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Conserved domains on  [gi|515927832|ref|WP_017358415|]
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glycosyltransferase [Bacillus altitudinis]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11440297)

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

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0006486|GO:0016757
PubMed:  9445404|10521532|12691742|12200473|10508766
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 3.78e-69

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: 216.71  E-value: 3.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPfaGKGKSTALNGGLKA 132
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPK--LEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKE--NGGKAGALNAGLRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 133 STGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETICFQWMAQGGRWKWFGIATIPG 212
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156

                        170       180
                 ....*....|....*....|....
gi 515927832 213 TNFAIRRHILEELGGWDVHALAED 236
Cdd:cd06423  157 AFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 10-413 1.95e-66

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: 214.22  E-value: 1.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  10 LILIWIMLLYHMFLMQggfqhyltyekVLPKWTKQGKDLPTVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDN 89
Cdd:COG1215    1 LLLLLALLALLYLLLL-----------ALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  90 SSDRTGEIVQSFSEQYDHVHMIETKPpfaGKGKSTALNGGLKASTGDVICVYDADNMPEKKAVYHLVlGLLNDPKAGAvv 169
Cdd:COG1215   70 STDETAEIARELAAEYPRVRVIERPE---NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA-- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 170 gkfrvinaaknlltkfinieticfqwmaqggrwkwfgiatiPGTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYV 249
Cdd:COG1215  144 -----------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYR 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 250 IRFFPAAITWEQEPETWKVWWRQRTRWARGNQYVVLKFLRqfmklkrkrmifdlfyffftyflfffgvlLSNGIFIVNLF 329
Cdd:COG1215  183 IVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRP-----------------------------LLRPRRLLLFL 233

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 330 VDLHLSVGAVALILWGLAFFLFLTEVMITLSIEKTEltkQNILIVVLMYFTYSQVWIAlvvyslcveakSRLLKQEVKWY 409
Cdd:COG1215  234 LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALR---RRRLLLPLLHLLYGLLLLL-----------AALRGKKVVWK 299


                 ....
gi 515927832 410 KTER 413
Cdd:COG1215  300 KTPR 303
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 53-236 3.78e-69

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: 216.71  E-value: 3.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPfaGKGKSTALNGGLKA 132
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPK--LEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKE--NGGKAGALNAGLRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 133 STGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETICFQWMAQGGRWKWFGIATIPG 212
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156

                        170       180
                 ....*....|....*....|....
gi 515927832 213 TNFAIRRHILEELGGWDVHALAED 236
Cdd:cd06423  157 AFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 10-413 1.95e-66

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: 214.22  E-value: 1.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  10 LILIWIMLLYHMFLMQggfqhyltyekVLPKWTKQGKDLPTVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDN 89
Cdd:COG1215    1 LLLLLALLALLYLLLL-----------ALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  90 SSDRTGEIVQSFSEQYDHVHMIETKPpfaGKGKSTALNGGLKASTGDVICVYDADNMPEKKAVYHLVlGLLNDPKAGAvv 169
Cdd:COG1215   70 STDETAEIARELAAEYPRVRVIERPE---NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA-- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 170 gkfrvinaaknlltkfinieticfqwmaqggrwkwfgiatiPGTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYV 249
Cdd:COG1215  144 -----------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYR 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 250 IRFFPAAITWEQEPETWKVWWRQRTRWARGNQYVVLKFLRqfmklkrkrmifdlfyffftyflfffgvlLSNGIFIVNLF 329
Cdd:COG1215  183 IVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRP-----------------------------LLRPRRLLLFL 233

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 330 VDLHLSVGAVALILWGLAFFLFLTEVMITLSIEKTEltkQNILIVVLMYFTYSQVWIAlvvyslcveakSRLLKQEVKWY 409
Cdd:COG1215  234 LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALR---RRRLLLPLLHLLYGLLLLL-----------AALRGKKVVWK 299


                 ....
gi 515927832 410 KTER 413
Cdd:COG1215  300 KTPR 303
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 52-224 1.64e-32

