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Conserved domains on  [gi|123796900|sp|Q3U129|]
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RecName: Full=Queuosine-tRNA galactosyltransferase; Short=QTGAL; AltName: Full=UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like protein 1; Short=BGnT-like protein 1; Short=Beta1,3-N-acetylglucosaminyltransferase-like protein 1; Short=Beta3Gn-T-like protein 1; Short=Beta3GnTL1

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 1.80e-166

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: 463.08  E-value: 1.80e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDFEGAMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDSPSPRGVGYSKNQAV 97
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTERYTRWINHLTSDQLLTQVFTSHGPTVIMPT 177
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123796900 178 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLYAATHSV 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 1.80e-166

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: 463.08  E-value: 1.80e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDFEGAMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDSPSPRGVGYSKNQAV 97
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTERYTRWINHLTSDQLLTQVFTSHGPTVIMPT 177
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123796900 178 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLYAATHSV 236
Cdd:cd06913  161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 15-228 3.84e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.93  E-value: 3.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  15 LVSIILPVHNAEQWLDECLMSVLQQDFEGAmELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSPRGVGYSKN 94
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDF-EIIVVDDGSTDGTAEILRELAAK--DPRIRVI----RLERNRGKGAARN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  95 QAVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDppDSTERYTRWINHLTS-DQLLTQVFTSHGPTV 173
Cdd:COG0463   76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIR--EGESDLRRLGSRLFNlVRLLTNLPDSTSGFR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 123796900 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 2.58e-24

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 97.47  E-value: 2.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900   17 SIILPVHNAEQWLDECLMSVLQQDFEgAMELSVFNDASKDKSRAIIEKWKVKleDSGISVVIgghdSPSPRGVGYSKNQA 96
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900   97 VAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTE--RYTRWINHLTSDQLLTQVFTSHGPTVI 174
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 123796900  175 MPTWFCSRAWFSH 187
Cdd:pfam00535 154 GGFALYRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 15-117 3.02e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.69  E-value: 3.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  15 LVSIILPVHNAEQWLDECLMSVLQQDFEgAMELSVFNDASKDKSRAIIEKWKVKL--------EDSGISVvigghdspsp 86
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYphvrllhqANAGVSV---------- 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 123796900  87 rgvgySKNQAVAQSTGSYLCFLDSDDVMMPQ 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 1.80e-166

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: 463.08  E-value: 1.80e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDFEGAMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDSPSPRGVGYSKNQAV 97
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNSPSPKGVGYAKNQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTERYTRWINHLTSDQLLTQVFTSHGPTVIMPT 177
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQVYTSHGPTVIMPT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 123796900 178 WFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFRVDHSLLLYRYHLYAATHSV 236
Cdd:cd06913  161 WFCSREWFSHVGPFDEGGKGVPEDLLFFYEHLRKGGGVYRVDRCLLLYRYHPGATTHSV 219
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 15-228 3.84e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.93  E-value: 3.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  15 LVSIILPVHNAEQWLDECLMSVLQQDFEGAmELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSPRGVGYSKN 94
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDF-EIIVVDDGSTDGTAEILRELAAK--DPRIRVI----RLERNRGKGAARN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  95 QAVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDppDSTERYTRWINHLTS-DQLLTQVFTSHGPTV 173
Cdd:COG0463   76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIR--EGESDLRRLGSRLFNlVRLLTNLPDSTSGFR 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 123796900 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 2.58e-24

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 97.47  E-value: 2.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900   17 SIILPVHNAEQWLDECLMSVLQQDFEgAMELSVFNDASKDKSRAIIEKWKVKleDSGISVVIgghdSPSPRGVGYSKNQA 96
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKK--DPRVRVIR----LPENRGKAGARNAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900   97 VAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTE--RYTRWINHLTSDQLLTQVFTSHGPTVI 174
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEyrRASRITLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 123796900  175 MPTWFCSRAWFSH 187
Cdd:pfam00535 154 GGFALYRREALEE 166
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 18-217 2.71e-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: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDFEgAMELSVFNDASKDKSRAIIEKWKVKledsGISVVIggHDSPSPRGVGYSKNQAV 97
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKK----DPRVIR--VINEENQGLAAARNAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPT-SIIGCQvrrdppdsterytrwinhltsdqlltqvftshgptvimP 176
Cdd:cd00761   74 KAARGEYILFLDADDLLLPDWLERLVAELLADPEaDAVGGP--------------------------------------G 115

