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Conserved domains on  [gi|736847552|ref|WP_034847880|]
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glycosyltransferase family 2 protein [Elizabethkingia anophelis]

Protein Classification

glycosyltransferase( domain architecture ID 11440269)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-322 2.63e-41

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: 145.65  E-value: 2.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   1 MKISIVVAIFNRKDELFELLNSLSHQTC--KDFEVIIVDDGSKIELQPTV-DMFKEMLTIRYF-KKENTGPGLSRNYGAH 76
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIArELAAEYPRVRVIeRPENGGKAAALNAGLK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  77 RAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGadkahkgfnllqkaisysmtsvfttggirgnkkavskfqprs 156
Cdd:COG1215  109 AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGA------------------------------------------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 157 fNMGVKKAVFLDVGGFSEMRIGEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQVYQFGVARPILNQRHPAYTK 236
Cdd:COG1215  147 -NLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLR 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 237 LTFWFpsVFLVGYCMGIIhyffehngIILSLYGLYTFLVFAHATLITRNISIGALAVVTTYVQMFSYGYGFLESWIKLN- 315
Cdd:COG1215  226 PRRLL--LFLLLLLLPLL--------LLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKk 295

                 ....*...
gi 736847552 316 -VFRKEPR 322
Cdd:COG1215  296 vVWKKTPR 303
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-322 2.63e-41

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: 145.65  E-value: 2.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   1 MKISIVVAIFNRKDELFELLNSLSHQTC--KDFEVIIVDDGSKIELQPTV-DMFKEMLTIRYF-KKENTGPGLSRNYGAH 76
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIArELAAEYPRVRVIeRPENGGKAAALNAGLK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  77 RAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGadkahkgfnllqkaisysmtsvfttggirgnkkavskfqprs 156
Cdd:COG1215  109 AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGA------------------------------------------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 157 fNMGVKKAVFLDVGGFSEMRIGEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQVYQFGVARPILNQRHPAYTK 236
Cdd:COG1215  147 -NLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLR 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 237 LTFWFpsVFLVGYCMGIIhyffehngIILSLYGLYTFLVFAHATLITRNISIGALAVVTTYVQMFSYGYGFLESWIKLN- 315
Cdd:COG1215  226 PRRLL--LFLLLLLLPLL--------LLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKk 295

                 ....*...
gi 736847552 316 -VFRKEPR 322
Cdd:COG1215  296 vVWKKTPR 303
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-246 8.62e-29

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: 111.17  E-value: 8.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   2 KISIVVAIFNRKDELFELLNSLSHQT--CKDFEVIIVDDGSKIElqpTVDMFKEMLT----IRYFK--KENTGPGlsRNY 73
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDG---TREIVQEYAAkdprIRLIDnpKRIQSAG--LNI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  74 GAHRAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGADKAhKGFNLLQKAISYSMTSVFTTGGIRGNKKAVS-KF 152
Cdd:cd02525   76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMET-IGESKFQKAIAVAQSSPLGSGGSAYRGGAVKiGY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 153 QPRSFNMGVKKAVFLDVGGFSEMRI-GEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQVYQFGVARPILNQRH 231
Cdd:cd02525  155 VDTVHHGAYRREVFEKVGGFDESLVrNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRARTLRKH 234
                        250
                 ....*....|....*
gi 736847552 232 PAYTKLTFWFPSVFL 246
Cdd:cd02525  235 RKSLSLRHLLPLAFV 249
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-115 1.88e-23

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: 94.77  E-value: 1.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552    4 SIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIElqpTVDMFKEMLT----IRYF-KKENTGPGLSRNYGAHRA 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDG---TVEIAEEYAKkdprVRVIrLPENRGKAGARNAGLRAA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 736847552   79 EGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGA 115
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGS 114
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-89 8.23e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 61.99  E-value: 8.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   2 KISIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIELQPTVDMFKEMLT-IRYFKKENTGPGLSRNYGAHRAEG 80
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARNTGLAVATG 86

                 ....*....
gi 736847552  81 EWLVFLDSD 89
Cdd:PRK10073  87 KYVAFPDAD 95
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-322 2.63e-41

