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Conserved domains on  [gi|1540053721|emb|VEH13070|]
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glycosyl transferase, family 2 [Legionella jordanis]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 10-210 6.15e-55

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06433:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 202  Bit Score: 177.74  E-value: 6.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF-YYESHANMGQAETLNKGWRLSKGEILA 88
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKItYWISEPDKGIYDAMNKGIALATGDIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  89 YLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNHYQMYLNATTPvAVASFFRRKAFEQLGG 168
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPIC-HQATFFRRSLFEKYGG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1540053721 169 WDKNYRQIGDYEYHLRLIRMGD-FKRIPQILGYHRVHEKSASY 210
Cdd:cd06433   160 FDESYRIAADYDLLLRLLLAGKiFKYLPEVLAAFRLGGVSSTS 202
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 10-210 6.15e-55

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: 177.74  E-value: 6.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF-YYESHANMGQAETLNKGWRLSKGEILA 88
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKItYWISEPDKGIYDAMNKGIALATGDIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  89 YLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNHYQMYLNATTPvAVASFFRRKAFEQLGG 168
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPIC-HQATFFRRSLFEKYGG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1540053721 169 WDKNYRQIGDYEYHLRLIRMGD-FKRIPQILGYHRVHEKSASY 210
Cdd:cd06433   160 FDESYRIAADYDLLLRLLLAGKiFKYLPEVLAAFRLGGVSSTS 202
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 7-213 4.67e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.84  E-value: 4.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF----YYESHANMGQAETLNKGWRLS 82
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDprirVIRLERNRGKGAARNAGLAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  83 KGEILAYLSADDKLTPNATSLSVATLMQNPEVIltYADNLLINSESQPIRKLLTPEFNHYQMYLNATTPVAVASFFRRKA 162
Cdd:COG0463    82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADL--VYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1540053721 163 FEQLgGWDKNYRQigDYEYhLRLIRMG-DFKRIPQilgYHRVHEKSASYAKM 213
Cdd:COG0463   160 LEEL-GFDEGFLE--DTEL-LRALRHGfRIAEVPV---RYRAGESKLNLRDL 204
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 10-165 1.97e-28

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: 107.87  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF----YYESHANMGQAETLNKGWRLSKGE 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDprvrVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  86 ILAYLSADDKLTPNAtsLS-VATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNHYQMYL-------NATTPVAVASF 157
Cdd:pfam00535  81 YIAFLDADDEVPPDW--LEkLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLglrllglNLPFLIGGFAL 158


                  ....*...
gi 1540053721 158 FRRKAFEQ 165
Cdd:pfam00535 159 YRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-99 1.18e-18

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 85.10  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   1 MSSSSlPLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQFyyeSH------ANMGQAET 74
Cdd:PRK10073    1 MMNST-PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENY---PHvrllhqANAGVSVA 76

                          90       100
                  ....*....|....*....|....*
gi 1540053721  75 LNKGWRLSKGEILAYLSADDKLTPN 99
Cdd:PRK10073   77 RNTGLAVATGKYVAFPDADDVVYPT 101
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 10-210 6.15e-55

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: 177.74  E-value: 6.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF-YYESHANMGQAETLNKGWRLSKGEILA 88
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKItYWISEPDKGIYDAMNKGIALATGDIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  89 YLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNHYQMYLNATTPvAVASFFRRKAFEQLGG 168
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPIC-HQATFFRRSLFEKYGG 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1540053721 169 WDKNYRQIGDYEYHLRLIRMGD-FKRIPQILGYHRVHEKSASY 210
Cdd:cd06433   160 FDESYRIAADYDLLLRLLLAGKiFKYLPEVLAAFRLGGVSSTS 202
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 7-213 4.67e-42

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.84  E-value: 4.67e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF----YYESHANMGQAETLNKGWRLS 82
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDprirVIRLERNRGKGAARNAGLAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  83 KGEILAYLSADDKLTPNATSLSVATLMQNPEVIltYADNLLINSESQPIRKLLTPEFNHYQMYLNATTPVAVASFFRRKA 162
Cdd:COG0463    82 RGDYIAFLDADDQLDPEKLEELVAALEEGPADL--VYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1540053721 163 FEQLgGWDKNYRQigDYEYhLRLIRMG-DFKRIPQilgYHRVHEKSASYAKM 213
Cdd:COG0463   160 LEEL-GFDEGFLE--DTEL-LRALRHGfRIAEVPV---RYRAGESKLNLRDL 204
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 11-194 4.51e-36

