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Conserved domains on  [gi|1926944026|ref|XP_036919578|]
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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 isoform X6 [Sturnira hondurensis]

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 ...
 7-185 1.08e-128

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 cd06913:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 219  Bit Score: 364.47  E-value: 1.08e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDFEGPMELSVFNDASKDKSMAIVEKWKVTLEGSGIRVVIGGHDSPSPRGVGYSKNQAI 86
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  87 AQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTERYTRWINQLTSDQLLTQVFTSNGPTVIMPS 166
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                         170
                  ....*....|....*....
gi 1926944026 167 WFCSRAWFSHVGPFDEGGQ 185
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGK 179
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 7-185 1.08e-128

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: 364.47  E-value: 1.08e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDFEGPMELSVFNDASKDKSMAIVEKWKVTLEGSGIRVVIGGHDSPSPRGVGYSKNQAI 86
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  87 AQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTERYTRWINQLTSDQLLTQVFTSNGPTVIMPS 166
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                         170
                  ....*....|....*....
gi 1926944026 167 WFCSRAWFSHVGPFDEGGQ 185
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGK 179
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-189 1.42e-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: 1.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWkvTLEGSGIRVVigghDSPSPRGVGYSKNQ 84
Cdd:COG0463     4 VSVVIPTYNEEEYLEEALESLLAQTYP-DFEIIVVDDGSTDGTAEILREL--AAKDPRIRVI----RLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  85 AIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCqvRREPPNSTERYTRWINQLTS-DQLLTQVFTSNGPTVI 163
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG--SRLIREGESDLRRLGSRLFNlVRLLTNLPDSTSGFRL 154

                         170       180
                  ....*....|....*....|....*..
gi 1926944026 164 MpswfcSRAWFSHVGpFDEG-GQDHHL 189
Cdd:COG0463   155 F-----RREVLEELG-FDEGfLEDTEL 175
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-176 1.17e-24

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: 96.70  E-value: 1.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   6 SVILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWKvtLEGSGIRVVIgghdSPSPRGVGYSKNQA 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYA--KKDPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  86 IAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTE--RYTRWINQLTSDQLLTQVFTSNGPTVI 163
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 1926944026 164 MPSWFCSRAWFSH 176
Cdd:pfam00535 154 GGFALYRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-125 5.54e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 67.76  E-value: 5.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   2 ETQVSVILPVHDAEPWLDECLRSVLQQDFEGpMELSVFNDASKDKSMAIVEKWKVTLegSGIRVVigghDSPSpRGVGYS 81
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQTWTA-LEIIIVNDGSTDNSVEIAKHYAENY--PHVRLL----HQAN-AGVSVA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1926944026  82 KNQAIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGC 125
Cdd:PRK10073   77 RNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQC 120
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 7-185 1.08e-128

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: 364.47  E-value: 1.08e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDFEGPMELSVFNDASKDKSMAIVEKWKVTLEGSGIRVVIGGHDSPSPRGVGYSKNQAI 86
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  87 AQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTERYTRWINQLTSDQLLTQVFTSNGPTVIMPS 166
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                         170
                  ....*....|....*....
gi 1926944026 167 WFCSRAWFSHVGPFDEGGQ 185
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGK 179
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-189 1.42e-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: 1.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWkvTLEGSGIRVVigghDSPSPRGVGYSKNQ 84
Cdd:COG0463     4 VSVVIPTYNEEEYLEEALESLLAQTYP-DFEIIVVDDGSTDGTAEILREL--AAKDPRIRVI----RLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  85 AIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCqvRREPPNSTERYTRWINQLTS-DQLLTQVFTSNGPTVI 163
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG--SRLIREGESDLRRLGSRLFNlVRLLTNLPDSTSGFRL 154

                         170       180
                  ....*....|....*....|....*..
gi 1926944026 164 MpswfcSRAWFSHVGpFDEG-GQDHHL 189
Cdd:COG0463   155 F-----RREVLEELG-FDEGfLEDTEL 175
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-176 1.17e-24

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: 96.70  E-value: 1.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   6 SVILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWKvtLEGSGIRVVIgghdSPSPRGVGYSKNQA 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYA--KKDPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  86 IAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTE--RYTRWINQLTSDQLLTQVFTSNGPTVI 163
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 1926944026 164 MPSWFCSRAWFSH 176
Cdd:pfam00535 154 GGFALYRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-130 1.23e-24