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: 120.58  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832   52 SILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKppfAGKGKSTALNGGLK 131
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN--FEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLP---ENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  132 ASTGDVICVYDADNMPEKKAVYHLVlGLLNDPKAGAVVGKFRVINAAKNLLTKFINIeTICFQWMAQGGRWKWFGIATIP 211
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLV-EALEEDGADVVVGSRYVIFGETGEYRRASRI-TLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 515927832  212 GTNFAIRRHILEE 224
Cdd:pfam00535 154 GGFALYRREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 49-254 2.93e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 118.65  E-value: 2.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPFagkGKSTALNG 128
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD--FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNR---GKGAARNA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 129 GLKASTGDVICVYDAD--NMPEKkavYHLVLGLLNDPKAGAVVGKfRVINAAKNLLTKFINIETICFQWMaqggrwkwFG 206
Cdd:COG0463   77 GLAAARGDYIAFLDADdqLDPEK---LEELVAALEEGPADLVYGS-RLIREGESDLRRLGSRLFNLVRLL--------TN 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515927832 207 IATIPGTNFAIRRHILEELgGWDvHALAEDTELtIRVYNLGYVIRFFP 254
Cdd:COG0463  145 LPDSTSGFRLFRREVLEEL-GFD-EGFLEDTEL-LRALRHGFRIAEVP 189
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 49-145 7.32e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 66.22  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEE--------VVIRQTLKAmvqlsypkhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETkppfAGK 120
Cdd:PRK10073   6 PKLSIIIPLYNAGkdfrafmeSLIAQTWTA----------LEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQ----ANA 71

                         90       100
                 ....*....|....*....|....*
gi 515927832 121 GKSTALNGGLKASTGDVICVYDADN 145
Cdd:PRK10073  72 GVSVARNTGLAVATGKYVAFPDADD 96
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 53-236 3.78e-69

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: 216.71  E-value: 3.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPfaGKGKSTALNGGLKA 132
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPK--LEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKE--NGGKAGALNAGLRH 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 133 STGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETICFQWMAQGGRWKWFGIATIPG 212
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156

                        170       180
                 ....*....|....*....|....
gi 515927832 213 TNFAIRRHILEELGGWDVHALAED 236
Cdd:cd06423  157 AFGAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 10-413 1.95e-66

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: 214.22  E-value: 1.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  10 LILIWIMLLYHMFLMQggfqhyltyekVLPKWTKQGKDLPTVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDN 89
Cdd:COG1215    1 LLLLLALLALLYLLLL-----------ALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDG 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  90 SSDRTGEIVQSFSEQYDHVHMIETKPpfaGKGKSTALNGGLKASTGDVICVYDADNMPEKKAVYHLVlGLLNDPKAGAvv 169
Cdd:COG1215   70 STDETAEIARELAAEYPRVRVIERPE---NGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA-- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 170 gkfrvinaaknlltkfinieticfqwmaqggrwkwfgiatiPGTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYV 249
Cdd:COG1215  144 -----------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYR 182

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 250 IRFFPAAITWEQEPETWKVWWRQRTRWARGNQYVVLKFLRqfmklkrkrmifdlfyffftyflfffgvlLSNGIFIVNLF 329
Cdd:COG1215  183 IVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRP-----------------------------LLRPRRLLLFL 233

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 330 VDLHLSVGAVALILWGLAFFLFLTEVMITLSIEKTEltkQNILIVVLMYFTYSQVWIAlvvyslcveakSRLLKQEVKWY 409
Cdd:COG1215  234 LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALR---RRRLLLPLLHLLYGLLLLL-----------AALRGKKVVWK 299


                 ....
gi 515927832 410 KTER 413
Cdd:COG1215  300 KTPR 303
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 30-280 4.98e-40

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: 143.49  E-value: 4.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  30 HYLTYEKVLPKWTK---------QGKDLPTVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQS 100
Cdd:cd06439    1 TYFGYPLLLKLLARlrpkppslpDPAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEIARE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 101 FSEQYDHVHMIETKppfagKGKSTALNGGLKASTGDVICVYDADNMPEKKAVYHLVlGLLNDPKAGAVVGKFRVINAAKn 180
Cdd:cd06439   81 YADKGVKLLRFPER-----RGKAAALNRALALATGEIVVFTDANALLDPDALRLLV-RHFADPSVGAVSGELVIVDGGG- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 181 lltkfinieticfqwMAQGGR--WKWFG--------IATIPGTN---FAIRRHILEELggwDVHALAEDTELTIRVYNLG 247
Cdd:cd06439  154 ---------------SGSGEGlyWKYENwlkraesrLGSTVGANgaiYAIRRELFRPL---PADTINDDFVLPLRIARQG 215

                        250       260       270
                 ....*....|....*....|....*....|...
gi 515927832 248 YVIRFFPAAITWEQEPETWKVWWRQRTRWARGN 280
Cdd:cd06439  216 YRVVYEPDAVAYEEVAEDGSEEFRRRVRIAAGN 248
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 49-279 3.39e-39

