd02520  126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRL--GYRVVLSPYVVM-QPLGSTSLASFW-----RRQLRW 192
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
106-284 2.22e-60

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: 192.11  E-value: 2.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  106 PNVDArLFIGGKKVGINPKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTE-KVGLVHGLPYVADRQGFAATL 184
Cdd:pfam13506   1 PSVRA-LVVGGPPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADpKVGLVTSPPVGSDPKGLAAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  185 EQVYFGTsHPRsYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRWTKLRINMLPATIICEPI 264
Cdd:pfam13506  80 EAAFFNT-LAG-VLQAALSGIGFAVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPR 157
                         170       180
                  ....*....|....*....|
gi 568926416  265 SECFVAsliigwAAHHVFRW 284
Cdd:pfam13506 158 RTSFRA------FMARQLRW 171
HpnI TIGR03472
hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes ...
51-358 1.34e-41

hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0974) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4902) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnI) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. Hopanoids are known to feature polar glycosyl head groups in many organisms.


Pssm-ID: 132512 [Multi-domain]  Cd Length: 373  Bit Score: 149.45  E-value: 1.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416   51 PGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMP 130
Cdd:TIGR03472  41 PPVSVLKPLHGDEPELYENLASFCRQDYPGFQMLFGVQDPDDPALAVVRRLRADFPDADIDLVIDARRHGPNRKVSNLIN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  131 AYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEK-VGLV----HGLPyVAdrqGFAATLEQVyfGTSH---PRSYISANV 202
Cdd:TIGR03472 121 MLPHARHDILVIADSDISVGPDYLRQVVAPLADPdVGLVtclyRGRP-VP---GFWSRLGAM--GINHnflPSVMVARAL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  203 TGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIadRWTKLRInMLPATIICEPISECFVASLiigWAahHVF 282
Cdd:TIGR03472 195 GRARFCFGATMALRRATLEAIGGLAALAHHLADDYWLGELV--RALGLRV-VLAPVVVDTDVHETSFATL---LA--HEL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  283 RW----------DIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVA-------------WFI----RESMTIYIF 335
Cdd:TIGR03472 267 RWsrtiravnpvGYAGSFITQPVPLAVLALLLGAAWAWPLVAAALAARALLrlvmsratgaplrAAWllplRDLLSFAIW 346
                         330       340
                  ....*....|....*....|...
gi 568926416  336 LSALWDPTISWRTGRYRLRCGGT 358
Cdd:TIGR03472 347 VASFFGSRVVWRGRRFRVDRDGR 369
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-246 5.86e-20

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


Pssm-ID: 224136 [Multi-domain]  Cd Length: 439  Bit Score: 90.38  E-value: 5.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416   1 MALLDLAQEGMALFGFVLFVVLWLMHFMSIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLI-NNLETFFELDYP 79
Cdd:COG1215    4 DLLLELVFWGLILILLLILSIITLLLGYLLLVLPLSRPRKKLPKDADKLLPKVSVIIPAYNEEPEVLeETLESLLSQDYP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  80 KYEVLLCVQDHDDPAIDVCKKLLGKYPNvDARLFIGGKKVGInpKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVN 159
Cdd:COG1215   84 RYEVIVVDDGSTDETYEILEELGAEYGP-NFRVIYPEKKNGG--KAGALNNGLKRAKGDVVVILDADTVPEPDALRELVS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 160 QM-TEKVGLVHGLPYVADRQGFA--ATLEQVYFGTSHPRS-YISANVTGFKCVTGMSCLM-RKDVLDQAGGLiaFAQYIA 234
Cdd:COG1215  161 PFeDPPVGAVVGTPRIRNRPDPSnlLGRIQAIEYLSAFYFrLRAASKGGLISFLSGSSSAfRRSALEEVGGW--LEDTIT 238
                        250
                 ....*....|..
gi 568926416 235 EDYFMAKAIADR 246
Cdd:COG1215  239 EDADLTLRLHLR 250
 
Name Accession Description Interval E-value
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
51-284 3.04e-90

