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Conserved domains on  [gi|492503189|ref|WP_005868377|]
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MULTISPECIES: glycosyltransferase [Parabacteroides]

Protein Classification

glycosyltransferase family protein( domain architecture ID 1003037)

glycosyltransferase family protein belongs to a functionally diverse family, and may transfer sugar from sources such as UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose, or CDP-abequose, to one or more of a range of substrates

EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  9334165

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10073 super family cl32454
putative glycosyl transferase; Provisional
 2-250 1.79e-40

putative glycosyl transferase; Provisional


The actual alignment was detected with superfamily member PRK10073:

Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 143.65  E-value: 1.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   2 DKNLVSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQYNQGPSVTRNKGYEY 81
Cdd:PRK10073   4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189  82 TQGKYVYFMDSDDYLEPEALETCYIKCERQALDFVFFDAD-ILNKEKHKNISLNYQRKDCTNpelVYQGPYILKLLIDHK 160
Cdd:PRK10073  84 ATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADwCFRDTGETWQSIPSDRLRSTG---VLSGPDWLRMALSSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189 161 AYSPSPCLNFIRREYLTEIQLDFLPGIIHEDQLFTCLLYLQAQRVSSIHKDFFKRRLREDSIM-TSKFSMRNMES---YF 236
Cdd:PRK10073 161 RWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSrLPRQGNKNLNYqrhYI 240

                        250
                 ....*....|....
gi 492503189 237 TITAHLSKFADSHP 250
Cdd:PRK10073 241 KITRMLEKLNRRYA 254
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-250 1.79e-40

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 143.65  E-value: 1.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   2 DKNLVSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQYNQGPSVTRNKGYEY 81
Cdd:PRK10073   4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189  82 TQGKYVYFMDSDDYLEPEALETCYIKCERQALDFVFFDAD-ILNKEKHKNISLNYQRKDCTNpelVYQGPYILKLLIDHK 160
Cdd:PRK10073  84 ATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADwCFRDTGETWQSIPSDRLRSTG---VLSGPDWLRMALSSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189 161 AYSPSPCLNFIRREYLTEIQLDFLPGIIHEDQLFTCLLYLQAQRVSSIHKDFFKRRLREDSIM-TSKFSMRNMES---YF 236
Cdd:PRK10073 161 RWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSrLPRQGNKNLNYqrhYI 240

                        250
                 ....*....|....
gi 492503189 237 TITAHLSKFADSHP 250
Cdd:PRK10073 241 KITRMLEKLNRRYA 254
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-117 1.05e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 132.90  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   5 LVSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYT-QYNQGPSVTRNKGYEYTQ 83
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRlERNRGKGAARNAGLAAAR 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 492503189  84 GKYVYFMDSDDYLEPEALETCYIKCERQALDFVF 117
Cdd:COG0463   83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-176 3.76e-31

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: 114.41  E-value: 3.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189    7 SVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQ-YNQGPSVTRNKGYEYTQGK 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLpENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   86 YVYFMDSDDYLEPEALETCYikcerQALDFVFFDADILNKEKHKNISLNYQRKDCTNPELVYQgpYILKLLIDHKAYSPS 165
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLV-----EALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPF--FLGLRLLGLNLPFLI 153

                         170
                  ....*....|.
gi 492503189  166 PCLNFIRREYL 176
Cdd:pfam00535 154 GGFALYRREAL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-106 6.37e-30

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: 111.06  E-value: 6.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADE-DKRIRIYTQYNQGPSVTRNKGYEYTQGKY 86
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKdPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100
                 ....*....|....*....|
gi 492503189  87 VYFMDSDDYLEPEALETCYI 106
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVA 100
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-98 4.87e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 44.40  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   7 SVIIPLYNTEE---FVEEAVRSimCQTLREI--EIIVINDGSTDNSLSIIKRLA---DEDKRIRIYTQYNQGPSVTRNKG 78
Cdd:NF038302   4 TVAIPTYNGANrlpEVLERLRS--QIGTESLswEIIVVDNNSTDNTAQVVQEYQknwPSPYPLRYCFEPQQGAAFARQRA 81

                         90       100
                 ....*....|....*....|
gi 492503189  79 YEYTQGKYVYFMDSDDYLEP 98
Cdd:NF038302  82 IQEAKGELIGFLDDDNLPAP 101
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-250 1.79e-40

