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Conserved domains on  [gi|1995625991|gb|QSG30251|]
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CDP-glycerol glycerophosphotransferase family protein [Actinobacillus pleuropneumoniae serovar 19]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
 491-852 1.77e-61

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


:

Pssm-ID: 441491  Cd Length: 369  Bit Score: 214.86  E-value: 1.77e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  491 WLLMDRE-TKADDNAEHFYRYMQAHHPEQRCYFVLNKSSidwQRLKKDKFNLVEFGSIEYERRLEKASKIISSHLEAHIN 569
Cdd:COG1887     24 ILFESRNgRSYSDNPKALFEYLRKNHPDYEVVWVVDDDS---KRLPKEGVKVVKRGSLKYLYALARAKYLVSNHYFPFPS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  570 NYfgdNYDFSKKFIFLQHG-----ITKDDLSQWFNTKKNLSG----VITATiPEYNSIVEElnKYKIGKKETFLTGFPRH 640
Cdd:COG1887    101 YF---RKRKGQKYVQLWHGtplkkIGLDDPPRYLKRVLREYRnwdyLLSSS-EESTEIFRR--AFGYPEGEVLETGYPRN 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  641 DKLLS--------------GNIKGAKTILIVPTWRhyimgtqigkgantrelnkafmTTNYAKAWYNLLHSQELKNLIKN 706
Cdd:COG1887    175 DVLFDadreelreelrerlGIPEDKKVILYAPTWR----------------------DDEDNFDDYLDLDLERLAELLGD 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  707 lGYKVIFAPHPNIEPYLNEFNIPQYIDVWKSaisrESMQSLFQQSNLLITDYSSIAFEMAFLGKQTIYYQFDKEEFRSGi 786
Cdd:COG1887    233 -DYVLLVRLHPFVKDSLDEKYSDRIIDVSDY----PDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRDE- 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1995625991  787 htyQQGYFEYEKDGFGPVAETLDALFAHLDKFVKGENDYINIYQSRIQKTFKYRDTNNCQRVYEAI 852
Cdd:COG1887    307 ---RGFYFDYEEDAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 46-184 1.66e-27

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: 109.52  E-value: 1.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNLsfkKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKYVQ 125
Cdd:cd00761      1 VIIPAYNEEPYLERCLESLLAQTY---PNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1995625991  126 TEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFFMeKKEIITDKHPLKFRFE 184
Cdd:cd00761     78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLLF-RRELLEEIGGFDEALL 135
 
Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
 491-852 1.77e-61

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 441491  Cd Length: 369  Bit Score: 214.86  E-value: 1.77e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  491 WLLMDRE-TKADDNAEHFYRYMQAHHPEQRCYFVLNKSSidwQRLKKDKFNLVEFGSIEYERRLEKASKIISSHLEAHIN 569
Cdd:COG1887     24 ILFESRNgRSYSDNPKALFEYLRKNHPDYEVVWVVDDDS---KRLPKEGVKVVKRGSLKYLYALARAKYLVSNHYFPFPS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  570 NYfgdNYDFSKKFIFLQHG-----ITKDDLSQWFNTKKNLSG----VITATiPEYNSIVEElnKYKIGKKETFLTGFPRH 640
Cdd:COG1887    101 YF---RKRKGQKYVQLWHGtplkkIGLDDPPRYLKRVLREYRnwdyLLSSS-EESTEIFRR--AFGYPEGEVLETGYPRN 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  641 DKLLS--------------GNIKGAKTILIVPTWRhyimgtqigkgantrelnkafmTTNYAKAWYNLLHSQELKNLIKN 706
Cdd:COG1887    175 DVLFDadreelreelrerlGIPEDKKVILYAPTWR----------------------DDEDNFDDYLDLDLERLAELLGD 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  707 lGYKVIFAPHPNIEPYLNEFNIPQYIDVWKSaisrESMQSLFQQSNLLITDYSSIAFEMAFLGKQTIYYQFDKEEFRSGi 786
Cdd:COG1887    233 -DYVLLVRLHPFVKDSLDEKYSDRIIDVSDY----PDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRDE- 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1995625991  787 htyQQGYFEYEKDGFGPVAETLDALFAHLDKFVKGENDYINIYQSRIQKTFKYRDTNNCQRVYEAI 852
Cdd:COG1887    307 ---RGFYFDYEEDAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
 491-852 1.21e-39

