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Conserved domains on  [gi|1958660088|ref|XP_038942443|]
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UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1 isoform X2 [Rattus norvegicus]

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
PubMed:  10521532|12691742|9445404|12200473|10508766
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 ...
 18-236 1.23e-168

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: 469.63  E-value: 1.23e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDFEGTMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDSPSPRGVGYSKNQAI 97
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDSTERYTRWINQLTSDQLLTQVFTSHGPTVIMPT 177
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660088 178 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLCAATHSV 236
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 ...
 18-236 1.23e-168

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: 469.63  E-value: 1.23e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDFEGTMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDSPSPRGVGYSKNQAI 97
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDSTERYTRWINQLTSDQLLTQVFTSHGPTVIMPT 177
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660088 178 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLCAATHSV 236
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 15-228 2.27e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.78  E-value: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  15 LVSIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSPRGVGYSKN 94
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYP-DFEIIVVDDGSTDGTAEILRELAAK--DPRIRVI----RLERNRGKGAARN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  95 QAIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDppDSTERYTRWINQLTS-DQLLTQVFTSHGPTV 173
Cdd:COG0463    76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIR--EGESDLRRLGSRLFNlVRLLTNLPDSTSGFR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958660088 174 IMptwfcSRAWFSHVGpFDEggqGVPEDLLFFYeHLRKGGGVFRVDHsllLYRYH 228
Cdd:COG0463   154 LF-----RREVLEELG-FDE---GFLEDTELLR-ALRHGFRIAEVPV---RYRAG 195
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 17-187 8.68e-25

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: 99.01  E-value: 8.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  17 SIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKleDSGISVVIgghdSPSPRGVGYSKNQA 96
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  97 IAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDSTE--RYTRWINQLTSDQLLTQVFTSHGPTVI 174
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 1958660088 175 MPTWFCSRAWFSH 187
Cdd:pfam00535 154 GGFALYRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 15-117 4.58e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.30  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  15 LVSIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKL--------EDSGISVvigghdspsp 86
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYphvrllhqANAGVSV---------- 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958660088  87 rgvgySKNQAIAQSTGSYLCFLDSDDVMMPQ 117
Cdd:PRK10073   76 -----ARNTGLAVATGKYVAFPDADDVVYPT 101
 
Name Accession Description Interval E-value
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 18-236 1.23e-168

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: 469.63  E-value: 1.23e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDFEGTMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDSPSPRGVGYSKNQAI 97
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDSTERYTRWINQLTSDQLLTQVFTSHGPTVIMPT 177
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958660088 178 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLCAATHSV 236
Cdd:cd06913   161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 15-228 2.27e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.78  E-value: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  15 LVSIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSPRGVGYSKN 94
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYP-DFEIIVVDDGSTDGTAEILRELAAK--DPRIRVI----RLERNRGKGAARN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  95 QAIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDppDSTERYTRWINQLTS-DQLLTQVFTSHGPTV 173
Cdd:COG0463    76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIR--EGESDLRRLGSRLFNlVRLLTNLPDSTSGFR 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958660088 174 IMptwfcSRAWFSHVGpFDEggqGVPEDLLFFYeHLRKGGGVFRVDHsllLYRYH 228
Cdd:COG0463   154 LF-----RREVLEELG-FDE---GFLEDTELLR-ALRHGFRIAEVPV---RYRAG 195
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 18-217 5.51e-25

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 99.50  E-value: 5.51e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKledsGISVVIggHDSPSPRGVGYSKNQAI 97
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKK----DPRVIR--VINEENQGLAAARNAGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHP-ASIIGCQvrrdppdsterytrwinqltsdqlltqvftshgptvimP 176
Cdd:cd00761    74 KAARGEYILFLDADDLLLPDWLERLVAELLADPeADAVGGP--------------------------------------G 115

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958660088 177 TWFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFR 217
Cdd:cd00761   116 NLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 17-187 8.68e-25

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: 99.01  E-value: 8.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  17 SIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKleDSGISVVIgghdSPSPRGVGYSKNQA 96
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  97 IAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDSTE--RYTRWINQLTSDQLLTQVFTSHGPTVI 174
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 1958660088 175 MPTWFCSRAWFSH 187
Cdd:pfam00535 154 GGFALYRREALEE 166
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 17-228 1.47e-19