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: 145.65  E-value: 2.63e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   1 MKISIVVAIFNRKDELFELLNSLSHQTC--KDFEVIIVDDGSKIELQPTV-DMFKEMLTIRYF-KKENTGPGLSRNYGAH 76
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIArELAAEYPRVRVIeRPENGGKAAALNAGLK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  77 RAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGadkahkgfnllqkaisysmtsvfttggirgnkkavskfqprs 156
Cdd:COG1215  109 AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGA------------------------------------------ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 157 fNMGVKKAVFLDVGGFSEMRIGEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQVYQFGVARPILNQRHPAYTK 236
Cdd:COG1215  147 -NLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLR 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 237 LTFWFpsVFLVGYCMGIIhyffehngIILSLYGLYTFLVFAHATLITRNISIGALAVVTTYVQMFSYGYGFLESWIKLN- 315
Cdd:COG1215  226 PRRLL--LFLLLLLLPLL--------LLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKk 295

                 ....*...
gi 736847552 316 -VFRKEPR 322
Cdd:COG1215  296 vVWKKTPR 303
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-241 1.55e-37

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 132.81  E-value: 1.55e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   1 MKISIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKielQPTVDMFKEMLT--IRYFK-KENTGPGLSRNYGAHR 77
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGST---DGTAELLAALAFprVRVIRnPENLGFAAARNLGLRA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  78 AEGEWLVFLDSDVIVETDYIEQVCknideiptdafggadkahkgfnllqkaisysmtsvfttggirgnkkavskfqpRSF 157
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLERLL-----------------------------------------------------AAA 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 158 NMGVKKAVFLDVGGFSE-MRI-GEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQvYQFGVARPILNQRHPAYT 235
Cdd:COG1216  107 CLLIRREVFEEVGGFDErFFLyGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRA-YYLGRNRLLFLRKHGPRP 185

                 ....*.
gi 736847552 236 KLTFWF 241
Cdd:COG1216  186 LLRLAL 191
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-246 8.62e-29

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: 111.17  E-value: 8.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   2 KISIVVAIFNRKDELFELLNSLSHQT--CKDFEVIIVDDGSKIElqpTVDMFKEMLT----IRYFK--KENTGPGlsRNY 73
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDG---TREIVQEYAAkdprIRLIDnpKRIQSAG--LNI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  74 GAHRAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGADKAhKGFNLLQKAISYSMTSVFTTGGIRGNKKAVS-KF 152
Cdd:cd02525   76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMET-IGESKFQKAIAVAQSSPLGSGGSAYRGGAVKiGY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 153 QPRSFNMGVKKAVFLDVGGFSEMRI-GEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQVYQFGVARPILNQRH 231
Cdd:cd02525  155 VDTVHHGAYRREVFEKVGGFDESLVrNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRARTLRKH 234
                        250
                 ....*....|....*
gi 736847552 232 PAYTKLTFWFPSVFL 246
Cdd:cd02525  235 RKSLSLRHLLPLAFV 249
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-211 3.33e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.55  E-value: 3.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   1 MKISIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKielQPTVDMFKEMLT----IRYFK-KENTGPGLSRNYGA 75
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGST---DGTAEILRELAAkdprIRVIRlERNRGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  76 HRAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGADKAHKGFNLLQKAISYSMTSVFTTGGIRGnkkavskfqPR 155
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPD---------ST 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 736847552 156 SFNMGVKKAVFLDVgGFSEmRIGEDPDLsMTLWEKGYQTAFFDHIgvYHKRRTDLG 211
Cdd:COG0463  150 SGFRLFRREVLEEL-GFDE-GFLEDTEL-LRALRHGFRIAEVPVR--YRAGESKLN 200
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-115 9.06e-25

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: 97.96  E-value: 9.06e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIElqpTVDMFKEMLT-----IRYFKKENTGPGLSRNYGAHRAE 79
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDG---TLEILEEYAKkdprvIRVINEENQGLAAARNAGLKAAR 77
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 736847552  80 GEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGA 115
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGG 113
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-115 1.88e-23