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 143.65  E-value: 1.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   2 DKNLVSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQYNQGPSVTRNKGYEY 81
Cdd:PRK10073   4 STPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189  82 TQGKYVYFMDSDDYLEPEALETCYIKCERQALDFVFFDAD-ILNKEKHKNISLNYQRKDCTNpelVYQGPYILKLLIDHK 160
Cdd:PRK10073  84 ATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADwCFRDTGETWQSIPSDRLRSTG---VLSGPDWLRMALSSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189 161 AYSPSPCLNFIRREYLTEIQLDFLPGIIHEDQLFTCLLYLQAQRVSSIHKDFFKRRLREDSIM-TSKFSMRNMES---YF 236
Cdd:PRK10073 161 RWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSrLPRQGNKNLNYqrhYI 240

                        250
                 ....*....|....
gi 492503189 237 TITAHLSKFADSHP 250
Cdd:PRK10073 241 KITRMLEKLNRRYA 254
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-117 1.05e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 132.90  E-value: 1.05e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   5 LVSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYT-QYNQGPSVTRNKGYEYTQ 83
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRlERNRGKGAARNAGLAAAR 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 492503189  84 GKYVYFMDSDDYLEPEALETCYIKCERQALDFVF 117
Cdd:COG0463   83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVY 116
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-176 3.76e-31

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: 114.41  E-value: 3.76e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189    7 SVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQ-YNQGPSVTRNKGYEYTQGK 85
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLpENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   86 YVYFMDSDDYLEPEALETCYikcerQALDFVFFDADILNKEKHKNISLNYQRKDCTNPELVYQgpYILKLLIDHKAYSPS 165
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLV-----EALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPF--FLGLRLLGLNLPFLI 153

                         170
                  ....*....|.
gi 492503189  166 PCLNFIRREYL 176
Cdd:pfam00535 154 GGFALYRREAL 164
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-106 6.37e-30

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: 111.06  E-value: 6.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADE-DKRIRIYTQYNQGPSVTRNKGYEYTQGKY 86
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKdPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100
                 ....*....|....*....|
gi 492503189  87 VYFMDSDDYLEPEALETCYI 106
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVA 100
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 6-104 4.33e-25

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: 102.13  E-value: 4.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   6 VSVIIPLYNTEEFVEEAVRSIMCQTLRE--IEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQ-YNQGPSVTRNKGYEYT 82
Cdd:COG1215   31 VSVIIPAYNEEAVIEETLRSLLAQDYPKekLEVIVVDDGSTDETAEIARELAAEYPRVRVIERpENGGKAAALNAGLKAA 110

                         90       100
                 ....*....|....*....|..
gi 492503189  83 QGKYVYFMDSDDYLEPEALETC 104
Cdd:COG1215  111 RGDIVVFLDADTVLDPDWLRRL 132
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
6-102 8.70e-24

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 96.22  E-value: 8.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   6 VSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIrIYTQYNQGPSVTRNKGYEYTQGK 85
Cdd:COG1216    5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRV-IRNPENLGFAAARNLGLRAAGGD 83

                         90
                 ....*....|....*..
gi 492503189  86 YVYFMDSDDYLEPEALE 102
Cdd:COG1216   84 YLLFLDDDTVVEPDWLE 100
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 5-179 6.24e-23

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: 93.81  E-value: 6.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   5 LVSVIIPLYNT-EEFVEEAVRSIMCQTLREIEIIVINDGSTDNSL-SIIKRLADEDKRIRI-YTQYNQGPSVTRNKGYEY 81
Cdd:cd04184    2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEVkRVLKKYAAQDPRIKVvFREENGGISAATNSALEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189  82 TQGKYVYFMDSDDYLEPEALeTCYIKC--ERQALDFVFFDADILNkeKHKNISLNYQRKDcTNPELVYQGPYILKLLIdh 159
Cdd:cd04184   82 ATGEFVALLDHDDELAPHAL-YEVVKAlnEHPDADLIYSDEDKID--EGGKRSEPFFKPD-WSPDLLLSQNYIGHLLV-- 155

                        170       180
                 ....*....|....*....|
gi 492503189 160 kayspspclnfIRREYLTEI 179
Cdd:cd04184  156 -----------YRRSLVRQV 164
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 7-129 1.78e-20

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: 87.22  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   7 SVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLadEDKRIRIYTQYNQGPSVTRNKGYEYTQGKY 86
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKY--EDKITYWISEPDKGIYDAMNKGIALATGDI 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 492503189  87 VYFMDSDDYLEPEALET-CYIKCERQALDFVFFDADILNKEKHK 129
Cdd:cd06433   79 IGFLNSDDTLLPGALLAvVAAFAEHPEVDVVYGDVLLVDENGRV 122
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 8-110 1.33e-17