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 151.35  E-value: 1.21e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  491 WLLMDRETKADDNAEHFYRYMQAHHPEQRCYFVLNKSSIDwqRLKKDKfNLVEFGSIEYERRLEKASKIISshleahiNN 570
Cdd:pfam04464    8 LFESFWGRGYSDNPKAIYEYLRELAPGYRIVWVVKKDHSA--RLPKGV-PVVVRNSFRYLYLLLRAKYLVS-------NS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  571 YFGDNYDFSK--KFIFLQHGIT-----KDDLSQ-WFNTKKNLSGV------ITATIPEYNSIVEELnkYKIGKKETFLTG 636
Cdd:pfam04464   78 NFPLYVVKRKnqVYLQTWHGTPlkhmgLDILEVpMANTGQNFLRNvdrwdyLISANPHSTNIFARA--FNIDKERILETG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  637 FPRHDKLLS-------------GNIKGAKTILIVPTWRHYIMGtqigkgantrelnkafmttnyAKAWYNLLHSQELKNL 703
Cdd:pfam04464  156 YPRNDVLFNannedvqrirerlGIPLGKKVILYAPTWRDDERG---------------------SIGSYRFELLIDLERL 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  704 IKNLG--YKVIFAPHPNIEpylNEFNIPQYIDVWKSAISRESMQSLFQQSNLLITDYSSIAFEMAFLGKQTIYYQFDKEE 781
Cdd:pfam04464  215 AFALGndYVILLKMHPLIQ---NNIDIFESSGYVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLET 291

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1995625991  782 FRsgihtYQQG-YFEYEKDGFGPVAETLDALFAHLDKFVKGENDYINIYQSRIQKTFKYRDTNNCQRVYEAI 852
Cdd:pfam04464  292 YS-----ATRGfYLDYESEAPGPVVETFDELIDALKSGDWDDDYYARKRRAFRDRFCKYDDGRSSERVVRLI 358
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 46-184 1.66e-27

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: 109.52  E-value: 1.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNLsfkKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKYVQ 125
Cdd:cd00761      1 VIIPAYNEEPYLERCLESLLAQTY---PNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1995625991  126 TEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFFMeKKEIITDKHPLKFRFE 184
Cdd:cd00761     78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLLF-RRELLEEIGGFDEALL 135
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 44-267 3.84e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.40  E-value: 3.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   44 FTIVSAVYNVEKYLDDFFDSIVKQNLsfkKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKY 123
Cdd:COG0463      4 VSVVIPTYNEEEYLEEALESLLAQTY---PDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  124 VQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKnIAMIVCNLLFfmekKEIITDKHPLKFRFEKDVNCLS-IKDLNNNLNLs 202
Cdd:COG0463     81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLI----REGESDLRRLGSRLFNLVRLLTnLPDSTSGFRL- 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1995625991  203 vatsfFRTSVIQgnQLLFDNRvkpnfedgkFISDY-LFELQHYNALFLKKPVYfYRKREDGTSTLD 267
Cdd:COG0463    155 -----FRREVLE--ELGFDEG---------FLEDTeLLRALRHGFRIAEVPVR-YRAGESKLNLRD 203
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 45-183 1.05e-22

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 96.31  E-value: 1.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   45 TIVSAVYNVEKYLDDFFDSIVKQNlsfKKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKYV 124
Cdd:pfam00535    1 SVIIPTYNEEKYLLETLESLLNQT---YPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1995625991  125 QTEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFFMEKKEIITDKHPLKFRF 183
Cdd:pfam00535   78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRL 136
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 43-138 1.48e-20

