NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15595902|ref|NP_249396|]
View 

alpha-1,6-rhamnosyltransferase MigA [Pseudomonas aeruginosa PAO1]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

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:  16037492|18518825

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 16-231 2.90e-46

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 154.86  E-value: 2.90e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  16 APLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHG-FQLYR-QQNQGVSAALNFGLRH 93
Cdd:COG0463   1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPrIRVIRlERNRGKGAARNAGLAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  94 ARGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIyidSEGQETKRQNGNRIrqLDFDYLLGNAYVCGAPVSLY 173
Cdd:COG0463  81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRL--FNLVRLLTNLPDSTSGFRLF 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595902 174 RMEALRAAGFydPEIKVQDFQMtLRIASQGYQIHKLPVlvtRYRRHPDNLSRRYKVLL 231
Cdd:COG0463 156 RREVLEELGF--DEGFLEDTEL-LRALRHGFRIAEVPV---RYRAGESKLNLRDLLRL 207
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 16-231 2.90e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 154.86  E-value: 2.90e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  16 APLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHG-FQLYR-QQNQGVSAALNFGLRH 93
Cdd:COG0463   1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPrIRVIRlERNRGKGAARNAGLAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  94 ARGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIyidSEGQETKRQNGNRIrqLDFDYLLGNAYVCGAPVSLY 173
Cdd:COG0463  81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRL--FNLVRLLTNLPDSTSGFRLF 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595902 174 RMEALRAAGFydPEIKVQDFQMtLRIASQGYQIHKLPVlvtRYRRHPDNLSRRYKVLL 231
Cdd:COG0463 156 RREVLEELGF--DEGFLEDTEL-LRALRHGFRIAEVPV---RYRAGESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 20-179 8.13e-40

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: 136.76  E-value: 8.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    20 SVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKV-HGFQLYRQ-QNQGVSAALNFGLRHARGD 97
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKdPRVRVIRLpENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    98 YVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQETKRQNG---NRIRQLDFDYLLGNAYVCGAPVSLYR 174
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRItlsRLPFFLGLRLLGLNLPFLIGGFALYR 160


                  ....*
gi 15595902   175 MEALR 179
Cdd:pfam00535 161 REALE 165
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 21-207 6.05e-38

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: 131.86  E-value: 6.05e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQK--VHGFQLYRQQNQGVSAALNFGLRHARGDY 98
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKkdPRVIRVINEENQGLAAARNAGLKAARGEY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  99 VATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGalviyidsegqetkrqngnrirqldfdyllgnayvcGAPVSLYRMEAL 178
Cdd:cd00761  81 ILFLDADDLLLPDWLERLVAELLADPEADAVG------------------------------------GPGNLLFRRELL 124

                       170       180       190
                ....*....|....*....|....*....|.
gi 15595902 179 RAAGFYDPEIKV--QDFQMTLRIASQGYQIH 207
Cdd:cd00761 125 EEIGGFDEALLSgeEDDDFLLRLLRGGKVAF 155
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 15-110 5.41e-28

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 110.14  E-value: 5.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   15 DAPLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHG-FQLYRQQNQGVSAALNFGLRH 93
Cdd:PRK10073   4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARNTGLAV 83

                         90
                 ....*....|....*..
gi 15595902   94 ARGDYVATPDLDDIMLP 110
Cdd:PRK10073  84 ATGKYVAFPDADDVVYP 100
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
20-127 3.58e-08

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 53.64  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   20 SVVAPCFNAEKYLEEALRSIYEQDYP---NFEVIIVDDGSTDNSYAMLEQLQK--VHGFQL--YRQQNQGVSAALNFGLR 92
Cdd:NF038302   4 TVAIPTYNGANRLPEVLERLRSQIGTeslSWEIIVVDNNSTDNTAQVVQEYQKnwPSPYPLryCFEPQQGAAFARQRAIQ 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15595902   93 HARGDYVATpdLDDIMLPHSLSVRAAYL--DQHPEVG 127
Cdd:NF038302  84 EAKGELIGF--LDDDNLPAPNWVAAAYAfgQEHPQAG 118
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 19-97 2.09e-07

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 50.59  E-value: 2.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595902    19 VSVVAPCFNAEKYLEEALRSIYEQDYPnFEVIIVDDGSTDNSYAMLEQLqkvhGFQLYRQQnQGVSAALNFGLRHARGD 97
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGD-AEVIVVDGGSTDGTVEIARSL----GAKVIHSP-KGRARQMNAGAALAKGD 73
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 16-231 2.90e-46

