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Conserved domains on  [gi|515631413|ref|WP_017064013|]
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MULTISPECIES: glycosyltransferase family 2 protein [Vibrio]

Protein Classification

glycosyltransferase( domain architecture ID 11440269)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
5-385 4.38e-38

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: 138.72  E-value: 4.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   5 IITTLLCIVTVKFLITLANLERhrihiepkisfKRTEWPTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFS 84
Cdd:COG1215    2 LLLLALLALLYLLLLALARRRR-----------APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  85 TDSTRAKVEALISKFDvNARCISGRTLPtgwlGKSNACMAGALNASGEYVYFIDADTDSAPAMLQSVIDFaiqqktdlls 164
Cdd:COG1215   71 TDETAEIARELAAEYP-RVRVIERPENG----GKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAA---------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 165 fnpkqtfasvaekatlpgiflsiasymnfknsndMTKEEAIANGQAMLFTRKSYDAVGGHAavANAISEDIAFAKVMKVN 244
Cdd:COG1215  136 ----------------------------------FADPGVGASGANLAFRREALEEVGGFD--EDTLGEDLDLSLRLLRA 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 245 GFKIFWAfADKLMSTHMYSDFNSIWAGFSKNMNLIVncQSQAQALKVFIKANIIAWAGPLLMLVSANAFIsdmsaIHAYS 324
Cdd:COG1215  180 GYRIVYV-PDAVVYEEAPETLRALFRQRRRWARGGL--QLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLL-----LALLA 251
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631413 325 LIVSSVMLLVSIVTYFILVKELFVPAKFALtvpfgicvqsLLVLNSYRLSKTNKISWKGRS 385
Cdd:COG1215  252 LLLLLLPALLLALLLALRRRRLLLPLLHLL----------YGLLLLLAALRGKKVVWKKTP 302
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
5-385 4.38e-38

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: 138.72  E-value: 4.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   5 IITTLLCIVTVKFLITLANLERhrihiepkisfKRTEWPTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFS 84
Cdd:COG1215    2 LLLLALLALLYLLLLALARRRR-----------APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  85 TDSTRAKVEALISKFDvNARCISGRTLPtgwlGKSNACMAGALNASGEYVYFIDADTDSAPAMLQSVIDFaiqqktdlls 164
Cdd:COG1215   71 TDETAEIARELAAEYP-RVRVIERPENG----GKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAA---------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 165 fnpkqtfasvaekatlpgiflsiasymnfknsndMTKEEAIANGQAMLFTRKSYDAVGGHAavANAISEDIAFAKVMKVN 244
Cdd:COG1215  136 ----------------------------------FADPGVGASGANLAFRREALEEVGGFD--EDTLGEDLDLSLRLLRA 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 245 GFKIFWAfADKLMSTHMYSDFNSIWAGFSKNMNLIVncQSQAQALKVFIKANIIAWAGPLLMLVSANAFIsdmsaIHAYS 324
Cdd:COG1215  180 GYRIVYV-PDAVVYEEAPETLRALFRQRRRWARGGL--QLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLL-----LALLA 251
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631413 325 LIVSSVMLLVSIVTYFILVKELFVPAKFALtvpfgicvqsLLVLNSYRLSKTNKISWKGRS 385
Cdd:COG1215  252 LLLLLLPALLLALLLALRRRRLLLPLLHLL----------YGLLLLLAALRGKKVVWKKTP 302
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
44-269 5.45e-31

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: 118.49  E-value: 5.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  44 TVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALISKFDvNARCIS--GRTLPTGWlgksNa 121
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDP-RIRLIDnpKRIQSAGL----N- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 122 cmAGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQK-------TDLLSFNPKQTFASVAEKaTLPGifLSIASYMNfk 194
Cdd:cd02525   75 --IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGadnvggpMETIGESKFQKAIAVAQS-SPLG--SGGSAYRG-- 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631413 195 NSNDMTKEEAIANGqamLFTRKSYDAVGGH--AAVANaisEDIAFAKVMKVNGFKIfWAFADKLMSTHMYSDFNSIW 269
Cdd:cd02525  148 GAVKIGYVDTVHHG---AYRREVFEKVGGFdeSLVRN---EDAELNYRLRKAGYKI-WLSPDIRVYYYPRSTLKKLA 217
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
46-219 1.07e-24

