NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|735022022|gb|KHO55814|]
View 

Glycosyl transferase, family 2 [archaeon GW2011_AR21]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11440371)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  9445404|12691742

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-219 5.52e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 109.70  E-value: 5.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   1 MKPQASILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVLELYKRFE-KKIKILNSGS-KGRVKLLNYGIGKS 78
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAfPRVRVIRNPEnLGFAAARNLGLRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  79 RADFVCVSAGDCILEKGFLRKILRLFgqdkngklafvspfsetggnCTVFRKKVLEEMQGFSNDFndgkTGFRDDTDLAF 158
Cdd:COG1216   81 GGDYLLFLDDDTVVEPDWLERLLAAA--------------------CLLIRREVFEEVGGFDERF----FLYGEDVDLCL 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 735022022 159 RIWDKGYKSVFTYEPKFQHEHKSPEGLGKKLAYawtrvkIHRFDALLFKKHSERAAMFFDV 219
Cdd:COG1216  137 RLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY------LGRNRLLFLRKHGPRPLLRLAL 191
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-219 5.52e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 109.70  E-value: 5.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   1 MKPQASILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVLELYKRFE-KKIKILNSGS-KGRVKLLNYGIGKS 78
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAfPRVRVIRNPEnLGFAAARNLGLRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  79 RADFVCVSAGDCILEKGFLRKILRLFgqdkngklafvspfsetggnCTVFRKKVLEEMQGFSNDFndgkTGFRDDTDLAF 158
Cdd:COG1216   81 GGDYLLFLDDDTVVEPDWLERLLAAA--------------------CLLIRREVFEEVGGFDERF----FLYGEDVDLCL 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 735022022 159 RIWDKGYKSVFTYEPKFQHEHKSPEGLGKKLAYawtrvkIHRFDALLFKKHSERAAMFFDV 219
Cdd:COG1216  137 RLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY------LGRNRLLFLRKHGPRPLLRLAL 191
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-169 5.54e-22

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: 89.87  E-value: 5.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   7 ILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRS----RAEVLELYKRFEKKIKILNSGSKGRVKLLNYGIGKSRADF 82
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGStdgtLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  83 VCVSAGDCILEKGFLRKILRLFgqDKNGKLAFVspfseTGGNCTVFRKKVLEEMQGFsndfnDGKTGFRDDTDLAFRIWD 162
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAEL--LADPEADAV-----GGPGNLLFRRELLEEIGGF-----DEALLSGEEDDDFLLRLL 148


                 ....*..
gi 735022022 163 KGYKSVF 169
Cdd:cd00761  149 RGGKVAF 155
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-107 5.89e-16

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: 73.97  E-value: 5.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022    6 SILIATRNQPETIQQAIESALKQEGYRTEVLVLDD----RSRAEVLELYKRFEKKIKILNSGSKGRVKLLNYGIGKSRAD 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDgstdGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|....*.
gi 735022022   82 FVCVSAGDCILEKGFLRKILRLFGQD 107
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEED 106
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-219 5.52e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 109.70  E-value: 5.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   1 MKPQASILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVLELYKRFE-KKIKILNSGS-KGRVKLLNYGIGKS 78
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAfPRVRVIRNPEnLGFAAARNLGLRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  79 RADFVCVSAGDCILEKGFLRKILRLFgqdkngklafvspfsetggnCTVFRKKVLEEMQGFSNDFndgkTGFRDDTDLAF 158
Cdd:COG1216   81 GGDYLLFLDDDTVVEPDWLERLLAAA--------------------CLLIRREVFEEVGGFDERF----FLYGEDVDLCL 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 735022022 159 RIWDKGYKSVFTYEPKFQHEHKSPEGLGKKLAYawtrvkIHRFDALLFKKHSERAAMFFDV 219
Cdd:COG1216  137 RLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY------LGRNRLLFLRKHGPRPLLRLAL 191
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-217 1.98e-28