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: 78.81  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKR--IRIYTQYNQGPSVTRNKGYEYTQGK 85
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRrvLVVRDKENGGKAGALNAGLRHAKGD 80

                         90       100
                 ....*....|....*....|....*
gi 492503189  86 YVYFMDSDDYLEPEALETCYIKCER 110
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFA 105
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 5-116 4.48e-17

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: 78.81  E-value: 4.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   5 LVSVIIPLYNTEEFVEEAVRSIMCQT--LREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQYNQGPSVTRNKGYEYT 82
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRNS 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 492503189  83 QGKYVYFMDSDDYLEPEALETCYIKCERQALDFV 116
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNV 114
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 8-117 5.63e-17

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: 77.23  E-value: 5.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSI--MCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYT-QYNQGPSVTRNKGYEYTQG 84
Cdd:cd04179    1 VVIPAYNEEENIPELVERLlaVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRlSRNFGKGAAVRAGFKAARG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 492503189  85 KYVYFMDSDDYLEPEALETCYIKCERQALDFVF 117
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVI 113
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-103 6.11e-17

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: 77.67  E-value: 6.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   7 SVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQYNQGPSVTRN--KGYEYTQG 84
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNfeSLLQAADG 80

                         90
                 ....*....|....*....
gi 492503189  85 KYVYFMDSDDYLEPEALET 103
Cdd:cd04196   81 DYVFFCDQDDIWLPDKLER 99
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 8-93 1.91e-16

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: 75.59  E-value: 1.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMcQTLREI----EIIVINDGSTDNSLSIIKRLADEDKRIRIYtqynqgpSVTRNKGYE--- 80
Cdd:cd04187    1 IVVPVYNEEENLPELYERLK-AVLESLgydyEIIFVDDGSTDRTLEILRELAARDPRVKVI-------RLSRNFGQQaal 72

                         90
                 ....*....|....*...
gi 492503189  81 -----YTQGKYVYFMDSD 93
Cdd:cd04187   73 lagldHARGDAVITMDAD 90
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 7-102 2.06e-13

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: 69.23  E-value: 2.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189    7 SVIIPLYNTEE--FVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEdkRIRIY----TQYNQGPSVTRNKGYE 80
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDH--NLQVYypnaPDTTYSLAASRNRGTS 78

                          90       100
                  ....*....|....*....|..
gi 492503189   81 YTQGKYVYFMDSDDYLEPEALE 102
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFE 100
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-105 1.78e-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: 64.12  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRiyTQYNQGPSVTRNKGYEYTQGKYV 87
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIR--NGENLGFGAGNNQGIREAKGDYV 78

                         90
                 ....*....|....*...
gi 492503189  88 YFMDSDDYLEPEALETCY 105
Cdd:cd04186   79 LLLNPDTVVEPGALLELL 96
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 8-105 2.85e-12

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: 64.79  E-value: 2.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTLR-EIEIIVINDGSTDNSLSIIK--RLADEDKRIRIYTQYNQGPS-----VTRNKGY 79
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEgTLELSVFNDASTDKSAEIIEkwRKKLEDSGVIVLVGSHNSPSpkgvgYAKNQAI 80

                         90       100
                 ....*....|....*....|....*.
gi 492503189  80 EYTQGKYVYFMDSDDYLEPEALETCY 105
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQY 106
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 6-102 1.95e-11

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: 62.69  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   6 VSVIIPLYNTEEFVEEAVRSIMCQTlreIEIIVINDGSTDNSLSIIKRLADedkriRIYTQYNQGPSVTRNKGYEYTQGK 85
Cdd:cd02511    2 LSVVIITKNEERNIERCLESVKWAV---DEIIVVDSGSTDRTVEIAKEYGA-----KVYQRWWDGFGAQRNFALELATND 73

                         90
                 ....*....|....*..
gi 492503189  86 YVYFMDSDDYLEPEALE 102
Cdd:cd02511   74 WVLSLDADERLTPELAD 90
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 6-102 2.08e-10

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: 59.90  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   6 VSVIIPLYNTEEFVEEAVRSIMCQTLRE--IEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQyNQGPSVTRNKGYEYTQ 83
Cdd:cd06439   31 VTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADKGVKLLRFPE-RRGKAAALNRALALAT 109

                         90
                 ....*....|....*....
gi 492503189  84 GKYVYFMDSDDYLEPEALE 102
Cdd:cd06439  110 GEIVVFTDANALLDPDALR 128
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 6-119 1.81e-09