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: 96.42  E-value: 1.23e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWKVTlegsGIRVVIggHDSPSPRGVGYSKNQAI 86
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKK----DPRVIR--VINEENQGLAAARNAGL 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1926944026  87 AQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHP-ASIVGCQ----VRRE 130
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELLADPeADAVGGPgnllFRRE 122
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 5-125 4.74e-19

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: 84.79  E-value: 4.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSVLQQDF-EGPMELSVFNDASKDKSMAIVEKWKvtLEGSGIRVVigghDSPSPRGVGYSKN 83
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYpKEKLEVIVVDDGSTDETAEIARELA--AEYPRVRVI----ERPENGGKAAALN 104

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1926944026  84 QAIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGC 125
Cdd:COG1215   105 AGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGA 146
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-105 3.91e-17

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 77.73  E-value: 3.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   1 METQVSVILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWKVtlegSGIRVVigghDSPSPRGVGY 80
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYP-PFEVIVVDNGSTDGTAELLAALAF----PRVRVI----RNPENLGFAA 71

                          90       100
                  ....*....|....*....|....*
gi 1926944026  81 SKNQAIAQSSGSYLCFLDADDVMMP 105
Cdd:COG1216    72 ARNLGLRAAGGDYLLFLDDDTVVEP 96
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 6-182 7.34e-15

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: 71.42  E-value: 7.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   6 SVILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWkvtlEGSGIRVVigghdSPSPRGVGYSKNQA 85
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYP-NIEYIVIDGGSTDGTVDIIKKY----EDKITYWI-----SEPDKGIYDAMNKG 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  86 IAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPAS--IVGCQVRREPPNSTERYTRWINQLTSDQLLTQVFTSngptvi 163
Cdd:cd06433    71 IALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVdvVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPICH------ 144

                         170
                  ....*....|....*....
gi 1926944026 164 mPSWFCSRAWFSHVGPFDE 182
Cdd:cd06433   145 -QATFFRRSLFEKYGGFDE 162
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-125 5.54e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 67.76  E-value: 5.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   2 ETQVSVILPVHDAEPWLDECLRSVLQQDFEGpMELSVFNDASKDKSMAIVEKWKVTLegSGIRVVigghDSPSpRGVGYS 81
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQTWTA-LEIIIVNDGSTDNSVEIAKHYAENY--PHVRLL----HQAN-AGVSVA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1926944026  82 KNQAIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGC 125
Cdd:PRK10073   77 RNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQC 120
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-143 3.82e-12

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: 63.40  E-value: 3.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWKVTLEGSGIRVVIGGHdspspRGVGYSKNQAI 86
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN-----GGKAGALNAGL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1926944026  87 AQSSGSYLCFLDADDVmMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTERY-TRWIN 143
Cdd:cd06423    75 RHAKGDIVVVLDADTI-LEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLlTRLQA 131
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 5-125 6.28e-11

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: 61.06  E-value: 6.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSVLQQDFEGP-MELSVFNDASKDKSMAIVEKWkvtlEGSGIRVviggHDSPSPRGVGYSKN 83
Cdd:cd06439    31 VTIIIPAYNEEAVIEAKLENLLALDYPRDrLEIIVVSDGSTDGTAEIAREY----ADKGVKL----LRFPERRGKAAALN 102

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1926944026  84 QAIAQSSGSYLCFLDAdDVMMPPRVRLQLEAAVQHPAsiVGC 125
Cdd:cd06439   103 RALALATGEIVVFTDA-NALLDPDALRLLVRHFADPS--VGA 141
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-127 8.90e-11

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: 59.11  E-value: 8.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSmaiVEKWKVTLEgsgiRVVIggHDSPSPRGVGYSKNQAI 86
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYP-DFEVIVVDNASTDGS---VELLRELFP----EVRL--IRNGENLGFGAGNNQGI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1926944026  87 AQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHP-ASIVGCQV 127
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPdVGIVGPKV 112
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 5-190 4.83e-10