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: 140.85  E-value: 3.39e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQSFsEQYDHVHMIETkPPFAGKGKSTALNG 128
Cdd:cd06427    1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARAL-RLPSIFRVVVV-PPSQPRTKPKACNY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 129 GLKASTGDVICVYDADNMPE----KKAVYHLVLGllnDPKAGAVVGKFRVINAAKNLLTKFINIE-TICFQWMAQG-GRW 202
Cdd:cd06427   79 ALAFARGEYVVIYDAEDAPDpdqlKKAVAAFARL---DDKLACVQAPLNYYNARENWLTRMFALEyAAWFDYLLPGlARL 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515927832 203 KWfgiaTIP--GTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYVIRFFPAAiTWEQEPETWKVWWRQRTRWARG 279
Cdd:cd06427  156 GL----PIPlgGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNST-TLEEANNALGNWIRQRSRWIKG 229
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 49-280 4.26e-38

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: 137.70  E-value: 4.26e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEEV-VIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPFAgkgKSTALN 127
Cdd:cd06421    1 PTVDVFIPTYNEPLeIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHA---KAGNLN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 128 GGLKASTGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVG--KFRVINAAKNLLTKFINIETICFQWMAQGGrwKWF 205
Cdd:cd06421   78 NALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTpqFFYNPDPFDWLADGAPNEQELFYGVIQPGR--DRW 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515927832 206 GIATIPGTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYVIRFFPAAITWEQEPETWKVWWRQRTRWARGN 280
Cdd:cd06421  156 GAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGM 230
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 52-224 1.64e-32

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: 120.58  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832   52 SILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKppfAGKGKSTALNGGLK 131
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN--FEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLP---ENRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  132 ASTGDVICVYDADNMPEKKAVYHLVlGLLNDPKAGAVVGKFRVINAAKNLLTKFINIeTICFQWMAQGGRWKWFGIATIP 211
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLV-EALEEDGADVVVGSRYVIFGETGEYRRASRI-TLSRLPFFLGLRLLGLNLPFLI 153

                         170
                  ....*....|...
gi 515927832  212 GTNFAIRRHILEE 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 2.04e-32

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: 122.42  E-value: 2.04e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVInDNSSDRTGEIVQSFSEQY-----DHVHMI-ETKPPFagkgK 122
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVL-DDSTDETVRLAREIVEEYaaqgvNIKHVRrADRTGY----K 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 123 STALNGGLKASTGDVICVYDADNMPEKKAVyHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETICFQWMAQGGRW 202
Cdd:cd06437   76 AGALAEGMKVAKGEYVAIFDADFVPPPDFL-QKTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515927832 203 KWFGIATIPGTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYVIRFFPAAITWEQEPETWKVWWRQRTRWARG 279
Cdd:cd06437  155 STGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 49-254 2.93e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 118.65  E-value: 2.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPFagkGKSTALNG 128
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD--FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNR---GKGAARNA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 129 GLKASTGDVICVYDAD--NMPEKkavYHLVLGLLNDPKAGAVVGKfRVINAAKNLLTKFINIETICFQWMaqggrwkwFG 206
Cdd:COG0463   77 GLAAARGDYIAFLDADdqLDPEK---LEELVAALEEGPADLVYGS-RLIREGESDLRRLGSRLFNLVRLL--------TN 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 515927832 207 IATIPGTNFAIRRHILEELgGWDvHALAEDTELtIRVYNLGYVIRFFP 254
Cdd:COG0463  145 LPDSTSGFRLFRREVLEEL-GFD-EGFLEDTEL-LRALRHGFRIAEVP 189
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 53-279 2.24e-30

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: 117.00  E-value: 2.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQS-FSEQYDHVHMIETKPPFAgKGKSTALNGGLK 131
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFaAAKPNFQLKILNNSRVSI-SGKKNALTTAIK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 132 ASTGDVICVYDAD-NMPEKKAvyHLVLGLLNDPKAGAVVGKFRVInAAKNLLTKFINIETICFQWMAQGgrwkWFGIAtI 210
Cdd:cd04192   80 AAKGDWIVTTDADcVVPSNWL--LTFVAFIQKEQIGLVAGPVIYF-KGKSLLAKFQRLDWLSLLGLIAG----SFGLG-K 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515927832 211 P----GTNFAIRRHILEELGGWD--VHALAEDTELTIRVYNLGYV-IRF--FPAAITWEQEPETWKVWWRQRTRWARG 279
Cdd:cd04192  152 PfmcnGANMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYPkVAYlkNPEALVTTQPVTSWKELLNQRKRWASK 229
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 49-279 2.46e-30