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: 94.77  E-value: 1.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552    4 SIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIElqpTVDMFKEMLT----IRYF-KKENTGPGLSRNYGAHRA 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDG---TVEIAEEYAKkdprVRVIrLPENRGKAGARNAGLRAA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 736847552   79 EGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGA 115
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGS 114
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
5-191 1.05e-19

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: 84.94  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIELQPTVDMFKEM--LTIRYFKKENTG--PGLSRNYGAHRAEG 80
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQfpIPIKHVWQEDEGfrKAKIRNKAIAAAKG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  81 EWLVFLDSDVIVETDYIEQVCKNideiptdafggadkAHKGFNLLQKAISYSMTsvFTTGGIRGNkkavskfqprsfNMG 160
Cdd:cd06420   81 DYLIFIDGDCIPHPDFIADHIEL--------------AEPGVFLSGSRVLLNEK--LTERGIRGC------------NMS 132
                        170       180       190
                 ....*....|....*....|....*....|....
gi 736847552 161 VKKAVFLDVGGFSEMRIG---EDPDLSMTLWEKG 191
Cdd:cd06420  133 FWKKDLLAVNGFDEEFTGwggEDSELVARLLNSG 166
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-180 1.47e-17

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: 79.19  E-value: 1.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSK-----IELQPTVDMFKEMLTIRyfKKENTGPGLSRNYGAHRAE 79
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTddtleILEELAALYIRRVLVVR--DKENGGKAGALNAGLRHAK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  80 GEWLVFLDSDVIVETDYIEQVCKN-IDEIPTDAFGGADKAHKGF-NLLQKAISYSMTSVFTTG-GIRGNKKAVskFQPRS 156
Cdd:cd06423   79 GDIVVVLDADTILEPDALKRLVVPfFADPKVGAVQGRVRVRNGSeNLLTRLQAIEYLSIFRLGrRAQSALGGV--LVLSG 156
                        170       180
                 ....*....|....*....|....
gi 736847552 157 FNMGVKKAVFLDVGGFSEMRIGED 180
Cdd:cd06423  157 AFGAFRREALREVGGWDEDTLTED 180
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-206 2.89e-15

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: 72.21  E-value: 2.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKielQPTVDMFKEMLT--IRYFKKENTGPGLSRNYGAHRAEGEW 82
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNAST---DGSVELLRELFPevRLIRNGENLGFGAGNNQGIREAKGDY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  83 LVFLDSDVIVETDYIEqvcknideiptdafggadkahkgfNLLQKAisysmtsvfttggiRGNKKAVSkFQPR---SFnM 159
Cdd:cd04186   78 VLLLNPDTVVEPGALL------------------------ELLDAA--------------EQDPDVGI-VGPKvsgAF-L 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 736847552 160 GVKKAVFLDVGGFSEmRI---GEDPDLSMTLWEKGYQTAFFDHIGVYHKR 206
Cdd:cd04186  118 LVRREVFEEVGGFDE-DFflyYEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
3-191 2.71e-13

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: 67.98  E-value: 2.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   3 ISIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKielQPTVDMFKEMLTIRYfkKENTGPGLSRNYGAHRAEGEW 82
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGST---DGTVAIARSAGVVVI--SSPKGRARQMNAGAAAARGDW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  83 LVFLDSDVIVETDYIEQVckNIDEIPTDAFGGA-----DKAHKGFNLLQKAI-SYSMTSvFTTGGIRGnkkavskfqprs 156
Cdd:cd02522   76 LLFLHADTRLPPDWDAAI--IETLRADGAVAGAfrlrfDDPGPRLRLLELGAnLRSRLF-GLPYGDQG------------ 140
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 736847552 157 fnMGVKKAVFLDVGGFSEMRIGEDPDLSMTLWEKG 191
Cdd:cd02522  141 --LFIRRELFEELGGFPELPLMEDVELVRRLRRRG 173
PRK10073 PRK10073
putative glycosyl transferase; Provisional
2-89 8.23e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 61.99  E-value: 8.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   2 KISIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIELQPTVDMFKEMLT-IRYFKKENTGPGLSRNYGAHRAEG 80
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhVRLLHQANAGVSVARNTGLAVATG 86