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 99.01  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   46 SVIIPARNEEDNIEISLGSLLKQSYPKdkFEVIVVDDFSTDSTRAKVEALISKFDvnarCISGRTLPTGWlGKSNACMAG 125
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN--FEIIVVDDGSTDGTVEIAEEYAKKDP----RVRVIRLPENR-GKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  126 ALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLSFNPKQTFASVAEKATLPGIFLSIasYMNFKNSNDMTKEEAI 205
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSR--LPFFLGLRLLGLNLPF 151
                         170
                  ....*....|....
gi 515631413  206 ANGQAMLFTRKSYD 219
Cdd:pfam00535 152 LIGGFALYRREALE 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
45-239 5.26e-16

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 76.40  E-value: 5.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   45 VSVIIPARNEEDNIEISLGSLLKQSYPkdkFEVIVVDDFSTDSTRAKVEALiskfdvNARCIS---GRtlptgwlgksnA 121
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGD---AEVIVVDGGSTDGTVEIARSL------GAKVIHspkGR-----------A 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  122 C-M-AGALNASGEYVYFIDADT---DSAPAMLQSVI----------DFAIQQKTDLLSFnpkqtfasvaekatlpgifls 186
Cdd:TIGR04283  61 RqMnAGAALAKGDILLFLHADTrlpKDFLEAIRRALakpgyvagafDLRFDGPGLLLRL--------------------- 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515631413  187 IASYMNFKnsndmTKEEAIANG-QAMLFTRKSYDAVGGHAAVanAISEDIAFAK 239
Cdd:TIGR04283 120 IEWGVNLR-----SRLTGIPYGdQGLFVRRSLFEQIGGFPDI--PLMEDIELSR 166
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
38-162 3.34e-11

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 62.79  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  38 KRTEWPTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALISKFDvNARcISGRTLPtGWLG 117
Cdd:PLN02726   4 PGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYG-EDR-ILLRPRP-GKLG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515631413 118 KSNACMAGALNASGEYVYFIDADTDSAPAMLQSVIdfAIQQKTDL 162
Cdd:PLN02726  81 LGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFI--KKQRETGA 123
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
5-385 4.38e-38

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: 138.72  E-value: 4.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   5 IITTLLCIVTVKFLITLANLERhrihiepkisfKRTEWPTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFS 84
Cdd:COG1215    2 LLLLALLALLYLLLLALARRRR-----------APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  85 TDSTRAKVEALISKFDvNARCISGRTLPtgwlGKSNACMAGALNASGEYVYFIDADTDSAPAMLQSVIDFaiqqktdlls 164
Cdd:COG1215   71 TDETAEIARELAAEYP-RVRVIERPENG----GKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAA---------- 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 165 fnpkqtfasvaekatlpgiflsiasymnfknsndMTKEEAIANGQAMLFTRKSYDAVGGHAavANAISEDIAFAKVMKVN 244
Cdd:COG1215  136 ----------------------------------FADPGVGASGANLAFRREALEEVGGFD--EDTLGEDLDLSLRLLRA 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 245 GFKIFWAfADKLMSTHMYSDFNSIWAGFSKNMNLIVncQSQAQALKVFIKANIIAWAGPLLMLVSANAFIsdmsaIHAYS 324
Cdd:COG1215  180 GYRIVYV-PDAVVYEEAPETLRALFRQRRRWARGGL--QLLLKHRPLLRPRRLLLFLLLLLLPLLLLLLL-----LALLA 251
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515631413 325 LIVSSVMLLVSIVTYFILVKELFVPAKFALtvpfgicvqsLLVLNSYRLSKTNKISWKGRS 385
Cdd:COG1215  252 LLLLLLPALLLALLLALRRRRLLLPLLHLL----------YGLLLLLAALRGKKVVWKKTP 302
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
44-269 5.45e-31