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: 116.70  E-value: 2.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832   49 PTVSILIPAHNEEVVIRQTLKAMVQLSYPkhLLEIIVINDNSSDRTGEIVQSFSEQYDHVHM---IETKPPFAGkGKSTA 125
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARFPDVRLrviRNARLLGPT-GKSRG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  126 LNGGLKASTGDVICVYDADNMPEKKAVyHLVLGLLNDPKAGAVVGKFRViNAAKNLLTKFINIETicFQWMAQ-GGRWKW 204
Cdd:pfam13641  79 LNHGFRAVKSDLVVLHDDDSVLHPGTL-KKYVQYFDSPKVGAVGTPVFS-LNRSTMLSALGALEF--ALRHLRmMSLRLA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515927832  205 FGIATIPGTNFAIRRHILEELGGWDVH-ALAEDTELTIRVYNLGYVIRFFPAAITWEQEPETWKVWWRQRTRWARG 279
Cdd:pfam13641 155 LGVLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 53-239 2.18e-28

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: 110.00  E-value: 2.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQSFSeqydhVHMIETKPPfAGKGKSTALNGGLK- 131
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADNCTDDTAQVARAAG-----ATVLERHDP-ERRGKGYALDFGFRh 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 132 ----ASTGDVICVYDADNMPEKkavyHLVLGLLNDPKAGA--VVGKFRVINAAKNLLTKFINIETICFQWMAQGGRWKWF 205
Cdd:cd06438   75 llnlADDPDAVVVFDADNLVDP----NALEELNARFAAGArvVQAYYNSKNPDDSWITRLYAFAFLVFNRLRPLGRSNLG 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 515927832 206 GIATIPGTNFAIRRHILEElGGWDVHALAEDTEL 239
Cdd:cd06438  151 LSCQLGGTGMCFPWAVLRQ-APWAAHSLTEDLEF 183
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 53-252 1.33e-27

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 107.21  E-value: 1.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPfagKGKSTALNGGLKA 132
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPN--FEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEEN---QGLAAARNAGLKA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 133 STGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKfrvinaaknlltkfinieticfqwmaqggrwkwfgiatipg 212
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGP----------------------------------------- 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 515927832 213 TNFAIRRHILEELGGWDVHALA--EDTELTIRVYNLGYVIRF 252
Cdd:cd00761  115 GNLLFRRELLEEIGGFDEALLSgeEDDDFLLRLLRGGKVAFR 156
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 50-291 6.49e-27

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: 108.09  E-value: 6.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  50 TVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKppfaGKGKSTALNGG 129
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNP----KRIQSAGLNIG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 130 LKASTGDVICVYDADNMPEKKAVYHLVLGLLnDPKAGAVVGkfrvinaaknlltkfiNIETI---CFQW---MAQGGRWK 203
Cdd:cd02525   77 IRNSRGDIIIRVDAHAVYPKDYILELVEALK-RTGADNVGG----------------PMETIgesKFQKaiaVAQSSPLG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 204 wFGIA-----------TIPGTNFAIRRHILEELGGWD---VHalAEDTELTIRVYNLGYVIRFFPAAITWEQEPETWKVW 269
Cdd:cd02525  140 -SGGSayrggavkigyVDTVHHGAYRREVFEKVGGFDeslVR--NEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKL 216

                        250       260
                 ....*....|....*....|....*..
gi 515927832 270 WRQRTRWARGNQYVVLK-----FLRQF 291
Cdd:cd02525  217 ARQYFRYGKWRARTLRKhrkslSLRHL 243
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 52-279 2.01e-24

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: 100.94  E-value: 2.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  52 SILIPAHNE--EVVIrQTLKAMVQLSYPKhlLEIIVINDNSSDRT-----GEIVQSFSEQYDHVHMietkPPFAGkGKST 124
Cdd:cd06435    1 SIHVPCYEEppEMVK-ETLDSLAALDYPN--FEVIVIDNNTKDEAlwkpvEAHCAQLGERFRFFHV----EPLPG-AKAG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 125 ALNGGLKASTGD--VICVYDADNMPEKKAVYHLVlGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETICFQWMAQGGRW 202
Cdd:cd06435   73 ALNYALERTAPDaeIIAVIDADYQVEPDWLKRLV-PIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRN 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515927832 203 KWFGIATIpGTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYVIRFFPAAITWEQEPETWKVWWRQRTRWARG 279
Cdd:cd06435  152 ERNAIIQH-GTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYG 227
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
49-298 9.61e-24

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 97.76  E-value: 9.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEEVVIRQTLKAMVQLSYPKHllEIIVINDNSSDRTGEIVQSFseQYDHVHMIETKPPFagkGKSTALNG 128
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENL---GFAAARNL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 129 GLKASTGDVICVYDADNMPEKKAVYHLVlgllndpkagavvgkfrviNAAknlltkfinieticfqwmaqggrwkwfgia 208
Cdd:COG1216   76 GLRAAGGDYLLFLDDDTVVEPDWLERLL-------------------AAA------------------------------ 106