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 123796900 177 TWFCSRAWFSHVGPFDEGGQGVPEDLLFFYEHLRKGGGVFR 217
Cdd:cd00761  116 NLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 17-228 1.99e-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: 85.29  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  17 SIILPVHNAEQWLDECLMSVLQQDFEgAMELSVFNDASKDKSRAIIEKWKVKL------EDSGISVVIgghdspsprgvg 90
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYP-NIEYIVIDGGSTDGTVDIIKKYEDKItywisePDKGIYDAM------------ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  91 yskNQAVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTS--IIGCQVRRDPPDSTERYTRWINHLTSDqLLTQVFTS 168
Cdd:cd06433   68 ---NKGIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVdvVYGDVLLVDENGRVIGRRRPPPFLDKF-LLYGMPIC 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123796900 169 HgptvimPTWFCSRAWFSHVGPFDE----GGqgvpeDLLFFYEHLRKGGGVFRVDHSLLLYRYH 228
Cdd:cd06433  144 H------QATFFRRSLFEKYGGFDEsyriAA-----DYDLLLRLLLAGKIFKYLPEVLAAFRLG 196
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 9-120 2.20e-17

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: 81.33  E-value: 2.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900   9 TRGSLALVSIILPVHNAEQWLDECLMSVLQQDF-EGAMELSVFNDASKDKSRAIIEKWkvKLEDSGISVVigghDSPSPR 87
Cdd:COG1215   24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpKEKLEVIVVDDGSTDETAEIAREL--AAEYPRVRVI----ERPENG 97

                         90       100       110
                 ....*....|....*....|....*....|...
gi 123796900  88 GVGYSKNQAVAQSTGSYLCFLDSDDVMMPQRVR 120
Cdd:COG1215   98 GKAAALNAGLKAARGDIVVFLDADTVLDPDWLR 130
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
16-245 1.50e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 74.26  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  16 VSIILPVHNAEQWLDECLMSVLQQDFEGAmELSVFNDASKDKSRAIIEKWKvkleDSGISVVigghDSPSPRGVGYSKNQ 95
Cdd:COG1216    5 VSVVIPTYNRPELLRRCLESLLAQTYPPF-EVIVVDNGSTDGTAELLAALA----FPRVRVI----RNPENLGFAAARNL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  96 AVAQSTGSYLCFLDSDDVMMPQrvrmqyeaagqhptsiigcqvrrdppdsterytrWInhltsDQLLTQVFtshgptvim 175
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPD----------------------------------WL-----ERLLAAAC--------- 107

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 123796900 176 ptWFCSRAWFSHVGPFDE--GGQGvpEDLLFFYEHLRKGGGVFRVDHSLLlyrYHLYAATHSVLEMTIWTHR 245
Cdd:COG1216  108 --LLIRREVFEEVGGFDErfFLYG--EDVDLCLRLRKAGYRIVYVPDAVV---YHLGGASSGPLLRAYYLGR 172
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 15-117 3.02e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.69  E-value: 3.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  15 LVSIILPVHNAEQWLDECLMSVLQQDFEgAMELSVFNDASKDKSRAIIEKWKVKL--------EDSGISVvigghdspsp 86
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYphvrllhqANAGVSV---------- 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 123796900  87 rgvgySKNQAVAQSTGSYLCFLDSDDVMMPQ 117
Cdd:PRK10073  76 -----ARNTGLAVATGKYVAFPDADDVVYPT 101
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 16-204 2.56e-10

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: 59.51  E-value: 2.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  16 VSIILPVHNAEQWLDECLmSVLQQDFEGAMELSVFNDASKDKSRAIIEKWKVkledsgisVVIgghdsPSPRGVGYSKNQ 95
Cdd:cd02522    1 LSIIIPTLNEAENLPRLL-ASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGV--------VVI-----SSPKGRARQMNA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  96 AVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTER--------YTRWINHLTSDQLLtqvft 167
Cdd:cd02522   67 GAAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDDPGPRLRllelganlRSRLFGLPYGDQGL----- 141

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 123796900 168 shgptvimptwFCSRAWFSHVGPFDEggqgVP--EDLLF 204
Cdd:cd02522  142 -----------FIRRELFEELGGFPE----LPlmEDVEL 165
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 17-228 3.00e-10