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 94.34  E-value: 1.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   43 QFTIVSAVYNVEKYLDDFFDSIVKQNLSfkkHIQIILVDDGSKDSSATIIKKWQKKYPnNIHYYYKENGGQASARNLGLK 122
Cdd:PRK10073     7 KLSIIIPLYNAGKDFRAFMESLIAQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGLA 82

                           90
                   ....*....|....*.
gi 1995625991  123 YVQTEWVTFIDPDDFL 138
Cdd:PRK10073    83 VATGKYVAFPDADDVV 98
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 43-234 3.19e-03

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: 40.36  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   43 QFTIVSAVYNVEKYLDdffdSIVKQNLSFKKHIQIIlVDDGSKDSSATIIKKWQKKYPN-NIHY--YYKENGGQASARNL 119
Cdd:TIGR04440    1 KLTIIIPTYNRPEYLK----RWLRYYSDFGCDYRII-IADSSDEKFNENNLKVFKNYSNpNITYlhYPDLGVPFYEKLLD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  120 GLKYVQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFF-MEKKEIITDKhPLKFRFEKDVNCLSIKDLNNN 198
Cdd:TIGR04440   76 ALEQVETPYVVICADDDFIIPSGLTECLSFLEANPDYSAAQGRYVYFeDRGDRVYGDQ-PFQYYPDYSIEQDDPIERLAQ 154

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1995625991  199 LN---LSVATSFFRTSVIqgnQLLFDNRVKPNFEDGKFI 234
Cdd:TIGR04440  155 FFsnyMHLWYSVFRTDVI---KKAYKDLKDLNIRNPNFS 190
 
Name Accession Description Interval E-value
TagB COG1887
CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope ...
 491-852 1.77e-61

CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 441491  Cd Length: 369  Bit Score: 214.86  E-value: 1.77e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  491 WLLMDRE-TKADDNAEHFYRYMQAHHPEQRCYFVLNKSSidwQRLKKDKFNLVEFGSIEYERRLEKASKIISSHLEAHIN 569
Cdd:COG1887     24 ILFESRNgRSYSDNPKALFEYLRKNHPDYEVVWVVDDDS---KRLPKEGVKVVKRGSLKYLYALARAKYLVSNHYFPFPS 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  570 NYfgdNYDFSKKFIFLQHG-----ITKDDLSQWFNTKKNLSG----VITATiPEYNSIVEElnKYKIGKKETFLTGFPRH 640
Cdd:COG1887    101 YF---RKRKGQKYVQLWHGtplkkIGLDDPPRYLKRVLREYRnwdyLLSSS-EESTEIFRR--AFGYPEGEVLETGYPRN 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  641 DKLLS--------------GNIKGAKTILIVPTWRhyimgtqigkgantrelnkafmTTNYAKAWYNLLHSQELKNLIKN 706
Cdd:COG1887    175 DVLFDadreelreelrerlGIPEDKKVILYAPTWR----------------------DDEDNFDDYLDLDLERLAELLGD 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  707 lGYKVIFAPHPNIEPYLNEFNIPQYIDVWKSaisrESMQSLFQQSNLLITDYSSIAFEMAFLGKQTIYYQFDKEEFRSGi 786
Cdd:COG1887    233 -DYVLLVRLHPFVKDSLDEKYSDRIIDVSDY----PDINDLLLASDVLITDYSSVMFDFALLDRPIIFYAYDLEEYRDE- 306

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1995625991  787 htyQQGYFEYEKDGFGPVAETLDALFAHLDKFVKGENDYINIYQSRIQKTFKYRDTNNCQRVYEAI 852
Cdd:COG1887    307 ---RGFYFDYEEDAPGPVVTTFEELIDAIEDILENGDEYAEKYKAFRERFFPYDDGNASERVVDAI 369
Glyphos_transf pfam04464
CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids ...
 491-852 1.21e-39

CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase; Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid.