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: 58.40  E-value: 4.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSVLQQDFE-GPMELSVFNDASKDKSMAIVEKWKVtlEGSGIRVVigghDSPSpRGVGYSKN 83
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPkDLIEIIVVDGGSTDGTREIVQEYAA--KDPRIRLI----DNPK-RIQSAGLN 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  84 QAIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTERYTRWINQ---LTSDQLLTQVFTSNGP 160
Cdd:cd02525    75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSsplGSGGSAYRGGAVKIGY 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1926944026 161 TVIMPSWFCSRAWFSHVGPFDEG---GQDHHLD 190
Cdd:cd02525   155 VDTVHHGAYRREVFEKVGGFDESlvrNEDAELN 187
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 5-105 6.14e-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: 57.60  E-value: 6.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDA-EPWLDECLRSVLQQDFEGpMELSVFNDASKDKSMAIVEKWKVTLEgSGIRVVIgghdSPSPRGVGYSKN 83
Cdd:cd04184     3 ISIVMPVYNTpEKYLREAIESVRAQTYPN-WELCIADDASTDPEVKRVLKKYAAQD-PRIKVVF----REENGGISAATN 76

                          90       100
                  ....*....|....*....|..
gi 1926944026  84 QAIAQSSGSYLCFLDADDVMMP 105
Cdd:cd04184    77 SALELATGEFVALLDHDDELAP 98
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-182 1.52e-09

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: 56.81  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSvLQQDFEGPMELSVFNDASKDKSMAIVEKwkvtlegSGIRVVigghdsPSPRGVGYSKNQ 84
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLAS-LRRLNPLPLEIIVVDGGSTDGTVAIARS-------AGVVVI------SSPKGRARQMNA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  85 AIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNSTER--------YTRWINQLTSDQLLtqvft 156
Cdd:cd02522    67 GAAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDDPGPRLRllelganlRSRLFGLPYGDQGL----- 141

                         170       180
                  ....*....|....*....|....*.
gi 1926944026 157 sngptvimpswFCSRAWFSHVGPFDE 182
Cdd:cd02522   142 -----------FIRRELFEELGGFPE 156
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-119 1.14e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 54.17  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   6 SVILPVHDAEPWLDECLRSVLQQDFEgPMELSVFNDASKDKSMAIVEKWKVTlEGSGIRVVIGGHdspsprGVGYSKN-- 83
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYK-NDELIISDDGSTDGTVEIIKEYIDK-DPFIIILIRNGK------NLGVARNfe 72

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1926944026  84 QAIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHP 119
Cdd:cd04196    73 SLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKDD 108
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-166 3.42e-08

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: 52.76  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSVLQQDFeGPMELSVFNDASKDKSMAIVEKWKVTLEGSGIRVVIGGHDsPSPRGVGYSKNQ 84
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPY-PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARL-LGPTGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  85 AIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHPASIVGCQVRREPPNST------ERYTRWINQLTSDQLLTQVFTSN 158
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMlsalgaLEFALRHLRMMSLRLALGVLPLS 161


                  ....*...
gi 1926944026 159 GPTVIMPS 166
Cdd:pfam13641 162 GAGSAIRR 169
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 7-100 5.36e-07

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: 49.10  E-value: 5.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAE----PWLDEcLRSVLQQDFEGPMELSVFNDASKDKSMAIVEK--WKVtleGSGIRVVigghDSPSPRGVGY 80
Cdd:cd04188     1 VVIPAYNEEkrlpPTLEE-AVEYLEERPSFSYEIIVVDDGSKDGTAEVARKlaRKN---PALIRVL----TLPKNRGKGG 72

                          90       100
                  ....*....|....*....|
gi 1926944026  81 SKNQAIAQSSGSYLCFLDAD 100
Cdd:cd04188    73 AVRAGMLAARGDYILFADAD 92
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 7-105 1.98e-05

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: 44.11  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDfEGPMELSVFNDASKDKSMAIVEKWKvtlegsgirvviggHDSPSP------RGVGY 80
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQS-ILPFEVIIADDGSTEETKELIEEFK--------------SQFPIPikhvwqEDEGF 65

                          90       100
                  ....*....|....*....|....*....
gi 1926944026  81 SK----NQAIAQSSGSYLCFLDADDVMMP 105
Cdd:cd06420    66 RKakirNKAIAAAKGDYLIFIDGDCIPHP 94
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 6-141 1.83e-04

