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Conserved domains on  [gi|2410432431|ref|WP_268418027|]
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glycosyltransferase [Bacillus inaquosorum]

Protein Classification

glycosyltransferase( domain architecture ID 11440297)

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

EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  12691742|9445404
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-236 1.21e-70

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: 220.56  E-value: 1.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPNagKGKSSALNSGFAE 132
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN--GGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 133 SNGDVICVYDADNTPEKMAVYYLVLGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQGGRWKWFKIATIPG 212
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156
                         170       180
                  ....*....|....*....|....
gi 2410432431 213 TNFAIRRSIIEKLGGWDDKALAED 236
Cdd:cd06423   157 AFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
8-413 2.20e-68

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: 218.84  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431   8 ISLSLIWVMLLYHMFLMqggfrhymtfernIPKWRENMKELPKVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVN 87
Cdd:COG1215     1 LLLLLALLALLYLLLLA-------------LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  88 DNSSDRTGDIVNEFSEKYDFIKmVITKPPNagKGKSSALNSGFAESNGDVICVYDADNTPEKMAVYYLVlGLMNDEKAGA 167
Cdd:COG1215    68 DGSTDETAEIARELAAEYPRVR-VIERPEN--GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 168 vvgkfrvinatktlltkfinieticfqwmaqggrwkwfkiatiPGTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLG 247
Cdd:COG1215   144 -------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAG 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 248 YHIRFFPAAITWEQEPETWKVWWRQRTRWARGNQYVVLKFLAQFfklkrkriifdlfyffftyflfffgvimsNTIFVVN 327
Cdd:COG1215   181 YRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLL-----------------------------RPRRLLL 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 328 LFYDLHLSVGFLAMILWILAFFLFMTEVMITLSIEKTemnRQNFFIVFLMYFTYSQAWIVlviyslfveikHRLFKQEVK 407
Cdd:COG1215   232 FLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLAL---RRRRLLLPLLHLLYGLLLLL-----------AALRGKKVV 297

                  ....*.
gi 2410432431 408 WYKTER 413
Cdd:COG1215   298 WKKTPR 303
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-236 1.21e-70

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: 220.56  E-value: 1.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPNagKGKSSALNSGFAE 132
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN--GGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 133 SNGDVICVYDADNTPEKMAVYYLVLGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQGGRWKWFKIATIPG 212
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156
                         170       180
                  ....*....|....*....|....
gi 2410432431 213 TNFAIRRSIIEKLGGWDDKALAED 236
Cdd:cd06423   157 AFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
8-413 2.20e-68

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: 218.84  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431   8 ISLSLIWVMLLYHMFLMqggfrhymtfernIPKWRENMKELPKVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVN 87
Cdd:COG1215     1 LLLLLALLALLYLLLLA-------------LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  88 DNSSDRTGDIVNEFSEKYDFIKmVITKPPNagKGKSSALNSGFAESNGDVICVYDADNTPEKMAVYYLVlGLMNDEKAGA 167
Cdd:COG1215    68 DGSTDETAEIARELAAEYPRVR-VIERPEN--GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 168 vvgkfrvinatktlltkfinieticfqwmaqggrwkwfkiatiPGTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLG 247
Cdd:COG1215   144 -------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAG 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 248 YHIRFFPAAITWEQEPETWKVWWRQRTRWARGNQYVVLKFLAQFfklkrkriifdlfyffftyflfffgvimsNTIFVVN 327
Cdd:COG1215   181 YRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLL-----------------------------RPRRLLL 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 328 LFYDLHLSVGFLAMILWILAFFLFMTEVMITLSIEKTemnRQNFFIVFLMYFTYSQAWIVlviyslfveikHRLFKQEVK 407
Cdd:COG1215   232 FLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLAL---RRRRLLLPLLHLLYGLLLLL-----------AALRGKKVV 297

                  ....*.
gi 2410432431 408 WYKTER 413
Cdd:COG1215   298 WKKTPR 303
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
49-254 1.60e-33

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 124.81  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKmVITKPPNagKGKSSALNS 128
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAKDPRIR-VIRLERN--RGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 129 GFAESNGDVICVYDAD--NTPEKMAVyylVLGLMNDEKAGAVVGKfRVINATKTLLTKFINIETICFQWMaqggrwkwFK 206
Cdd:COG0463    77 GLAAARGDYIAFLDADdqLDPEKLEE---LVAALEEGPADLVYGS-RLIREGESDLRRLGSRLFNLVRLL--------TN 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2410432431 207 IATIPGTNFAIRRSIIEKLGgwDDKALAEDTELtIRVYNLGYHIRFFP 254
Cdd:COG0463   145 LPDSTSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
52-224 9.59e-33