Pssm-ID: 398259  Cd Length: 360  Bit Score: 151.35  E-value: 1.21e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  491 WLLMDRETKADDNAEHFYRYMQAHHPEQRCYFVLNKSSIDwqRLKKDKfNLVEFGSIEYERRLEKASKIISshleahiNN 570
Cdd:pfam04464    8 LFESFWGRGYSDNPKAIYEYLRELAPGYRIVWVVKKDHSA--RLPKGV-PVVVRNSFRYLYLLLRAKYLVS-------NS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  571 YFGDNYDFSK--KFIFLQHGIT-----KDDLSQ-WFNTKKNLSGV------ITATIPEYNSIVEELnkYKIGKKETFLTG 636
Cdd:pfam04464   78 NFPLYVVKRKnqVYLQTWHGTPlkhmgLDILEVpMANTGQNFLRNvdrwdyLISANPHSTNIFARA--FNIDKERILETG 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  637 FPRHDKLLS-------------GNIKGAKTILIVPTWRHYIMGtqigkgantrelnkafmttnyAKAWYNLLHSQELKNL 703
Cdd:pfam04464  156 YPRNDVLFNannedvqrirerlGIPLGKKVILYAPTWRDDERG---------------------SIGSYRFELLIDLERL 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  704 IKNLG--YKVIFAPHPNIEpylNEFNIPQYIDVWKSAISRESMQSLFQQSNLLITDYSSIAFEMAFLGKQTIYYQFDKEE 781
Cdd:pfam04464  215 AFALGndYVILLKMHPLIQ---NNIDIFESSGYVVDVSDYEDVEDLLLASDILITDYSSVMFDYAVLDRPIIFYAYDLET 291

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1995625991  782 FRsgihtYQQG-YFEYEKDGFGPVAETLDALFAHLDKFVKGENDYINIYQSRIQKTFKYRDTNNCQRVYEAI 852
Cdd:pfam04464  292 YS-----ATRGfYLDYESEAPGPVVETFDELIDALKSGDWDDDYYARKRRAFRDRFCKYDDGRSSERVVRLI 358
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 46-184 1.66e-27

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: 109.52  E-value: 1.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNLsfkKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKYVQ 125
Cdd:cd00761      1 VIIPAYNEEPYLERCLESLLAQTY---PNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1995625991  126 TEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFFMeKKEIITDKHPLKFRFE 184
Cdd:cd00761     78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLLF-RRELLEEIGGFDEALL 135
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 44-267 3.84e-25

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.40  E-value: 3.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   44 FTIVSAVYNVEKYLDDFFDSIVKQNLsfkKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKY 123
Cdd:COG0463      4 VSVVIPTYNEEEYLEEALESLLAQTY---PDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  124 VQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKnIAMIVCNLLFfmekKEIITDKHPLKFRFEKDVNCLS-IKDLNNNLNLs 202
Cdd:COG0463     81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLI----REGESDLRRLGSRLFNLVRLLTnLPDSTSGFRL- 154

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1995625991  203 vatsfFRTSVIQgnQLLFDNRvkpnfedgkFISDY-LFELQHYNALFLKKPVYfYRKREDGTSTLD 267
Cdd:COG0463    155 -----FRREVLE--ELGFDEG---------FLEDTeLLRALRHGFRIAEVPVR-YRAGESKLNLRD 203
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 45-183 1.05e-22

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 96.31  E-value: 1.05e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   45 TIVSAVYNVEKYLDDFFDSIVKQNlsfKKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKYV 124
Cdd:pfam00535    1 SVIIPTYNEEKYLLETLESLLNQT---YPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAA 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1995625991  125 QTEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFFMEKKEIITDKHPLKFRF 183
Cdd:pfam00535   78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRL 136
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 43-138 1.48e-20