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: 269.08  E-value: 3.04e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  51 PGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMP 130
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNLIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 131 AYEVAKYDLIWICDSGIRVIPDTLTDMVNQ-MTEKVGLVHGLpyvadrqgfaatleqvyfgtshprsyisanvtgfkCVT 209
Cdd:cd02520   81 GYEEARYDILVISDSDISVPPDYLRRMVAPlMDPGVGLVTCL-----------------------------------CAF 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568926416 210 GMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRwtKLRINMLPATIIcEPISECFVASLIigwaaHHVFRW 284
Cdd:cd02520  126 GKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRL--GYRVVLSPYVVM-QPLGSTSLASFW-----RRQLRW 192
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
106-284 2.22e-60

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: 192.11  E-value: 2.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  106 PNVDArLFIGGKKVGINPKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTE-KVGLVHGLPYVADRQGFAATL 184
Cdd:pfam13506   1 PSVRA-LVVGGPPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADpKVGLVTSPPVGSDPKGLAAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  185 EQVYFGTsHPRsYISANVTGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIADRWTKLRINMLPATIICEPI 264
Cdd:pfam13506  80 EAAFFNT-LAG-VLQAALSGIGFAVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPR 157
                         170       180
                  ....*....|....*....|
gi 568926416  265 SECFVAsliigwAAHHVFRW 284
Cdd:pfam13506 158 RTSFRA------FMARQLRW 171
HpnI TIGR03472
hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes ...
51-358 1.34e-41

hopanoid biosynthesis associated glycosyl transferase protein HpnI; This family of genes include a glycosyl transferase, group 2 domain (pfam00535) which are responsible, generally for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The member of this clade from Acidithiobacillus ferrooxidans ATCC 23270 (AFE_0974) is found in the same locus as squalene-hopene cyclase (SHC, TIGR01507) and other genes associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha JMP134 (Reut_B4902) this gene is adjacent to HpnAB, IspH and HpnH (TIGR03470), although SHC itself is elsewhere in the genome. Notably, this gene (here named HpnI) and three others form a conserved set (HpnIJKL) which occur in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF). Continuing past SHC are found a phosphorylase enzyme (ZMO0873, i.e. HpnG, TIGR03468) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. Hopanoids are known to feature polar glycosyl head groups in many organisms.


Pssm-ID: 132512 [Multi-domain]  Cd Length: 373  Bit Score: 149.45  E-value: 1.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416   51 PGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMP 130
Cdd:TIGR03472  41 PPVSVLKPLHGDEPELYENLASFCRQDYPGFQMLFGVQDPDDPALAVVRRLRADFPDADIDLVIDARRHGPNRKVSNLIN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  131 AYEVAKYDLIWICDSGIRVIPDTLTDMVNQMTEK-VGLV----HGLPyVAdrqGFAATLEQVyfGTSH---PRSYISANV 202
Cdd:TIGR03472 121 MLPHARHDILVIADSDISVGPDYLRQVVAPLADPdVGLVtclyRGRP-VP---GFWSRLGAM--GINHnflPSVMVARAL 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  203 TGFKCVTGMSCLMRKDVLDQAGGLIAFAQYIAEDYFMAKAIadRWTKLRInMLPATIICEPISECFVASLiigWAahHVF 282
Cdd:TIGR03472 195 GRARFCFGATMALRRATLEAIGGLAALAHHLADDYWLGELV--RALGLRV-VLAPVVVDTDVHETSFATL---LA--HEL 266
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  283 RW----------DIMVFFMCHCLAWFIFDYIQLRGVQGGTLCFSKLDYAVA-------------WFI----RESMTIYIF 335
Cdd:TIGR03472 267 RWsrtiravnpvGYAGSFITQPVPLAVLALLLGAAWAWPLVAAALAARALLrlvmsratgaplrAAWllplRDLLSFAIW 346
                         330       340
                  ....*....|....*....|...
gi 568926416  336 LSALWDPTISWRTGRYRLRCGGT 358
Cdd:TIGR03472 347 VASFFGSRVVWRGRRFRVDRDGR 369
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-246 5.86e-20