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: 59.18  E-value: 3.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  17 SIILPVHNAEQWLDECLMSVLQQDFEGAmELSVFNDASKDKSRAIIEKWkVKLEDSGISVVIGGHdspsprGVGYSKN-- 94
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKND-ELIISDDGSTDGTVEIIKEY-IDKDPFIIILIRNGK------NLGVARNfe 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  95 QAVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHP--------TSII---GCQVRRDPPDsterYTRWINHLTSDQLLT 163
Cdd:cd04196   73 SLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKDDkpllvysdLELVdenGNPIGESFFE----YQKIKPGTSFNNLLF 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 123796900 164 QVFTShGPTVIMptwfcSRAWFSHVGPFDEGGQGVPEDLLffYEHLRKGGGVFRVDHSLLLYRYH 228
Cdd:cd04196  149 QNVVT-GCTMAF-----NRELLELALPFPDADVIMHDWWL--ALLASAFGKVVFLDEPLILYRQH 205
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 15-227 5.78e-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: 59.17  E-value: 5.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  15 LVSIILPVHNAEQWLDECLMSVLQQDFE-GAMELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSpRGVGYSK 93
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYPkDLIEIIVVDGGSTDGTREIVQEYAAK--DPRIRLI----DNPK-RIQSAGL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  94 NQAVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDSTERYTRWI----------NHLTSDqlLT 163
Cdd:cd02525   74 NIGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQKAIAVAqssplgsggsAYRGGA--VK 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 123796900 164 QVFTSHGPTVIMPtwfcsRAWFSHVGPFDEgGQGVPEDLLFFYEhLRKGGGVFRVDHSLLLYRY 227
Cdd:cd02525  152 IGYVDTVHHGAYR-----REVFEKVGGFDE-SLVRNEDAELNYR-LRKAGYKIWLSPDIRVYYY 208
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 15-116 6.26e-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: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  15 LVSIILPVHNA-EQWLDECLMSVLQQDFEGaMELSVFNDASKDKSRAIIEKWkVKLEDSGISVVIgghdSPSPRGVGYSK 93
Cdd:cd04184    2 LISIVMPVYNTpEKYLREAIESVRAQTYPN-WELCIADDASTDPEVKRVLKK-YAAQDPRIKVVF----REENGGISAAT 75

                         90       100
                 ....*....|....*....|...
gi 123796900  94 NQAVAQSTGSYLCFLDSDDVMMP 116
Cdd:cd04184   76 NSALELATGEFVALLDHDDELAP 98
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 18-154 2.98e-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: 55.70  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDFEgAMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHdspspRGVGYSKNQAV 97
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN-----GGKAGALNAGL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 123796900  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTsIIGCQVRRDPPDSTERY-TRWIN 154
Cdd:cd06423   75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADPK-VGAVQGRVRVRNGSENLlTRLQA 131
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 16-120 3.30e-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: 56.82  E-value: 3.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  16 VSIILPVHNAEQWLDECLMSVLQQDFEG-AMELSVFNDASKDKSRAIIEKWkvklEDSGISVviggHDSPSPRGVGYSKN 94
Cdd:cd06439   31 VTIIIPAYNEEAVIEAKLENLLALDYPRdRLEIIVVSDGSTDGTAEIAREY----ADKGVKL----LRFPERRGKAAALN 102

                         90       100
                 ....*....|....*....|....*.
gi 123796900  95 QAVAQSTGSYLCFLDSDDVMMPQRVR 120
Cdd:cd06439  103 RALALATGEIVVFTDANALLDPDALR 128
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 18-138 7.89e-08

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 51.41  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDFEGAmELSVFNDASKDKSRAIIEKwkvklEDSGISVviggHDSPSPRGVGYSKNQAV 97
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGSVELLRE-----LFPEVRL----IRNGENLGFGAGNNQGI 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 123796900  98 AQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHP-TSIIGCQV 138
Cdd:cd04186   71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPdVGIVGPKV 112
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 18-111 4.26e-07

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 49.87  E-value: 4.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECL---MSVLQQDFEGAMELSVFNDASKDKSRAIIEKWKVKLedSGISVVIgghDSPSPRGVGYSKN 94
Cdd:cd04188    1 VVIPAYNEEKRLPPTLeeaVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKN--PALIRVL---TLPKNRGKGGAVR 75

                         90
                 ....*....|....*..
gi 123796900  95 QAVAQSTGSYLCFLDSD 111
Cdd:cd04188   76 AGMLAARGDYILFADAD 92
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
15-119 7.14e-07

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 49.99  E-value: 7.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  15 LVSIILPVHNAEQWLDECLMSVLQQDFEGaMELSVFNDASKDKSRaiIEKWKVKLEDSGISVVIGGHDSpsprGVGYSKN 94
Cdd:PRK10018   6 LISIYMPTWNRQQLAIRAIKSVLRQDYSN-WEMIIVDDCSTSWEQ--LQQYVTALNDPRITYIHNDINS----GACAVRN 78

                         90       100
                 ....*....|....*....|....*
gi 123796900  95 QAVAQSTGSYLCFLDSDDVMMPQRV 119
Cdd:PRK10018  79 QAIMLAQGEYITGIDDDDEWTPNRL 103
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 18-230 1.01e-06