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 94.34  E-value: 1.48e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   43 QFTIVSAVYNVEKYLDDFFDSIVKQNLSfkkHIQIILVDDGSKDSSATIIKKWQKKYPnNIHYYYKENGGQASARNLGLK 122
Cdd:PRK10073     7 KLSIIIPLYNAGKDFRAFMESLIAQTWT---ALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGLA 82

                           90
                   ....*....|....*.
gi 1995625991  123 YVQTEWVTFIDPDDFL 138
Cdd:PRK10073    83 VATGKYVAFPDADDVV 98
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 44-165 6.57e-20

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: 91.73  E-value: 6.57e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   44 FTIVSAVYNVEKYLDDFFDSIVKQNLSfKKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKY 123
Cdd:COG1215     31 VSVIIPAYNEEAVIEETLRSLLAQDYP-KEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKA 109

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1995625991  124 VQTEWVTFIDPDDFLSLNYFLEVDKKLsEHKNIAMIVCNLLF 165
Cdd:COG1215    110 ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGASGANLAF 150
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 45-256 1.05e-17

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: 82.98  E-value: 1.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   45 TIVSAVYNVEKYLDDFFDSIVKQNLsfkKHIQIILVDDGSKDSSATIIKKwqkkYPNNIHYYYKEN-GGQASARNLGLKY 123
Cdd:cd06433      1 SIITPTYNQAETLEETIDSVLSQTY---PNIEYIVIDGGSTDGTVDIIKK----YEDKITYWISEPdKGIYDAMNKGIAL 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  124 VQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFFMEKKEIITDKHPLKFRFEKdvnclsikdLNNNLNLSV 203
Cdd:cd06433     74 ATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKF---------LLYGMPICH 144

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1995625991  204 ATSFFRTSVIQgNQLLFDnrvkpnfEDGKFISDYLFELQhynaLFLKKPVYFY 256
Cdd:cd06433    145 QATFFRRSLFE-KYGGFD-------ESYRIAADYDLLLR----LLLAGKIFKY 185
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
41-139 3.60e-15

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.41  E-value: 3.60e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   41 KHQFTIVSAVYNVEKYLDDFFDSIVKQNlsfKKHIQIILVDDGSKDSSATIIKKWQkkYPNNIHYYYKENGGQASARNLG 120
Cdd:COG1216      2 RPKVSVVIPTYNRPELLRRCLESLLAQT---YPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLG 76

                           90
                   ....*....|....*....
gi 1995625991  121 LKYVQTEWVTFIDPDDFLS 139
Cdd:COG1216     77 LRAAGGDYLLFLDDDTVVE 95
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 45-257 3.04e-14

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: 73.05  E-value: 3.04e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   45 TIVSAVYNVEKYLDDFFDSIVKQNLSFkkhIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYY-KENGGqaSARN--LGL 121
Cdd:cd04196      1 AVLMATYNGEKYLREQLDSILAQTYKN---DELIISDDGSTDGTVEIIKEYIDKDPFIIILIRnGKNLG--VARNfeSLL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  122 KYVQTEWVTFIDPDD-FLS--LNYFLevdKKLSEHKNIAMIVCNLLFFMEKKEIItdkHPLKFRFEKDVNCLSIKDLNNN 198
Cdd:cd04196     76 QAADGDYVFFCDQDDiWLPdkLERLL---KAFLKDDKPLLVYSDLELVDENGNPI---GESFFEYQKIKPGTSFNNLLFQ 149

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1995625991  199 LNLSVATSFFRTSVIqgnqllfdNRVKPNFEDGKFISD---YLFELQHYNALFLKKPVYFYR 257
Cdd:cd04196    150 NVVTGCTMAFNRELL--------ELALPFPDADVIMHDwwlALLASAFGKVVFLDEPLILYR 203
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 46-135 1.50e-13

