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Conserved domains on  [gi|1622882705|ref|XP_028692883|]
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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 isoform X7 [Macaca mulatta]

Protein Classification

queuosine-tRNA galactosyltransferase( domain architecture ID 10161044)

queuosine-tRNA galactosyltransferase (QTGAL) specifically catalyzes galactosylation of cytoplasmic tRNA(Tyr) modified with queuosine at position 34 (queuosine(34)). Galactosylates the cyclopentene hydroxyl group of queuosine(34) in tRNA(Tyr) to form galactosyl-queuosine(34)

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0141125|GO:0006417|GO:0006400
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
7-225 9.48e-164

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: 457.30  E-value: 9.48e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDSLSPRGVGYSKNQAV 86
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  87 AQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRRDPPNSTERYTRWINQLTPEQLLTQVFTANGPTVIMPT 166
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622882705 167 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVVRVDQSLLLYRYHPRAATHSV 225
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
7-225 9.48e-164

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: 457.30  E-value: 9.48e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDSLSPRGVGYSKNQAV 86
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  87 AQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRRDPPNSTERYTRWINQLTPEQLLTQVFTANGPTVIMPT 166
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622882705 167 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVVRVDQSLLLYRYHPRAATHSV 225
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
5-224 2.05e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 102.09  E-value: 2.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSVLQQDFEGtMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIigghdSLSP-RGVGYSKN 83
Cdd:COG0463     4 VSVVIPTYNEEEYLEEALESLLAQTYPD-FEIIVVDDGSTDGTAEILRELAAK--DPRIRVI-----RLERnRGKGAARN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  84 QAVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIV-GCRVRRDPPNSTERYTRWInqLTPEQLLTQVFTANGPTV 162
Cdd:COG0463    76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVyGSRLIREGESDLRRLGSRL--FNLVRLLTNLPDSTSGFR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622882705 163 IMptwfcSRAWFSHVGpFDEggqGVPEDLLFFYeHLRKGGGVVRVDqslllYRYHPRAATHS 224
Cdd:COG0463   154 LF-----RREVLEELG-FDE---GFLEDTELLR-ALRHGFRIAEVP-----VRYRAGESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
6-176 1.62e-23

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 95.92  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   6 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIIGGHDslspRGVGYSKNQA 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIRLPEN----RGKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  86 VAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRR--DPPNSTERYTRWINQLTPEQLLTQVFTANGPTVI 163
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVifGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 1622882705 164 MPTWFCSRAWFSH 176
Cdd:pfam00535 154 GGFALYRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
5-106 3.74e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.69  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKLEDsgVHVIigghdSLSPRGVGYSKNQ 84
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLL-----HQANAGVSVARNT 79
                          90       100
                  ....*....|....*....|..
gi 1622882705  85 AVAQSSGSYLCFLDSDDVMMPQ 106
Cdd:PRK10073   80 GLAVATGKYVAFPDADDVVYPT 101
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
7-225 9.48e-164

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: 457.30  E-value: 9.48e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDSLSPRGVGYSKNQAV 86
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  87 AQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRRDPPNSTERYTRWINQLTPEQLLTQVFTANGPTVIMPT 166
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622882705 167 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVVRVDQSLLLYRYHPRAATHSV 225
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
5-224 2.05e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 102.09  E-value: 2.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSVLQQDFEGtMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIigghdSLSP-RGVGYSKN 83
Cdd:COG0463     4 VSVVIPTYNEEEYLEEALESLLAQTYPD-FEIIVVDDGSTDGTAEILRELAAK--DPRIRVI-----RLERnRGKGAARN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  84 QAVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIV-GCRVRRDPPNSTERYTRWInqLTPEQLLTQVFTANGPTV 162
Cdd:COG0463    76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVyGSRLIREGESDLRRLGSRL--FNLVRLLTNLPDSTSGFR 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622882705 163 IMptwfcSRAWFSHVGpFDEggqGVPEDLLFFYeHLRKGGGVVRVDqslllYRYHPRAATHS 224
Cdd:COG0463   154 LF-----RREVLEELG-FDE---GFLEDTELLR-ALRHGFRIAEVP-----VRYRAGESKLN 200
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
7-206 3.37e-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: 97.19  E-value: 3.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKledsGVHVIIggHDSLSPRGVGYSKNQAV 86
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKK----DPRVIR--VINEENQGLAAARNAGL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  87 AQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPS-SIVGCRvrrdppnsterytrwinqltpeqlltqvftangptvimP 165
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELLADPEaDAVGGP--------------------------------------G 115
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1622882705 166 TWFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVVR 206
Cdd:cd00761   116 NLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
6-176 1.62e-23