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: 110.60  E-value: 1.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   3 PQASILIATRNQPETIQQAIESALKQE--GYRTEVLVLDDRSR---AEVLELYKRFEKKIKIL-NSGSKGRVKLLNYGIG 76
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTdetAEIARELAAEYPRVRVIeRPENGGKAAALNAGLK 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  77 KSRADFVCVSAGDCILEKGFLRKILRLFgqdKNGKLAFVspfsetgGNCTVFRKKVLEEMQGFSNDFndgktgFRDDTDL 156
Cdd:COG1215  109 AARGDIVVFLDADTVLDPDWLRRLVAAF---ADPGVGAS-------GANLAFRREALEEVGGFDEDT------LGEDLDL 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 735022022 157 AFRIWDKGYKSVFTYEPKFQHEhkSPEGLGK----KLAYAWTRVKIHRFDALLFKKHSERAAMFF 217
Cdd:COG1215  173 SLRLLRAGYRIVYVPDAVVYEE--APETLRAlfrqRRRWARGGLQLLLKHRPLLRPRRLLLFLLL 235
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-169 5.54e-22

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: 89.87  E-value: 5.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   7 ILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRS----RAEVLELYKRFEKKIKILNSGSKGRVKLLNYGIGKSRADF 82
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGStdgtLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  83 VCVSAGDCILEKGFLRKILRLFgqDKNGKLAFVspfseTGGNCTVFRKKVLEEMQGFsndfnDGKTGFRDDTDLAFRIWD 162
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAEL--LADPEADAV-----GGPGNLLFRRELLEEIGGF-----DEALLSGEEDDDFLLRLL 148


                 ....*..
gi 735022022 163 KGYKSVF 169
Cdd:cd00761  149 RGGKVAF 155
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-192 1.73e-20

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 87.06  E-value: 1.73e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   2 KPQASILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSR---AEVLELYKRFEKKIKIL-NSGSKGRVKLLNYGIGK 77
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTdgtAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  78 SRADFVCVSAGDCILEKGFLRKILRLFGQD-----------KNGKLAF-------------VSPFSETGGNCTVFRKKVL 133
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGpadlvygsrliREGESDLrrlgsrlfnlvrlLTNLPDSTSGFRLFRREVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 735022022 134 EEMqGFSNdfndgktGFRDDTDLaFRIWDKGYKsvFTYEPKFQHEHKSPEGLGKKLAYA 192
Cdd:COG0463  161 EEL-GFDE-------GFLEDTEL-LRALRHGFR--IAEVPVRYRAGESKLNLRDLLRLL 208
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-179 2.90e-19

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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 82.61  E-value: 2.90e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   7 ILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVLELYKRFEKKIKILNSG-----SKGRvkllNYGIGKSRAD 81
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGenlgfGAGN----NQGIREAKGD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  82 FVCVSAGDCILEKGFLRKILRLFGQDKNgkLAFVSPfsETGGNCTVFRKKVLEEMQGFSNDFndgkTGFRDDTDLAFRIW 161
Cdd:cd04186   77 YVLLLNPDTVVEPGALLELLDAAEQDPD--VGIVGP--KVSGAFLLVRREVFEEVGGFDEDF----FLYYEDVDLCLRAR 148

                        170
                 ....*....|....*...
gi 735022022 162 DKGYKSVFTYEPKFQHEH 179
Cdd:cd04186  149 LAGYRVLYVPQAVIYHHG 166
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-142 3.12e-16

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: 74.96  E-value: 3.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   7 ILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSR---AEVLELYKRFEKKIKIL--NSGSKGRVKLLNYGIGKSRAD 81
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTddtLEILEELAALYIRRVLVvrDKENGGKAGALNAGLRHAKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  82 FVCVSAGDCILEKGFLRKILRLFGQDKN-----GKLAFVSP-----------------------------FSETGGNCTV 127
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADPKvgavqGRVRVRNGsenlltrlqaieylsifrlgrraqsalggVLVLSGAFGA 160

                        170
                 ....*....|....*
gi 735022022 128 FRKKVLEEMQGFSND 142
Cdd:cd06423  161 FRREALREVGGWDED 175
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-107 5.89e-16

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: 73.97  E-value: 5.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022    6 SILIATRNQPETIQQAIESALKQEGYRTEVLVLDD----RSRAEVLELYKRFEKKIKILNSGSKGRVKLLNYGIGKSRAD 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDgstdGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|....*.
gi 735022022   82 FVCVSAGDCILEKGFLRKILRLFGQD 107
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEED 106
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-195 7.31e-11