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: 85.67  E-value: 1.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  17 SIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKL------EDSGISVVIgghdspsprgvg 90
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYP-NIEYIVIDGGSTDGTVDIIKKYEDKItywisePDKGIYDAM------------ 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  91 yskNQAIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPAS--IIGCQVRRDPPDSTERYTRWINQLTSDqLLTQVFTS 168
Cdd:cd06433    68 ---NKGIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVdvVYGDVLLVDENGRVIGRRRPPPFLDKF-LLYGMPIC 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958660088 169 HgptvimPTWFCSRAWFSHVGPFDE----GGqgvpeDLLFFYEHLRKGGGVFRVDHSLLLYRYH 228
Cdd:cd06433   144 H------QATFFRRSLFEKYGGFDEsyriAA-----DYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 9-136 2.62e-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: 84.41  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088   9 KRAPLALVSIILPVHNAEQWLDECLMSVLQQDF-EGTMELSVFNDASKDKSRAIIEKWkvKLEDSGISVVigghDSPSPR 87
Cdd:COG1215    24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpKEKLEVIVVDDGSTDETAEIAREL--AAEYPRVRVI----ERPENG 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958660088  88 GVGYSKNQAIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGC 136
Cdd:COG1215    98 GKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGA 146
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
16-235 1.30e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.64  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  16 VSIILPVHNAEQWLDECLMSVLQQDFEGtMELSVFNDASKDKSRAIIEKWKvkleDSGISVVigghDSPSPRGVGYSKNQ 95
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPP-FEVIVVDNGSTDGTAELLAALA----FPRVRVI----RNPENLGFAAARNL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  96 AIAQSTGSYLCFLDSDDVMMPQrvrmqyeaavqhpasiigcqvrrdppdsterytrWInqltsDQLLTQVFtshgptvim 175
Cdd:COG1216    76 GLRAAGGDYLLFLDDDTVVEPD----------------------------------WL-----ERLLAAAC--------- 107

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660088 176 ptWFCSRAWFSHVGPFDE--GGQGvpEDLLFFYEHLRKGGGVFRVDHSLLlyrYHLCAATHS 235
Cdd:COG1216   108 --LLIRREVFEEVGGFDErfFLYG--EDVDLCLRLRKAGYRIVYVPDAVV---YHLGGASSG 162
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 15-117 4.58e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.30  E-value: 4.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  15 LVSIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKL--------EDSGISVvigghdspsp 86
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYphvrllhqANAGVSV---------- 75

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958660088  87 rgvgySKNQAIAQSTGSYLCFLDSDDVMMPQ 117
Cdd:PRK10073   76 -----ARNTGLAVATGKYVAFPDADDVVYPT 101
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 17-228 6.65e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 61.49  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  17 SIILPVHNAEQWLDECLMSVLQQDFEGTmELSVFNDASKDKSRAIIEKWkVKLEDSGISVVIGGHdspsprGVGYSKN-- 94
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKND-ELIISDDGSTDGTVEIIKEY-IDKDPFIIILIRNGK------NLGVARNfe 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  95 QAIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHP--------ASII---GCQVRRDPPDsterYTRWINQLTSDQLLT 163
Cdd:cd04196    73 SLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKDDkpllvysdLELVdenGNPIGESFFE----YQKIKPGTSFNNLLF 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958660088 164 QVFTShGPTVIMptwfcSRAWFSHVGPFDEGGQGVPEDLLffYEHLRKGGGVFRVDHSLLLYRYH 228
Cdd:cd04196   149 QNVVT-GCTMAF-----NRELLELALPFPDADVIMHDWWL--ALLASAFGKVVFLDEPLILYRQH 205
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 15-116 7.04e-11

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: 61.06  E-value: 7.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  15 LVSIILPVHNA-EQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWkVKLEDSGISVVIgghdSPSPRGVGYSK 93
Cdd:cd04184     2 LISIVMPVYNTpEKYLREAIESVRAQTYP-NWELCIADDASTDPEVKRVLKK-YAAQDPRIKVVF----REENGGISAAT 75