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 95.92  E-value: 1.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   6 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIIGGHDslspRGVGYSKNQA 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIRLPEN----RGKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  86 VAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRR--DPPNSTERYTRWINQLTPEQLLTQVFTANGPTVI 163
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVifGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 1622882705 164 MPTWFCSRAWFSH 176
Cdd:pfam00535 154 GGFALYRREALEE 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-238 5.45e-18

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 81.58  E-value: 5.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   1 MQAHVSIILPVHNAEPWLDECLRSVLQQDFEGtMELSVFNDASKDKSGAIIEKWRvkleDSGVHVIIGGHdslsPRGVGY 80
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPP-FEVIVVDNGSTDGTAELLAALA----FPRVRVIRNPE----NLGFAA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  81 SKNQAVAQSSGSYLCFLDSDDVMMPQrvrlqhqaavqhpssivgcrvrrdppnsterytrWInqltpEQLLTQVFtangp 160
Cdd:COG1216    72 ARNLGLRAAGGDYLLFLDDDTVVEPD----------------------------------WL-----ERLLAAAC----- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705 161 tvimptWFCSRAWFSHVGPFDE--GGQGvpEDLLFFYEHLRKGGGVVRVDQSLLlyrYHPRAATHSVLETTIWTHRVRFL 238
Cdd:COG1216   108 ------LLIRREVFEEVGGFDErfFLYG--EDVDLCLRLRKAGYRIVYVPDAVV---YHLGGASSGPLLRAYYLGRNRLL 176
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
5-261 8.55e-18

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: 82.87  E-value: 8.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSVLQQDF-EGTMELSVFNDASKDKSGAIIEKWrvKLEDSGVHVIIGGHDslspRGVGYSKN 83
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYpKEKLEVIVVDDGSTDETAEIAREL--AAEYPRVRVIERPEN----GGKAAALN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  84 QAVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAvQHPSsiVGcrvrrdppnsterytrwinqltpeqlltqvftANGPTVI 163
Cdd:COG1215   105 AGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPG--VG--------------------------------ASGANLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705 164 MptwfcSRAWFSHVGPFDEGGQGvpEDLLFFYEHLRKGGGVVrvdqslllyrYHPRAATHSVLETTIWTHRVRFLeeqal 243
Cdd:COG1215   150 F-----RREALEEVGGFDEDTLG--EDLDLSLRLLRAGYRIV----------YVPDAVVYEEAPETLRALFRQRR----- 207
                         250
                  ....*....|....*...
gi 1622882705 244 pRWAAFTIWNAGKQGRRL 261
Cdd:COG1215   208 -RWARGGLQLLLKHRPLL 224
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
6-217 3.20e-16