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: 121.35  E-value: 9.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  52 SVLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKmVITKPPNagKGKSSALNSGFA 131
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP--NFEIIVVDDGSTDGTVEIAEEYAKKDPRVR-VIRLPEN--RGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 132 ESNGDVICVYDADNTPEKMAVYYLVlGLMNDEKAGAVVGKFRVINATKTLLTKFINIeTICFQWMAQGGRWKWFKIATIP 211
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLV-EALEEDGADVVVGSRYVIFGETGEYRRASRI-TLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 2410432431 212 GTNFAIRRSIIEK 224
Cdd:pfam00535 154 GGFALYRREALEE 166
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-145 1.81e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 61.71  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431   7 FISLSLIWVMLLYHMFLMQGGFRHYMTFERNIPKWRENMKELPKV----------SVLIPAHNEEVVIRQTLKAMV---- 72
Cdd:PTZ00260   18 GLVVGLALLFYPYISWPDDDKVIRQVKSSVIHEKSKEVDKENYINnilkdsdvdlSIVIPAYNEEDRLPKMLKETIkyle 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2410432431  73 --NLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDF--IKM-VITKPPNAGKGksSALNSGFAESNGDVICVYDADN 145
Cdd:PTZ00260   98 srSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnIDIrLLSLLRNKGKG--GAVRIGMLASRGKYILMVDADG 173
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-236 1.21e-70

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: 220.56  E-value: 1.21e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPNagKGKSSALNSGFAE 132
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKEN--GGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 133 SNGDVICVYDADNTPEKMAVYYLVLGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQGGRWKWFKIATIPG 212
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156
                         170       180
                  ....*....|....*....|....
gi 2410432431 213 TNFAIRRSIIEKLGGWDDKALAED 236
Cdd:cd06423   157 AFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
8-413 2.20e-68

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: 218.84  E-value: 2.20e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431   8 ISLSLIWVMLLYHMFLMqggfrhymtfernIPKWRENMKELPKVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVN 87
Cdd:COG1215     1 LLLLLALLALLYLLLLA-------------LARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  88 DNSSDRTGDIVNEFSEKYDFIKmVITKPPNagKGKSSALNSGFAESNGDVICVYDADNTPEKMAVYYLVlGLMNDEKAGA 167
Cdd:COG1215    68 DGSTDETAEIARELAAEYPRVR-VIERPEN--GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 168 vvgkfrvinatktlltkfinieticfqwmaqggrwkwfkiatiPGTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLG 247
Cdd:COG1215   144 -------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAG 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 248 YHIRFFPAAITWEQEPETWKVWWRQRTRWARGNQYVVLKFLAQFfklkrkriifdlfyffftyflfffgvimsNTIFVVN 327
Cdd:COG1215   181 YRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLL-----------------------------RPRRLLL 231
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 328 LFYDLHLSVGFLAMILWILAFFLFMTEVMITLSIEKTemnRQNFFIVFLMYFTYSQAWIVlviyslfveikHRLFKQEVK 407
Cdd:COG1215   232 FLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLAL---RRRRLLLPLLHLLYGLLLLL-----------AALRGKKVV 297

                  ....*.
gi 2410432431 408 WYKTER 413
Cdd:COG1215   298 WKKTPR 303
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
46-280 2.77e-37

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: 135.79  E-value: 2.77e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  46 KELPKVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKydFIKmVITKPPNAGKGksSA 125
Cdd:cd06439    26 AYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEIAREYADK--GVK-LLRFPERRGKA--AA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 126 LNSGFAESNGDVICVYDADNTPEKMAVYYLVlGLMNDEKAGAVVGKFRVINATKTLltkfinieticfqwMAQGGRWKWF 205
Cdd:cd06439   101 LNRALALATGEIVVFTDANALLDPDALRLLV-RHFADPSVGAVSGELVIVDGGGSG--------------SGEGLYWKYE 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 206 --------KIATIPGTN---FAIRRSIIEklgGWDDKALAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRT 274
Cdd:cd06439   166 nwlkraesRLGSTVGANgaiYAIRRELFR---PLPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRV 242

                  ....*.
gi 2410432431 275 RWARGN 280
Cdd:cd06439   243 RIAAGN 248
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
49-280 1.28e-36

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: 133.85  E-value: 1.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEV-VIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDFIkmVITKPPNAGKgKSSALN 127
Cdd:cd06421     1 PTVDVFIPTYNEPLeIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYR--YLTRPDNRHA-KAGNLN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 128 SGFAESNGDVICVYDADNTPEKMavyYL--VLGLMNDEKAGAVVG---KFRVINATKTLLTKFINIETICFQWMAQGGrw 202
Cdd:cd06421    78 NALAHTTGDFVAILDADHVPTPD---FLrrTLGYFLDDPKVALVQtpqFFYNPDPFDWLADGAPNEQELFYGVIQPGR-- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2410432431 203 KWFKIATIPGTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRTRWARGN 280
Cdd:cd06421   153 DRWGAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGM 230
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
49-279 5.78e-34