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 209 tipgtNFAIRRHILEELGGWD--VHALAEDTELTIRVYNLGYVIRFFPAAITWEQEPETWKVWWRQRtRWARGNQYVVLK 286
Cdd:COG1216  107 -----CLLIRREVFEEVGGFDerFFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY-YLGRNRLLFLRK 180

                        250       260
                 ....*....|....*....|..
gi 515927832 287 ----------FLRQFMKLKRKR 298
Cdd:COG1216  181 hgprpllrlaLLRGLRLRLRGR 202
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 53-225 1.19e-21

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: 91.48  E-value: 1.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKPPFagkGKSTALNGGLKA 132
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNF---GKGAAVRAGFKA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 133 STGDVICVYDADN--MPEkkAVYHLVLGLLNDPkAGAVVG--KFRVINAAKNLLTKFINietICFQWMAqggrWKWFGIA 208
Cdd:cd04179   78 ARGDIVVTMDADLqhPPE--DIPKLLEKLLEGG-ADVVIGsrFVRGGGAGMPLLRRLGS---RLFNFLI----RLLLGVR 147

                        170
                 ....*....|....*....
gi 515927832 209 TIPGTN--FAIRRHILEEL 225
Cdd:cd04179  148 ISDTQSgfRLFRREVLEAL 166
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 53-236 1.29e-20

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: 88.98  E-value: 1.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKHlleIIVINDNSSDRTGEIVQSFsEQYDHVHMIETKPPFAGKGKSTALNGG--- 129
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNKPNFL---VLVIDDASDDDTAGIVRLA-ITDSRVHLLRRHLPNARTGKGDALNAAydq 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 130 LKASTGD--------VICVYDADNMPEKKAVYHlVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETICFQWMAQGGR 201
Cdd:cd06436   77 IRQILIEegadpervIIAVIDADGRLDPNALEA-VAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQSLR 155

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515927832 202 WKWfGIATIPGTNFAIRRHILEELGG---WDvHALAED 236
Cdd:cd06436  156 ALT-GTVGLGGNGQFMRLSALDGLIGeepWS-DSLLED 191
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 162-280 3.00e-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: 82.38  E-value: 3.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  162 DPKAGAVVGKfRVINAAKNLLTKFINIET------ICFQWMAQGGRwkwfgiATIPGTNFAIRRHILEELGGWDVHALAE 235
Cdd:pfam13632  25 SPEVAIIQGP-ILPMNVGNYLEELAALFFaddhgkSIPVRMALGRV------LPFVGSGAFLRRSALQEVGGWDDGSVSE 97

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 515927832  236 DTELTIRVYNLGYVIRFFPAAITWEQEPETWKVWWRQRTRWARGN 280
Cdd:pfam13632  98 DFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGC 142
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 51-289 6.44e-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: 82.23  E-value: 6.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  51 VSILIPAHNEEVVIRQTLKAMVQLsyPKHLLEIIVINDNSSDRTGEIVQSFseqydHVHMIETKPpfagkGKSTALNGGL 130
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRL--NPLPLEIIVVDGGSTDGTVAIARSA-----GVVVISSPK-----GRARQMNAGA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 131 KASTGDVICVYDADNMPEKKAVYHLVLGLLNDpkaGAVVGKFRVinaaknlltKFINiETICFQWMAQGG--RWKWFGIA 208
Cdd:cd02522   69 AAARGDWLLFLHADTRLPPDWDAAIIETLRAD---GAVAGAFRL---------RFDD-PGPRLRLLELGAnlRSRLFGLP 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 209 TipGTN-FAIRRHILEELGGWDVHALAEDTELTIRVYNLGyVIRFFPAAIT-----WEQEPetwkvWWRQRTRwargNQY 282
Cdd:cd02522  136 Y--GDQgLFIRRELFEELGGFPELPLMEDVELVRRLRRRG-RPALLPSPVTtsarrWERNG-----WLRTTLL----NWL 203


                 ....*..
gi 515927832 283 VVLKFLR 289
Cdd:cd02522  204 LLLLYLL 210
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 115-278 3.13e-17