                 ....*....
gi 736847552  81 EWLVFLDSD 89
Cdd:PRK10073  87 KYVAFPDAD 95
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
2-207 1.69e-10

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: 59.52  E-value: 1.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   2 KISIVVAIFNRKDE-LFELLNSLSHQTCKDFEVIIVDDGS-KIELQPTVDMFKEM-LTIRY-FKKENTGPGLSRNYGAHR 77
Cdd:cd04184    2 LISIVMPVYNTPEKyLREAIESVRAQTYPNWELCIADDAStDPEVKRVLKKYAAQdPRIKVvFREENGGISAATNSALEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  78 AEGEWLVFLDSDvivetdyieqvckniDEIPTDAFGGADKAHKGFNllQKAISYSMTSVFTTGGIRGNKKAVSKFQP--- 154
Cdd:cd04184   82 ATGEFVALLDHD---------------DELAPHALYEVVKALNEHP--DADLIYSDEDKIDEGGKRSEPFFKPDWSPdll 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 736847552 155 RSFNM-----GVKKAVFLDVGGF-SEMRIGEDPDLSMTLWEKGYQTAFFDHIgVYHKRR 207
Cdd:cd04184  145 LSQNYighllVYRRSLVRQVGGFrEGFEGAQDYDLVLRVSEHTDRIAHIPRV-LYHWRA 202
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
3-216 1.37e-09

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: 57.38  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552    3 ISIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKielQPTVDMFKEML------TIRYFKKEN----TGPGLSRN 72
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSD---AETLDVAEEIAarfpdvRLRVIRNARllgpTGKSRGLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   73 YGAHRAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGADKAHKG---FNLLQK---AISYSMTSVFTtggirgnk 146
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRstmLSALGAlefALRHLRMMSLR-------- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736847552  147 KAVSKFQPRSFNMGVKKAVFLDVGGFSEMRI-GEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQ 216
Cdd:pfam13641 153 LALGVLPLSGAGSAIRREVLKELGLFDPFFLlGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQ 223
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-203 8.66e-09

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: 54.63  E-value: 8.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   4 SIVVAIFNRKDELF--ELLNSLSHQTCKDFEVIIVDDGS-KIELQPTVDMFKEMLTIRYFKKE-NTGPGLSRNYGAHRAE 79
Cdd:cd04195    1 SVLMSVYIKEKPEFlrEALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPLEkNRGLGKALNEGLKHCT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  80 GEWLVFLDSDVIVETDYIEQVCKNIDEIPT-DAFGGAdkahkgfnLLQkaISYSMTSVFTTGGIRGNKKAVSKFQPRS-F 157
Cdd:cd04195   81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEiDIVGGG--------VLE--FDSDGNDIGKRRLPTSHDDILKFARRRSpF 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 736847552 158 N-MGV--KKAVFLDVGGFSEMRIGEDPDLSMTLWEKGYQTAFFDHIGVY 203
Cdd:cd04195  151 NhPTVmfRKSKVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVK 199
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-89 1.00e-08

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: 54.02  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSH---QTCKDFEVIIVDDGSKielQPTVDMFKEML----TIRYFKkentgpgLSRNYGAHR 77
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAvleSLGYDYEIIFVDDGST---DRTLEILRELAardpRVKVIR-------LSRNFGQQA 70
                         90       100
                 ....*....|....*....|
gi 736847552  78 A--------EGEWLVFLDSD 89
Cdd:cd04187   71 AllagldhaRGDAVITMDAD 90
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
4-200 3.44e-08

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: 52.93  E-value: 3.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   4 SIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIElqpTVDmfkemlTIRYFkkentGPGLSR------------ 71
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDG---TVD------IIKKY-----EDKITYwisepdkgiyda 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  72 -NYGAHRAEGEWLVFLDSDVIVETDYIEQVCKNIDEIPTDAFGGADkahkgfnllqkaisysMTSVFTTGGIRGNKKAVS 150
Cdd:cd06433   67 mNKGIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGD----------------VLLVDENGRVIGRRRPPP 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552 151 KFqPRSFNMG---------VKKAVFLDVGGFSE-MRIGEDPDLSMTLWEKGYQTAFFDHI 200
Cdd:cd06433  131 FL-DKFLLYGmpichqatfFRRSLFEKYGGFDEsYRIAADYDLLLRLLLAGKIFKYLPEV 189
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
82-275 5.55e-08