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 154.86  E-value: 2.90e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  16 APLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHG-FQLYR-QQNQGVSAALNFGLRH 93
Cdd:COG0463   1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPrIRVIRlERNRGKGAARNAGLAA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  94 ARGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIyidSEGQETKRQNGNRIrqLDFDYLLGNAYVCGAPVSLY 173
Cdd:COG0463  81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRL--FNLVRLLTNLPDSTSGFRLF 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595902 174 RMEALRAAGFydPEIKVQDFQMtLRIASQGYQIHKLPVlvtRYRRHPDNLSRRYKVLL 231
Cdd:COG0463 156 RREVLEELGF--DEGFLEDTEL-LRALRHGFRIAEVPV---RYRAGESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 20-179 8.13e-40

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: 136.76  E-value: 8.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    20 SVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKV-HGFQLYRQ-QNQGVSAALNFGLRHARGD 97
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKdPRVRVIRLpENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    98 YVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQETKRQNG---NRIRQLDFDYLLGNAYVCGAPVSLYR 174
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRItlsRLPFFLGLRLLGLNLPFLIGGFALYR 160


                  ....*
gi 15595902   175 MEALR 179
Cdd:pfam00535 161 REALE 165
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 5-228 6.38e-39

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: 138.72  E-value: 6.38e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   5 ATSSKHSGTTDAPLVSVVAPCFNAEKYLEEALRSIYEQDYP--NFEVIIVDDGSTDNSYAMLEQLQKVHGF--QLYRQQN 80
Cdd:COG1215  17 ALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELAAEYPRvrVIERPEN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  81 QGVSAALNFGLRHARGDYVATPDLDDIMLPHSLSVRAAYLdQHPEVGCVGALViyidsegqetkrqngnrirqldfdyll 160
Cdd:COG1215  97 GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGASGANL--------------------------- 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595902 161 gnayvcgapvsLYRMEALRAAGFYDPEIKVQDFQMTLRIASQGYQIHKLPVLVTRYRRhPDNLSRRYK 228
Cdd:COG1215 149 -----------AFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEA-PETLRALFR 204
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 21-207 6.05e-38

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: 131.86  E-value: 6.05e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQK--VHGFQLYRQQNQGVSAALNFGLRHARGDY 98
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKkdPRVIRVINEENQGLAAARNAGLKAARGEY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  99 VATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGalviyidsegqetkrqngnrirqldfdyllgnayvcGAPVSLYRMEAL 178
Cdd:cd00761  81 ILFLDADDLLLPDWLERLVAELLADPEADAVG------------------------------------GPGNLLFRRELL 124

                       170       180       190
                ....*....|....*....|....*....|.
gi 15595902 179 RAAGFYDPEIKV--QDFQMTLRIASQGYQIH 207
Cdd:cd00761 125 EEIGGFDEALLSgeEDDDFLLRLLRGGKVAF 155
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 20-219 5.07e-37

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: 130.74  E-value: 5.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  20 SVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSyamLEQLQKVHGFQLY--RQQNQGVSAALNFGLRHARGD 97
Cdd:cd06433   1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGT---VDIIKKYEDKITYwiSEPDKGIYDAMNKGIALATGD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  98 YVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQETKRqngNRIRQLDFDYLLGNAYVCgAPVSLYRMEA 177
Cdd:cd06433  78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGR---RRPPPFLDKFLLYGMPIC-HQATFFRRSL 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15595902 178 LRAAGFYDPEIK-VQDFQMTLRIASQGYQIHKLPVLVTRYRRH 219
Cdd:cd06433 154 FEKYGGFDESYRiAADYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 21-187 7.83e-35

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: 124.26  E-value: 7.83e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQLYR---QQNQGVSAALNFGLRHARGD 97
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVvrdKENGGKAGALNAGLRHAKGD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  98 YVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYID------SEGQETKRQNGNRIRQLdFDYLLGNAYVCGAPVS 171
Cdd:cd06423  81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNgsenllTRLQAIEYLSIFRLGRR-AQSALGGVLVLSGAFG 159

                       170
                ....*....|....*.
gi 15595902 172 LYRMEALRAAGFYDPE 187
Cdd:cd06423 160 AFRREALREVGGWDED 175
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 17-212 4.05e-33