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: 127.62  E-value: 4.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQ----FYYESHANMGQAETLNKGWRLSKGEI 86
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKdprvIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  87 LAYLSADDKLTPNATSLSVATLMQNPEVILTYADNLLinsesqpirklltpefnhyqmylnattpvavasFFRRKAFEQL 166
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL---------------------------------LFRRELLEEI 127

                         170       180
                  ....*....|....*....|....*...
gi 1540053721 167 GGWDKNYRQIGDYEYHLRLIRMGDFKRI 194
Cdd:cd00761   128 GGFDEALLSGEEDDDFLLRLLRGGKVAF 155
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 2-215 1.04e-34

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: 128.32  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   2 SSSSLPLVSIVIPCYNGMPYLEEAIESVLAQDYP--NIELIVLDDGSTDGSMELLRRYEGQF----YYESHANMGQAETL 75
Cdd:COG1215    24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELAAEYprvrVIERPENGGKAAAL 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  76 NKGWRLSKGEILAYLSADDKLTPNATSLSVAtLMQNPEVILTyadnllinsesqpirklltpefnhyqmylnattpvAVA 155
Cdd:COG1215   104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVA-AFADPGVGAS-----------------------------------GAN 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1540053721 156 SFFRRKAFEQLGGWDKNYrqIG-DYEYHLRLIRMG-DFKRIPQILGYHRVHEKSASYAKMNF 215
Cdd:COG1215   148 LAFRREALEEVGGFDEDT--LGeDLDLSLRLLRAGyRIVYVPDAVVYEEAPETLRALFRQRR 207
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
7-212 8.92e-33

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 120.48  E-value: 8.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF--YYESHANMGQAETLNKGWRLSKG 84
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRvrVIRNPENLGFAAARNLGLRAAGG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  85 EILAYLSADDKLTPNAtslsvatlmqnpeviltyadnllinsesqpIRKLLTpefnhyqmylnattpvAVASFFRRKAFE 164
Cdd:COG1216    83 DYLLFLDDDTVVEPDW------------------------------LERLLA----------------AACLLIRREVFE 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1540053721 165 QLGGWDKNYRQIG-DYEYHLRLIRMG-DFKRIPQILGYHRVHEKSASYAK 212
Cdd:COG1216   117 EVGGFDERFFLYGeDVDLCLRLRKAGyRIVYVPDAVVYHLGGASSGPLLR 166
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 7-202 2.95e-32

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: 118.84  E-value: 2.95e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMP-YLEEAIESVLAQDYPNIELIVLDDGSTDGSM-ELLRRYEGQ------FYYEShaNMGQAETLNKG 78
Cdd:cd04184     1 PLISIVMPVYNTPEkYLREAIESVRAQTYPNWELCIADDASTDPEVkRVLKKYAAQdprikvVFREE--NGGISAATNSA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  79 WRLSKGEILAYLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNH----YQMYlnaTTPVAV 154
Cdd:cd04184    79 LELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFKPDWSPdlllSQNY---IGHLLV 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1540053721 155 asfFRRKAFEQLGGWDKNYRQIGDYEYHLRLIRMGD-FKRIPQILgYHR 202
Cdd:cd04184   156 ---YRRSLVRQVGGFREGFEGAQDYDLVLRVSEHTDrIAHIPRVL-YHW 200
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 11-170 3.38e-29

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: 110.39  E-value: 3.38e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQFYYESH-----ANMGQAETLNKGWRLSKGE 85
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLvvrdkENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  86 ILAYLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPIRKLLTPEFN-------HYQMYLNATTPVA-VASF 157
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLsifrlgrRAQSALGGVLVLSgAFGA 160

                         170
                  ....*....|...
gi 1540053721 158 FRRKAFEQLGGWD 170
Cdd:cd06423   161 FRREALREVGGWD 173
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 10-165 1.97e-28

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: 107.87  E-value: 1.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF----YYESHANMGQAETLNKGWRLSKGE 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDprvrVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  86 ILAYLSADDKLTPNAtsLS-VATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNHYQMYL-------NATTPVAVASF 157
Cdd:pfam00535  81 YIAFLDADDEVPPDW--LEkLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLglrllglNLPFLIGGFAL 158