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: 48.34  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQ---DFEgameLSVFNDASKDKSRAIIEKWKvkledsgisvviggHDSPSP------RG 88
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQsilPFE----VIIADDGSTEETKELIEEFK--------------SQFPIPikhvwqED 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  89 VGYSK----NQAVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAgQHPTSIIGCQVRRDPPdSTERYTRWINhltsdqlltq 164
Cdd:cd06420   63 EGFRKakirNKAIAAAKGDYLIFIDGDCIPHPDFIADHIELA-EPGVFLSGSRVLLNEK-LTERGIRGCN---------- 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123796900 165 vftshgptviMPTWfcsRAWFSHVGPFDEGGQG-VPEDLLFFYEHLRKGGGVFRVDHSLLLyrYHLY 230
Cdd:cd06420  131 ----------MSFW---KKDLLAVNGFDEEFTGwGGEDSELVARLLNSGIKFRKLKFAAIV--FHLW 182
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 16-236 1.76e-06

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: 48.52  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900   16 VSIILPVHNAEQWLDECLMSVLQQDFeGAMELSVFNDASKDKSRAIIEKWKVKLEDSGISVVIGGHDsPSPRGVGYSKNQ 95
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPY-PPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARL-LGPTGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900   96 AVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSIIGCQVRRDPPDST------ERYTRWINHLTSDQLLTQVFTSH 169
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRSTMlsalgaLEFALRHLRMMSLRLALGVLPLS 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 123796900  170 GPTVIMPtwfcsRAWFSHVGPFDEGGqGVPEDLLFFYEHLRKGGGVFrvdhslllyrYHLYAATHSV 236
Cdd:pfam13641 162 GAGSAIR-----REVLKELGLFDPFF-LLGDDKSLGRRLRRHGWRVA----------YAPDAAVRTV 212
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 18-134 1.46e-05

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: 45.26  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDFEG-AMELSVFNDASKDKSRAIIEKWKVKleDSGISVVigghDSPSPRGVGYSKNQA 96
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGyDYEIIVVDDGSTDGTAEIARELAAR--VPRVRVI----RLSRNFGKGAAVRAG 74

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 123796900  97 VAQSTGSYLCFLDSDdvmmpqrvrmqyeaaGQHPTSII 134
Cdd:cd04179   75 FKAARGDIVVTMDAD---------------LQHPPEDI 97
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 17-157 4.82e-05

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: 43.84  E-value: 4.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  17 SIILPVHNAE--QWLDECLMSVLQQDFEGAMELSVFNDASKDKSRAIIEKWKVKLedsGISVVIgghdSPSPRGVGYSKN 94
Cdd:cd04195    1 SVLMSVYIKEkpEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFKRKL---PLKVVP----LEKNRGLGKALN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  95 QAVAQSTGSYLCFLDSDDVMMPQRVRMQYEAAGQHPTSII-GCQV------------RRDPP--DSTERYTRW---INHL 156
Cdd:cd04195   74 EGLKHCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIvGGGVlefdsdgndigkRRLPTshDDILKFARRrspFNHP 153


                 .
gi 123796900 157 T 157
Cdd:cd04195  154 T 154
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 18-117 2.94e-03

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 38.81  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDECLMSVLQQDF-EGAMELSVFNDASKDKSRAIIEkwkVKLEDSGISVVIGGHDSPSPRGVGYSKNQA 96
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYpKEKFEVILVDDHSTDGTVQILE---FAAAKPNFQLKILNNSRVSISGKKNALTTA 77

                         90       100
                 ....*....|....*....|.
gi 123796900  97 VAQSTGSYLCFLDSDDVMMPQ 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 3.43e-03

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: 37.84  E-value: 3.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  18 IILPVHNAEQWLDEC---LMSVLQQDFEgAMELsVF-NDASKDKSRAIIEKWkvKLEDSGIsvvigghdspspRGVGYSK 93
Cdd:cd04187    1 IVVPVYNEEENLPELyerLKAVLESLGY-DYEI-IFvDDGSTDRTLEILREL--AARDPRV------------KVIRLSR 64

                         90       100
                 ....*....|....*....|....*.
gi 123796900  94 N--QAVA------QSTGSYLCFLDSD 111
Cdd:cd04187   65 NfgQQAAllagldHARGDAVITMDAD 90
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 17-111 4.13e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 38.59  E-value: 4.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 123796900  17 SIILPVHNAEQWLDECLMSVLQ-----QDFEGAM--ELSVFNDASKDKSRAIIEKW--KVKLEDSGISVVigghDSPSPR 87
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETIKylesrSRKDPKFkyEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLL----SLLRNK 148

                         90       100
                 ....*....|....*....|....
gi 123796900  88 GVGYSKNQAVAQSTGSYLCFLDSD 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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