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: 76.43  E-value: 3.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   6 SIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWrvklEDSGVHVIIGghdslsP-RGVGYSKNQ 84
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYP-NIEYIVIDGGSTDGTVDIIKKY----EDKITYWISE------PdKGIYDAMNK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  85 AVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSS--IVGCRVRRDPPNsterytRWINQLTPEQLLTQVFTANGPTV 162
Cdd:cd06433    70 GIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVdvVYGDVLLVDENG------RVIGRRRPPPFLDKFLLYGMPIC 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622882705 163 ImPTWFCSRAWFSHVGPFDE----GGqgvpeDLLFFYEHLRKGGGVVRVDQSLLLYRYH 217
Cdd:cd06433   144 H-QATFFRRSLFEKYGGFDEsyriAA-----DYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
PRK10073 PRK10073
putative glycosyl transferase; Provisional
5-106 3.74e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.69  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKLEDsgVHVIigghdSLSPRGVGYSKNQ 84
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLL-----HQANAGVSVARNT 79
                          90       100
                  ....*....|....*....|..
gi 1622882705  85 AVAQSSGSYLCFLDSDDVMMPQ 106
Cdd:PRK10073   80 GLAVATGKYVAFPDADDVVYPT 101
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-222 6.79e-12

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: 64.19  E-value: 6.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   6 SIILPVHNAEPWLDECLRSVLQQDFEGTmELSVFNDASKDKSGAIIEKWrVKLEDSGVHVIIGGHdslsprGVGYSKN-- 83
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKND-ELIISDDGSTDGTVEIIKEY-IDKDPFIIILIRNGK------NLGVARNfe 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  84 QAVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGC-RVRRDPPN------STERYTRWINQLTPEQLLTQVFt 156
Cdd:cd04196    73 SLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYsDLELVDENgnpigeSFFEYQKIKPGTSFNNLLFQNV- 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622882705 157 ANGPTVIMptwfcSRAWFSHVGPFDEGGQGVPEDLLffYEHLRKGGGVVRVDQSLLLYRYHPRAAT 222
Cdd:cd04196   152 VTGCTMAF-----NRELLELALPFPDADVIMHDWWL--ALLASAFGKVVFLDEPLILYRQHGNNVV 210
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
7-190 2.05e-11

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: 62.24  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHdslspRGVGYSKNQAV 86
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN-----GGKAGALNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  87 AQSSGSYLCFLDSDDVM---MPQRVRLQHQA-----AVQhpssiVGCRVRRDPPN-----STERYTRWINQLTP-EQLLT 152
Cdd:cd06423    75 RHAKGDIVVVLDADTILepdALKRLVVPFFAdpkvgAVQ-----GRVRVRNGSENlltrlQAIEYLSIFRLGRRaQSALG 149
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1622882705 153 QVFTANGPTVImptwFcSRAWFSHVGPFDEGGQGvpED 190
Cdd:cd06423   150 GVLVLSGAFGA----F-RREALREVGGWDEDTLT--ED 180
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
4-125 4.45e-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: 62.60  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   4 HVSIILPVHNAEPWLDECLRSVLQQDFEG-TMELSVFNDASKDKSGAIIEKWRvkleDSGVHVIIGGHDslspRGVGYSK 82
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDYPRdRLEIIVVSDGSTDGTAEIAREYA----DKGVKLLRFPER----RGKAAAL 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622882705  83 NQAVAQSSGSYLCFLDSDDVMMPQRVRLqhqaAVQH---PSsiVGC 125
Cdd:cd06439   102 NRALALATGEIVVFTDANALLDPDALRL----LVRHfadPS--VGA 141
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
5-105 5.62e-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: 58.37  E-value: 5.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNA-EPWLDECLRSVLQQDFEgTMELSVFNDASKDKSGAIIEKWRVKlEDSGVHVIIGGHDSlsprGVGYSKN 83
Cdd:cd04184     3 ISIVMPVYNTpEKYLREAIESVRAQTYP-NWELCIADDASTDPEVKRVLKKYAA-QDPRIKVVFREENG----GISAATN 76
                          90       100
                  ....*....|....*....|..
gi 1622882705  84 QAVAQSSGSYLCFLDSDDVMMP 105
Cdd:cd04184    77 SALELATGEFVALLDHDDELAP 98
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
5-219 1.62e-09