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: 70.29  E-value: 1.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIvKQNLSFKKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKYVQ 125
Cdd:cd04179      1 VVIPAYNEEENIPELVERL-LAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAAR 79

                           90
                   ....*....|
gi 1995625991  126 TEWVTFIDPD 135
Cdd:cd04179     80 GDIVVTMDAD 89
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 45-150 2.15e-12

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: 68.41  E-value: 2.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   45 TIVSAVYNVEKYLDDFFDSIVKQNLSFKKhIQIILVDDGSKDSSATIIKKWQKKYPnNIHYYYKENGGQASARNLGLKYV 124
Cdd:cd02525      3 SIIIPVRNEEKYIEELLESLLNQSYPKDL-IEIIVVDGGSTDGTREIVQEYAAKDP-RIRLIDNPKRIQSAGLNIGIRNS 80

                           90       100
                   ....*....|....*....|....*.
gi 1995625991  125 QTEWVTFIDPDDFLSLNYFLEVDKKL 150
Cdd:cd02525     81 RGDIIIRVDAHAVYPKDYILELVEAL 106
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 46-159 8.43e-12

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 64.89  E-value: 8.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNlsfKKHIQIILVDDGSKDSSATIIKKwqkKYPNNIHYYYKENGGQASARNLGLKYVQ 125
Cdd:cd04186      1 IIIVNYNSLEYLKACLDSLLAQT---YPDFEVIVVDNASTDGSVELLRE---LFPEVRLIRNGENLGFGAGNNQGIREAK 74

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1995625991  126 TEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMI 159
Cdd:cd04186     75 GDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIV 108
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 46-159 3.06e-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: 64.15  E-value: 3.06e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNV-EKYLDDFFDSIVKQNLSfkkHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYY-KENGGQASARNLGLKY 123
Cdd:cd04184      5 IVMPVYNTpEKYLREAIESVRAQTYP---NWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFrEENGGISAATNSALEL 81

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1995625991  124 VQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMI 159
Cdd:cd04184     82 ATGEFVALLDHDDELAPHALYEVVKALNEHPDADLI 117
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 46-213 3.46e-11

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 63.40  E-value: 3.46e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNLsfkKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYY-KENGGQASARNLGLKYV 124
Cdd:cd06423      1 IIVPAYNEEAVIERTIESLLALDY---PKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRdKENGGKAGALNAGLRHA 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  125 QTEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMI---------VCNLLFFMEKKEIItdkhpLKFRFEKDVNCLsikdL 195
Cdd:cd06423     78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVqgrvrvrngSENLLTRLQAIEYL-----SIFRLGRRAQSA----L 148

                          170
                   ....*....|....*...
gi 1995625991  196 NNNLNLSVATSFFRTSVI 213
Cdd:cd06423    149 GGVLVLSGAFGAFRREAL 166
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 46-135 2.59e-10

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: 60.95  E-value: 2.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNLSFKKHIQIILVDDGSKDSSATIIKKWQKKYPnNIHYY-YKENGGQASARNLGLKYV 124
Cdd:cd04187      1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDP-RVKVIrLSRNFGQQAALLAGLDHA 79

                           90
                   ....*....|.
gi 1995625991  125 QTEWVTFIDPD 135
Cdd:cd04187     80 RGDAVITMDAD 90
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 46-135 3.72e-08

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: 55.27  E-value: 3.72e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVK-QNLSFKKHIQIILVDDGSKDSSATIIKKWQKKYPNNI-HYYYKENGGQASARNLGLKY 123
Cdd:cd04188      1 VVIPAYNEEKRLPPTLEEAVEyLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIrVLTLPKNRGKGGAVRAGMLA 80

                           90
                   ....*....|..
gi 1995625991  124 VQTEWVTFIDPD 135
Cdd:cd04188     81 ARGDYILFADAD 92
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 45-136 4.27e-08