                  ....*...
gi 1540053721 158 FRRKAFEQ 165
Cdd:pfam00535 159 YRREALEE 166
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 8-215 7.67e-25

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: 100.38  E-value: 7.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   8 LVSIVIPCYNGMPYLEEAIESVLAQDYP--NIELIVLDDGSTDGSMELLRRYEGQF----YYEshaNMG--QAETLNKGW 79
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYAAKDprirLID---NPKriQSAGLNIGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  80 RLSKGEILAYLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPI--RKLLTPEFNHYQMY-LNATTPVAVAS 156
Cdd:cd02525    78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAiaVAQSSPLGSGGSAYrGGAVKIGYVDT 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540053721 157 ----FFRRKAFEQLGGWDKNYRQIGDYEYHLRLIRMG-DFKRIPQILGYHRVHEKSASYAKMNF 215
Cdd:cd02525   158 vhhgAYRREVFEKVGGFDESLVRNEDAELNYRLRKAGyKIWLSPDIRVYYYPRSTLKKLARQYF 221
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-133 4.22e-21

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: 89.61  E-value: 4.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQ-----FYYESHANMGQAETLNKGWRLSKG 84
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKdpfiiILIRNGKNLGVARNFESLLQAADG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1540053721  85 EILAYLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPIRK 133
Cdd:cd04196    81 DYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGE 129
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-203 2.18e-20

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: 86.46  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF-YYESHANMGQAETLNKGWRLSKGEILAY 89
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVrLIRNGENLGFGAGNNQGIREAKGDYVLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  90 LSADDKLTPNATSLSVATLMQNPEViltyadnllinsesqpirKLLTPefnhyqmylNATtpvAVASFFRRKAFEQLGGW 169
Cdd:cd04186    81 LNPDTVVEPGALLELLDAAEQDPDV------------------GIVGP---------KVS---GAFLLVRREVFEEVGGF 130

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1540053721 170 DKNYRQIG-DYEYHLRLIRMGdfKRI---PQILGYHRV 203
Cdd:cd04186   131 DEDFFLYYeDVDLCLRARLAG--YRVlyvPQAVIYHHG 166
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 4-217 2.91e-19

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: 85.33  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   4 SSLPLVSIVIPCYNGMPYLEEAIESVLAQDYPN--IELIVLDDGSTDGSMELLRRYEGQFY--YESHANMGQAETLNKGW 79
Cdd:cd06439    26 AYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADKGVklLRFPERRGKAAALNRAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  80 RLSKGEILAYLSADDKLTPNATSLSVAtLMQNPEViltyadnLLINSESQPIRKLLTPEF-NHYQMYLNA---------T 149
Cdd:cd06439   106 ALATGEIVVFTDANALLDPDALRLLVR-HFADPSV-------GAVSGELVIVDGGGSGSGeGLYWKYENWlkraesrlgS 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1540053721 150 TPVAVASF--FRRKAFEQLggwdKNYRQIGDYEYHLRLIRMGdfKRI---PQILGYhrvhEKSASYAKMNFER 217
Cdd:cd06439   178 TVGANGAIyaIRRELFRPL----PADTINDDFVLPLRIARQG--YRVvyePDAVAY----EEVAEDGSEEFRR 240
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-99 1.18e-18

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 85.10  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   1 MSSSSlPLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQFyyeSH------ANMGQAET 74
Cdd:PRK10073    1 MMNST-PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENY---PHvrllhqANAGVSVA 76

                          90       100
                  ....*....|....*....|....*
gi 1540053721  75 LNKGWRLSKGEILAYLSADDKLTPN 99
Cdd:PRK10073   77 RNTGLAVATGKYVAFPDADDVVYPT 101
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 9-195 2.33e-17

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: 79.54  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   9 VSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQFYyesHANMGQAETLNKGWRLSKGEILA 88
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVVI---SSPKGRARQMNAGAAAARGDWLL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  89 YLSADDKLTPNATSLSVATLMQNPEVIltYADNLLINSESQPIRKLLtpefnhyqMYLNATTPVAV------ASFFRRKA 162
Cdd:cd02522    78 FLHADTRLPPDWDAAIIETLRADGAVA--GAFRLRFDDPGPRLRLLE--------LGANLRSRLFGlpygdqGLFIRREL 147