                          90       100
                  ....*....|....*....|...
gi 1958660088  94 NQAIAQSTGSYLCFLDSDDVMMP 116
Cdd:cd04184    76 NSALELATGEFVALLDHDDELAP 98
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 15-227 1.47e-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: 61.09  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  15 LVSIILPVHNAEQWLDECLMSVLQQDFEGT-MELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSpRGVGYSK 93
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDlIEIIVVDGGSTDGTREIVQEYAAK--DPRIRLI----DNPK-RIQSAGL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  94 NQAIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDSTERYTRWI--------NQLTSDQLLTQV 165
Cdd:cd02525    74 NIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAqssplgsgGSAYRGGAVKIG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660088 166 FTSHGPTVIMPtwfcsRAWFSHVGPFDEgGQGVPEDLLFFYEhLRKGGGVFRVDHSLLLYRY 227
Cdd:cd02525   154 YVDTVHHGAYR-----REVFEKVGGFDE-SLVRNEDAELNYR-LRKAGYKIWLSPDIRVYYY 208
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 18-154 1.43e-09

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: 56.85  E-value: 1.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHdspspRGVGYSKNQAI 97
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN-----GGKAGALNAGL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958660088  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPaSIIGCQVRRDPPDSTERY-TRWIN 154
Cdd:cd06423    75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADP-KVGAVQGRVRVRNGSENLlTRLQA 131
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 16-153 2.10e-09

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: 57.59  E-value: 2.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  16 VSIILPVHNAEQWLDECLMSVLQQDFEG-TMELSVFNDASKDKSRAIIEKWkvklEDSGISVviggHDSPSPRGVGYSKN 94
Cdd:cd06439    31 VTIIIPAYNEEAVIEAKLENLLALDYPRdRLEIIVVSDGSTDGTAEIAREY----ADKGVKL----LRFPERRGKAAALN 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  95 QAIAQSTGSYLCFLDSDDVMMPQRVRmqyeAAVQHPAS-IIGC------QVRRDPPDSTE----RYTRWI 153
Cdd:cd06439   103 RALALATGEIVVFTDANALLDPDALR----LLVRHFADpSVGAvsgelvIVDGGGSGSGEglywKYENWL 168
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 16-204 2.39e-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: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  16 VSIILPVHNAEQWLDECLmSVLQQDFEGTMELSVFNDASKDKSRAIIEKWKVkledsgisVVIgghdsPSPRGVGYSKNQ 95
Cdd:cd02522     1 LSIIIPTLNEAENLPRLL-ASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGV--------VVI-----SSPKGRARQMNA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  96 AIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDSTER--------YTRWINQLTSDQLLtqvft 167
Cdd:cd02522    67 GAAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDDPGPRLRllelganlRSRLFGLPYGDQGL----- 141

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958660088 168 shgptvimptwFCSRAWFSHVGPFDEggqgVP--EDLLF 204
Cdd:cd02522   142 -----------FIRRELFEELGGFPE----LPlmEDVEL 165
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 18-138 4.19e-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: 55.26  E-value: 4.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDFEGTmELSVFNDASKDKSRAIIEKwkvklEDSGISVviggHDSPSPRGVGYSKNQAI 97
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGSVELLRE-----LFPEVRL----IRNGENLGFGAGNNQGI 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958660088  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHP-ASIIGCQV 138
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPdVGIVGPKV 112
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 16-216 6.48e-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: 6.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  16 VSIILPVHNAEQWLDECLMSVLQQDFeGTMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDsPSPRGVGYSKNQ 95
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPY-PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARL-LGPTGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  96 AIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASIIGCQVRRDPPDST------ERYTRWINQLTSDQLLTQVFTSH 169
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMlsalgaLEFALRHLRMMSLRLALGVLPLS 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958660088 170 GPTVIMPtwfcsRAWFSHVGPFDEGGqGVPEDLLFFYEHLRKGGGVF 216
Cdd:pfam13641 162 GAGSAIR-----REVLKELGLFDPFF-LLGDDKSLGRRLRRHGWRVA 202
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 18-111 1.48e-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: 51.41  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECL---MSVLQQDFEGTMELSVFNDASKDKSRAIIEKWKVKLedSGISVVIgghDSPSPRGVGYSKN 94
Cdd:cd04188     1 VVIPAYNEEKRLPPTLeeaVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKN--PALIRVL---TLPKNRGKGGAVR 75