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: 58.01  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSVLQQDFEGT-MELSVFNDASKDKSGAIIEKWRVKLEDsgvHVIIGGHDSLSPRGVgyskN 83
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKDlIEIIVVDGGSTDGTREIVQEYAAKDPR---IRLIDNPKRIQSAGL----N 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  84 QAVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRRDPPNSTERYTRWInQLTPEQLLTQVF--TANGPT 161
Cdd:cd02525    75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVA-QSSPLGSGGSAYrgGAVKIG 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705 162 VIMPTWFC--SRAWFSHVGPFDEgGQGVPEDLLFFYEhLRKGGGVVRVDQSLLLYrYHPR 219
Cdd:cd02525   154 YVDTVHHGayRREVFEKVGGFDE-SLVRNEDAELNYR-LRKAGYKIWLSPDIRVY-YYPR 210
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-127 1.92e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 56.03  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDFEGTmELSVFNDASKDKSgaiIEKWRVKLEDsgVHVIIGGHdslsPRGVGYSKNQAV 86
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGS---VELLRELFPE--VRLIRNGE----NLGFGAGNNQGI 70
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622882705  87 AQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPS-SIVGCRV 127
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDvGIVGPKV 112
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
2-231 1.64e-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: 54.68  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   2 QAHVSIILPVHNAEPWLDECLRSVLQQDFeGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHVIIGGHDsLSPRGVGYS 81
Cdd:pfam13641   1 PPDVSVVVPAFNEDSVLGRVLEAILAQPY-PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARL-LGPTGKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  82 KNQAVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRRDPPNST------ERYTRWINQLTPEQLLTQVF 155
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMlsalgaLEFALRHLRMMSLRLALGVL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622882705 156 TANGPTVIMPtwfcsRAWFSHVGPFDEGGqGVPEDLLFFYEHLRKGGGVVrvdqslllyrYHPRAATHSVLETTIW 231
Cdd:pfam13641 159 PLSGAGSAIR-----REVLKELGLFDPFF-LLGDDKSLGRRLRRHGWRVA----------YAPDAAVRTVFPTYLA 218
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
5-193 4.55e-08

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 53.34  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSvLQQDFEGTMELSVFNDASKDKSGAIIekwrvklEDSGVHVIigghdsLSPRGVGYSKNQ 84
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLAS-LRRLNPLPLEIIVVDGGSTDGTVAIA-------RSAGVVVI------SSPKGRARQMNA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  85 AVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRRDPPNSTER--------YTRWINQLTPEQLLtqvft 156
Cdd:cd02522    67 GAAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDDPGPRLRllelganlRSRLFGLPYGDQGL----- 141
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1622882705 157 angptvimptwFCSRAWFSHVGPFDEggqgVP--EDLLF 193
Cdd:cd02522   142 -----------FIRRELFEELGGFPE----LPlmEDVEL 165
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
7-145 8.98e-08

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: 51.81  E-value: 8.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDFEG-TMELSVFNDASKDKSGAIIEKWRVKleDSGVHVIigghdSLSP-RGVGYSKNQ 84
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGyDYEIIVVDDGSTDGTAEIARELAAR--VPRVRVI-----RLSRnFGKGAAVRA 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622882705  85 AVAQSSGSYLCFLDSDdvmmpqrvrLQH---------QAAVQHPSSIV-GCRVRRDPPNSTERYTRWINQL 145
Cdd:cd04179    74 GFKAARGDIVVTMDAD---------LQHppedipkllEKLLEGGADVViGSRFVRGGGAGMPLLRRLGSRL 135
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
7-202 5.38e-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: 49.50  E-value: 5.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQ---DFEgtmeLSVFNDASKDKSGAIIEKWRvklEDSGVHVIIGGHDSlsprgVGYSK- 82
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQsilPFE----VIIADDGSTEETKELIEEFK---SQFPIPIKHVWQED-----EGFRKa 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  83 ---NQAVAQSSGSYLCFLDSDDVMMPQRVRlQHQAAVQHPSSIVGCRVRRDpPNSTERYTRWINqltpeqlltqvftang 159
Cdd:cd06420    69 kirNKAIAAAKGDYLIFIDGDCIPHPDFIA-DHIELAEPGVFLSGSRVLLN-EKLTERGIRGCN---------------- 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1622882705 160 ptviMPTWfcsRAWFSHVGPFDEGGQG-VPEDLLFFYEHLRKGG 202
Cdd:cd06420   131 ----MSFW---KKDLLAVNGFDEEFTGwGGEDSELVARLLNSGI 167
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
7-126 1.05e-06

