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Conserved domains on  [gi|818317757|gb|KKQ01261|]
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MAG: Glycosyltransferase, group 1 family protein [Candidatus Moranbacteria bacterium GW2011_GWD1_36_198]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135509)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-227 5.56e-42

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: 141.54  E-value: 5.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSATQEDMEMMMREDYADVKFFSFEKNVGFQALVKIGLDNSVGKYIL 84
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLA-QTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  85 MLNGDILVTPDSVTKMLEFLKTDASIGMVGPKllnfngtlqpscfrfykpitivyrrtflskfsfakkhldwflmkdydh 164
Cdd:cd04186   80 LLNPDTVVEPGALLELLDAAEQDPDVGIVGPK------------------------------------------------ 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818317757 165 sepkevdwIMGSAVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKVIYFPLVSMHHYH 227
Cdd:cd04186  112 --------VSGAFLLVRREVFEEVGGFDEDFFLYYEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
 
Name Accession Description Interval E-value
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-227 5.56e-42

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: 141.54  E-value: 5.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSATQEDMEMMMREDYADVKFFSFEKNVGFQALVKIGLDNSVGKYIL 84
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLA-QTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  85 MLNGDILVTPDSVTKMLEFLKTDASIGMVGPKllnfngtlqpscfrfykpitivyrrtflskfsfakkhldwflmkdydh 164
Cdd:cd04186   80 LLNPDTVVEPGALLELLDAAEQDPDVGIVGPK------------------------------------------------ 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818317757 165 sepkevdwIMGSAVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKVIYFPLVSMHHYH 227
Cdd:cd04186  112 --------VSGAFLLVRREVFEEVGGFDEDFFLYYEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-265 2.75e-37

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 130.50  E-value: 2.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   1 MELSIIVTSYRNPELLRVCLDSIRKCvTGIAYELIVADSA-TQEDMEMMMREDYADVKFFSFEKNVGFQALVKIGLDNSV 79
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQ-TYPPFEVIVVDNGsTDGTAELLAALAFPRVRVIRNPENLGFAAARNLGLRAAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  80 GKYILMLNGDILVTPDSVTKMLEFlktdasigmvgpkllnfngtlqpscfrfykpitivyrrtflskfsfakkhldwflm 159
Cdd:COG1216   82 GDYLLFLDDDTVVEPDWLERLLAA-------------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757 160 kdydhsepkevdwimgSAVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKVIYFPLVSMHHYHGKGSakGGVIRS 239
Cdd:COG1216  106 ----------------ACLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPLLRA 167
                        250       260
                 ....*....|....*....|....*.
gi 818317757 240 LLfnkytwiHIASGIKYFKKFLGKPL 265
Cdd:COG1216  168 YY-------LGRNRLLFLRKHGPRPL 186
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-150 1.01e-13

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: 67.42  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757    4 SIIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSA----TQEDMEMMMREDYaDVKFFSFEKNVGFQALVKIGLDNSV 79
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN-QTYPNFEIIVVDDGstdgTVEIAEEYAKKDP-RVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818317757   80 GKYILMLNGDILVTPDSVTKMLEFLK---TDASIGMVGPKLLNFNGTLQPSCFRFYKPITIVYRRTFLSKFSFA 150
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEedgADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL 152
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
3-107 1.16e-04

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 42.28  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757    3 LSIIVTSYRNPELLRVCLD--SIRKCvtgiAYELIVADSATQE-------DMEMMMredYADVKFFSFEKNVGFQALVKI 73
Cdd:TIGR04440   2 LTIIIPTYNRPEYLKRWLRyySDFGC----DYRIIIADSSDEKfnennlkVFKNYS---NPNITYLHYPDLGVPFYEKLL 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 818317757   74 GLDNSV-GKYILMLNGDILVTPDSVTKMLEFLKTD 107
Cdd:TIGR04440  75 DALEQVeTPYVVICADDDFIIPSGLTECLSFLEAN 109
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
3-113 6.64e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 40.52  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   3 LSIIVTSYRNPELLRVCLDSIRKCVTG-------IAYELIVADSATQEDMEMMMrEDYA--------DVKFFSFEKNVGF 67
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKETIKYLESrsrkdpkFKYEIIIVNDGSKDKTLKVA-KDFWrqninpniDIRLLSLLRNKGK 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 818317757  68 QALVKIGLDNSVGKYILMLNGDILVTPDSVTKMLEFL--KTDASIGMV 113
Cdd:PTZ00260 151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMlkIEQNGLGIV 198
 