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 120.39  E-value: 4.05e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  17 PLVSVVAPCFNA-EKYLEEALRSIYEQDYPNFEVIIVDDGSTD-------NSYAMLEQLQKVHgfqlYRQQNQGVSAALN 88
Cdd:cd04184   1 PLISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDpevkrvlKKYAAQDPRIKVV----FREENGGISAATN 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  89 FGLRHARGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGcvgalVIYIDsegqETKRQNGNRIRQLDF------DYLLGN 162
Cdd:cd04184  77 SALELATGEFVALLDHDDELAPHALYEVVKALNEHPDAD-----LIYSD----EDKIDEGGKRSEPFFkpdwspDLLLSQ 147

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15595902 163 AYVCGapVSLYRMEALRAAGFYDPEI-KVQDFQMTLRIASQGYQIHKLP-VL 212
Cdd:cd04184 148 NYIGH--LLVYRRSLVRQVGGFREGFeGAQDYDLVLRVSEHTDRIAHIPrVL 197
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 17-206 1.18e-28

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. 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 of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 109.98  E-value: 1.18e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  17 PLVSVVAPCFNAEKYLEEALRSIYEQDYPN--FEVIIVDDGSTDNSYAMLEQLQKvHGFQLYRQ-QNQGVSAALNFGLRH 93
Cdd:cd06439  29 PTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYAD-KGVKLLRFpERRGKAAALNRALAL 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  94 ARGDYVATPDLDDIMLPHSLSVRAAYLdQHPEVGCV-GALVIY---IDSEGQETKRQNGNRIRQLdfDYLLGNayVCGAP 169
Cdd:cd06439 108 ATGEIVVFTDANALLDPDALRLLVRHF-ADPSVGAVsGELVIVdggGSGSGEGLYWKYENWLKRA--ESRLGS--TVGAN 182

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15595902 170 VSLYrmeALRAAGF--YDPEIKVQDFQMTLRIASQGYQI 206
Cdd:cd06439 183 GAIY---AIRRELFrpLPADTINDDFVLPLRIARQGYRV 218
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 20-224 1.47e-28

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: 108.87  E-value: 1.47e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  20 SVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQLYRQQNQG-VSAALNF--GLRHARG 96
Cdd:cd04196   1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKnLGVARNFesLLQAADG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  97 DYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQ---ETKRQNGNRIRQLDFDYLLGNAYVCGApVSLY 173
Cdd:cd04196  81 DYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNpigESFFEYQKIKPGTSFNNLLFQNVVTGC-TMAF 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15595902 174 RMEALRAA-GFYDPEIKVQDFQMTLrIASQGYQIHKLPVLVTRYRRHPDNLS 224
Cdd:cd04196 160 NRELLELAlPFPDADVIMHDWWLAL-LASAFGKVVFLDEPLILYRQHGNNVV 210
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 18-227 3.62e-28

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: 108.86  E-value: 3.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  18 LVSVVAPCFNAEKYLEEALRSIYEQDYP--NFEVIIVDDGSTDNSYAMLEQLQKVHG-FQLYRQQNQGVSAALNFGLRHA 94
Cdd:cd02525   1 FVSIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYAAKDPrIRLIDNPKRIQSAGLNIGIRNS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  95 RGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQ-------ETKRQNGN-RIRQLDFDyllgNAYVC 166
Cdd:cd02525  81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQkaiavaqSSPLGSGGsAYRGGAVK----IGYVD 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595902 167 GAPVSLYRMEALRAAGFYDPE-IKVQDFQMTLRIASQGYQIHKLPVLVTRY--RRHPDNLSRRY 227
Cdd:cd02525 157 TVHHGAYRREVFEKVGGFDESlVRNEDAELNYRLRKAGYKIWLSPDIRVYYypRSTLKKLARQY 220
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 15-110 5.41e-28

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 110.14  E-value: 5.41e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   15 DAPLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHG-FQLYRQQNQGVSAALNFGLRH 93
Cdd:PRK10073   4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARNTGLAV 83

                         90
                 ....*....|....*..
gi 15595902   94 ARGDYVATPDLDDIMLP 110
Cdd:PRK10073  84 ATGKYVAFPDADDVVYP 100
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 20-217 3.80e-27