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1540053721 163 FEQLGGwdknYRQIG---DYEYHLRLIRMGDFKRIP 195
Cdd:cd02522   148 FEELGG----FPELPlmeDVELVRRLRRRGRPALLP 179
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 11-211 2.63e-16

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: 76.34  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLAQDYPN-IELIVLDDGSTDGSMELLRRYE------------GQFYYESHANMGQAEtlNK 77
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRkkledsgvivlvGSHNSPSPKGVGYAK--NQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  78 GWRLSKGEILAYLSADDKLTPNATSLSVATLMQNPeviltyadNLLINSESQPIRKLLTPEFNHY-------QMYLNATT 150
Cdd:cd06913    79 AIAQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHP--------NSIIGCQVRRIPEDSTERYTRWintltreQLLTQVYT 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1540053721 151 ---PVAVAS--FFRRKAFEQLGGWDKNYRQI-GDYEYHLRLIRM-GDFKRIPQILGYHRVHEKSASYA 211
Cdd:cd06913   151 shgPTVIMPtwFCSREWFSHVGPFDEGGKGVpEDLLFFYEHLRKgGGVYRVDRCLLLYRYHPGATTHS 218
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 10-209 1.44e-13

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: 69.61  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNG--MPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRY---EGQFYY--ESHANMGQAETLNKGWRLS 82
Cdd:pfam10111   1 SVVIPVYNGekTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIkdhNLQVYYpnAPDTTYSLAASRNRGTSHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  83 KGEILAYLSADDKLTPN--ATSLSVAT---LMQNPEVILTYADNLLINSESQPIRK---------LLTPEFNHYQMYLNA 148
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDkfEKQLKIATslaLQENIQAAVVLPVTDLNDESSNFLRRggdltasgdVLRDLLVFYSPLAIF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1540053721 149 TTPVAVASFFRRKAFEQLGGWDKNYRQIG--DYEYHLRL-IRMGDFKRIPQILGYhRVHEKSAS 209
Cdd:pfam10111 161 FAPNSSNALINRQAFIEVGGFDESFRGHGaeDFDIFLRLaARYPFVAVMPPQLLY-RLSAKSMS 223
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
7-259 2.59e-13

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 68.87  E-value: 2.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTdgSMELLRRYEGQF------YYESHANMGQAETLNKGWR 80
Cdd:PRK10018    5 PLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTALndpritYIHNDINSGACAVRNQAIM 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  81 LSKGEILAYLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSE--SQPIRKLLTPEfnhyqmylnatTPVAVASFF 158
Cdd:PRK10018   83 LAQGEYITGIDDDDEWTPNRLSVFLAHKQQLVTHAFLYANDYVCQGEvySQPASLPLYPK-----------SPYSRRLFY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721 159 RRKAF-EQLGGW---------DKNYRQIGDYEYHLRL-IRMGD---FKRIPQIL-----------------GYHRVHEKS 207
Cdd:PRK10018  152 KRNIIgNQVFTWawrfkeclfDTELKAAQDYDIFLRMvVEYGEpwkVEEATQILhinhgemqitsspkkfsGYFHFYRKH 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1540053721 208 asyaKMNFERADEYKQLLTsvieqcqdnyLLELKNKvlsqaylisgRTHWRS 259
Cdd:PRK10018  232 ----KDKFDRASKKYQLFT----------LYQIRNK----------RMTWRT 259
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 10-202 1.43e-12

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: 65.41  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNG--MPYLEEAIESVLAQDYPNIELIVLDDGS-TDGSMELLRRYEGQFYYESHA---NMGQAETLNKGWRLSK 83
Cdd:cd04195     1 SVLMSVYIKekPEFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPlekNRGLGKALNEGLKHCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  84 GEILAYLSADDKLTPNATSLSVATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNH--YQMYLNAtTPV---AVAsfF 158
Cdd:cd04195    81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRRLPTSHDdiLKFARRR-SPFnhpTVM--F 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1540053721 159 RRKAFEQLGGWdKNYRQIGDYEYHLRLIRMG-DFKRIPQILGYHR 202
Cdd:cd04195   158 RKSKVLAVGGY-QDLPLVEDYALWARMLANGaRFANLPEILVKAR 201
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 11-104 1.93e-12