Name Accession Description Interval E-value
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-227 5.56e-42

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: 141.54  E-value: 5.56e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSATQEDMEMMMREDYADVKFFSFEKNVGFQALVKIGLDNSVGKYIL 84
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLA-QTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  85 MLNGDILVTPDSVTKMLEFLKTDASIGMVGPKllnfngtlqpscfrfykpitivyrrtflskfsfakkhldwflmkdydh 164
Cdd:cd04186   80 LLNPDTVVEPGALLELLDAAEQDPDVGIVGPK------------------------------------------------ 111
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818317757 165 sepkevdwIMGSAVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKVIYFPLVSMHHYH 227
Cdd:cd04186  112 --------VSGAFLLVRREVFEEVGGFDEDFFLYYEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-265 2.75e-37

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 130.50  E-value: 2.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   1 MELSIIVTSYRNPELLRVCLDSIRKCvTGIAYELIVADSA-TQEDMEMMMREDYADVKFFSFEKNVGFQALVKIGLDNSV 79
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQ-TYPPFEVIVVDNGsTDGTAELLAALAFPRVRVIRNPENLGFAAARNLGLRAAG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  80 GKYILMLNGDILVTPDSVTKMLEFlktdasigmvgpkllnfngtlqpscfrfykpitivyrrtflskfsfakkhldwflm 159
Cdd:COG1216   82 GDYLLFLDDDTVVEPDWLERLLAA-------------------------------------------------------- 105
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757 160 kdydhsepkevdwimgSAVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKVIYFPLVSMHHYHGKGSakGGVIRS 239
Cdd:COG1216  106 ----------------ACLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASS--GPLLRA 167
                        250       260
                 ....*....|....*....|....*.
gi 818317757 240 LLfnkytwiHIASGIKYFKKFLGKPL 265
Cdd:COG1216  168 YY-------LGRNRLLFLRKHGPRPL 186
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-231 3.89e-22

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 90.92  E-value: 3.89e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   1 MELSIIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSATQEDMEMMMRE---DYADVKFFSFEKNVGFQALVKIGLDN 77
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLA-QTYPDFEIIVVDDGSTDGTAEILRElaaKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  78 SVGKYILMLNGDILVTPDSVTKMLEFLKTDaSIGMVgpkllnfngtlqpSCFRFYKPITIVYRRTFLSKFSFAKkhldwF 157
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEG-PADLV-------------YGSRLIREGESDLRRLGSRLFNLVR-----L 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818317757 158 LMKDYDHSepkevdwimGSAVMISRSALEKVGiMDPRyfmYMEDVDWCrRFWENGFKVIYFPlvsMHHYHGKGS 231
Cdd:COG0463  142 LTNLPDST---------SGFRLFRREVLEELG-FDEG---FLEDTELL-RALRHGFRIAEVP---VRYRAGESK 198
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
6-233 6.86e-20

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 85.80  E-value: 6.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   6 IVTSYrNPELlRVCLDSIRKCVTGIaYELIVADSATQEDMEMMMREDYADVKFFSFEKNVGFQALVKIGLDNSVGK---Y 82
Cdd:cd02526    2 VVVTY-NPDL-SKLKELLAALAEQV-DKVVVVDNSSGNDIELRLRLNSEKIELIHLGENLGIAKALNIGIKAALENgadY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  83 ILMLNGDILVTPDSVTKMLEFLK---TDASIGMVGPKllnfngtlqpscfrfykpitIVYRRTFLSKFSFAKKHLDWFLM 159
Cdd:cd02526   79 VLLFDQDSVPPPDMVEKLLAYKIlsdKNSNIGAVGPR--------------------IIDRRTGENSPGVRKSGYKLRIQ 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818317757 160 KDYDHsEPKEVDWIMGSAVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKVIYFPLVSMHHYHGKGSAK 233
Cdd:cd02526  139 KEGEE-GLKEVDFLITSGSLISLEALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHELGDKRVK 211
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-150 1.01e-13