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: 118.49  E-value: 5.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  44 TVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALISKFDvNARCIS--GRTLPTGWlgksNa 121
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDP-RIRLIDnpKRIQSAGL----N- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 122 cmAGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQK-------TDLLSFNPKQTFASVAEKaTLPGifLSIASYMNfk 194
Cdd:cd02525   75 --IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGadnvggpMETIGESKFQKAIAVAQS-SPLG--SGGSAYRG-- 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515631413 195 NSNDMTKEEAIANGqamLFTRKSYDAVGGH--AAVANaisEDIAFAKVMKVNGFKIfWAFADKLMSTHMYSDFNSIW 269
Cdd:cd02525  148 GAVKIGYVDTVHHG---AYRREVFEKVGGFdeSLVRN---EDAELNYRLRKAGYKI-WLSPDIRVYYYPRSTLKKLA 217
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
43-248 3.35e-30

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 115.18  E-value: 3.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARNEEDNIEISLGSLLKQSYPkdKFEVIVVDDFSTDSTRAKVEALISKfDVNARCISGRTlptgWLGKSNAC 122
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAK-DPRIRVIRLER----NRGKGAAR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 123 MAGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLSFNPKQTFASVAEKATLPGIFLSIASYMNFKNSndmtke 202
Cdd:COG0463   75 NAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDS------ 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 515631413 203 eaiaNGQAMLFTRKSYDAVGghaaVANAISEDIAFAKVMKvNGFKI 248
Cdd:COG0463  149 ----TSGFRLFRREVLEELG----FDEGFLEDTELLRALR-HGFRI 185
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
47-246 6.74e-26

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: 103.91  E-value: 6.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALISKFDVNARCISGRTLPtgWLGKSNACMAGA 126
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVS--ISGKKNALTTAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 127 LNASGEYVYFIDADTDSAPAMLQsVIDFAIQQKTDLL-----SFNPKQTFASVAEKATLPGIFLSIASYMNFKNSNdmtk 201
Cdd:cd04192   79 KAAKGDWIVTTDADCVVPSNWLL-TFVAFIQKEQIGLvagpvIYFKGKSLLAKFQRLDWLSLLGLIAGSFGLGKPF---- 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515631413 202 eeaIANGQAMLFTRKSYDAVGGHAAVANAISEDIAFAKVMKVNGF 246
Cdd:cd04192  154 ---MCNGANMAYRKEAFFEVGGFEGNDHIASGDDELLLAKVASKY 195
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
46-219 1.07e-24

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


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 99.01  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   46 SVIIPARNEEDNIEISLGSLLKQSYPKdkFEVIVVDDFSTDSTRAKVEALISKFDvnarCISGRTLPTGWlGKSNACMAG 125
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN--FEIIVVDDGSTDGTVEIAEEYAKKDP----RVRVIRLPENR-GKAGARNAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  126 ALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLSFNPKQTFASVAEKATLPGIFLSIasYMNFKNSNDMTKEEAI 205
Cdd:pfam00535  74 LRAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSR--LPFFLGLRLLGLNLPF 151
                         170
                  ....*....|....
gi 515631413  206 ANGQAMLFTRKSYD 219
Cdd:pfam00535 152 LIGGFALYRREALE 165
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
47-141 4.13e-23

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: 94.50  E-value: 4.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYPkdKFEVIVVDDFSTDSTRAKVEALISKFDVNARCISGRtlptgWLGKSNACMAGA 126
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYP--NFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEE-----NQGLAAARNAGL 73
                         90
                 ....*....|....*
gi 515631413 127 LNASGEYVYFIDADT 141
Cdd:cd00761   74 KAARGEYILFLDADD 88
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
47-162 1.52e-19

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: 85.32  E-value: 1.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALISKfDVNARCISgrtLPTGwLGKSNACMAGA 126
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAAR-VPRVRVIR---LSRN-FGKGAAVRAGF 75
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515631413 127 LNASGEYVYFIDAD-TDSaPAMLQSVIDFAIQQKTDL 162
Cdd:cd04179   76 KAARGDIVVTMDADlQHP-PEDIPKLLEKLLEGGADV 111
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
17-141 3.49e-19