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: 65.28  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNG----MPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF-----YYESHANMGQAETLNKGWRL 81
Cdd:cd04188     1 VVIPAYNEekrlPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNpalirVLTLPKNRGKGGAVRAGMLA 80

                          90       100
                  ....*....|....*....|...
gi 1540053721  82 SKGEILAYLSADdkltpNATSLS 104
Cdd:cd04188    81 ARGDYILFADAD-----LATPFE 98
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 11-93 2.12e-12

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: 64.52  E-value: 2.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLA--QDYPNIELIVLDDGSTDGSMELLRRY---EGQFYYESHA-NMGQAETLNKGWRLSKG 84
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELaarVPRVRVIRLSrNFGKGAAVRAGFKAARG 80


                  ....*....
gi 1540053721  85 EILAYLSAD 93
Cdd:cd04179    81 DIVVTMDAD 89
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 7-189 8.18e-12

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: 63.93  E-value: 8.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGS----MELLRRYEGQ-----FYYESHANMGQAETLNK 77
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETldvaEEIAARFPDVrlrviRNARLLGPTGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  78 GWRLSKGEILAYLSADDKLTPNATSLSVATLMQNPEVILT---YADNLlinsesqpiRKLLTP----EFNHYQMY----- 145
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGtpvFSLNR---------STMLSAlgalEFALRHLRmmslr 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1540053721 146 --LNATTPVAVASFFRRKAFEQLGGWDKNYRQIGDYEYHLRLIRMG 189
Cdd:pfam13641 153 laLGVLPLSGAGSAIRREVLKELGLFDPFFLLGDDKSLGRRLRRHG 198
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 11-56 4.29e-11

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: 60.95  E-value: 4.29e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1540053721  11 IVIPCYNGMPYLEE---AIESVLAQDYPNIELIVLDDGSTDGSMELLRR 56
Cdd:cd04187     1 IVVPVYNEEENLPElyeRLKAVLESLGYDYEIIFVDDGSTDRTLEILRE 49
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 10-189 6.01e-11

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: 61.65  E-value: 6.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYNGMP-YLEEAIESVLAQDYPNIELIVLDDGSTDGSM---------ELLRRYegQFYYESHANMGQAETLNKGW 79
Cdd:cd06435     1 SIHVPCYEEPPeMVKETLDSLAALDYPNFEVIVIDNNTKDEALwkpveahcaQLGERF--RFFHVEPLPGAKAGALNYAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  80 RLSKG--EILAYLSADDKLTPNATSlSVATLMQNPEVILTYADNLLINSESQPIRKLLTPE---FNHYQMYL----NATT 150
Cdd:cd06435    79 ERTAPdaEIIAVIDADYQVEPDWLK-RLVPIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEykgFFDIGMVSrnerNAII 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1540053721 151 PVAVASFFRRKAFEQLGGWDKnYRQIGDYEYHLRLIRMG 189
Cdd:cd06435   158 QHGTMCLIRRSALDDVGGWDE-WCITEDSELGLRMHEAG 195
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-217 4.22e-09

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: 55.72  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  12 VIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRR--YEGQFYYES-HANMGQAETLNKGWRLSKGEILA 88
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSlgDLDNIVYLRlPENLGGAGGFYEGVRRAYELGYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  89 YLS-ADDKLTPNATSLSvatlmqnpeviltyadnLLINSESQPIRKLLTPefnhyqMYLNATTPVaVASFFRRKAFEQLG 167
Cdd:cd04185    82 WIWlMDDDAIPDPDALE-----------------KLLAYADKDNPQFLAP------LVLDPDGSF-VGVLISRRVVEKIG 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1540053721 168 --------GWDknyrqigDYEYHLRLIRMGDFKRIPQILGYHRVHEKSASYAKMNFER 217
Cdd:cd04185   138 lpdkeffiWGD-------DTEYTLRASKAGPGIYVPDAVVVHKTAINKGSSAVVNIDP 188
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 7-169 1.84e-07