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: 54.63  E-value: 4.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   45 TIVSAVYNVEK--YLDDFFDSIVKQNLSFKkhiQIILVDDGS-KDSSATIIKKWQKKYPNNIHYYyKENGGQASARNLGL 121
Cdd:cd04195      1 SVLMSVYIKEKpeFLREALESILKQTLPPD---EVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPL-EKNRGLGKALNEGL 76

                           90
                   ....*....|....*
gi 1995625991  122 KYVQTEWVTFIDPDD 136
Cdd:cd04195     77 KHCTYDWVARMDTDD 91
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 46-160 5.29e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 54.99  E-value: 5.29e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNLSfKKHIQIILVDDGSKDSSATIIKK-WQKKYPN--NIHYYYKENGGQASARNLGLK 122
Cdd:cd04192      1 VVIAARNEAENLPRLLQSLSALDYP-KEKFEVILVDDHSTDGTVQILEFaAAKPNFQlkILNNSRVSISGKKNALTTAIK 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1995625991  123 YVQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKnIAMIV 160
Cdd:cd04192     80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQ-IGLVA 116
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 46-136 6.87e-08

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: 54.39  E-value: 6.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   46 IVSAVYNVEKYLDDFFDSIVKQNlsFKKHIQIILVDDGSKDSSATIIKKWQKKYPNN------IHYYYKENGGQASARNL 119
Cdd:cd06913      1 IILPVHNGEQWLDECLESVLQQD--FEGTLELSVFNDASTDKSAEIIEKWRKKLEDSgvivlvGSHNSPSPKGVGYAKNQ 78

                           90
                   ....*....|....*..
gi 1995625991  120 GLKYVQTEWVTFIDPDD 136
Cdd:cd06913     79 AIAQSSGRYLCFLDSDD 95
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 44-139 2.39e-07

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: 53.36  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   44 FTIVSAVYNVEKYLDDFFDSIVkqNLSFKKH-IQIILVDDGSKDSSATIIKKWQKKypNNIHYYYKENGGQASARNLGLK 122
Cdd:cd06439     31 VTIIIPAYNEEAVIEAKLENLL--ALDYPRDrLEIIVVSDGSTDGTAEIAREYADK--GVKLLRFPERRGKAAALNRALA 106

                           90
                   ....*....|....*..
gi 1995625991  123 YVQTEWVTFIDPDDFLS 139
Cdd:cd06439    107 LATGEIVVFTDANALLD 123
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 76-169 4.71e-07

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: 52.29  E-value: 4.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   76 QIILVDDGSKDSSATIIKKWqkkypnNIHYYYKENGGQASARNLGLKYVQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKN 155
Cdd:cd02511     28 EIIVVDSGSTDRTVEIAKEY------GAKVYQRWWDGFGAQRNFALELATNDWVLSLDADERLTPELADEILALLATDDY 101

                           90
                   ....*....|....
gi 1995625991  156 IAMIVCNLLFFMEK 169
Cdd:cd02511    102 DGYYVPRRNFFLGR 115
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 45-160 3.56e-06

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 49.97  E-value: 3.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   45 TIVSAVYNVEKYlDDFFDSIVKQNLSFKKHIQIILVDDGSKDSSATIIKKWQKkypNNIHYYYKE----NGGQASARNLG 120
Cdd:pfam10111    1 SVVIPVYNGEKT-HWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKD---HNLQVYYPNapdtTYSLAASRNRG 76

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1995625991  121 LKYVQTEWVTFIDPDDFLSLNYFlEVDKKLSEHKNIAMIV 160
Cdd:pfam10111   77 TSHAIGEYISFIDGDCLWSPDKF-EKQLKIATSLALQENI 115
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 51-152 4.24e-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: 48.73  E-value: 4.24e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   51 YNVEKYLDDFFDSIVKQ-NLSFkkhiQIILVDDGSKDSSATIIKKWQKKYPNNI-HYYYKENGGQASA-RNLGLKYVQTE 127
Cdd:cd06420      6 YNRPEALELVLKSVLNQsILPF----EVIIADDGSTEETKELIEEFKSQFPIPIkHVWQEDEGFRKAKiRNKAIAAAKGD 81