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: 126.99  E-value: 5.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTgdivNEFSEKYDFIKM--VITKPPNAGKGKSSAL 126
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEET----IAAARALRLPSIfrVVVVPPSQPRTKPKAC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 127 NSGFAESNGDVICVYDADNTPE----KMAVYYLVLGlmnDEKAGAVVGKFRVINATKTLLTKFINIE-TICFQWMAQG-G 200
Cdd:cd06427    77 NYALAFARGEYVVIYDAEDAPDpdqlKKAVAAFARL---DDKLACVQAPLNYYNARENWLTRMFALEyAAWFDYLLPGlA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 201 RWKWfkiaTIP--GTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLGYHIRFFPAAiTWEQEPETWKVWWRQRTRWAR 278
Cdd:cd06427   154 RLGL----PIPlgGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNST-TLEEANNALGNWIRQRSRWIK 228

                  .
gi 2410432431 279 G 279
Cdd:cd06427   229 G 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
49-254 1.60e-33

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 124.81  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKmVITKPPNagKGKSSALNS 128
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAKDPRIR-VIRLERN--RGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 129 GFAESNGDVICVYDAD--NTPEKMAVyylVLGLMNDEKAGAVVGKfRVINATKTLLTKFINIETICFQWMaqggrwkwFK 206
Cdd:COG0463    77 GLAAARGDYIAFLDADdqLDPEKLEE---LVAALEEGPADLVYGS-RLIREGESDLRRLGSRLFNLVRLL--------TN 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2410432431 207 IATIPGTNFAIRRSIIEKLGgwDDKALAEDTELtIRVYNLGYHIRFFP 254
Cdd:COG0463   145 LPDSTSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
52-224 9.59e-33

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: 121.35  E-value: 9.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  52 SVLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKmVITKPPNagKGKSSALNSGFA 131
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP--NFEIIVVDDGSTDGTVEIAEEYAKKDPRVR-VIRLPEN--RGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 132 ESNGDVICVYDADNTPEKMAVYYLVlGLMNDEKAGAVVGKFRVINATKTLLTKFINIeTICFQWMAQGGRWKWFKIATIP 211
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLV-EALEEDGADVVVGSRYVIFGETGEYRRASRI-TLSRLPFFLGLRLLGLNLPFLI 153
                         170
                  ....*....|...
gi 2410432431 212 GTNFAIRRSIIEK 224
Cdd:pfam00535 154 GGFALYRREALEE 166
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
49-279 1.20e-30

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: 117.80  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDN---SSDRTGDIVNEFSEKYDFIKMVITkpPNAGKGKSSA 125
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDStdeTVRLAREIVEEYAAQGVNIKHVRR--ADRTGYKAGA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 126 LNSGFAESNGDVICVYDADNTPEKmavYYL--VLGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQGGRWK 203
Cdd:cd06437    79 LAEGMKVAKGEYVAIFDADFVPPP---DFLqkTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2410432431 204 WFKIATIPGTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRTRWARG 279
Cdd:cd06437   156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
50-286 9.27e-29

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: 113.10  E-value: 9.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  50 KVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVitkpPNAGKGKSSALNSG 129
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLI----DNPKRIQSAGLNIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 130 FAESNGDVICVYDADNTPEKMAVYYLVLGLMNDEkAGAVVGKFRVINATKTlltkfinIETICfqwMAQ----------- 198
Cdd:cd02525    77 IRNSRGDIIIRVDAHAVYPKDYILELVEALKRTG-ADNVGGPMETIGESKF-------QKAIA---VAQssplgsggsay 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 199 -GGRWKWFKIATIPgtNFAIRRSIIEKLGGWDDKAL-AEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRTRW 276
Cdd:cd02525   146 rGGAVKIGYVDTVH--HGAYRREVFEKVGGFDESLVrNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRY 223
                         250
                  ....*....|
gi 2410432431 277 ARGNQYVVLK 286
Cdd:cd02525   224 GKWRARTLRK 233
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-279 1.22e-28

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: 112.00  E-value: 1.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPNAGKGKSSALNSGFAE 132
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRVSISGKKNALTTAIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 133 SNGDVICVYDAD-NTPEK-----MAVYylvlglmNDEKAGAVVGKFRVINAtKTLLTKFINIEticfqWMAQGGRWKWFK 206
Cdd:cd04192    81 AKGDWIVTTDADcVVPSNwlltfVAFI-------QKEQIGLVAGPVIYFKG-KSLLAKFQRLD-----WLSLLGLIAGSF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 207 IATIP----GTNFAIRRSIIEKLGGWD--DKALAEDTELTIRVYNLGY---HIRFFPAAITWEQEPETWKVWWRQRTRWA 277
Cdd:cd04192   148 GLGKPfmcnGANMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYpkvAYLKNPEALVTTQPVTSWKELLNQRKRWA 227