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: 60.85  E-value: 7.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022    6 SILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVL----ELYKRFEK-KIKIL----NSGSKGRVKLLNYGIG 76
Cdd:pfam13641   5 SVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLdvaeEIAARFPDvRLRVIrnarLLGPTGKSRGLNHGFR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   77 KSRADFVCVSAGDCILEKGFLRKILRLFGQDK-----------NGKLAFVSP----FSET----------------GGNC 125
Cdd:pfam13641  85 AVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKvgavgtpvfslNRSTMLSALgaleFALRhlrmmslrlalgvlplSGAG 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  126 TVFRKKVLEEMQGFsndfnDGKTGFRDDTDLAFRIWDKGYKSVFTYEPKFQHEHKSPEGLGKKLAYAWTR 195
Cdd:pfam13641 165 SAIRREVLKELGLF-----DPFFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVY 229
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 3-173 7.48e-10

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: 57.97  E-value: 7.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   3 PQASILIATRNQP-ETIQQAIESALKQE--GYRTEVLVLDDRSRAEVLELYKRFEKKIKIlNSGSKGRVKL-----LNYG 74
Cdd:cd06421    1 PTVDVFIPTYNEPlEIVRKTLRAALAIDypHDKLRVYVLDDGRRPELRALAAELGVEYGY-RYLTRPDNRHakagnLNNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  75 IGKSRADFVCVSAGDCILEKGFLRKILRLFgqDKNGKLAFVS---------PFSETG----------------------- 122
Cdd:cd06421   80 LAHTTGDFVAILDADHVPTPDFLRRTLGYF--LDDPKVALVQtpqffynpdPFDWLAdgapneqelfygviqpgrdrwga 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 735022022 123 ----GNCTVFRKKVLEEMQGFSNDFndgktgFRDDTDLAFRIWDKGYKSVFTYEP 173
Cdd:cd06421  158 afccGSGAVVRREALDEIGGFPTDS------VTEDLATSLRLHAKGWRSVYVPEP 206
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 7-167 1.51e-09

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 56.05  E-value: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   7 ILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVLELYKRFEKK----IKILNSGSKG--RVKLLNYGIGKSRA 80
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQfpipIKHVWQEDEGfrKAKIRNKAIAAAKG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  81 DFVCVSAGDCILEKGFLRKILRLfgQDKNgklAFVS--------PFSETGGN-CTV-FRKKVLEEMQGFSNDFndgkTGF 150
Cdd:cd06420   81 DYLIFIDGDCIPHPDFIADHIEL--AEPG---VFLSgsrvllneKLTERGIRgCNMsFWKKDLLAVNGFDEEF----TGW 151

                        170
                 ....*....|....*...
gi 735022022 151 -RDDTDLAFRIWDKGYKS 167
Cdd:cd06420  152 gGEDSELVARLLNSGIKF 169
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 6-169 7.80e-09

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 54.47  E-value: 7.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   6 SILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVLELYKRFEKKIKILNSGS-KGRVKLLNYGIGKSRADFVC 84
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPdKGIYDAMNKGIALATGDIIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  85 V-SAGDcILEKGFLRKILRLFGQ--------------DKNGKLAFV------SPFSETGGNC-----TVFRKKVLEEMQG 138
Cdd:cd06433   81 FlNSDD-TLLPGALLAVVAAFAEhpevdvvygdvllvDENGRVIGRrrpppfLDKFLLYGMPichqaTFFRRSLFEKYGG 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 735022022 139 FSNDFndgKTGFrdDTDLAFRIWDKGYKSVF 169
Cdd:cd06433  160 FDESY---RIAA--DYDLLLRLLLAGKIFKY 185
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 6-166 1.70e-08

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 54.16  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   6 SILIATRNQPETIQQAIESALKQ--EGYRTEVLVLD----DRSRAEVLELYKRFEkKIKILNSGSKGRVKLLNYGIGKSR 79
Cdd:cd02525    3 SIIIPVRNEEKYIEELLESLLNQsyPKDLIEIIVVDggstDGTREIVQEYAAKDP-RIRLIDNPKRIQSAGLNIGIRNSR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  80 ADFVCVSAGDCILEKGFLRKIL---------------RLFGQDKNGK---LAFVSPFSeTGG---------NCTV----- 127
Cdd:cd02525   82 GDIIIRVDAHAVYPKDYILELVealkrtgadnvggpmETIGESKFQKaiaVAQSSPLG-SGGsayrggavkIGYVdtvhh 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 735022022 128 --FRKKVLEEMQGFSNDFNDGKtgfrdDTDLAFRIWDKGYK 166
Cdd:cd02525  161 gaYRREVFEKVGGFDESLVRNE-----DAELNYRLRKAGYK 196
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 6-109 3.14e-06