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: 52.34  E-value: 5.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   82 WLVFLDSDVIVETDYIEQVCKNIDE-------IPTDAFGGADKAHKGF-----NLLQKAISYSMTS---VFTTGGirgnk 146
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASpevaiiqGPILPMNVGNYLEELAalffaDDHGKSIPVRMALgrvLPFVGS----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  147 kavskfqprsfNMGVKKAVFLDVGGFSEMRIGEDPDLSMTLWEKGYQTAFFDHIGVYHKRRTDLGKFSKQVYQ-FGVARP 225
Cdd:pfam13632  76 -----------GAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRwAYGCLL 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 736847552  226 ILNQRHPAYTKLTFWFPSVFLVgyCMGIIHYFFEHNGIILSLYGLYTFLV 275
Cdd:pfam13632 145 ILLIRLLGYLGTLLWSGLPLAL--LLLLLFSISSLALVLLLLALLAGLLL 192
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-180 5.92e-08

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: 52.68  E-value: 5.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSHQTCKD--FEVIIVDDGSKIElqpTVDMFKEMLTIRYF--------KKENTGPGLSRNYG 74
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDG---TVQILEFAAAKPNFqlkilnnsRVSISGKKNALTTA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  75 AHRAEGEWLVFLDSDVIVETDYIEQVCKNI-DEIPTDAFGGADKAHKG--FNLLQKaISYSMTSVFTTGGIrGNKKAvsk 151
Cdd:cd04192   78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIqKEQIGLVAGPVIYFKGKslLAKFQR-LDWLSLLGLIAGSF-GLGKP--- 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 736847552 152 FQPRSFNMGVKKAVFLDVGGFSE---MRIGED 180
Cdd:cd04192  153 FMCNGANMAYRKEAFFEVGGFEGndhIASGDD 184
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
4-198 1.17e-07

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: 52.02  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   4 SIVVAIFNRKDE-LFELLNSLSHQTCKDFEVIIVDDGSKIEL--QPtVDMFKEMLTIRY-FKKENTGPGL---SRNYGAH 76
Cdd:cd06435    1 SIHVPCYEEPPEmVKETLDSLAALDYPNFEVIVIDNNTKDEAlwKP-VEAHCAQLGERFrFFHVEPLPGAkagALNYALE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  77 RA--EGEWLVFLDSDVIVETDYIEQVCKNIDEiPTDAFGGADKAHKGFN--LLQKAISYSMTSVFTTGG-IRGNKKAVsk 151
Cdd:cd06435   80 RTapDAEIIAVIDADYQVEPDWLKRLVPIFDD-PRVGFVQAPQDYRDGEesLFKRMCYAEYKGFFDIGMvSRNERNAI-- 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 736847552 152 FQPRSFNMgVKKAVFLDVGGFSEMRIGEDPDLSMTLWEKGYQTAFFD 198
Cdd:cd06435  157 IQHGTMCL-IRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVA 202
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-183 2.59e-07

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: 51.12  E-value: 2.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552    4 SIVVAIFNRKDELF--ELLNSLSHQTCKDFEVIIVDDGSKIELQPTVDMFKEMLTIRYFKKENT---GPGLSRNYGAHRA 78
Cdd:pfam10111   1 SVVIPVYNGEKTHWiqERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDttySLAASRNRGTSHA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   79 EGEWLVFLDSDVIVETDYIEQVCK-----NIDEIPTD--AFGGADKAHKGFNLLQKAISYSMTSVFTTGGIRGNKKAVSK 151
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKiatslALQENIQAavVLPVTDLNDESSNFLRRGGDLTASGDVLRDLLVFYSPLAIF 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 736847552  152 FQPRSFNMGVKKAVFLDVGGFSEMRIG---EDPDL 183
Cdd:pfam10111 161 FAPNSSNALINRQAFIEVGGFDESFRGhgaEDFDI 195
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-98 8.43e-07