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


Pssm-ID: 224136 [Multi-domain]  Cd Length: 439  Bit Score: 90.38  E-value: 5.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416   1 MALLDLAQEGMALFGFVLFVVLWLMHFMSIIYTRLHLNKKATDKQPYSKLPGVSLLKPLKGVDPNLI-NNLETFFELDYP 79
Cdd:COG1215    4 DLLLELVFWGLILILLLILSIITLLLGYLLLVLPLSRPRKKLPKDADKLLPKVSVIIPAYNEEPEVLeETLESLLSQDYP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  80 KYEVLLCVQDHDDPAIDVCKKLLGKYPNvDARLFIGGKKVGInpKINNLMPAYEVAKYDLIWICDSGIRVIPDTLTDMVN 159
Cdd:COG1215   84 RYEVIVVDDGSTDETYEILEELGAEYGP-NFRVIYPEKKNGG--KAGALNNGLKRAKGDVVVILDADTVPEPDALRELVS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 160 QM-TEKVGLVHGLPYVADRQGFA--ATLEQVYFGTSHPRS-YISANVTGFKCVTGMSCLM-RKDVLDQAGGLiaFAQYIA 234
Cdd:COG1215  161 PFeDPPVGAVVGTPRIRNRPDPSnlLGRIQAIEYLSAFYFrLRAASKGGLISFLSGSSSAfRRSALEEVGGW--LEDTIT 238
                        250
                 ....*....|..
gi 568926416 235 EDYFMAKAIADR 246
Cdd:COG1215  239 EDADLTLRLHLR 250
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
51-239 8.78e-15

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: 72.79  E-value: 8.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416   51 PGVSLLKPLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMP 130
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTGKSRGLNH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  131 AYEVAKYDLIWICDSGIRVIPDTLtDMVNQM--TEKVGLVHGLPYVADRQGFAATLEQVYFGTSHPRSYISANVTGFKCV 208
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTL-KKYVQYfdSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRLALGVLPL 160
                         170       180       190
                  ....*....|....*....|....*....|.
gi 568926416  209 TGMSCLMRKDVLDQAGGLIAFAqYIAEDYFM 239
Cdd:pfam13641 161 SGAGSAIRREVLKELGLFDPFF-LLGDDKSL 190
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
75-236 4.77e-08

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 52.23  E-value: 4.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  75 ELDYPKYEVLLcVQDH-DDPAIDVCKKLLGKYPNVdaRLFI-----GGKKVGINpkinnlmPAYEVAKYDLIWICDSGIR 148
Cdd:cd06423   21 ALDYPKLEVIV-VDDGsTDDTLEILEELAALYIRR--VLVVrdkenGGKAGALN-------AGLRHAKGDIVVVLDADTI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 149 VIPDTLTDMVNQM--TEKVGLVHGLPYVADR-QGFAATLEQVYFGTSHpRSYISA--NVTGFKCVTGMSCLMRKDVLDQA 223
Cdd:cd06423   91 LEPDALKRLVVPFfaDPKVGAVQGRVRVRNGsENLLTRLQAIEYLSIF-RLGRRAqsALGGVLVLSGAFGAFRREALREV 169
                        170
                 ....*....|....
gi 568926416 224 GGliaFAQY-IAED 236
Cdd:cd06423  170 GG---WDEDtLTED 180
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
58-252 1.07e-06

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.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 47.89  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  58 PLKGVDPNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVdaRLFIGGKKVGINPKINNLMPAyevAKY 137
Cdd:cd00761    4 PAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRV--IRVINEENQGLAAARNAGLKA---ARG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 138 DLIWICDSGIRVIPDTLTDMVNQMTE--KVGLVHGLPyvadrqgfaatleqvyfgtshprsyisanvtgfkcvtgmSCLM 215
Cdd:cd00761   79 EYILFLDADDLLLPDWLERLVAELLAdpEADAVGGPG---------------------------------------NLLF 119
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 568926416 216 RKDVLDQAGGLIAFAQYIAEDYFMAKAIADRWTKLRI 252
Cdd:cd00761  120 RRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
64-222 4.73e-05