                          90
                  ....*....|....*..
gi 1958660088  95 QAIAQSTGSYLCFLDSD 111
Cdd:cd04188    76 AGMLAARGDYILFADAD 92
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
15-119 2.95e-07

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 51.53  E-value: 2.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  15 LVSIILPVHNAEQWLDECLMSVLQQDFEgTMELSVFNDASKDKSRaiIEKWKVKLEDSGISVVIGGHDSpsprGVGYSKN 94
Cdd:PRK10018    6 LISIYMPTWNRQQLAIRAIKSVLRQDYS-NWEMIIVDDCSTSWEQ--LQQYVTALNDPRITYIHNDINS----GACAVRN 78

                          90       100
                  ....*....|....*....|....*
gi 1958660088  95 QAIAQSTGSYLCFLDSDDVMMPQRV 119
Cdd:PRK10018   79 QAIMLAQGEYITGIDDDDEWTPNRL 103
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 18-120 4.34e-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: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQ---DFEgtmeLSVFNDASKDKSRAIIEKWKvkledsgisvviggHDSPSP------RG 88
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQsilPFE----VIIADDGSTEETKELIEEFK--------------SQFPIPikhvwqED 62

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958660088  89 VGYSK----NQAIAQSTGSYLCFLDSDDVMMPQRVR 120
Cdd:cd06420    63 EGFRKakirNKAIAAAKGDYLIFIDGDCIPHPDFIA 98
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 18-167 1.67e-06

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: 47.95  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDFEG-TMELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSPRGVGYSKNQA 96
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGyDYEIIVVDDGSTDGTAEIARELAAR--VPRVRVI----RLSRNFGKGAAVRAG 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958660088  97 IAQSTGSYLCFLDSDDVMMPQRV-RMqYEAAVQHPASI-IGCQVRRDPPDSTERYTRWINQLTSdqLLTQVFT 167
Cdd:cd04179    75 FKAARGDIVVTMDADLQHPPEDIpKL-LEKLLEGGADVvIGSRFVRGGGAGMPLLRRLGSRLFN--FLIRLLL 144
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 17-152 1.97e-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: 41.92  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  17 SIILPVHNAE--QWLDECLMSVLQQDFEGTMELSVFNDASKDKSRAIIEKWKVKLedsGISVVIgghdSPSPRGVGYSKN 94
Cdd:cd04195     1 SVLMSVYIKEkpEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKL---PLKVVP----LEKNRGLGKALN 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958660088  95 QAIAQSTGSYLCFLDSDDVMMPQRVRMQYEAAVQHPASII-GCQV------------RRDPP--DSTERYTRW 152
Cdd:cd04195    74 EGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIvGGGVlefdsdgndigkRRLPTshDDILKFARR 146
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 18-117 7.07e-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: 40.73  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDECLMSVLQQDF-EGTMELSVFNDASKDKSRAIIEkwkVKLEDSGISVVIGGHDSPSPRGVGYSKNQA 96
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpKEKFEVILVDDHSTDGTVQILE---FAAAKPNFQLKILNNSRVSISGKKNALTTA 77

                          90       100
                  ....*....|....*....|.
gi 1958660088  97 IAQSTGSYLCFLDSDDVMMPQ 117
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSN 98
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 18-111 8.76e-04

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: 39.77  E-value: 8.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  18 IILPVHNAEQWLDEC---LMSVLQQDFEgTMELsVF-NDASKDKSRAIIEKWkvKLEDSGIsvvigghdspspRGVGYSK 93
Cdd:cd04187     1 IVVPVYNEEENLPELyerLKAVLESLGY-DYEI-IFvDDGSTDRTLEILREL--AARDPRV------------KVIRLSR 64

                          90       100
                  ....*....|....*....|....*.
gi 1958660088  94 N---QA-----IAQSTGSYLCFLDSD 111
Cdd:cd04187    65 NfgqQAallagLDHARGDAVITMDAD 90
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 17-111 5.23e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 38.59  E-value: 5.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660088  17 SIILPVHNAEQWLDECLMSVLQ-----QDFEGTM--ELSVFNDASKDKSRAIIEKW--KVKLEDSGISVVigghDSPSPR 87
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKylesrSRKDPKFkyEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLL----SLLRNK 148

                          90       100
                  ....*....|....*....|....
gi 1958660088  88 GVGYSKNQAIAQSTGSYLCFLDSD 111
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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