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: 41.53  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   6 SVILPVHDAEP--WLDECLRSVLQQDfEGPMELSVFNDASKDKSM-AIVEKWKVTLegsGIRVVIgghdSPSPRGVGYSK 82
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQT-LPPDEVVLVKDGPVTQSLnEVLEEFKRKL---PLKVVP----LEKNRGLGKAL 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1926944026  83 NQAIAQSSGSYLCFLDADDVMMPPRVRLQLEAAVQHP-ASIVGCQV------------RREPPNSTE--RYTRW 141
Cdd:cd04195    73 NEGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPeIDIVGGGVlefdsdgndigkRRLPTSHDDilKFARR 146
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-187 3.68e-04

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: 41.11  E-value: 3.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   6 SVILPV--HDAEPWLDECLRsvLQQDFEGPM-ELSVFNDASKDKSMAIVEKWKvTLEGSgirvVIGGHDSPSPRGVGYSK 82
Cdd:pfam10111   1 SVVIPVynGEKTHWIQERIL--NQTFQYDPEfELIIINDGSTDKTLEEVSSIK-DHNLQ----VYYPNAPDTTYSLAASR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026  83 NQAIAQSSGSYLCFLDADDVMMPPRVRLQLEAAV-----QHPASIVGCQVRREPPNSTERYTRWINQLTSDQLLTQVFTS 157
Cdd:pfam10111  74 NRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIATslalqENIQAAVVLPVTDLNDESSNFLRRGGDLTASGDVLRDLLVF 153

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1926944026 158 NGPTVIM-----PSWFCSRAWFSHVGPFDEGGQDH 187
Cdd:pfam10111 154 YSPLAIFfapnsSNALINRQAFIEVGGFDESFRGH 188
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
5-118 5.50e-04

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 40.75  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEPWLDECLRSVLQQDFEGpMELSVFNDASKdkSMAIVEKWKVTLEGSGIRVVIGGHDSpsprGVGYSKNQ 84
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSN-WEMIIVDDCST--SWEQLQQYVTALNDPRITYIHNDINS----GACAVRNQ 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1926944026  85 AIAQSSGSYLCFLDADDVMMPPRVRLQL---EAAVQH 118
Cdd:PRK10018   80 AIMLAQGEYITGIDDDDEWTPNRLSVFLahkQQLVTH 116
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 5-107 7.07e-04

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: 39.93  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   5 VSVILPVHDAEP-WLDECLRSVLQQDfegPMELSVFNDASKDKSMAIVEKwkvtLEGSGIRVVIgghdsPSPRGvgySKN 83
Cdd:cd06434     2 VTVIIPVYDEDPdVFRECLRSILRQK---PLEIIVVTDGDDEPYLSILSQ----TVKYGGIFVI-----TVPHP---GKR 66

                          90       100
                  ....*....|....*....|....*...
gi 1926944026  84 QAIAQS----SGSYLCFLDaDDVMMPPR 107
Cdd:cd06434    67 RALAEGirhvTTDIVVLLD-SDTVWPPN 93
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 2-100 9.18e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 40.14  E-value: 9.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   2 ETQVSVILPVHDAEPWLDECLRSVLQ-----QDFEGPM--ELSVFNDASKDKSMAIVEKW--KVTLEGSGIRVVigghDS 72
Cdd:PTZ00260   69 DVDLSIVIPAYNEEDRLPKMLKETIKylesrSRKDPKFkyEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLL----SL 144

                          90       100
                  ....*....|....*....|....*...
gi 1926944026  73 PSPRGVGYSKNQAIAQSSGSYLCFLDAD 100
Cdd:PTZ00260  145 LRNKGKGGAVRIGMLASRGKYILMVDAD 172
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-127 4.14e-03

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: 37.65  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1926944026   7 VILPVHDAEPWLDECLRSVLQQDFEGP-MELSVFNDASKDKSMAIVEkwkVTLEGSGIRVVIGGHDSPSPRGVGYSKNQA 85
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKEkFEVILVDDHSTDGTVQILE---FAAAKPNFQLKILNNSRVSISGKKNALTTA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1926944026  86 IAQSSGSYLCFLDAdDVMMPP-----RVRLQLEAAVQHPASIVGCQV 127
Cdd:cd04192    78 IKAAKGDWIVTTDA-DCVVPSnwlltFVAFIQKEQIGLVAGPVIYFK 123
 
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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