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: 51.16  E-value: 1.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPN--IELIVLDDgSTDGSMELLRRYEGQFY-------YESHANMG--QAETL 75
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKdrLEIQVLDD-STDETVRLAREIVEEYAaqgvnikHVRRADRTgyKAGAL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  76 NKGWRLSKGEILAYLSADdkLTPNATSLS-VATLMQNPEVILTYADNLLINSESQPIRKLLTPEFNHYQMY--------- 145
Cdd:cd06437    80 AEGMKVAKGEYVAIFDAD--FVPPPDFLQkTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIeqvarsstg 157

                         170       180
                  ....*....|....*....|....*...
gi 1540053721 146 ----LNATtpvavASFFRRKAFEQLGGW 169
Cdd:cd06437   158 lffnFNGT-----AGVWRKECIEDAGGW 180
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 11-93 2.06e-07

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: 50.27  E-value: 2.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQF----YYESHANMG--QAETLNKGWRLSKG 84
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFpipiKHVWQEDEGfrKAKIRNKAIAAAKG 80


                  ....*....
gi 1540053721  85 EILAYLSAD 93
Cdd:cd06420    81 DYLIFIDGD 89
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 9-100 7.29e-07

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: 49.21  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   9 VSIVIPCYNGMPYLEEAIESVL-AQDypniELIVLDDGSTDGSMELLRRYEGQFYYesHANMGQAETLNKGWRLSKGE-I 86
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKwAVD----EIIVVDSGSTDRTVEIAKEYGAKVYQ--RWWDGFGAQRNFALELATNDwV 75

                          90
                  ....*....|....
gi 1540053721  87 LaYLSADDKLTPNA 100
Cdd:cd02511    76 L-SLDADERLTPEL 88
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 11-93 2.93e-06

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: 47.67  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLAQDYP--NIELIVLDDGSTDGSMELL--RRYEGQFY------YESHANmGQAETLNKGWR 80
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPkeKFEVILVDDHSTDGTVQILefAAAKPNFQlkilnnSRVSIS-GKKNALTTAIK 79

                          90
                  ....*....|...
gi 1540053721  81 LSKGEILAYLSAD 93
Cdd:cd04192    80 AAKGDWIVTTDAD 92
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 7-169 6.42e-06

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: 46.41  E-value: 6.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYN-GMPYLEEAIESVLAQDYPNIEL--IVLDDGSTDGSMELLRRYEGQFYYES-------HANMGQaetLN 76
Cdd:cd06421     1 PTVDVFIPTYNePLEIVRKTLRAALAIDYPHDKLrvYVLDDGRRPELRALAAELGVEYGYRYltrpdnrHAKAGN---LN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  77 KGWRLSKGEILAYLSADDKLTPNATSLSVATLMQNPEVILT----YADNllINSESQPIRKLLTPE--FNHYQM----YL 146
Cdd:cd06421    78 NALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVqtpqFFYN--PDPFDWLADGAPNEQelFYGVIQpgrdRW 155

                         170       180
                  ....*....|....*....|...
gi 1540053721 147 NATTPVAVASFFRRKAFEQLGGW 169
Cdd:cd06421   156 GAAFCCGSGAVVRREALDEIGGF 178
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 9-121 8.37e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 46.65  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   9 VSIVIPCYNGMPYLEEAIESVLA------QDYpniELIVLDDGSTDGSMELLRRYEGQfyYESHA-------NMGQAETL 75
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRRTTAaceslgKEY---EILLIDDGSSDNSAEMLVEAAQA--PDSHIvaillnrNYGQHSAI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1540053721  76 NKGWRLSKGEILAYLSADDKLTPNATSLSVATLMQNPEVILTYADN 121
Cdd:PRK10714   83 MAGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQN 128
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 9-102 1.47e-05

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: 45.32  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   9 VSIVIPCYNGMP-YLEEAIESVLAQDypNIELIVLDDGSTDG---SMELLRRYEGQF-YYESHAnmGQAETLNKGWRLSK 83
Cdd:cd06434     2 VTVIIPVYDEDPdVFRECLRSILRQK--PLEIIVVTDGDDEPylsILSQTVKYGGIFvITVPHP--GKRRALAEGIRHVT 77

                          90
                  ....*....|....*....
gi 1540053721  84 GEILAYLSADDKLTPNATS 102
Cdd:cd06434    78 TDIVVLLDSDTVWPPNALP 96
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 11-93 2.01e-05