                  ..
gi 2410432431 278 RG 279
Cdd:cd04192   228 SK 229
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
49-279 1.71e-27

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: 109.00  E-value: 1.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPNAG--KGKSSAL 126
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLgpTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 127 NSGFAESNGDVICVYDADNTPEKMAVYYLVlGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQggRWKWFK 206
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYV-QYFDSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMS--LRLALG 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2410432431 207 IATIPGTNFAIRRSIIEKLGGWDDK-ALAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRTRWARG 279
Cdd:pfam13641 157 VLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
53-253 6.66e-24

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 96.81  E-value: 6.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPKdrLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPnagKGKSSALNSGFAE 132
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPN--FEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEEN---QGLAAARNAGLKA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 133 SNGDVICVYDADNTPEKMAVYYLVLGLMNDEKAGAVVGKfrvinatktlltkfinieticfqwmaqggrwkwfkiatipg 212
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGP----------------------------------------- 114
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2410432431 213 TNFAIRRSIIEKLGGWDDKALA-EDTELTIRVYNLGYHIRFF 253
Cdd:cd00761   115 GNLLFRRELLEEIGGFDEALLSgEEDDDFLLRLLRGGKVAFR 156
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
53-239 9.20e-24

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: 97.29  E-value: 9.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSekydfiKMVITKPPNAGKGKSSALNSGFAE 132
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADNCTDDTAQVARAAG------ATVLERHDPERRGKGYALDFGFRH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 133 SNG-----DVICVYDADNTPEKmaVYYLVLGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQGGRWKWFKI 207
Cdd:cd06438    75 LLNladdpDAVVVFDADNLVDP--NALEELNARFAAGARVVQAYYNSKNPDDSWITRLYAFAFLVFNRLRPLGRSNLGLS 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2410432431 208 ATIPGTNFAIRRSIIEKlGGWDDKALAEDTEL 239
Cdd:cd06438   153 CQLGGTGMCFPWAVLRQ-APWAAHSLTEDLEF 183
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
53-146 4.72e-22

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: 92.64  E-value: 4.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKmVITKPPNAGKGksSALNSGFAE 132
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVR-VIRLSRNFGKG--AAVRAGFKA 77
                          90
                  ....*....|....
gi 2410432431 133 SNGDVICVYDADNT 146
Cdd:cd04179    78 ARGDIVVTMDADLQ 91
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
49-288 2.78e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.21  E-value: 2.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFseKYDFIKmVITKPPNAGKGKssALNS 128
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYP--PFEVIVVDNGSTDGTAELLAAL--AFPRVR-VIRNPENLGFAA--ARNL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 129 GFAESNGDVICVYDADNTPEKmavyylvlglmndekagavvgkfrviNATKTLLTKFinieticfqwmaqggrwkwfkia 208
Cdd:COG1216    76 GLRAAGGDYLLFLDDDTVVEP--------------------------DWLERLLAAA----------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 209 tipgtNFAIRRSIIEKLGGWDDK--ALAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRtRWARGNQYVVLK 286
Cdd:COG1216   107 -----CLLIRREVFEEVGGFDERffLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY-YLGRNRLLFLRK 180

                  ..
gi 2410432431 287 FL 288
Cdd:COG1216   181 HG 182
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
52-279 3.14e-19

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 86.30  E-value: 3.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  52 SVLIPAHNE--EVVIrQTLKAMVNLYYPKdrLEIIVVNDNSSDRT-----GDIVNEFSEKYDFIKMvitkPPNAGkGKSS 124
Cdd:cd06435     1 SIHVPCYEEppEMVK-ETLDSLAALDYPN--FEVIVIDNNTKDEAlwkpvEAHCAQLGERFRFFHV----EPLPG-AKAG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 125 ALNSGFAESNGD--VICVYDADNTPEKMAVYYLVlGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQGGRW 202
Cdd:cd06435    73 ALNYALERTAPDaeIIAVIDADYQVEPDWLKRLV-PIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRN 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2410432431 203 KWFKIATIpGTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRTRWARG 279
Cdd:cd06435   152 ERNAIIQH-GTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYG 227
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
142-280 5.19e-18

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


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 81.61  E-value: 5.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 142 DADNTPEKMAVYYLVLgLMNDEKAGAVVGKfRVINATKTLLTKFINIET------ICFQWMAQGGRwkwfkiATIPGTNF 215
Cdd:pfam13632   6 DADTVLPPDCLLGIAN-EMASPEVAIIQGP-ILPMNVGNYLEELAALFFaddhgkSIPVRMALGRV------LPFVGSGA 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2410432431 216 AIRRSIIEKLGGWDDKALAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRTRWARGN 280
Cdd:pfam13632  78 FLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGC 142
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
53-145 1.34e-17