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: 86.10  E-value: 3.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  17 FLITLANLERHRIHIEPKisfkrTEWPTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALI 96
Cdd:cd06439    8 LLKLLARLRPKPPSLPDP-----AYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEIAREYA 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 515631413  97 skfDVNARCI--SGRtlptgwLGKSNACMAGALNASGEYVYFIDADT 141
Cdd:cd06439   83 ---DKGVKLLrfPER------RGKAAALNRALALATGEIVVFTDANA 120
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
45-239 1.02e-18

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: 84.16  E-value: 1.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  45 VSVIIPARNEEDNIEISLGSLLKQ-SYPkdkFEVIVVDDFSTDSTRAKVEALiskfdvNARCISGRTlptgwlGKSNACM 123
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLnPLP---LEIIVVDGGSTDGTVAIARSA------GVVVISSPK------GRARQMN 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 124 AGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLSFNPKqtFASvaekatlPGIFLSIASYMNFKNSNDMTkee 203
Cdd:cd02522   66 AGAAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAFRLR--FDD-------PGPRLRLLELGANLRSRLFG--- 133
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 515631413 204 aIANG-QAMLFTRKSYDAVGGHAAVanAISEDIAFAK 239
Cdd:cd02522  134 -LPYGdQGLFIRRELFEELGGFPEL--PLMEDVELVR 167
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
47-141 1.29e-18

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: 82.66  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYPkdKFEVIVVDDFSTDSTRAKVEAL-ISKFDVNARCISGRTlptgwLGKSNACMAG 125
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELaALYIRRVLVVRDKEN-----GGKAGALNAG 73
                         90
                 ....*....|....*.
gi 515631413 126 ALNASGEYVYFIDADT 141
Cdd:cd06423   74 LRHAKGDIVVVLDADT 89
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
43-155 3.02e-17

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 79.27  E-value: 3.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARNEEDNIEISLGSLLKQSYPkdKFEVIVVDDFSTDSTRAKVEALISKfdvNARCISGrtlpTGWLGKSNAC 122
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYP--PFEVIVVDNGSTDGTAELLAALAFP---RVRVIRN----PENLGFAAAR 73
                         90       100       110
                 ....*....|....*....|....*....|...
gi 515631413 123 MAGALNASGEYVYFIDADTDSAPAMLQSVIDFA 155
Cdd:COG1216   74 NLGLRAAGGDYLLFLDDDTVVEPDWLERLLAAA 106
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
45-239 5.26e-16

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 76.40  E-value: 5.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   45 VSVIIPARNEEDNIEISLGSLLKQSYPkdkFEVIVVDDFSTDSTRAKVEALiskfdvNARCIS---GRtlptgwlgksnA 121
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGD---AEVIVVDGGSTDGTVEIARSL------GAKVIHspkGR-----------A 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  122 C-M-AGALNASGEYVYFIDADT---DSAPAMLQSVI----------DFAIQQKTDLLSFnpkqtfasvaekatlpgifls 186
Cdd:TIGR04283  61 RqMnAGAALAKGDILLFLHADTrlpKDFLEAIRRALakpgyvagafDLRFDGPGLLLRL--------------------- 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515631413  187 IASYMNFKnsndmTKEEAIANG-QAMLFTRKSYDAVGGHAAVanAISEDIAFAK 239
Cdd:TIGR04283 120 IEWGVNLR-----SRLTGIPYGdQGLFVRRSLFEQIGGFPDI--PLMEDIELSR 166
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
47-140 6.27e-16

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: 75.68  E-value: 6.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLK--QSYPKDKFEVIVVDDFSTDSTRAKVEALISKFDVNARCIsgrTLPTGwLGKSNACMA 124
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEylEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVL---TLPKN-RGKGGAVRA 76
                         90
                 ....*....|....*.
gi 515631413 125 GALNASGEYVYFIDAD 140
Cdd:cd04188   77 GMLAARGDYILFADAD 92
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
47-162 2.30e-14