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: 44.83  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYN---GMPYLEEAIESVLAQdyPNIELIVLDDGSTDGSMELLRRYEGQFYYESH------ANMGQAETlnKGWRL 81
Cdd:cd06442     1 IIIPTYNereNIPELIERLDAALKG--IDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLivrpgkRGLGSAYI--EGFKA 76

                          90
                  ....*....|..
gi 1540053721  82 SKGEILAYLSAD 93
Cdd:cd06442    77 ARGDVIVVMDAD 88
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 7-189 5.04e-05

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: 43.78  E-value: 5.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVL-----DDGSTDGSMELLRRyegqfyyESHANM-----GQAET-- 74
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKllleeDDEETIAAARALRL-------PSIFRVvvvppSQPRTkp 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  75 --LNKGWRLSKGEILAYLSADDKLTPNATSLSVATLMQNPEVI------LTYAdnlliNSESQPIRKLLTPEF-NHYQMY 145
Cdd:cd06427    74 kaCNYALAFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDKLacvqapLNYY-----NARENWLTRMFALEYaAWFDYL 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1540053721 146 L------NATTPVAVAS-FFRRKAFEQLGGWDKnYRQIGDYEYHLRLIRMG 189
Cdd:cd06427   149 LpglarlGLPIPLGGTSnHFRTDVLRELGGWDP-FNVTEDADLGLRLARAG 198
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 7-114 6.72e-04

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: 40.27  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   7 PLVSIVIPCYNGMPYLEEAIESVLAQDYPNIELIVLDDGSTDGSMELLRRYEGQFYY---------ESHANMGQAETLNK 77
Cdd:cd02520     1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNvdarlliggEKVGINPKVNNLIK 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1540053721  78 GWRLSKGEILAYLSADDKLTPNATSLSVATLMqNPEV 114
Cdd:cd02520    81 GYEEARYDILVISDSDISVPPDYLRRMVAPLM-DPGV 116
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 9-93 1.51e-03

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 39.90  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721   9 VSIVIPCYNgmpylEEA-----IESVLAQ-DYPNI-ELIVLDDGSTDGSMELLRRYEGQFYYESHANMGQAETLNKG--- 78
Cdd:PRK13915   33 VSVVLPALN-----EEEtvgkvVDSIRPLlMEPLVdELIVIDSGSTDATAERAAAAGARVVSREEILPELPPRPGKGeal 107

                          90
                  ....*....|....*...
gi 1540053721  79 WR---LSKGEILAYLSAD 93
Cdd:PRK13915  108 WRslaATTGDIVVFVDAD 125
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 10-93 1.69e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 39.75  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  10 SIVIPCYN-----------GMPYLEEAIESVLAQDYpniELIVLDDGSTDGSMELLRRYEGQFYYES--------HANMG 70
Cdd:PTZ00260   73 SIVIPAYNeedrlpkmlkeTIKYLESRSRKDPKFKY---EIIIVNDGSKDKTLKVAKDFWRQNINPNidirllslLRNKG 149

                          90       100
                  ....*....|....*....|...
gi 1540053721  71 QAETLNKGWRLSKGEILAYLSAD 93
Cdd:PTZ00260  150 KGGAVRIGMLASRGKYILMVDAD 172
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 11-168 2.30e-03

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: 38.52  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  11 IVIPCYNGMPYLEEAIESVLAqDYPNIELIVLDDGSTDGSME------------LLRRyegqfyYESHANMGQAETLNKG 78
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLR-NKPNFLVLVIDDASDDDTAGivrlaitdsrvhLLRR------HLPNARTGKGDALNAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1540053721  79 W------RLSKG-----EILAYLSADDKLTPNATSlSVATLMQNPEVILTYADNLLINSESQPIRKLLTPEF----NHYQ 143
Cdd:cd06436    74 YdqirqiLIEEGadperVIIAVIDADGRLDPNALE-AVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFfiiiAATQ 152

                         170       180
                  ....*....|....*....|....*...
gi 1540053721 144 MYLNATTPVAVA---SFFRRKAFEQLGG 168
Cdd:cd06436   153 SLRALTGTVGLGgngQFMRLSALDGLIG 180
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 7-55 6.81e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 37.37  E-value: 6.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1540053721   7 PLVSIVIPCYN---GMPYLEEAIESVLaQDYPNIELIVLDDGSTDGSMELLR 55
Cdd:PLN02726    9 MKYSIIVPTYNerlNIALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVK 59
 
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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