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


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 56.81  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   6 VSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADedkrIRIYTQynQGPSVTRNKGYEYTQGK 85
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGV----VVISSP--KGRARQMNAGAAAARGD 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 492503189  86 YVYFMDSDDYLEPEALETCYIKCERQALDFVFFD 119
Cdd:cd02522   75 WLLFLHADTRLPPDWDAAIIETLRADGAVAGAFR 108
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-102 4.45e-09

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 55.33  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDKRIRIYTQYNQGPSVTRNKG--YEYTQG- 84
Cdd:cd04185    1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYEGvrRAYELGy 80

                         90
                 ....*....|....*...
gi 492503189  85 KYVYFMDSDDYLEPEALE 102
Cdd:cd04185   81 DWIWLMDDDAIPDPDALE 98
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 8-93 6.82e-09

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: 54.88  E-value: 6.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEE----FVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLADEDK-RIRIYTQ-YNQGpsvtrnKGYEY 81
Cdd:cd04188    1 VVIPAYNEEKrlppTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPaLIRVLTLpKNRG------KGGAV 74

                         90
                 ....*....|....*...
gi 492503189  82 TQG------KYVYFMDSD 93
Cdd:cd04188   75 RAGmlaargDYILFADAD 92
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 8-116 3.12e-07

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: 50.22  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMcQTLREI--EIIVINDGSTDNSLSIIKRLADEDKRIRIYTQYNQ---GPSVTRnkGYEYT 82
Cdd:cd06442    1 IIIPTYNERENIPELIERLD-AALKGIdyEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKrglGSAYIE--GFKAA 77

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 492503189  83 QGKYVYFMDSD-----DYLePEALEtcyiKCERQALDFV 116
Cdd:cd06442   78 RGDVIVVMDADlshppEYI-PELLE----AQLEGGADLV 111
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 7-126 6.65e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 50.15  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   7 SVIIPLYNTEEFVEEAVRSiMCQTLRE---------IEIIVINDGSTDNSLSIIKRLADEDKR----IRIYT-QYNQGPS 72
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKE-TIKYLESrsrkdpkfkYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSlLRNKGKG 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492503189  73 VTRNKGYEYTQGKYVYFMDSD---DYLEPEALETCYIKCERQALDFVFFDADILNKE 126
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDADgatDIDDFDKLEDIMLKIEQNGLGIVFGSRNHLVDS 208
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 3-116 7.46e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 49.31  E-value: 7.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   3 KNLVSVIIPLYNTEEFVeeavrSIMCQTLRE-------IEIIVINDGSTDNSLSIIKRLAD--EDKRIRIYTQYNQ-GPS 72
Cdd:PLN02726   8 AMKYSIIVPTYNERLNI-----ALIVYLIFKalqdvkdFEIIVVDDGSPDGTQDVVKQLQKvyGEDRILLRPRPGKlGLG 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 492503189  73 VTRNKGYEYTQGKYVYFMDSDDYLEPEALETCYIKCERQALDFV 116
Cdd:PLN02726  83 TAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIV 126
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 6-102 7.86e-07

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: 49.17  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   6 VSVIIPLYNT--EEFvEEAVRSIMCQTlrEIEIIVINDGSTDNSLSIIKRLADeDKRIRIYTQynqgpsVTRNK------ 77
Cdd:cd06434    2 VTVIIPVYDEdpDVF-RECLRSILRQK--PLEIIVVTDGDDEPYLSILSQTVK-YGGIFVITV------PHPGKrralae 71

                         90       100
                 ....*....|....*....|....*
gi 492503189  78 GYEYTQGKYVYFMDSDDYLEPEALE 102
Cdd:cd06434   72 GIRHVTTDIVVLLDSDTVWPPNALP 96
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
2-101 8.06e-07

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 49.61  E-value: 8.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   2 DKNLVSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTdnSLSIIKRLADE--DKRIR-IYTQYNQGPSVTRNKG 78
Cdd:PRK10018   3 DNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTAlnDPRITyIHNDINSGACAVRNQA 80

                         90       100
                 ....*....|....*....|...
gi 492503189  79 YEYTQGKYVYFMDSDDYLEPEAL 101
Cdd:PRK10018  81 IMLAQGEYITGIDDDDEWTPNRL 103
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 6-99 1.12e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 49.35  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   6 VSVIIPLYNTEEFVEEAVR--SIMCQTL-REIEIIVINDGSTDNSLSIIKRLADEDKR--IRIYTQYNQGPSVTRNKGYE 80
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRrtTAACESLgKEYEILLIDDGSSDNSAEMLVEAAQAPDShiVAILLNRNYGQHSAIMAGFS 87