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: 71.80  E-value: 2.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYPKDkFEVIVVDDFSTDSTRAKVEALISKFDvNARCISgrtlPTGWLGKSNACMAGA 126
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGID-YEIIVVDDNSPDGTAEIVRELAKEYP-RVRLIV----RPGKRGLGSAYIEGF 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515631413 127 LNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDL 162
Cdd:cd06442   75 KAARGDVIVVMDADLSHPPEYIPELLEAQLEGGADL 110
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
44-140 5.21e-14

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: 70.78  E-value: 5.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  44 TVSVIIPARNEEDNIEISLGSLLKQSypkDkfEVIVVDDFSTDSTRAKVEALISKFDVNArcisgrtlptgWLGKSNACM 123
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAV---D--EIIVVDSGSTDRTVEIAKEYGAKVYQRW-----------WDGFGAQRN 64
                         90
                 ....*....|....*..
gi 515631413 124 AGALNASGEYVYFIDAD 140
Cdd:cd02511   65 FALELATNDWVLSLDAD 81
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
47-140 7.05e-13

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: 66.35  E-value: 7.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEI---SLGSLLKQsyPKDKFEVIVVDDFSTDSTRAKVEALISKfDVNARCISgrtlptgwL----GKS 119
Cdd:cd04187    1 IVVPVYNEEENLPElyeRLKAVLES--LGYDYEIIFVDDGSTDRTLEILRELAAR-DPRVKVIR--------LsrnfGQQ 69
                         90       100
                 ....*....|....*....|.
gi 515631413 120 NACMAGALNASGEYVYFIDAD 140
Cdd:cd04187   70 AALLAGLDHARGDAVITMDAD 90
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
43-251 9.72e-13

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: 67.01  E-value: 9.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   43 PTVSVIIPARNEEDNIEISLGSLLKQSYPKdkFEVIVVDDFSTDSTRAKVEALISKF-DVNARCISgRTLPTGWLGKSNA 121
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPP--VEVVVVVNPSDAETLDVAEEIAARFpDVRLRVIR-NARLLGPTGKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  122 CMAGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQK-----TDLLSFNPKqTFASVAEKATLPGIFLSIASYMNFKNS 196
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKvgavgTPVFSLNRS-TMLSALGALEFALRHLRMMSLRLALGV 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 515631413  197 ndmtkeeAIANGQAMLFTRKSYDAVGGHAAvANAISEDIAFAKVMKVNGFKIFWA 251
Cdd:pfam13641 158 -------LPLSGAGSAIRREVLKELGLFDP-FFLLGDDKSLGRRLRRHGWRVAYA 204
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
38-162 3.34e-11

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 62.79  E-value: 3.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  38 KRTEWPTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALISKFDvNARcISGRTLPtGWLG 117
Cdd:PLN02726   4 PGEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYG-EDR-ILLRPRP-GKLG 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 515631413 118 KSNACMAGALNASGEYVYFIDADTDSAPAMLQSVIdfAIQQKTDL 162
Cdd:PLN02726  81 LGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFI--KKQRETGA 123
PRK10073 PRK10073
putative glycosyl transferase; Provisional
43-166 4.42e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.53  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARNEEDNIEISLGSLLKQSYpkDKFEVIVVDDFSTDSTRAKVEALISKFDvNARCIsgrTLPTGwlGKSNAC 122
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTW--TALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLL---HQANA--GVSVAR 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515631413 123 MAGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLSFN 166
Cdd:PRK10073  78 NTGLAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCN 121
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
46-223 1.57e-10