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 47.18  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   6 SILIATRNQPETIQQAIESALKQEGYRTEVLVLD----DRSRAEVLELYKRfekkikiLNSGSKGRVKLLNYGIGKSRAD 81
Cdd:cd02522    2 SIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDggstDGTVAIARSAGVV-------VISSPKGRARQMNAGAAAARGD 74

                         90       100
                 ....*....|....*....|....*...
gi 735022022  82 FVCVSAGDCILEKGFLRKILRLFGQDKN 109
Cdd:cd02522   75 WLLFLHADTRLPPDWDAAIIETLRADGA 102
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 3-174 3.75e-05

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 44.22  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   3 PQASILIATRNQPETIQQAIESA--LKQEGYRTEVLVLDD-------RSRAEVLElYKRFEKKIKILNSGSKGRVKL--L 71
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAAcaLDYPKDRLEIQVLDDstdetvrLAREIVEE-YAAQGVNIKHVRRADRTGYKAgaL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  72 NYGIGKSRADFVCVSAGDCILEKGFLRKILRLFgqdKNGKLAFVSP---------------------------------- 117
Cdd:cd06437   80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYF---ADPKLGFVQTrwghinanyslltrvqamsldyhftieqvarsst 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 735022022 118 -----FSETGGnctVFRKKVLEEMQGFSNDfndgktGFRDDTDLAFRIWDKGYKSVFTYEPK 174
Cdd:cd06437  157 glffnFNGTAG---VWRKECIEDAGGWNHD------TLTEDLDLSYRAQLKGWKFVYLDDVV 209
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-122 5.25e-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: 5.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   7 ILIATRNQPETIQQAIESALKQEgYRT---EVLVLDDRSR---AEVLELYKRF-EKKIKILNS---GSKGRVKLLNYGIG 76
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALD-YPKekfEVILVDDHSTdgtVQILEFAAAKpNFQLKILNNsrvSISGKKNALTTAIK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 735022022  77 KSRADFVCVSAGDCILEKGFLRKILRLFGQDKNGKLA-FVSPFSETG 122
Cdd:cd04192   80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAgPVIYFKGKS 126
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-134 5.75e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 43.39  E-value: 5.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   6 SILIATRNQPETIQQAIESALKQEGYRTEVLVLDDRSRAEVLELYKRFEKK-----IKILNSGSKGRVKLLNYGIGKSRA 80
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKdpfiiILIRNGKNLGVARNFESLLQAADG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  81 DFVCVSAGDCILEKGFLRKILRLFGQ--------------DKNGKLAFVSPFSETG-----------------GNCTVFR 129
Cdd:cd04196   81 DYVFFCDQDDIWLPDKLERLLKAFLKddkpllvysdlelvDENGNPIGESFFEYQKikpgtsfnnllfqnvvtGCTMAFN 160


                 ....*
gi 735022022 130 KKVLE 134
Cdd:cd04196  161 RELLE 165
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-146 6.09e-05

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 42.95  E-value: 6.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022   7 ILIATRNQPETIQQAIESALK--QEGYRTEVLVLDDRSR---AEVL-ELYKRFEKKIKILNSGSKGRVKLLNYGIGKSRA 80
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTdgtAEIArELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  81 DFVCVSAGD-----CILEKgFLRKIL----------RLFGQDKNG----------------KLAFVSPFSETGGNCTVFR 129
Cdd:cd04179   81 DIVVTMDADlqhppEDIPK-LLEKLLeggadvvigsRFVRGGGAGmpllrrlgsrlfnfliRLLLGVRISDTQSGFRLFR 159

                        170
                 ....*....|....*....
gi 735022022 130 KKVLEEM--QGFSNDFNDG 146
Cdd:cd04179  160 REVLEALlsLLESNGFEFG 178
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 112-207 9.25e-05

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: 42.32  E-value: 9.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 735022022  112 LAFVSPFSetgGNCTVFRKKVLEEMQGFsNDFNDGktgfrDDTDLAFRIWDKGYKSVFTYEPKFqHEhKSPEGLG--KKL 189
Cdd:pfam13632  66 LGRVLPFV---GSGAFLRRSALQEVGGW-DDGSVS-----EDFDFGLRLQRAGYRVRFAPYSAV-YE-KSPLTFRdfLRQ 134

                          90
                  ....*....|....*...
gi 735022022  190 AYAWTRVKIHRFDALLFK 207
Cdd:pfam13632 135 RRRWAYGCLLILLIRLLG 152
 
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