                           90       100
                   ....*....|....*....|....*
gi 1995625991  128 WVTFIDPDDFLSlNYFLEVDKKLSE 152
Cdd:cd06420     82 YLIFIDGDCIPH-PDFIADHIELAE 105
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 43-152 1.97e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 45.14  E-value: 1.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   43 QFTIVSAVYNVE----KYLDD---FFDSIVKQNLSFKkhIQIILVDDGSKDSSATIIKKWQKKYPNNIHYY----YKENG 111
Cdd:PTZ00260    71 DLSIVIPAYNEEdrlpKMLKEtikYLESRSRKDPKFK--YEIIIVNDGSKDKTLKVAKDFWRQNINPNIDIrllsLLRNK 148

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1995625991  112 GQASARNLGLKYVQTEWVTFIDPDDFLSLNYFLEVDKKLSE 152
Cdd:PTZ00260   149 GKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLK 189
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 68-135 3.74e-04

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; 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. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 43.29  E-value: 3.74e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1995625991   68 NLSFKKHIQIILVDDGSKDSSATIIKKWQKKYPNNIHYYYKENGGQASARNLGLKYVQTEWVTFIDPD 135
Cdd:cd06442     21 AALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDAD 88
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 37-135 2.16e-03

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 41.64  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   37 KYEGKHQFTIVSAVYNVEKYLDDFFDSIVKQNLSFKKHIQIILVDDGSKDSSATIIKKwQKKYPNN--IHYYYKENGGQA 114
Cdd:PRK10714     1 EIHPIKKVSVVIPVYNEQESLPELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPDShiVAILLNRNYGQH 79

                           90       100
                   ....*....|....*....|.
gi 1995625991  115 SARNLGLKYVQTEWVTFIDPD 135
Cdd:PRK10714    80 SAIMAGFSHVTGDLIITLDAD 100
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 43-234 3.19e-03

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: 40.36  E-value: 3.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   43 QFTIVSAVYNVEKYLDdffdSIVKQNLSFKKHIQIIlVDDGSKDSSATIIKKWQKKYPN-NIHY--YYKENGGQASARNL 119
Cdd:TIGR04440    1 KLTIIIPTYNRPEYLK----RWLRYYSDFGCDYRII-IADSSDEKFNENNLKVFKNYSNpNITYlhYPDLGVPFYEKLLD 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991  120 GLKYVQTEWVTFIDPDDFLSLNYFLEVDKKLSEHKNIAMIVCNLLFF-MEKKEIITDKhPLKFRFEKDVNCLSIKDLNNN 198
Cdd:TIGR04440   76 ALEQVETPYVVICADDDFIIPSGLTECLSFLEANPDYSAAQGRYVYFeDRGDRVYGDQ-PFQYYPDYSIEQDDPIERLAQ 154

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1995625991  199 LN---LSVATSFFRTSVIqgnQLLFDNRVKPNFEDGKFI 234
Cdd:TIGR04440  155 FFsnyMHLWYSVFRTDVI---KKAYKDLKDLNIRNPNFS 190
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 39-135 6.98e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 39.68  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1995625991   39 EGKHQFTIVSAVYN-----------VEKYLDDFFDsivkqnlsfkkhIQIILVDDGSKDSSATIIKKWQKKYPNNiHYYY 107
Cdd:PLN02726     6 EGAMKYSIIVPTYNerlnialivylIFKALQDVKD------------FEIIVVDDGSPDGTQDVVKQLQKVYGED-RILL 72

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1995625991  108 KENGGQ---ASARNLGLKYVQTEWVTFIDPD 135
Cdd:PLN02726    73 RPRPGKlglGTAYIHGLKHASGDFVVIMDAD 103
 
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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