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 104.70  E-value: 3.80e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  20 SVVAPCFNAEK--YLEEALRSIYEQDYPNFEVIIVDDGS-TDNSYAMLEQLQKVHGFQLYR-QQNQGVSAALNFGLRHAR 95
Cdd:cd04195   1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPlEKNRGLGKALNEGLKHCT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  96 GDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQETKRQ----NGNRIRQLD-----FDYllgnayvc 166
Cdd:cd04195  81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRrlptSHDDILKFArrrspFNH-------- 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15595902 167 gaPVSLYRMEALRAAGFYDPEIKVQDFQMTLRIASQGYQIHKLPVLVTRYR 217
Cdd:cd04195 153 --PTVMFRKSKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
15-227 6.31e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 98.91  E-value: 6.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  15 DAPLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQkVHGFQLYRQ-QNQGVSAALNFGLRH 93
Cdd:COG1216   1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALA-FPRVRVIRNpENLGFAAARNLGLRA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  94 ARGDYVATPDLDDIMLPHslsvraaYLDQHPEVGCVgalviyidsegqetkrqngnrirqldfdyllgnayvcgapvsLY 173
Cdd:COG1216  80 AGGDYLLFLDDDTVVEPD-------WLERLLAAACL------------------------------------------LI 110

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595902 174 RMEALRAAGFYDPEIKVQ--DFQMTLRIASQGYQIHKLP-VLVTRYRRH-PDNLSRRY 227
Cdd:COG1216 111 RREVFEEVGGFDERFFLYgeDVDLCLRLRKAGYRIVYVPdAVVYHLGGAsSGPLLRAY 168
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 21-210 1.83e-22

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: 91.47  E-value: 1.83e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKvhGFQLYRQQ-NQGVSAALNFGLRHARGDYV 99
Cdd:cd04186   1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFP--EVRLIRNGeNLGFGAGNNQGIREAKGDYV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902 100 ATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALviyidsegqetkrqngnrirqldfdyllgnayVCGAPVsLYRMEALR 179
Cdd:cd04186  79 LLLNPDTVVEPGALLELLDAAEQDPDVGIVGPK--------------------------------VSGAFL-LVRREVFE 125

                       170       180       190
                ....*....|....*....|....*....|...
gi 15595902 180 AAGFYDPEIKV--QDFQMTLRIASQGYQIHKLP 210
Cdd:cd04186 126 EVGGFDEDFFLyyEDVDLCLRARLAGYRVLYVP 158
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 21-105 5.40e-21

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic 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. 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 87.92  E-value: 5.40e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEE---ALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQK----VHGFQLYRqqNQGVSAALNFGLRH 93
Cdd:cd04187   1 IVVPVYNEEENLPElyeRLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAArdprVKVIRLSR--NFGQQAALLAGLDH 78

                        90
                ....*....|..
gi 15595902  94 ARGDYVATPDLD 105
Cdd:cd04187  79 ARGDAVITMDAD 90
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 21-101 1.69e-20

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: 86.47  E-value: 1.69e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSI--YEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQ--LYRQQNQGVSAALNFGLRHARG 96
Cdd:cd04179   1 VVIPAYNEEENIPELVERLlaVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVrvIRLSRNFGKGAAVRAGFKAARG 80


                ....*
gi 15595902  97 DYVAT 101
Cdd:cd04179  81 DIVVT 85
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 17-222 4.19e-18

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: 81.26  E-value: 4.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    17 PLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHG---FQLYRQQNQ----GVSAALNF 89
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvrLRVIRNARLlgptGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    90 GLRHARGDYVATPDLDDIMLPHSLSVRAAYLDqHPEVGCVGA--LVIYIDSEGQETKRQNGNR--IRQLDFDYLLGNAYV 165
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFD-SPKVGAVGTpvFSLNRSTMLSALGALEFALrhLRMMSLRLALGVLPL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595902   166 CGApVSLYRMEALRAAGFYDPE-IKVQDFQMTLRIASQGYQIHKLPVLVTRYRRHPDN 222
Cdd:pfam13641 161 SGA-GSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYL 217
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 21-163 2.61e-17

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: 78.87  E-value: 2.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYP--NFEVIIVDDGSTDNSYAMLE-QLQKVHgFQLYRQQNQGVSA-----ALNFGLR 92
Cdd:cd04192   1 VVIAARNEAENLPRLLQSLSALDYPkeKFEVILVDDHSTDGTVQILEfAAAKPN-FQLKILNNSRVSIsgkknALTTAIK 79

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595902  93 HARGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGAlVIYIDSEGQETKRQNgnrirqLDFDYLLGNA 163
Cdd:cd04192  80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGP-VIYFKGKSLLAKFQR------LDWLSLLGLI 143
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 17-205 3.46e-14