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: 67.42  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757    4 SIIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSA----TQEDMEMMMREDYaDVKFFSFEKNVGFQALVKIGLDNSV 79
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLN-QTYPNFEIIVVDDGstdgTVEIAEEYAKKDP-RVRVIRLPENRGKAGARNAGLRAAT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818317757   80 GKYILMLNGDILVTPDSVTKMLEFLK---TDASIGMVGPKLLNFNGTLQPSCFRFYKPITIVYRRTFLSKFSFA 150
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEedgADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL 152
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-217 3.60e-11

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: 59.83  E-value: 3.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSATQEDMEMM---MREDYADVKFFSFEKNVGFQALVKIGLDNSVGK 81
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLA-QTYPNFEVIVVDDGSTDGTLEIleeYAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  82 YILMLNGDILVTPDSVTKMLEFLKTDASIGMVGPKllnfngtlqpscfrfykpitivyrrtflskfsfakkhldwflmkd 161
Cdd:cd00761   80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGP--------------------------------------------- 114
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 818317757 162 ydhsepkevdwimgSAVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKVIY 217
Cdd:cd00761  115 --------------GNLLFRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
3-226 4.58e-10

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: 58.98  E-value: 4.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   3 LSIIVTSYRNPELLRVCLDSIRKC-VTGIAYELIVADSATQEDMEMMMRE---DYADVKFFSFEKNVGFQALVKIGLDNS 78
Cdd:COG1215   31 VSVIIPAYNEEAVIEETLRSLLAQdYPKEKLEVIVVDDGSTDETAEIARElaaEYPRVRVIERPENGGKAAALNAGLKAA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  79 VGKYILMLNGDILVTPDSVTKMLEFLKtDASIGMVgpkllnfngtlqpscfrfykpitivyrrtflskfsfakkhldwfl 158
Cdd:COG1215  111 RGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGAS--------------------------------------------- 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818317757 159 mkdydhsepkevdwimGSAVMISRSALEKVGIMDPRyfMYMEDVDWCRRFWENGFKVIYFPLVSMHHY 226
Cdd:COG1215  145 ----------------GANLAFRREALEEVGGFDED--TLGEDLDLSLRLLRAGYRIVYVPDAVVYEE 194
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
3-229 1.10e-08

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 54.30  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757    3 LSIIVTSYRNPELLRVCLDSIRKCvTGIAYELIV----ADSATQED-MEMMMREDYADVKFFSFEKNVGF----QALVkI 73
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQ-PYPPVEVVVvvnpSDAETLDVaEEIAARFPDVRLRVIRNARLLGPtgksRGLN-H 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   74 GLDNSVGKYILMLNGDILVTPDSVTKMLEFLKTdASIGMVG-PKLLNFNGTLQPscfrfykpitivyrrtFLSKFSFAKK 152
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGtPVFSLNRSTMLS----------------ALGALEFALR 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818317757  153 HLDWFLMKDYdhsepKEVDWIMGSAVMISRSALEKVGIMDPrYFMYMEDVDWCRRFWENGFKVIYFPLVSMHHYHGK 229
Cdd:pfam13641 145 HLRMMSLRLA-----LGVLPLSGAGSAIRREVLKELGLFDP-FFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPT 215
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-245 1.72e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 53.41  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTsYRNPELLRVCLDSIRKCVTGIAYELIVADSATQEDMEMMMREDYAD-VKFFSFEKNVG----FQALVKIGLDNSV 79
Cdd:cd04185    2 VVVT-YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDnIVYLRLPENLGgaggFYEGVRRAYELGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  80 gKYILMLNGDILVTPDSVTKMLEFLKTDASiGMVGPKLLNFNGTlqpscfrfykpitivyrrtFLSkfsfakkhldwflm 159
Cdd:cd04185   81 -DWIWLMDDDAIPDPDALEKLLAYADKDNP-QFLAPLVLDPDGS-------------------FVG-------------- 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757 160 kdydhsepkevdwimgsaVMISRSALEKVGIMDPRYFMYMEDVDWCRRFWENGFKvIYFPLVSMHHYH--GKGSAKGGVI 237
Cdd:cd04185  126 ------------------VLISRRVVEKIGLPDKEFFIWGDDTEYTLRASKAGPG-IYVPDAVVVHKTaiNKGSSAVVNI 186

                 ....*...
gi 818317757 238 RSLLFNKY 245
Cdd:cd04185  187 DPPWKLYY 194
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-193 7.13e-08