                         90
                 ....*....|....*....
gi 492503189  81 YTQGKYVYFMDSDDYLEPE 99
Cdd:PRK10714  88 HVTGDLIITLDADLQNPPE 106
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-197 1.35e-06

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 48.52  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189    6 VSVIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLAD--EDKRIRIYTQYNQ-GPSVTR---NKGY 79
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAArfPDVRLRVIRNARLlGPTGKSrglNHGF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   80 EYTQGKYVYFMDSDDYLEPEALetcyikceRQALDFVffdadilnkeKHKNISLNYQRKDCTNPELVYQGPYILKLLIDH 159
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTL--------KKYVQYF----------DSPKVGAVGTPVFSLNRSTMLSALGALEFALRH 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 492503189  160 K------AYSPSPCLN----FIRREYLTEIqLDFLPGIIHEDQLFTCL 197
Cdd:pfam13641 146 LrmmslrLALGVLPLSgagsAIRREVLKEL-GLFDPFFLLGDDKSLGR 192
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 8-98 2.32e-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: 47.19  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTLREIEIIVINDGSTDNSLSIIKRLAdEDKRIRIYT--QYNQG--PSVTRNKGYEYTQ 83
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFK-SQFPIPIKHvwQEDEGfrKAKIRNKAIAAAK 79

                         90
                 ....*....|....*
gi 492503189  84 GKYVYFMDSDDYLEP 98
Cdd:cd06420   80 GDYLIFIDGDCIPHP 94
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-93 2.54e-06

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: 47.67  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTL--REIEIIVINDGSTDNSLSIIKRLADED----KRIRIYTQYNQGPSVTRNKGYEY 81
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAKPnfqlKILNNSRVSISGKKNALTTAIKA 80

                         90
                 ....*....|..
gi 492503189  82 TQGKYVYFMDSD 93
Cdd:cd04192   81 AKGDWIVTTDAD 92
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 7-122 3.32e-06

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: 46.92  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   7 SVIIPLYNTE--EFVEEAVRSIMCQTLREIEIIVINDGSTDNSL-SIIKRLAdEDKRIRIYT-QYNQGPSVTRNKGYEYT 82
Cdd:cd04195    1 SVLMSVYIKEkpEFLREALESILKQTLPPDEVVLVKDGPVTQSLnEVLEEFK-RKLPLKVVPlEKNRGLGKALNEGLKHC 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492503189  83 QGKYVYFMDSDDYLEPEaletcyiKCERQaLDFVFFDADI 122
Cdd:cd04195   80 TYDWVARMDTDDISLPD-------RFEKQ-LDFIEKNPEI 111
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-98 4.87e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 44.40  E-value: 4.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   7 SVIIPLYNTEE---FVEEAVRSimCQTLREI--EIIVINDGSTDNSLSIIKRLA---DEDKRIRIYTQYNQGPSVTRNKG 78
Cdd:NF038302   4 TVAIPTYNGANrlpEVLERLRS--QIGTESLswEIIVVDNNSTDNTAQVVQEYQknwPSPYPLRYCFEPQQGAAFARQRA 81

                         90       100
                 ....*....|....*....|
gi 492503189  79 YEYTQGKYVYFMDSDDYLEP 98
Cdd:NF038302  82 IQEAKGELIGFLDDDNLPAP 101
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 8-102 1.01e-04

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 42.37  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492503189   8 VIIPLYNTEEFVEEAVRSIMCQTlREIEIIVINDGSTDNSLSIIkRLADEDKRIRIYTQY----NQGPSVTRNKGYEY-- 81
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNK-PNFLVLVIDDASDDDTAGIV-RLAITDSRVHLLRRHlpnaRTGKGDALNAAYDQir 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 492503189  82 --TQGKYVYF-------MDSDDYLEPEALE 102
Cdd:cd06436   79 qiLIEEGADPerviiavIDADGRLDPNALE 108
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 35-96 1.62e-03

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 37.22  E-value: 1.62e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492503189   35 EIIVINDGSTDNSLSIIKRLADED-KRIR-IYTQYNQGPSVTRNKGYEYTQGKYVYFMDSDDYL 96
Cdd:pfam13704  21 HIYVYDNGSDDGTAEILARLPDVSiLRSDlSYKDARFQVDWRNALLARYAEADWVLVVDADEFL 84
 
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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