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: 78.86  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  115 PPFAGKGKSTALNGGLKASTGDVICVYDADNMPEKKAVYHLVlGLLNDPKAGAVVGkFRVINAAKNLLTKFINIETICFQ 194
Cdd:pfam13506  11 PPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLL-APLADPKVGLVTS-PPVGSDPKGLAAALEAAFFNTLA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  195 WMAQGGrwkWFGIATIPGTNFAIRRHILEELGGWD--VHALAEDTELTIRVYNLGYVIRFFPAAITWE--QEPETWKVWW 270
Cdd:pfam13506  89 GVLQAA---LSGIGFAVGMSMAFRRADLERIGGFEalADYLAEDYALGKLLRAAGLKVVLSPRPILQTsgPRRTSFRAFM 165


                  ....*...
gi 515927832  271 RQRTRWAR 278
Cdd:pfam13506 166 ARQLRWAR 173
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 53-144 2.70e-14

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: 70.58  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQ-LSYPKHLLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIEtkppFAG-KGKSTALNGGL 130
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAvLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIR----LSRnFGQQAALLAGL 76

                         90
                 ....*....|....
gi 515927832 131 KASTGDVICVYDAD 144
Cdd:cd04187   77 DHARGDAVITMDAD 90
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 52-254 4.85e-14

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: 70.65  E-value: 4.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  52 SILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHmieTKPpfaGKGKSTALNGGLK 131
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPN--IEYIVIDGGSTDGTVDIIKKYEDKITYWI---SEP---DKGIYDAMNKGIA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 132 ASTGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETIcfqwmaqggRWKWFGIATIP 211
Cdd:cd06433   73 LATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFL---------DKFLLYGMPIC 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515927832 212 GTNFAIRRHILEELGGWDV--HaLAEDTELTIRVYNLGYVIRFFP 254
Cdd:cd06433  144 HQATFFRRSLFEKYGGFDEsyR-IAADYDLLLRLLLAGKIFKYLP 187
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 53-145 1.10e-12

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: 66.82  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQL--SYPKHLLEIIVINDNSSDRTGEIVQSFSEQY----DHVHMIETKppfaGKGKstAL 126
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYleERPSFSYEIIVVDDGSKDGTAEVARKLARKNpaliRVLTLPKNR----GKGG--AV 74

                         90
                 ....*....|....*....
gi 515927832 127 NGGLKASTGDVICVYDADN 145
Cdd:cd04188   75 RAGMLAARGDYILFADADL 93
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 50-282 1.54e-12

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: 66.89  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  50 TVSILIPAHNEEV-VIRQTLKAMVQLsypkHLLEIIVINDNSSDRTGEIVQSfSEQYDHVHMIETKPPfagkGKSTALNG 128
Cdd:cd06434    1 DVTVIIPVYDEDPdVFRECLRSILRQ----KPLEIIVVTDGDDEPYLSILSQ-TVKYGGIFVITVPHP----GKRRALAE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 129 GLKASTGDVICVYDADNMPEKKAVYHLvLGLLNDPKAGAVVGKFRVINA--------AKNLLTKFINIETICfqwMAQGG 200
Cdd:cd06434   72 GIRHVTTDIVVLLDSDTVWPPNALPEM-LKPFEDPKVGGVGTNQRILRPrdskwsflAAEYLERRNEEIRAA---MSYDG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 201 rwkwfGIATIPGTNFAIRRHIL-----------EELGGWDVHAlAEDTELTIRVYNLGY--VIRFFPAAITweQEPETWK 267
Cdd:cd06434  148 -----GVPCLSGRTAAYRTEILkdflfleeftnETFMGRRLNA-GDDRFLTRYVLSHGYktVYQYTSEAYT--ETPENYK 219

                        250
                 ....*....|....*
gi 515927832 268 VWWRQRTRWARGNQY 282
Cdd:cd06434  220 KFLKQQLRWSRSNWR 234
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 53-144 2.21e-12

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: 66.02  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNE----EVVIRQTLKAMVQLSYpkhllEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETKppfAGKGKSTALNG 128
Cdd:cd06442    1 IIIPTYNEreniPELIERLDAALKGIDY-----EIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRP---GKRGLGSAYIE 72

                         90
                 ....*....|....*.
gi 515927832 129 GLKASTGDVICVYDAD 144
Cdd:cd06442   73 GFKAARGDVIVVMDAD 88
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 49-278 5.11e-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: 64.54  E-value: 5.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDRTGEIVQSFSEQYDHVH---MIETKPPfAGKGKSTA 125
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPK--YEILFCVQDEDDPAIPVVRKLIAKYPNVDarlLIGGEKV-GINPKVNN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 126 LNGGLKASTGDVICVYDADNMPEKKAVYHLVLGlLNDPKAGAVVGKFrvinaaknlltkfinieticfqwmAQGgrwkwf 205
Cdd:cd02520   78 LIKGYEEARYDILVISDSDISVPPDYLRRMVAP-LMDPGVGLVTCLC------------------------AFG------ 126