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: 51.07  E-value: 7.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTSYRNPELLRVCLDSIRKCVTGiAYELIV-ADSATQEDMEMM--MREDYADVKFFSFEKNVGFQAL-VKIGLDNSVG 80
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVvDDGSTDDTLEILeeLAALYIRRVLVVRDKENGGKAGaLNAGLRHAKG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  81 KYILMLNGDILVTPDSVTKMLEFLKTDASIGMVGPKLLNFNGTLQPscfrFYKPITIVYRRTFLskFSFAKKHLDWFLMK 160
Cdd:cd06423   80 DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENL----LTRLQAIEYLSIFR--LGRRAQSALGGVLV 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 818317757 161 dydhsepkevdwIMGSAVMISRSALEKVGIMDP 193
Cdd:cd06423  154 ------------LSGAFGAFRREALREVGGWDE 174
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
5-105 2.91e-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: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTSYRNPELLRVCLDSIrKCVTGIAYELIVADSATQEDMEMMMREDYADVKF---FSFEKNVGFQaLVKI---GLDNS 78
Cdd:cd06420    1 LIITTYNRPEALELVLKSV-LNQSILPFEVIIADDGSTEETKELIEEFKSQFPIpikHVWQEDEGFR-KAKIrnkAIAAA 78
                         90       100
                 ....*....|....*....|....*..
gi 818317757  79 VGKYILMLNGDILVTPDSVTKMLEFLK 105
Cdd:cd06420   79 KGDYLIFIDGDCIPHPDFIADHIELAE 105
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
4-231 3.71e-05

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: 43.69  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   4 SIIVTSYRNPELLRVCLDSIRKcVTGIAYELIVADSA----TQEDMemmmrEDYADV--KFFSfEKNVG-FQALVKiGLD 76
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLS-QTYPNIEYIVIDGGstdgTVDII-----KKYEDKitYWIS-EPDKGiYDAMNK-GIA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  77 NSVGKYILMLN-GDILVtPDSVTKMLEFLKTDASIGMVGpkllnfngtlqpSCFRFYKPITIVYRRTFLSKFSFAKKHLD 155
Cdd:cd06433   73 LATGDIIGFLNsDDTLL-PGALLAVVAAFAEHPEVDVVY------------GDVLLVDENGRVIGRRRPPPFLDKFLLYG 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818317757 156 WFLMkdydHsepkevdwimgSAVMISRSALEKVGIMDPRYFMYMeDVDWCRRFWENGFKVIYFPLVSMHHYHGKGS 231
Cdd:cd06433  140 MPIC----H-----------QATFFRRSLFEKYGGFDESYRIAA-DYDLLLRLLLAGKIFKYLPEVLAAFRLGGVS 199
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
82-269 5.69e-05

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 42.71  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   82 YILMLNGDILVTPDSVTKMLEFLKTDaSIGMVGPkllnfngtlqpscfrfykPITIVYRRTFLSKFSFAkkHLDWFLMKD 161
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASP-EVAIIQG------------------PILPMNVGNYLEELAAL--FFADDHGKS 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  162 YDHSE-PKEVDWIMGSAVMISRSALEKVGIMDPryFMYMEDVDWCRRFWENGFKVIYFPLVSMHhyhgkgSAKGGVIRSL 240
Cdd:pfam13632  60 IPVRMaLGRVLPFVGSGAFLRRSALQEVGGWDD--GSVSEDFDFGLRLQRAGYRVRFAPYSAVY------EKSPLTFRDF 131
                         170       180
                  ....*....|....*....|....*....
gi 818317757  241 LFNKYTWIHIASGIKYFKKFLGKPLPIHN 269
Cdd:pfam13632 132 LRQRRRWAYGCLLILLIRLLGYLGTLLWS 160
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
3-107 1.16e-04

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 42.28  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757    3 LSIIVTSYRNPELLRVCLD--SIRKCvtgiAYELIVADSATQE-------DMEMMMredYADVKFFSFEKNVGFQALVKI 73
Cdd:TIGR04440   2 LTIIIPTYNRPEYLKRWLRyySDFGC----DYRIIIADSSDEKfnennlkVFKNYS---NPNITYLHYPDLGVPFYEKLL 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 818317757   74 GLDNSV-GKYILMLNGDILVTPDSVTKMLEFLKTD 107
Cdd:TIGR04440  75 DALEQVeTPYVVICADDDFIIPSGLTECLSFLEAN 109
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
4-219 1.62e-04