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: 81.07  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNL--YYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPNAGKGksSALNSGF 130
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYleERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPKNRGKG--GAVRAGM 78
                          90
                  ....*....|....*
gi 2410432431 131 AESNGDVICVYDADN 145
Cdd:cd04188    79 LAARGDYILFADADL 93
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
51-288 1.06e-16

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: 78.38  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  51 VSVLIPAHNEEVVIRQTLKAMVNLyyPKDRLEIIVVNDNSSDRTGDIVNEFSEKydfikmVITKPPnagkGKSSALNSGF 130
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRL--NPLPLEIIVVDGGSTDGTVAIARSAGVV------VISSPK----GRARQMNAGA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 131 AESNGDVICVYDADNTPEKMAVYYLVlglMNDEKAGAVVGKFRVinatktlltKFINiETICFQWMAQGgrWKW-FKIAT 209
Cdd:cd02522    69 AAARGDWLLFLHADTRLPPDWDAAII---ETLRADGAVAGAFRL---------RFDD-PGPRLRLLELG--ANLrSRLFG 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 210 IPGTN--FAIRRSIIEKLGGWDDKALAEDTELTIRVYNLGyHIRFFPAAIT-----WEQEPetwkvWWRQRTRwargNQY 282
Cdd:cd02522   134 LPYGDqgLFIRRELFEELGGFPELPLMEDVELVRRLRRRG-RPALLPSPVTtsarrWERNG-----WLRTTLL----NWL 203

                  ....*.
gi 2410432431 283 VVLKFL 288
Cdd:cd02522   204 LLLLYL 209
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
53-236 2.34e-16

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: 77.04  E-value: 2.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLyypKDRLEIIVVNDNSSDRTGDIVNEFSEKYDfIKMVITKPPNAGKGKSSALNSGFA- 131
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRN---KPNFLVLVIDDASDDDTAGIVRLAITDSR-VHLLRRHLPNARTGKGDALNAAYDq 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 132 ------ESNGD----VICVYDADNtpeKMAVYYL--VLGLMNDEKAGAVVGKFRVINATKTLLTKFINIETICFQWMAQG 199
Cdd:cd06436    77 irqiliEEGADpervIIAVIDADG---RLDPNALeaVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQS 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2410432431 200 GRWKWfKIATIPGTNFAIRRSIIEKLGG---WDDkALAED 236
Cdd:cd06436   154 LRALT-GTVGLGGNGQFMRLSALDGLIGeepWSD-SLLED 191
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
51-282 8.26e-14

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: 70.36  E-value: 8.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  51 VSVLIPAHNEEV-VIRQTLKAMVNLyypkDRLEIIVVNDNSSDRTGDIVnefSEKYDFIKMVITKPPNAGKgkSSALNSG 129
Cdd:cd06434     2 VTVIIPVYDEDPdVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSIL---SQTVKYGGIFVITVPHPGK--RRALAEG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 130 FAESNGDVICVYDADNTPEKMAVYYLvLGLMNDEKAGAVVGKFRVINATKT--------LLTKFINIETICfqwMAQGGr 201
Cdd:cd06434    73 IRHVTTDIVVLLDSDTVWPPNALPEM-LKPFEDPKVGGVGTNQRILRPRDSkwsflaaeYLERRNEEIRAA---MSYDG- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 202 wkwfKIATIPGTNFAIRRSII-----------EKLGGWDDKAlAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWW 270
Cdd:cd06434   148 ----GVPCLSGRTAAYRTEILkdflfleeftnETFMGRRLNA-GDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFL 222
                         250
                  ....*....|..
gi 2410432431 271 RQRTRWARGNQY 282
Cdd:cd06434   223 KQQLRWSRSNWR 234
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
111-278 7.50e-13

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: 66.54  E-value: 7.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 111 VITKPPNAGKGKSSALNSGFAESNGDVICVYDADNT--PEKMAvyyLVLGLMNDEKAGAVVGkFRVINATKTLLTKFINI 188
Cdd:pfam13506   7 VVGGPPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRvpPDYLR---DLLAPLADPKVGLVTS-PPVGSDPKGLAAALEAA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 189 ETICFQWMAQGGrWKWFKIATipGTNFAIRRSIIEKLGG---WDDKaLAEDTELTIRVYNLGYHIRFFPAAITWE--QEP 263
Cdd:pfam13506  83 FFNTLAGVLQAA-LSGIGFAV--GMSMAFRRADLERIGGfeaLADY-LAEDYALGKLLRAAGLKVVLSPRPILQTsgPRR 158
                         170
                  ....*....|....*
gi 2410432431 264 ETWKVWWRQRTRWAR 278
Cdd:pfam13506 159 TSFRAFMARQLRWAR 173
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
52-254 1.33e-12