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: 60.25  E-value: 1.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  46 SVIIPARNEEDNIEISLGSLLKQSYPkdKFEVIVVDDFSTDSTrakVEaLISKF-DVNARCISGRTlpTGwlgksnacMA 124
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYP--NIEYIVIDGGSTDGT---VD-IIKKYeDKITYWISEPD--KG--------IY 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 125 GALN-----ASGEYVYFIDADTDSAPAMLQSVID-FAIQQKTDLLSFNpkqtFASVAEKATLPGIFLSIASYMNFKNSND 198
Cdd:cd06433   65 DAMNkgialATGDIIGFLNSDDTLLPGALLAVVAaFAEHPEVDVVYGD----VLLVDENGRVIGRRRPPPFLDKFLLYGM 140
                        170       180
                 ....*....|....*....|....*
gi 515631413 199 MtkeeaIANgQAMLFTRKSYDAVGG 223
Cdd:cd06433  141 P-----ICH-QATFFRRSLFEKYGG 159
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
43-152 9.29e-10

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 58.48  E-value: 9.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDfSTDSTRAKVEALISK---FDVNARCISgRTLPTGWlgKS 119
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDD-STDETVRLAREIVEEyaaQGVNIKHVR-RADRTGY--KA 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 515631413 120 NACMAGALNASGEYVYFIDADTDSAPAMLQSVI 152
Cdd:cd06437   77 GALAEGMKVAKGEYVAIFDADFVPPPDFLQKTP 109
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
43-249 2.69e-09

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 56.45  E-value: 2.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARNEEDNIEISLGSLLKQSYPkdKFEVI-VVDDfSTDSTRAKVEALISKF-DVNARC-ISGRtlPTGWLGKS 119
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYP--KYEILfCVQD-EDDPAIPVVRKLIAKYpNVDARLlIGGE--KVGINPKV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 120 NACMAGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLSfnpkQTFasvaekatlpgiflsiasymnfknsndm 199
Cdd:cd02520   76 NNLIKGYEEARYDILVISDSDISVPPDYLRRMVAPLMDPGVGLVT----CLC---------------------------- 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 515631413 200 tkeeaiANGQAMLFTRKSYDAVGGHAAVANAISEDIAFAKVMKVNGFKIF 249
Cdd:cd02520  124 ------AFGKSMALRREVLDAIGGFEAFADYLAEDYFLGKLIWRLGYRVV 167
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
47-159 3.23e-09

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 55.64  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYPKdkFEVIVVDDFSTDSTRAKVEalisKFDVNARCISgrtlPTGWLGKSNACMAGA 126
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPD--FEVIVVDNASTDGSVELLR----ELFPEVRLIR----NGENLGFGAGNNQGI 70
                         90       100       110
                 ....*....|....*....|....*....|...
gi 515631413 127 LNASGEYVYFIDADTDSAPAMLQSVIDFAIQQK 159
Cdd:cd04186   71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDP 103
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
43-152 7.36e-09

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 55.66  E-value: 7.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARNEE-DNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALISKFDVNArcisgRTLPTGWLGKsna 121
Cdd:cd06421    1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRY-----LTRPDNRHAK--- 72
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515631413 122 cmAGALNA-----SGEYVYFIDADTDSAPAMLQSVI 152
Cdd:cd06421   73 --AGNLNNalahtTGDFVAILDADHVPTPDFLRRTL 106
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
46-200 2.27e-08

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: 54.98  E-value: 2.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413   46 SVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALIskfDVNARcISGRTLPTGWLGKSNACMAG 125
Cdd:pfam10111   1 SVVIPVYNGEKTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIK---DHNLQ-VYYPNAPDTTYSLAASRNRG 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631413  126 ALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKtdlLSFNPKQTFAsvaekatLPGIFLSIASYMNFKNSNDMT 200
Cdd:pfam10111  77 TSHAIGEYISFIDGDCLWSPDKFEKQLKIATSLA---LQENIQAAVV-------LPVTDLNDESSNFLRRGGDLT 141
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
47-94 3.08e-08

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 52.99  E-value: 3.08e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEA 94
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADNCTDDTAQVARA 48
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
46-140 3.68e-08