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515927832 206 giATIpgtnfAIRRHILEELGGWDVHA--LAEDTELTIRVYNLGYVIRFFPAAITWEQEPETWKVWWRQRTRWAR 278
Cdd:cd02520  127 --KSM-----ALRREVLDAIGGFEAFAdyLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 49-145 7.32e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 66.22  E-value: 7.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHNEE--------VVIRQTLKAmvqlsypkhlLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIETkppfAGK 120
Cdd:PRK10073   6 PKLSIIIPLYNAGkdfrafmeSLIAQTWTA----------LEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQ----ANA 71

                         90       100
                 ....*....|....*....|....*
gi 515927832 121 GKSTALNGGLKASTGDVICVYDADN 145
Cdd:PRK10073  72 GVSVARNTGLAVATGKYVAFPDADD 96
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 53-259 2.96e-11

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: 61.42  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYPKHllEIIVINDNSSDRTGEIVQsfsEQYDHVHMIETKPP--FAGkgkstALNGGL 130
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDF--EVIVVDNASTDGSVELLR---ELFPEVRLIRNGENlgFGA-----GNNQGI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 131 KASTGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKfrvinaaknlltkfinieticfqwmaqggrwkwfgiatI 210
Cdd:cd04186   71 REAKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPK--------------------------------------V 112

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 515927832 211 PGTNFAIRRHILEELGGWD--VHALAEDTELTIRVYNLGYVIRFFPAAITW 259
Cdd:cd04186  113 SGAFLLVRREVFEEVGGFDedFFLYYEDVDLCLRARLAGYRVLYVPQAVIY 163
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 38-279 1.88e-10

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 62.73  E-value: 1.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  38 LPKWTKQgkdLPTVSILIPAHNEEV-VIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQSFSEQY----DHVHmie 112
Cdd:PRK11498 252 LPKDMSL---WPTVDIFVPTYNEDLnVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKYiarpTHEH--- 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 113 tkppfagkGKSTALNGGLKASTGDVICVYDADNMPeKKAVYHLVLG-LLNDPKAGAV---------------VGKFRVIN 176
Cdd:PRK11498 326 --------AKAGNINNALKYAKGEFVAIFDCDHVP-TRSFLQMTMGwFLKDKKLAMMqtphhffspdpfernLGRFRKTP 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 177 AAKNLltkfinieticFQWMAQGGRWKWfgIAT-IPGTNFAIRRHILEELGGWDVHALAEDTELTIRVYNLGYV---IRF 252
Cdd:PRK11498 397 NEGTL-----------FYGLVQDGNDMW--DATfFCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTsayMRI 463

                        250       260
                 ....*....|....*....|....*..
gi 515927832 253 FPAAitwEQEPETWKVWWRQRTRWARG 279
Cdd:PRK11498 464 PQAA---GLATESLSAHIGQRIRWARG 487
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 52-145 2.87e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 61.32  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  52 SILIPAHNEEVVIRQTLKAMVQL------SYPKHLLEIIVINDNSSDRTGEIVQSFSEQYDHVHM-IETKPPFAGKGKST 124
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETIKYlesrsrKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdIRLLSLLRNKGKGG 152

                         90       100
                 ....*....|....*....|.
gi 515927832 125 ALNGGLKASTGDVICVYDADN 145
Cdd:PTZ00260 153 AVRIGMLASRGKYILMVDADG 173
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 49-254 4.94e-10

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: 58.75  E-value: 4.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  49 PTVSILIPAHN-EEVVIRQTLKAMVQLSYPKhlLEIIVINDNSSDR-TGEIVQSFSEQYDHVHMIetkppFAGK--GKST 124
Cdd:cd04184    1 PLISIVMPVYNtPEKYLREAIESVRAQTYPN--WELCIADDASTDPeVKRVLKKYAAQDPRIKVV-----FREEngGISA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 125 ALNGGLKASTGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFI----NIETICFQWMAqgg 200
Cdd:cd04184   74 ATNSALELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFkpdwSPDLLLSQNYI--- 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 515927832 201 rwkwfgiatipgTNFA-IRRHILEELGGWDV-HALAEDTELTIRVYNLGYVIRFFP 254
Cdd:cd04184  151 ------------GHLLvYRRSLVRQVGGFREgFEGAQDYDLVLRVSEHTDRIAHIP 194
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 43-144 1.18e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 58.56  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  43 KQGKDLPTVSILIPAHNEevviRQTLKAMVQLSYpKHL-----LEIIVINDNSSDRTGEIVQSFSEQY--DHVHMIetkp 115
Cdd:PLN02726   3 APGEGAMKYSIIVPTYNE----RLNIALIVYLIF-KALqdvkdFEIIVVDDGSPDGTQDVVKQLQKVYgeDRILLR---- 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 515927832 116 PFAGK-GKSTALNGGLKASTGDVICVYDAD 144
Cdd:PLN02726  74 PRPGKlGLGTAYIHGLKHASGDFVVIMDAD 103
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 39-173 1.36e-08