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: 66.41  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  52 SVLIPAHNEEVVIRQTLKAMVNLYYPKdrLEIIVVNDNSSDRTGDIVNEFSEKYDFIkmvITKPpnaGKGKSSALNSGFA 131
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPN--IEYIVIDGGSTDGTVDIIKKYEDKITYW---ISEP---DKGIYDAMNKGIA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 132 ESNGDVICVYDADNTPEKMAVYYLVLGLMNDEKAGAVVGKFRVINATKTLLTKFINIETIcfqwmaqggRWKWFKIATIP 211
Cdd:cd06433    73 LATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFL---------DKFLLYGMPIC 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2410432431 212 GTNFAIRRSIIEKLGGWDDK-ALAEDTELTIRVYNLGYHIRFFP 254
Cdd:cd06433   144 HQATFFRRSLFEKYGGFDESyRIAADYDLLLRLLLAGKIFKYLP 187
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
49-254 1.80e-12

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: 66.07  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHN-EEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDR-TGDIVNEFSEKYDFIKMVItkPPNAGkGKSSAL 126
Cdd:cd04184     1 PLISIVMPVYNtPEKYLREAIESVRAQTYP--NWELCIADDASTDPeVKRVLKKYAAQDPRIKVVF--REENG-GISAAT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 127 NSGFAESNGDVICVYDADNTPEKMAVYYLVLGLMNDEKAGAVVGKFRVINATKTLLTKFI----NIETICFQWMAqggrw 202
Cdd:cd04184    76 NSALELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFkpdwSPDLLLSQNYI----- 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2410432431 203 kwfkiatipgTNFA-IRRSIIEKLGGWDDK-ALAEDTELTIRVYNLGYHIRFFP 254
Cdd:cd04184   151 ----------GHLLvYRRSLVRQVGGFREGfEGAQDYDLVLRVSEHTDRIAHIP 194
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
49-278 3.09e-12

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: 64.93  E-value: 3.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  49 PKVSVLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTGDIVNEFSEKY--DFIKMVITKPPNAGKGKSSAL 126
Cdd:cd02520     1 PGVSILKPLCGVDPNLYENLESFFQQDYP--KYEILFCVQDEDDPAIPVVRKLIAKYpnVDARLLIGGEKVGINPKVNNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 127 NSGFAESNGDVICVYDADNTPEKMAVYYLVLGLMnDEKAGAVVGKFrvinatktlltkfinieticfqwmAQGgrwkwfk 206
Cdd:cd02520    79 IKGYEEARYDILVISDSDISVPPDYLRRMVAPLM-DPGVGLVTCLC------------------------AFG------- 126
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2410432431 207 iATIpgtnfAIRRSIIEKLGGWDDKA--LAEDTELTIRVYNLGYHIRFFPAAITWEQEPETWKVWWRQRTRWAR 278
Cdd:cd02520   127 -KSM-----ALRREVLDAIGGFEAFAdyLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
53-144 1.46e-11

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: 63.71  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNE----EVVIRQTLKAMVNLYYpkdrlEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVitkpPNAGK-GKSSALN 127
Cdd:cd06442     1 IIIPTYNEreniPELIERLDAALKGIDY-----EIIVVDDNSPDGTAEIVRELAKEYPRVRLI----VRPGKrGLGSAYI 71
                          90
                  ....*....|....*..
gi 2410432431 128 SGFAESNGDVICVYDAD 144
Cdd:cd06442    72 EGFKAARGDVIVVMDAD 88
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
53-148 1.65e-11

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: 62.49  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLY-YPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKmVITKPPNAgkGKSSALNSGFA 131
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVLeSLGYDYEIIFVDDGSTDRTLEILRELAARDPRVK-VIRLSRNF--GQQAALLAGLD 77
                          90
                  ....*....|....*....
gi 2410432431 132 ESNGDVICVYDAD--NTPE 148
Cdd:cd04187    78 HARGDAVITMDADlqDPPE 96
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-145 1.81e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 61.71  E-value: 1.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431   7 FISLSLIWVMLLYHMFLMQGGFRHYMTFERNIPKWRENMKELPKV----------SVLIPAHNEEVVIRQTLKAMV---- 72
Cdd:PTZ00260   18 GLVVGLALLFYPYISWPDDDKVIRQVKSSVIHEKSKEVDKENYINnilkdsdvdlSIVIPAYNEEDRLPKMLKETIkyle 97
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2410432431  73 --NLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYDF--IKM-VITKPPNAGKGksSALNSGFAESNGDVICVYDADN 145
Cdd:PTZ00260   98 srSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnIDIrLLSLLRNKGKG--GAVRIGMLASRGKYILMVDADG 173
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
50-150 3.04e-10