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: 70.29  E-value: 3.46e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  17 PLVSVVAPCFNAE-KYLEEALRSIYEQDYPN--FEVIIVDDGSTDNSYAMLEQLQKVHGFQ-LYRQQNQGVSA-ALNFGL 91
Cdd:cd06421   1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYPHdkLRVYVLDDGRRPELRALAAELGVEYGYRyLTRPDNRHAKAgNLNNAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  92 RHARGDYVATPDLDDIMLPHSLSVRAAYLDQHPEVGCVGALVIYIDSEGQETKRQNGNRIRQLDFDYLLGNAYVCGAPV- 170
Cdd:cd06421  81 AHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELFYGVIQPGRDRWGAAFc 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15595902 171 ----SLYRMEALRAAG-FYDPEIkVQDFQMTLRIASQGYQ 205
Cdd:cd06421 161 cgsgAVVRREALDEIGgFPTDSV-TEDLATSLRLHAKGWR 199
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
13-122 5.15e-14

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 70.79  E-value: 5.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   13 TTDAPLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTdnSYAMLEQ----LQKVHGFQLYRQQNQGVSAALN 88
Cdd:PRK10018   1 MKDNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQyvtaLNDPRITYIHNDINSGACAVRN 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 15595902   89 FGLRHARGDYVATPDLDDIMLPHSLSVRAAYLDQ 122
Cdd:PRK10018  79 QAIMLAQGEYITGIDDDDEWTPNRLSVFLAHKQQ 112
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 21-111 5.52e-13

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: 66.06  E-value: 5.52e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQLY--RQQNQG--VSAALNFGLRHARG 96
Cdd:cd06420   1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKhvWQEDEGfrKAKIRNKAIAAAKG 80

                        90
                ....*....|....*
gi 15595902  97 DYVATPDLDdiMLPH 111
Cdd:cd06420  81 DYLIFIDGD--CIPH 93
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 26-227 5.55e-13

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 66.50  E-value: 5.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  26 FNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQLYRQ-QNQGVSAALNFGLRHA--RG-DYVAT 101
Cdd:cd04185   6 YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLRLpENLGGAGGFYEGVRRAyeLGyDWIWL 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902 102 PDLDDIMLPHSLSVRAAYlDQHPEVGCVGALVIYIDsegqetkrqngnrirqldfdyllgnayvcGAPVS-LYRMEALRA 180
Cdd:cd04185  86 MDDDAIPDPDALEKLLAY-ADKDNPQFLAPLVLDPD-----------------------------GSFVGvLISRRVVEK 135

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595902 181 AGFYDPE--IKVQDFQMTLRIASQGYQI--------HKLPV-LVTRYRRHPDNLSRRY 227
Cdd:cd04185 136 IGLPDKEffIWGDDTEYTLRASKAGPGIyvpdavvvHKTAInKGSSAVVNIDPPWKLY 193
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 21-105 9.39e-13

DPG_synthase is involved in protein N-linked glycosylation; 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.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 66.05  E-value: 9.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYE--QDYPNF--EVIIVDDGSTDNSYAMLEQLQKVHG--FQLYRQ-QNQGVSAALNFGLRH 93
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVEylEERPSFsyEIIVVDDGSKDGTAEVARKLARKNPalIRVLTLpKNRGKGGAVRAGMLA 80

                        90
                ....*....|..
gi 15595902  94 ARGDYVATPDLD 105
Cdd:cd04188  81 ARGDYILFADAD 92
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 19-110 2.38e-12

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 65.00  E-value: 2.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  19 VSVVAPCFNAEKYLEEALRSIYEQ-DypnfEVIIVDDGSTDNSYAMLEQlqkvHGFQLYRQQNQGVSAALNFGLRHARGD 97
Cdd:cd02511   2 LSVVIITKNEERNIERCLESVKWAvD----EIIVVDSGSTDRTVEIAKE----YGAKVYQRWWDGFGAQRNFALELATND 73

                        90
                ....*....|...
gi 15595902  98 YVATPDLDDIMLP 110
Cdd:cd02511  74 WVLSLDADERLTP 86
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 21-128 2.58e-11

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 62.09  E-value: 2.58e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYPN-FEVIIVDDGSTDNSYAMLE----QLQKVHGFQLYRQQN----QGVSAALNFGL 91
Cdd:cd06913   1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEkwrkKLEDSGVIVLVGSHNspspKGVGYAKNQAI 80

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15595902  92 RHARGDYVATPDLDDIMLPHSLSVRAAYLDQHPE--VGC 128
Cdd:cd06913  81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNsiIGC 119
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 16-105 1.83e-10

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 60.10  E-value: 1.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   16 APLVSVVAPCFNAEKYLEEALRSIYE--QDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQLY----RQQNQGVSAALNF 89
Cdd:PLN02726   8 AMKYSIIVPTYNERLNIALIVYLIFKalQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRIllrpRPGKLGLGTAYIH 87