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: 48.79  E-value: 8.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   6 VVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKielqptvDMFKEMLTIRYFKKENTGPGLSRNYG----------- 74
Cdd:cd04185    2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNAST-------DGTAEWLTSLGDLDNIVYLRLPENLGgaggfyegvrr 74
                         90       100
                 ....*....|....*....|....
gi 736847552  75 AHRAEGEWLVFLDSDVIVETDYIE 98
Cdd:cd04185   75 AYELGYDWIWLMDDDAIPDPDALE 98
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
2-112 4.63e-06

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: 46.90  E-value: 4.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   2 KISIVVAIFNRKDELFELLNSLshQTCKDfEVIIVDDGSKIElqpTVDMFKEmLTIRYFKKENTGPGLSRNYGAHRAEGE 81
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESV--KWAVD-EIIVVDSGSTDR---TVEIAKE-YGAKVYQRWWDGFGAQRNFALELATND 73
                         90       100       110
                 ....*....|....*....|....*....|.
gi 736847552  82 WLVFLDSDVIVETDYIEQVCKNIDEIPTDAF 112
Cdd:cd02511   74 WVLSLDADERLTPELADEILALLATDDYDGY 104
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
78-196 1.46e-05

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: 44.58  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   78 AEGEWLVFLDSDVIVETDYIEQVCKNIDE--------IP--TDAFGGADKAHKGFNllqkaisySMTSVFTTGGIRGNKK 147
Cdd:pfam13506  29 AKYDLLVISDSDIRVPPDYLRDLLAPLADpkvglvtsPPvgSDPKGLAAALEAAFF--------NTLAGVLQAALSGIGF 100
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 736847552  148 AVSKFqprsfnMGVKKAVFLDVGGFSEMR--IGEDPDLSMTLWEKGYQTAF 196
Cdd:pfam13506 101 AVGMS------MAFRRADLERIGGFEALAdyLAEDYALGKLLRAAGLKVVL 145
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
4-89 2.38e-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: 44.54  E-value: 2.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   4 SIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKIElqpTVDMFKEM----LTIRYFKKENTGPGLSRNY--GAHR 77
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDG---TVEIIKEYidkdPFIIILIRNGKNLGVARNFesLLQA 77
                         90
                 ....*....|..
gi 736847552  78 AEGEWLVFLDSD 89
Cdd:cd04196   78 ADGDYVFFCDQD 89
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
4-188 2.74e-05

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 45.27  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   4 SIVVAIFNrkdELFELL----NSLSHQTCKDF--EVIIVDDGS-----KIELQPTVDMFKEMLTIRYFKKENtgpGL--S 70
Cdd:cd02510    1 SVIIIFHN---EALSTLlrtvHSVINRTPPELlkEIILVDDFSdkpelKLLLEEYYKKYLPKVKVLRLKKRE---GLirA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  71 RNYGAHRAEGEWLVFLDSDVIVETDYIEQ------------VCKNIDEIPTDAFggadkahkgfnllqkaiSYSMTSVFT 138
Cdd:cd02510   75 RIAGARAATGDVLVFLDSHCEVNVGWLEPllariaenrktvVCPIIDVIDADTF-----------------EYRGSSGDA 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 736847552 139 TGGI------------RGNKKAVSKFQP-RS--FNMGV---KKAVFLDVGGFSE-MRI--GEDPDLSMTLW 188
Cdd:cd02510  138 RGGFdwslhfkwlplpEEERRRESPTAPiRSptMAGGLfaiDREWFLELGGYDEgMDIwgGENLELSFKVW 208
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
2-90 4.21e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 44.73  E-value: 4.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   2 KISIVVAIFNRKDELFELLN---SLSHQTCKDFEVIIVDDGSKielqptvDMFKEMLTiryfkKENTGPG-------LSR 71
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRrttAACESLGKEYEILLIDDGSS-------DNSAEMLV-----EAAQAPDshivailLNR 74
                         90       100
                 ....*....|....*....|....*..
gi 736847552  72 NYGAHRA--------EGEWLVFLDSDV 90
Cdd:PRK10714  75 NYGQHSAimagfshvTGDLIITLDADL 101
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
14-89 6.41e-04