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 60.90  E-value: 3.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  50 KVSVLIPAHNEE----VVIRQTLKAMVNLYYPkdrLEIIVVNDNSSDRTGDIVNEFSEKYDfiKMVITKPPNAGKGKSSA 125
Cdd:PRK10714    7 KVSVVIPVYNEQeslpELIRRTTAACESLGKE---YEILLIDDGSSDNSAEMLVEAAQAPD--SHIVAILLNRNYGQHSA 81
                          90       100
                  ....*....|....*....|....*..
gi 2410432431 126 LNSGFAESNGDVICVYDAD--NTPEKM 150
Cdd:PRK10714   82 IMAGFSHVTGDLIITLDADlqNPPEEI 108
PRK10073 PRK10073
putative glycosyl transferase; Provisional
45-146 4.59e-10

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 60.44  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  45 MKELPKVSVLIPAHNEE--------VVIRQTLkamvnlyypkDRLEIIVVNDNSSDRTGDIVNEFSEKYDFIKmVITKpP 116
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGkdfrafmeSLIAQTW----------TALEIIIVNDGSTDNSVEIAKHYAENYPHVR-LLHQ-A 69
                          90       100       110
                  ....*....|....*....|....*....|
gi 2410432431 117 NAgkGKSSALNSGFAESNGDVICVYDADNT 146
Cdd:PRK10073   70 NA--GVSVARNTGLAVATGKYVAFPDADDV 97
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-259 6.77e-10

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 57.57  E-value: 6.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPkdRLEIIVVNDNSSDRTgdiVNEFSEKYDFIKmVITKPPNAGKGKssALNSGFAE 132
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYP--DFEVIVVDNASTDGS---VELLRELFPEVR-LIRNGENLGFGA--GNNQGIRE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 133 SNGDVICVYDADNTPEKMAVYYLVLGLMNDEKAGAVVGKfrvinatktlltkfinieticfqwmaqggrwkwfkiatIPG 212
Cdd:cd04186    73 AKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPK--------------------------------------VSG 114
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2410432431 213 TNFAIRRSIIEKLGGWDDKALA--EDTELTIRVYNLGYHIRFFPAAITW 259
Cdd:cd04186   115 AFLLVRREVFEEVGGFDEDFFLyyEDVDLCLRARLAGYRVLYVPQAVIY 163
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
45-144 2.25e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 57.40  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  45 MKELPKVSVLIPAHNEEV-------VIRQTLKAMvnlyypkDRLEIIVVNDNSSDRTGDIVNEFSEKY--DFIKMVitkp 115
Cdd:PLN02726    5 GEGAMKYSIIVPTYNERLnialivyLIFKALQDV-------KDFEIIVVDDGSPDGTQDVVKQLQKVYgeDRILLR---- 73
                          90       100       110
                  ....*....|....*....|....*....|
gi 2410432431 116 PNAGK-GKSSALNSGFAESNGDVICVYDAD 144
Cdd:PLN02726   74 PRPGKlGLGTAYIHGLKHASGDFVVIMDAD 103
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
52-225 3.09e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 56.87  E-value: 3.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  52 SVLIPAHNEEVVIRQTLKAMVNLYYPKDrlEIIVVNDNSSDRTGDIVNEFSEKYDFIKMVITKPPNAGKGKS--SALNsg 129
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKND--ELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNfeSLLQ-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 130 faESNGDVICVYDADN--TPEKMAVyyLVLGLMNDEKAGAVVGKFRVINA-TKTLLTKFINIETICfqwmAQGGRWKWFK 206
Cdd:cd04196    77 --AADGDYVFFCDQDDiwLPDKLER--LLKAFLKDDKPLLVYSDLELVDEnGNPIGESFFEYQKIK----PGTSFNNLLF 148
                         170
                  ....*....|....*....
gi 2410432431 207 IATIPGTNFAIRRSIIEKL 225
Cdd:cd04196   149 QNVVTGCTMAFNRELLELA 167
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
43-294 5.48e-09

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 58.11  E-value: 5.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  43 ENMKELPKVSVLIPAHNEEV-VIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKYdfikmvITKPPNAgKG 121
Cdd:PRK11498  254 KDMSLWPTVDIFVPTYNEDLnVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKY------IARPTHE-HA 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 122 KSSALNSGFAESNGDVICVYDADNTPEKmAVYYLVLG-LMNDEKAGAV---------------VGKFRVINATKTLltkf 185
Cdd:PRK11498  327 KAGNINNALKYAKGEFVAIFDCDHVPTR-SFLQMTMGwFLKDKKLAMMqtphhffspdpfernLGRFRKTPNEGTL---- 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 186 inieticFQWMAQGGRWKWfkIAT-IPGTNFAIRRSIIEKLGGWDDKALAEDTELTIRVYNLGYH---IRFFPAAitwEQ 261
Cdd:PRK11498  402 -------FYGLVQDGNDMW--DATfFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTsayMRIPQAA---GL 469
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2410432431 262 EPETWKVWWRQRTRWARGnqyvvlkfLAQFFKL 294
Cdd:PRK11498  470 ATESLSAHIGQRIRWARG--------MVQIFRL 494
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
53-155 2.62e-06