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 43.15  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416   64 PNLINNLETFFELDYPKYEVLLCVQDHDDPAIDVCKKLLGKYPNVdaRLFIGGKKVGinpKINNLMPAYEVAKYDLIWIC 143
Cdd:pfam00535  11 KYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRV--RVIRLPENRG---KAGARNAGLRAATGDYIAFL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  144 DSGIRVIPDTLTDMVNQMTE-KVGLVHGLPYVADRQGFAATLEQVYFGTSHPRSYISANV-TGFKCVTGMSCLMRKDVLD 221
Cdd:pfam00535  86 DADDEVPPDWLEKLVEALEEdGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLgLNLPFLIGGFALYRREALE 165

                  .
gi 568926416  222 Q 222
Cdd:pfam00535 166 E 166
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
65-260 8.56e-05

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 43.43  E-value: 8.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  65 NLINNLETFFELDYP--KYEVLLCvqdhDDPAIDVCKKLL-GKYPNVDARLF-IGGKKVGINPKINNLMPAYEVAKYDLI 140
Cdd:cd04192   11 NLPRLLQSLSALDYPkeKFEVILV----DDHSTDGTVQILeFAAAKPNFQLKiLNNSRVSISGKKNALTTAIKAAKGDWI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 141 WICDSGIRVIPDTLTDMVN-QMTEKVGLVHGLPYVADRQGFAATLEQVYFgtshprSYISANVTGF----KCVTGMSCLM 215
Cdd:cd04192   87 VTTDADCVVPSNWLLTFVAfIQKEQIGLVAGPVIYFKGKSLLAKFQRLDW------LSLLGLIAGSfglgKPFMCNGANM 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 568926416 216 --RKDVLDQAGGliaFAQ---YIAEDY-FMAKAIADRWTKLRINMLPATII 260
Cdd:cd04192  161 ayRKEAFFEVGG---FEGndhIASGDDeLLLAKVASKYPKVAYLKNPEALV 208
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
66-225 1.68e-04

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 42.39  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  66 LINNLETFFELDYPKYEVLLCVQDHDDPAI-----DVCKKLLGKYPNVDARLFIGGKKVGINPKINNLMPAYEVakydlI 140
Cdd:cd06435   14 VKETLDSLAALDYPNFEVIVIDNNTKDEALwkpveAHCAQLGERFRFFHVEPLPGAKAGALNYALERTAPDAEI-----I 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 141 WICDSGIRVIPDTLTDMVNQMTE-KVGLV---------HGLPYVADRQGFAATleqvYFGTSHP-RSYISANVTgfkcvT 209
Cdd:cd06435   89 AVIDADYQVEPDWLKRLVPIFDDpRVGFVqapqdyrdgEESLFKRMCYAEYKG----FFDIGMVsRNERNAIIQ-----H 159
                        170
                 ....*....|....*.
gi 568926416 210 GMSCLMRKDVLDQAGG 225
Cdd:cd06435  160 GTMCLIRRSALDDVGG 175
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
76-237 7.28e-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: 40.63  E-value: 7.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416  76 LDYP--KYEVLLCvQDHDDPAI-DVCKKL-LGKYPNVDARLFIGGKKVGinpKINNlmpAYEVAKYDLIWICDSGIRVIP 151
Cdd:cd06421   27 IDYPhdKLRVYVL-DDGRRPELrALAAELgVEYGYRYLTRPDNRHAKAG---NLNN---ALAHTTGDFVAILDADHVPTP 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568926416 152 DTLTDMVNQM--TEKVGLVHGL-------PYVADRQGFAATLEQVYFGTSHPRSYISAnvtGFKCvtGMSCLMRKDVLDQ 222
Cdd:cd06421  100 DFLRRTLGYFldDPKVALVQTPqffynpdPFDWLADGAPNEQELFYGVIQPGRDRWGA---AFCC--GSGAVVRREALDE 174
                        170
                 ....*....|....*.
gi 568926416 223 AGGliaFAQY-IAEDY 237
Cdd:cd06421  175 IGG---FPTDsVTEDL 187
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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