                         90
                 ....*....|....*.
gi 15595902   90 GLRHARGDYVATPDLD 105
Cdd:PLN02726  88 GLKHASGDFVVIMDAD 103
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 20-224 8.24e-10

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 58.44  E-value: 8.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    20 SVVAPCFNAEK--YLEEALRSIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQLYRQQNQ---GVSAALNFGLRHA 94
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDttySLAASRNRGTSHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    95 RGDYVATPDLDDIMLPHSLSVRAAY-----LDQHPEVGCVGALVIYIDsEGQETKRQNGNRIRQLDFDYLLGNAYVCG-- 167
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKIatslaLQENIQAAVVLPVTDLND-ESSNFLRRGGDLTASGDVLRDLLVFYSPLai 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595902   168 --APVS---LYRMEALRAAGFYDPEIK---VQDFQMTLRIASQGYQIHKLPVLVTrYRRHPDNLS 224
Cdd:pfam10111 160 ffAPNSsnaLINRQAFIEVGGFDESFRghgAEDFDIFLRLAARYPFVAVMPPQLL-YRLSAKSMS 223
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 17-213 1.21e-09

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: 56.84  E-value: 1.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  17 PLVSVVAPCFNAEKYLEEALRSIYEQDYPNFEVII-VDDGsTDNSYAMLEQLQK--------------VHGfqlyrqQNQ 81
Cdd:cd02520   1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFcVQDE-DDPAIPVVRKLIAkypnvdarlliggeKVG------INP 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  82 GVSaALNFGLRHARGDYVATPDlDDIMLPHSLSVRAAYLDQHPEVGCVGALviyidsegqetkrqngnrirqldfdyllg 161
Cdd:cd02520  74 KVN-NLIKGYEEARYDILVISD-SDISVPPDYLRRMVAPLMDPGVGLVTCL----------------------------- 122

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15595902 162 naYVCGaPVSLYRMEALRAAGFYDP--EIKVQDFQMTLRIASQGYQIHKLPVLV 213
Cdd:cd02520 123 --CAFG-KSMALRREVLDAIGGFEAfaDYLAEDYFLGKLIWRLGYRVVLSPYVV 173
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 20-207 2.30e-09

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: 56.64  E-value: 2.30e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  20 SVVAPCFNAE-KYLEEALRSIYEQDYPNFEVIIVDDGSTDNSY-----AMLEQLQKVHGFqLYRQQNQGVSA-ALNFGLR 92
Cdd:cd06435   1 SIHVPCYEEPpEMVKETLDSLAALDYPNFEVIVIDNNTKDEALwkpveAHCAQLGERFRF-FHVEPLPGAKAgALNYALE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  93 HARGD--YVATPDLDDIMLPHSLSVRAAYLDQhPEVGCVGALVIYIDSEGQETKRQnGNRIRQLDFDYLL-----GNAYV 165
Cdd:cd06435  80 RTAPDaeIIAVIDADYQVEPDWLKRLVPIFDD-PRVGFVQAPQDYRDGEESLFKRM-CYAEYKGFFDIGMvsrneRNAII 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15595902 166 CGAPVSLYRMEALRAAGFYDPEIKVQDFQMTLRIASQGYQIH 207
Cdd:cd06435 158 QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGV 199
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 17-206 2.38e-09

CESA_like_2 is a member of 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: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 56.49  E-value: 2.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  17 PLVSVVAPCFNAEKYLEEALRSIYEQDYPN--FEVIIV---DDgstdnsYAMLEQLQKVHGFQLYR------QQNQGVSA 85
Cdd:cd06427   1 PVYTILVPLYKEAEVLPQLIASLSALDYPRskLDVKLLleeDD------EETIAAARALRLPSIFRvvvvppSQPRTKPK 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  86 ALNFGLRHARGDYVATPDLDDIMLPHSLS-VRAAYLDQHPEVGCVGALVIYIDsegqetKRQNG-NRIRQLD----FDYL 159
Cdd:cd06427  75 ACNYALAFARGEYVVIYDAEDAPDPDQLKkAVAAFARLDDKLACVQAPLNYYN------ARENWlTRMFALEyaawFDYL 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15595902 160 LGNAYVCGAPVSL------YRMEALRAAGFYDPEIKVQDFQMTLRIASQGYQI 206
Cdd:cd06427 149 LPGLARLGLPIPLggtsnhFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRT 201
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 19-140 1.04e-08