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 54.39  E-value: 3.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  46 SVIIPARNEEDNIEISLGSLLK------QSYPKDKFEVIVVDDFSTDSTRAKVEALISKF---DVNARCISGRTLptgwL 116
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETIKylesrsRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNinpNIDIRLLSLLRN----K 148
                         90       100
                 ....*....|....*....|....
gi 515631413 117 GKSNACMAGALNASGEYVYFIDAD 140
Cdd:PTZ00260 149 GKGGAVRIGMLASRGKYILMVDAD 172
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
36-141 1.01e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 49.92  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  36 SFKRTEWP-----------TVSVIIPARNEEDNIE---ISLGSLLKQSYPkDkfEVIVVDDFSTDSTRAKVEAliskfdV 101
Cdd:PRK13915  13 TWHAPDWTieelvaakagrTVSVVLPALNEEETVGkvvDSIRPLLMEPLV-D--ELIVIDSGSTDATAERAAA------A 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 515631413 102 NARCISGRT----LPTGWlGKSNACMAGALNASGEYVYFIDADT 141
Cdd:PRK13915  84 GARVVSREEilpeLPPRP-GKGEALWRSLAATTGDIVVFVDADL 126
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
47-151 1.64e-06

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: 48.15  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQsypKDKFEVIVVDDFSTDSTRAKVEALISKFDVNarcISGRTLPTGWLGKSNACMAGA 126
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRN---KPNFLVLVIDDASDDDTAGIVRLAITDSRVH---LLRRHLPNARTGKGDALNAAY 74
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515631413 127 -----------LNASGEYVYFIDADTDSAPAMLQSV 151
Cdd:cd06436   75 dqirqilieegADPERVIIAVIDADGRLDPNALEAV 110
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
47-140 3.96e-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: 46.80  E-value: 3.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQS-YPkdkFEVIVVDDFSTDSTRAKVEALISKFDVNARCIsgrtlptgW---LGkSNAC 122
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSiLP---FEVIIADDGSTEETKELIEEFKSQFPIPIKHV--------WqedEG-FRKA 68
                         90       100
                 ....*....|....*....|.
gi 515631413 123 MA---GALNASGEYVYFIDAD 140
Cdd:cd06420   69 KIrnkAIAAAKGDYLIFIDGD 89
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
101-248 5.69e-06

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 46.12  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  101 VNARCISGRtlPTGWLGKSNACMAGALNASGEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLS----FNPKQTFASVAE 176
Cdd:pfam13506   3 VRALVVGGP--PVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTsppvGSDPKGLAAALE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515631413  177 KA---TLPGIFLSIASYMNFknsndmtkeeaiANGQAMLFTRKSYDAVGGHAAVANAISEDIAFAKVMKVNGFKI 248
Cdd:pfam13506  81 AAffnTLAGVLQAALSGIGF------------AVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKV 143
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
43-162 9.26e-06

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: 46.04  E-value: 9.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARN-EEDNIEISLGSLLKQSYPKdkFEVIVVDDFSTDSTRAKVEALISKFDVNARCIsgrtlptgwLGKSNA 121
Cdd:cd04184    1 PLISIVMPVYNtPEKYLREAIESVRAQTYPN--WELCIADDASTDPEVKRVLKKYAAQDPRIKVV---------FREENG 69
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515631413 122 CMAGALN-----ASGEYVYFIDADTDSAPAMLQSVIDfAIQQKTDL 162
Cdd:cd04184   70 GISAATNsalelATGEFVALLDHDDELAPHALYEVVK-ALNEHPDA 114
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
46-140 2.54e-05

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: 44.93  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  46 SVIIPARNEEDNIEISLGSLLKQSYPKDkfEVIVVDDFSTDSTRAKVEALISKFDVNARCIS-GRTLptGWlGKS--NAC 122
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKND--ELIISDDGSTDGTVEIIKEYIDKDPFIIILIRnGKNL--GV-ARNfeSLL 75
                         90
                 ....*....|....*...
gi 515631413 123 MAgalnASGEYVYFIDAD 140
Cdd:cd04196   76 QA----ADGDYVFFCDQD 89
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
43-171 6.97e-05