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: 1.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAE----PWLDEcLRSVLQQDFEGTMELSVFNDASKDKSGAIIEKWRVKLEDSGVHViigghDSLSPRGVGYSK 82
Cdd:cd04188     1 VVIPAYNEEkrlpPTLEE-AVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVL-----TLPKNRGKGGAV 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622882705  83 NQAVAQSSGSYLCFLDSD------DVMmpqrvRLQHQAAVQHPSSIVGCR 126
Cdd:cd04188    75 RAGMLAARGDYILFADADlatpfeELE-----KLEEALKTSGYDIAIGSR 119
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
5-118 2.04e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 48.84  E-value: 2.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   5 VSIILPVHNAEPWLDECLRSVLQQDFEgTMELSVFNDASKdkSGAIIEKWRVKLEDSGVHVIiggHDSLSpRGVGYSKNQ 84
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYS-NWEMIIVDDCST--SWEQLQQYVTALNDPRITYI---HNDIN-SGACAVRNQ 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1622882705  85 AVAQSSGSYLCFLDSDDVMMPQR--VRLQH-QAAVQH 118
Cdd:PRK10018   80 AIMLAQGEYITGIDDDDEWTPNRlsVFLAHkQQLVTH 116
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
7-112 3.04e-05

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: 44.39  E-value: 3.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDEC---LRSVLQQDFEgTMELsVF-NDASKDKSGAIIEKWRvkLEDSGVHVIigghdSLSpRGVGYSK 82
Cdd:cd04187     1 IVVPVYNEEENLPELyerLKAVLESLGY-DYEI-IFvDDGSTDRTLEILRELA--ARDPRVKVI-----RLS-RNFGQQA 70
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1622882705  83 nqAV----AQSSGSYLCFLDSDdvmmpqrvrLQH 112
Cdd:cd04187    71 --ALlaglDHARGDAVITMDAD---------LQD 93
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-248 1.10e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 43.05  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   7 IILPVHNAEPWLDECLRSVLQQDF-EGTMELSVFNDASKDKSGAIIEKWRvklEDSGVHV-IIGGHD-SLSPRgvgysKN 83
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpKEKFEVILVDDHSTDGTVQILEFAA---AKPNFQLkILNNSRvSISGK-----KN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705  84 ---QAVAQSSGSYLCFLDSDDVMMPQRVRLQHQAAVQHPSSIVGCRVRRDPPNSTERYTRWINQLTPEQLLTQVFTANGP 160
Cdd:cd04192    73 altTAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLLAKFQRLDWLSLLGLIAGSFGLGKP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705 161 TVIMPTWFC-SRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVVRvdqslllYRYHPraathsvlETTIWTHRVRFLE 239
Cdd:cd04192   153 FMCNGANMAyRKEAFFEVGGFEGNDHIASGDDELLLAKVASKYPKVA-------YLKNP--------EALVTTQPVTSWK 217
                         250
                  ....*....|.
gi 1622882705 240 E--QALPRWAA 248
Cdd:cd04192   218 EllNQRKRWAS 228
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
6-100 1.74e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 40.14  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622882705   6 SIILPVHNAEPWLDECLRSVLQ-----QDFEGTM--ELSVFNDASKDKSGAIIEK-WRVKL-EDSGVHVIigghDSLSPR 76
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKylesrSRKDPKFkyEIIIVNDGSKDKTLKVAKDfWRQNInPNIDIRLL----SLLRNK 148
                          90       100
                  ....*....|....*....|....
gi 1622882705  77 GVGYSKNQAVAQSSGSYLCFLDSD 100
Cdd:PTZ00260  149 GKGGAVRIGMLASRGKYILMVDAD 172
 
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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