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 41.53  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   4 SIIVTSY--RNPELLRVCLDSIRKcVTGIAYELI-VADSATQEDMEMMMRE--DYADVKFFSFEKNVGFQALVKIGLDNS 78
Cdd:cd04195    1 SVLMSVYikEKPEFLREALESILK-QTLPPDEVVlVKDGPVTQSLNEVLEEfkRKLPLKVVPLEKNRGLGKALNEGLKHC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757  79 VGKYILMLNGDILVTPDSVTKMLEFLKTDASIGMVGPKLLNFNgtlqpscfrfYKPITIVYRRTFLSK---FSFAKKHld 155
Cdd:cd04195   80 TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFD----------SDGNDIGKRRLPTSHddiLKFARRR-- 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818317757 156 wflmKDYDHsepkevdwimgSAVMISRSALEKVGIMDPryFMYMEDVDWCRRFWENGFKVIYFP 219
Cdd:cd04195  148 ----SPFNH-----------PTVMFRKSKVLAVGGYQD--LPLVEDYALWARMLANGARFANLP 194
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
5-142 3.02e-04

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 41.12  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVtsyRNPE-LLRVCLDSIRKCVTgiayELIVADS----ATQEdmemmMREDYAdVKFFSFeKNVGFQALVKIGLDNSV 79
Cdd:cd02511    6 IIT---KNEErNIERCLESVKWAVD----EIIVVDSgstdRTVE-----IAKEYG-AKVYQR-WWDGFGAQRNFALELAT 71
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818317757  80 GKYILMLNGDILVTPDSVTKMLEFLKTDASIGMVGPKLLNFNGTLQPSCFRFYKPITIVYRRT 142
Cdd:cd02511   72 NDWVLSLDADERLTPELADEILALLATDDYDGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRG 134
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
2-116 5.09e-04

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 40.32  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   2 ELSIIVTSYR-NPELLRVCLDSIRKCVtgiAYELIVA-DSATQEDMEMMMrEDYADVKFF-SFEKNVGFQALVKIGLDNS 78
Cdd:cd06434    1 DVTVIIPVYDeDPDVFRECLRSILRQK---PLEIIVVtDGDDEPYLSILS-QTVKYGGIFvITVPHPGKRRALAEGIRHV 76
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 818317757  79 VGKYILMLNGDILVTPDSVTKMLEFLKtDASIGMVGPK 116
Cdd:cd06434   77 TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTN 113
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
3-113 6.64e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 40.52  E-value: 6.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   3 LSIIVTSYRNPELLRVCLDSIRKCVTG-------IAYELIVADSATQEDMEMMMrEDYA--------DVKFFSFEKNVGF 67
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKETIKYLESrsrkdpkFKYEIIIVNDGSKDKTLKVA-KDFWrqninpniDIRLLSLLRNKGK 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 818317757  68 QALVKIGLDNSVGKYILMLNGDILVTPDSVTKMLEFL--KTDASIGMV 113
Cdd:PTZ00260 151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMlkIEQNGLGIV 198
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-110 2.99e-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: 37.46  E-value: 2.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   5 IIVTSYRNPELLRVCLDSIRKCVT--GIAYELIVAD--S--ATQEDMEMMMREDyADVKFFSFEKNVGFQALVKIGLDNS 78
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLEslGYDYEIIFVDdgStdRTLEILRELAARD-PRVKVIRLSRNFGQQAALLAGLDHA 79
                         90       100       110
                 ....*....|....*....|....*....|..
gi 818317757  79 VGKYILMLNGDILVTPDSVTKMLEFLKTDASI 110
Cdd:cd04187   80 RGDAVITMDADLQDPPELIPEMLAKWEEGYDV 111
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-95 3.52e-03

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: 37.57  E-value: 3.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818317757   3 LSIIVTSY-RNPELLRVCLDSIRKCVtgiaY---ELIVADSA-TQEDMEMMMREDYAD---VKFFSFEKNVGFQALVKIG 74
Cdd:cd04184    3 ISIVMPVYnTPEKYLREAIESVRAQT----YpnwELCIADDAsTDPEVKRVLKKYAAQdprIKVVFREENGGISAATNSA 78
                         90       100
                 ....*....|....*....|..
gi 818317757  75 LDNSVGKYI-LMLNGDILvTPD 95
Cdd:cd04184   79 LELATGEFVaLLDHDDEL-APH 99
 
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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