CESA_like_2 is a member of 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: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 43.78  E-value: 6.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  43 PTVSVIIPARNEEDNIEISLGSLLKQSYPKDKFEVIVVDDFSTDSTRAKVEALisKFDVNARCIsgrTLPTGWL-GKSNA 121
Cdd:cd06427    1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARAL--RLPSIFRVV---VVPPSQPrTKPKA 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515631413 122 CMAGALNASGEYVYFIDADTDSAPAML-QSVIDFA--------IQQKtdLLSFNPKQTF 171
Cdd:cd06427   76 CNYALAFARGEYVVIYDAEDAPDPDQLkKAVAAFArlddklacVQAP--LNYYNARENW 132
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
46-139 7.86e-05

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 44.12  E-value: 7.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  46 SVIIPARNEEDNIEI-SLGSLLKQSYPKDKFEVIVVDDFSTDS-TRAKVEALISKFDVNARCIsgrTLPTGwLGKSNACM 123
Cdd:cd02510    1 SVIIIFHNEALSTLLrTVHSVINRTPPELLKEIILVDDFSDKPeLKLLLEEYYKKYLPKVKVL---RLKKR-EGLIRARI 76
                         90
                 ....*....|....*.
gi 515631413 124 AGALNASGEYVYFIDA 139
Cdd:cd02510   77 AGARAATGDVLVFLDS 92
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
47-140 2.44e-04

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: 42.06  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  47 VIIPARNEEDNIEISLGSLLKQSYpKDKFEVIVVDDFSTDSTRAKVEALISKF-DVNARCISGRTL---PTGWLGKSNAC 122
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDF-EGTLELSVFNDASTDKSAEIIEKWRKKLeDSGVIVLVGSHNspsPKGVGYAKNQA 79
                         90
                 ....*....|....*...
gi 515631413 123 MAgalNASGEYVYFIDAD 140
Cdd:cd06913   80 IA---QSSGRYLCFLDSD 94
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
45-145 9.97e-04

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 40.87  E-value: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  45 VSVIIPARNEEDnieiSLGSLLKQSYPKDK-----FEVIVVDDFSTDSTrakVEALISKFDVNARCISGRTLPTGWlGKS 119
Cdd:PRK10714   8 VSVVIPVYNEQE----SLPELIRRTTAACEslgkeYEILLIDDGSSDNS---AEMLVEAAQAPDSHIVAILLNRNY-GQH 79
                         90       100
                 ....*....|....*....|....*.
gi 515631413 120 NACMAGALNASGEYVYFIDADTDSAP 145
Cdd:PRK10714  80 SAIMAGFSHVTGDLIITLDADLQNPP 105
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-181 1.35e-03

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 39.54  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  53 NEEDNIEISLGSLLKQSYPKDkfEVIVVDDFSTDSTRakvEALISKFDVnaRCISGRTLPT--GWLGKSNACMAGALNAS 130
Cdd:cd04185    7 NRLDLLKECLDALLAQTRPPD--HIIVIDNASTDGTA---EWLTSLGDL--DNIVYLRLPEnlGGAGGFYEGVRRAYELG 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413 131 GEYVYFIDADTDSAPAMLQSVIDFAIQQKTDLLS---FNPKQTF------ASVAEKATLP 181
Cdd:cd04185   80 YDWIWLMDDDAIPDPDALEKLLAYADKDNPQFLAplvLDPDGSFvgvlisRRVVEKIGLP 139
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
44-148 3.33e-03

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: 38.77  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515631413  44 TVSVIIPARNEEDNI-EISLGSLLKQsypkDKFEVIVVddfsTDSTRAKVEAlISKFDVNARCISGRTLPtgWLGKSNAC 122
Cdd:cd06434    1 DVTVIIPVYDEDPDVfRECLRSILRQ----KPLEIIVV----TDGDDEPYLS-ILSQTVKYGGIFVITVP--HPGKRRAL 69
                         90       100       110
                 ....*....|....*....|....*....|
gi 515631413 123 MAGALNASGEYVYFIDADT----DSAPAML 148
Cdd:cd06434   70 AEGIRHVTTDIVVLLDSDTvwppNALPEML 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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