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: 54.50  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  19 VSVVAPCFNAEKYLEEALRSIYEQDYPNFEVIIVDDGSTDNSyamlEQLQKVHGFQLYRQQnQGVSAALNFGLRHARGDY 98
Cdd:cd02522   1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGT----VAIARSAGVVVISSP-KGRARQMNAGAAAARGDW 75

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15595902  99 V----AtpdlDDIMLPHSLSVRAAYLDQHPEVGcvGALVIYIDSEG 140
Cdd:cd02522  76 LlflhA----DTRLPPDWDAAIIETLRADGAVA--GAFRLRFDDPG 115
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 21-105 1.80e-08

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 53.69  E-value: 1.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQ-DYPNFEVIIVDDGSTDNSYAMLEQLQKVHGFQ--LYRQQNQGVSAALNFGLRHARGD 97
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAAlKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVrlIVRPGKRGLGSAYIEGFKAARGD 80


                ....*...
gi 15595902  98 YVATPDLD 105
Cdd:cd06442  81 VIVVMDAD 88
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 20-105 2.04e-08

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 54.39  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   20 SVVAPCFNAE-----------KYLEEALRsiyEQDYPNFEVIIVDDGSTDNSYA-----MLEQLQKVHGFQLYR-QQNQG 82
Cdd:PTZ00260  73 SIVIPAYNEEdrlpkmlketiKYLESRSR---KDPKFKYEIIIVNDGSKDKTLKvakdfWRQNINPNIDIRLLSlLRNKG 149

                         90       100
                 ....*....|....*....|...
gi 15595902   83 VSAALNFGLRHARGDYVATPDLD 105
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDAD 172
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 32-207 3.36e-08

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 53.06  E-value: 3.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  32 LEEALRSIYEQDYpnfEVIIVDDGStDNSYAMLEQLQKVHGFQLYRQQNQGVSAALNFGLRHARG---DYVATPDLDDIM 108
Cdd:cd02526  13 LKELLAALAEQVD---KVVVVDNSS-GNDIELRLRLNSEKIELIHLGENLGIAKALNIGIKAALEngaDYVLLFDQDSVP 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902 109 LPHSLSVRAAYLDQHPEVGCVGALV-IYIDSEGQETKRQNGNRIRQLDFDYLLGNAYVCGAPV----SLYRMEALRAAGF 183
Cdd:cd02526  89 PPDMVEKLLAYKILSDKNSNIGAVGpRIIDRRTGENSPGVRKSGYKLRIQKEGEEGLKEVDFLitsgSLISLEALEKVGG 168

                       170       180
                ....*....|....*....|....*.
gi 15595902 184 YDPE--IKVQDFQMTLRIASQGYQIH 207
Cdd:cd02526 169 FDEDlfIDYVDTEWCLRARSKGYKIY 194
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
20-127 3.58e-08

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 53.64  E-value: 3.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   20 SVVAPCFNAEKYLEEALRSIYEQDYP---NFEVIIVDDGSTDNSYAMLEQLQK--VHGFQL--YRQQNQGVSAALNFGLR 92
Cdd:NF038302   4 TVAIPTYNGANRLPEVLERLRSQIGTeslSWEIIVVDNNSTDNTAQVVQEYQKnwPSPYPLryCFEPQQGAAFARQRAIQ 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 15595902   93 HARGDYVATpdLDDIMLPHSLSVRAAYL--DQHPEVG 127
Cdd:NF038302  84 EAKGELIGF--LDDDNLPAPNWVAAAYAfgQEHPQAG 118
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 19-105 4.63e-08

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 53.59  E-value: 4.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902   19 VSVVAPCFNAEKYLEEALR---SIYEQDYPNFEVIIVDDGSTDNSYAMLEQLQKV---HGFQLYRQQNQGVSAALNFGLR 92
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRrttAACESLGKEYEILLIDDGSSDNSAEMLVEAAQApdsHIVAILLNRNYGQHSAIMAGFS 87

                         90
                 ....*....|...
gi 15595902   93 HARGDYVATPDLD 105
Cdd:PRK10714  88 HVTGDLIITLDAD 100
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 19-208 1.02e-07