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: 48.22  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYpKDRLEIIVVNDNSSDRTGDIVNEFS---EKYDFIKMVITKPPNAGKGKSSALNSG 129
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDF-EGTLELSVFNDASTDKSAEIIEKWRkklEDSGVIVLVGSHNSPSPKGVGYAKNQA 79
                          90       100
                  ....*....|....*....|....*...
gi 2410432431 130 FAESNGDVICVYDADNT--PEKMAVYYL 155
Cdd:cd06913    80 IAQSSGRYLCFLDSDDVmmPQRIRLQYE 107
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
50-173 3.47e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 45.29  E-value: 3.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  50 KVSVLIPAHNEEVVIRQTLKAMVNLYYPKDRLEIIVVNDNSSDRTGDIVNEFSEKydfikmVITK-------PPNAGKGK 122
Cdd:PRK13915   32 TVSVVLPALNEEETVGKVVDSIRPLLMEPLVDELIVIDSGSTDATAERAAAAGAR------VVSReeilpelPPRPGKGE 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2410432431 123 ssALNSGFAESNGDVICVYDADNT-PEKMAVYYLVLGLMNDEKAGAVVGKFR 173
Cdd:PRK13915  106 --ALWRSLAATTGDIVVFVDADLInFDPMFVPGLLGPLLTDPGVHLVKAFYR 155
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
53-251 2.08e-04

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: 41.79  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  53 VLIPAHNEEVVIRQTLKAMVNLYYPKDrlEIIVVNDNSSDRTGDIVNEFSEKYDF-IKMVitKPPNAGKGKSSALNSGFA 131
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPF--EVIIADDGSTEETKELIEEFKSQFPIpIKHV--WQEDEGFRKAKIRNKAIA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 132 ESNGDVICVYDADNTPEKmavyYLVLGLMNDEKAGAVVGKFRViNATKTLLTKFINieticfqwmaqggrwkwfkiatip 211
Cdd:cd06420    77 AAKGDYLIFIDGDCIPHP----DFIADHIELAEPGVFLSGSRV-LLNEKLTERGIR------------------------ 127
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2410432431 212 GTNFAIRRSIIEKLGGWDDKAL---AEDTELTIRVYNLGYHIR 251
Cdd:cd06420   128 GCNMSFWKKDLLAVNGFDEEFTgwgGEDSELVARLLNSGIKFR 170
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
52-253 5.09e-04

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: 41.49  E-value: 5.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  52 SVLIP--AHNEEVVIRQTLKAMVNLYYPKdrLEIIVVNDNSSDRTGDIVNEFSEKYDFIKMviTKPPNAGKGKSSALNSG 129
Cdd:pfam10111   1 SVVIPvyNGEKTHWIQERILNQTFQYDPE--FELIIINDGSTDKTLEEVSSIKDHNLQVYY--PNAPDTTYSLAASRNRG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431 130 FAESNGDVICVYDADN--TP---EKMAVYYLVLGLMNDEKAGAVVGKFRVINATKTLLTKFINIE-TICFQWMAQGGRWK 203
Cdd:pfam10111  77 TSHAIGEYISFIDGDClwSPdkfEKQLKIATSLALQENIQAAVVLPVTDLNDESSNFLRRGGDLTaSGDVLRDLLVFYSP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2410432431 204 WFKIATIPGTNFAIRRSIIEKLGGWDDKAL---AEDTELTIRvynLGYHIRFF 253
Cdd:pfam10111 157 LAIFFAPNSSNALINRQAFIEVGGFDESFRghgAEDFDIFLR---LAARYPFV 206
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
50-104 6.27e-04

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


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 41.12  E-value: 6.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2410432431  50 KVSVLIPAHNEEVVIRQTLKAMVNLYypkDrlEIIVVNDNSSDRTGDIVNEFSEK 104
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAV---D--EIIVVDSGSTDRTVEIAKEYGAK 50
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
52-149 2.64e-03

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: 38.84  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2410432431  52 SVLIPAHNEE--VVIRQTLKAMVNLYYPKDrlEIIVVNDNS-SDRTGDIVNEFSEKYDFikMVITKPPNAGKGKssALNS 128
Cdd:cd04195     1 SVLMSVYIKEkpEFLREALESILKQTLPPD--EVVLVKDGPvTQSLNEVLEEFKRKLPL--KVVPLEKNRGLGK--ALNE 74
                          90       100
                  ....*....|....*....|...
gi 2410432431 129 GFAESNGDVICVYDAD--NTPEK 149
Cdd:cd04195    75 GLKHCTYDWVARMDTDdiSLPDR 97
 
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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