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: 40.24  E-value: 6.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552  14 DELFELLNSLSHQTckdFEVIIVDDGSKIElqpTVDMFKEM-----LTIRYFK-KENTGPGLSRNYGAHRAEGEWLVFLD 87
Cdd:cd04188   17 EEAVEYLEERPSFS---YEIIVVDDGSKDG---TAEVARKLarknpALIRVLTlPKNRGKGGAVRAGMLAARGDYILFAD 90

                 ..
gi 736847552  88 SD 89
Cdd:cd04188   91 AD 92
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-89 1.16e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 39.68  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   1 MKISIVVAIFNRKDELfELLNSLSHQT---CKDFEVIIVDDGSKIELQPTV----DMFKEMLTIRYFKKENTGPGLSRNY 73
Cdd:PLN02726   9 MKYSIIVPTYNERLNI-ALIVYLIFKAlqdVKDFEIIVVDDGSPDGTQDVVkqlqKVYGEDRILLRPRPGKLGLGTAYIH 87
                         90
                 ....*....|....*.
gi 736847552  74 GAHRAEGEWLVFLDSD 89
Cdd:PLN02726  88 GLKHASGDFVVIMDAD 103
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
5-89 1.38e-03

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: 39.09  E-value: 1.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSH--QTCKDFEVIIVDDGSK-------IELQPTVDMFKemlTIRyfkkentgpgLSRNYGA 75
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTdgtaeiaRELAARVPRVR---VIR----------LSRNFGK 67
                         90       100
                 ....*....|....*....|..
gi 736847552  76 HRA--------EGEWLVFLDSD 89
Cdd:cd04179   68 GAAvragfkaaRGDIVVTMDAD 89
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
4-99 1.42e-03

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: 39.57  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   4 SIVVAIFNRKDELFELLNSLSHQTCKdfeVIIVDDGSK--IELQPTVDMFKemltIRYFK-KENTGPGLSRNYG---AHR 77
Cdd:cd02526    1 AVVVTYNPDLSKLKELLAALAEQVDK---VVVVDNSSGndIELRLRLNSEK----IELIHlGENLGIAKALNIGikaALE 73
                         90       100
                 ....*....|....*....|..
gi 736847552  78 AEGEWLVFLDSDVIVETDYIEQ 99
Cdd:cd02526   74 NGADYVLLFDQDSVPPPDMVEK 95
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
3-107 1.52e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 39.75  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   3 ISIVVAIFNRKDELFELLNS----LSHQTCKD----FEVIIVDDGSKIE-LQPTVDMFKE-------MLTIRYfkKENTG 66
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKEtikyLESRSRKDpkfkYEIIIVNDGSKDKtLKVAKDFWRQninpnidIRLLSL--LRNKG 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 736847552  67 PGLSRNYGAHRAEGEWLVFLDSDVIVETDYIEQVCKNIDEI 107
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKI 190
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
3-89 4.48e-03

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 38.43  E-value: 4.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   3 ISIVVAIFNRKDELFELLNSLSHQTCKDFEVIIVDDGSKI--ELQPTVDMFKEMlTIRYFKKE-NTGPGLSRNYGAHRAE 79
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSweQLQQYVTALNDP-RITYIHNDiNSGACAVRNQAIMLAQ 85
                         90
                 ....*....|
gi 736847552  80 GEWLVFLDSD 89
Cdd:PRK10018  86 GEYITGIDDD 95
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
5-89 4.80e-03

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: 37.90  E-value: 4.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736847552   5 IVVAIFNRKDELFELLNSLSHQTCK-DFEVIIVDDGSkielqP--TVDMFKEMLTIRYFKK---ENTGPGLSRNY--GAH 76
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNS-----PdgTAEIVRELAKEYPRVRlivRPGKRGLGSAYieGFK 75
                         90
                 ....*....|...
gi 736847552  77 RAEGEWLVFLDSD 89
Cdd:cd06442   76 AARGDVIVVMDAD 88
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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