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 51.87  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  19 VSVVAPCFNA-EKYLEEALRSIYEQDyPNfEVIIVDDGSTDNSYAMLEQLQKVHGFQLYRQQNQGVSAALNFGLRHARGD 97
Cdd:cd06434   2 VTVIIPVYDEdPDVFRECLRSILRQK-PL-EIIVVTDGDDEPYLSILSQTVKYGGIFVITVPHPGKRRALAEGIRHVTTD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  98 YVATPDlDDIMLPHSLSVRAAYLDQHPEVGCVGalviyidsEGQETKRQNG--------NRIRQLDFDYLLGNAYVCGAP 169
Cdd:cd06434  80 IVVLLD-SDTVWPPNALPEMLKPFEDPKVGGVG--------TNQRILRPRDskwsflaaEYLERRNEEIRAAMSYDGGVP 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15595902 170 V-----SLYRMEALRAA----GFYDPEI-KVQ-----DFQMTLRIASQGYQIHK 208
Cdd:cd06434 151 ClsgrtAAYRTEILKDFlfleEFTNETFmGRRlnagdDRFLTRYVLSHGYKTVY 204
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 19-97 2.09e-07

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 50.59  E-value: 2.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595902    19 VSVVAPCFNAEKYLEEALRSIYEQDYPnFEVIIVDDGSTDNSYAMLEQLqkvhGFQLYRQQnQGVSAALNFGLRHARGD 97
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGD-AEVIVVDGGSTDGTVEIARSL----GAKVIHSP-KGRARQMNAGAALAKGD 73
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 17-129 1.96e-06

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: 48.08  E-value: 1.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  17 PLVSVVAPCFNaEKYL-EEALRSIYEQDYPNFEVII-VDDGSTDNSYAMLEQL------QKVHGFQLYRQQNQGVSA-AL 87
Cdd:cd06437   1 PMVTVQLPVFN-EKYVvERLIEAACALDYPKDRLEIqVLDDSTDETVRLAREIveeyaaQGVNIKHVRRADRTGYKAgAL 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15595902  88 NFGLRHARGDYVATPDLDDIMLPHSLSvRAAYLDQHPEVGCV 129
Cdd:cd06437  80 AEGMKVAKGEYVAIFDADFVPPPDFLQ-KTPPYFADPKLGFV 120
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 21-95 1.78e-05

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 44.68  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYeQDYPNFEVIIVDDGSTDNSYAMLE---QLQKVHgfqLYRQQ----NQGVSAALNFGLRH 93
Cdd:cd06436   1 VLVPCLNEEAVIQRTLASLL-RNKPNFLVLVIDDASDDDTAGIVRlaiTDSRVH---LLRRHlpnaRTGKGDALNAAYDQ 76


                ..
gi 15595902  94 AR 95
Cdd:cd06436  77 IR 78
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 27-118 4.44e-04

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 38.77  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    27 NAEKYLEEALRSIYEQDYPNFevIIVDDGSTDNSYAMLEQLQKVHGFQL---YRQQNQGVSAALNFGLRHARGDYVATPD 103
Cdd:pfam13704   2 NEADILPQWLAHHLALGFDHI--YVYDNGSDDGTAEILARLPDVSILRSdlsYKDARFQVDWRNALLARYAEADWVLVVD 79

                          90
                  ....*....|....*..
gi 15595902   104 LDDIML--PHSLSVRAA 118
Cdd:pfam13704  80 ADEFLVypPGDRSLRAL 96
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 21-126 1.07e-03

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 39.12  E-value: 1.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902  21 VVAPCFNAEKYLEEALRSIYEQDYP--NFEVIIVDDGSTDNSYAMLEQlqkvHGFQLYRQQNQ---GVSAALNFGLRHAR 95
Cdd:cd06438   1 ILIPAHNEEAVIGNTVRSLKAQDYPreLYRIFVVADNCTDDTAQVARA----AGATVLERHDPerrGKGYALDFGFRHLL 76

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15595902  96 G-----DYVATPDLDDIMLPHSLSVRAAYLDQHPEV 126
Cdd:cd06438  77 NladdpDAVVVFDADNLVDPNALEELNARFAAGARV 112
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 86-229 8.51e-03

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: 36.49  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595902    86 ALNFGLRHARGDYVATPDLDDIMLPHSLSVRAAYLdQHPEVGCVGALVIYIDSEGqetkrqngnRIRQLDFDYLLGNAYV 165
Cdd:pfam13506  21 NLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPL-ADPKVGLVTSPPVGSDPKG---------LAAALEAAFFNTLAGV 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15595902   166 CGAPVS----------LYRMEALRAAGFYDPeIK---VQDFQMTLRIASQGYQIHklpvLVTRYRRHPdNLSRRYKV 229
Cdd:pfam13506  91 LQAALSgigfavgmsmAFRRADLERIGGFEA-LAdylAEDYALGKLLRAAGLKVV----LSPRPILQT-SGPRRTSF 161
 
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