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 56.08  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  39 PKWT-------KQGKdlpTVSILIPAHNEEVVIRQTLKAMVQLSYPKHLLEIIVINDNSSDRTGEIVQSF-SEQYDHVHM 110
Cdd:PRK13915  17 PDWTieelvaaKAGR---TVSVVLPALNEEETVGKVVDSIRPLLMEPLVDELIVIDSGSTDATAERAAAAgARVVSREEI 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515927832 111 IETKPPFAGKGKstALNGGLKASTGDVICVYDADNM-PEKKAVYHLVLGLLNDPKAGAVVGKFR 173
Cdd:PRK13915  94 LPELPPRPGKGE--ALWRSLAATTGDIVVFVDADLInFDPMFVPGLLGPLLTDPGVHLVKAFYR 155
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 52-243 1.26e-07

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: 52.66  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832   52 SILIP--AHNEEVVIRQTLkaMVQLSYPKHLLEIIVINDNSSDRTGEIVQSFSeqyDHVHMIETK-PPFAGKGKSTALNG 128
Cdd:pfam10111   1 SVVIPvyNGEKTHWIQERI--LNQTFQYDPEFELIIINDGSTDKTLEEVSSIK---DHNLQVYYPnAPDTTYSLAASRNR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  129 GLKASTGDVICVYDAD-----NMPEKKAVYHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIE-TICFQWMAQGGRW 202
Cdd:pfam10111  76 GTSHAIGEYISFIDGDclwspDKFEKQLKIATSLALQENIQAAVVLPVTDLNDESSNFLRRGGDLTaSGDVLRDLLVFYS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 515927832  203 KWFGIATIPGTNFAIRRHILEELGGWD----VHAlAEDTELTIRV 243
Cdd:pfam10111 156 PLAIFFAPNSSNALINRQAFIEVGGFDesfrGHG-AEDFDIFLRL 199
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 51-149 1.84e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 52.43  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  51 VSILIPAHNEE----VVIRQTLKAMVQLSYPkhlLEIIVINDNSSDRTGEIVQSFSEQYD-HVHMIETKPPFagkGKSTA 125
Cdd:PRK10714   8 VSVVIPVYNEQeslpELIRRTTAACESLGKE---YEILLIDDGSSDNSAEMLVEAAQAPDsHIVAILLNRNY---GQHSA 81

                         90       100
                 ....*....|....*....|....*.
gi 515927832 126 LNGGLKASTGDVICVYDAD--NMPEK 149
Cdd:PRK10714  82 IMAGFSHVTGDLIITLDADlqNPPEE 107
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
 53-276 3.17e-07

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 51.15  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNE-EVVIRQTLKAMVQLSYP---------KHLLEIIVINDNSSDRTGEIvqsfseqYDHVHMIEtkppfagkgk 122
Cdd:cd04190    1 VCVTMYNEdEEELARTLDSILKNDYPfcarggdswKKIVVCVIFDGAIKKNRGKR-------DSQLWFFN---------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 123 stALNGGLKASTGDVICVYDADNMPEKKAVYHLVLGLLNDPKAGAVVGKFRVINAAKNLLTKFINIETICFQWMAqggrw 202
Cdd:cd04190   64 --YFCRVLFPDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAISHWLD----- 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 203 K----WFG-IATIPGTNFAIRRHILEE-LGGWDVHA-------------------LAED----TELTIRVYNLGYviRFF 253
Cdd:cd04190  137 KafesVFGfVTCLPGCFSMYRIEALKGdNGGKGPLLdyayltntvdslhkknnldLGEDrilcTLLLKAGPKRKY--LYV 214

                        250       260
                 ....*....|....*....|...
gi 515927832 254 PAAITWEQEPETWKVWWRQRTRW 276
Cdd:cd04190  215 PGAVAETDVPETFVELLSQRRRW 237
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 53-149 2.50e-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: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  53 ILIPAHNEEVVIRQTLKAMVQLSYpKHLLEIIVINDNSSDRTGEIVQSFSEQYD----HVHMIETKPPFAgKGKSTALNG 128
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDF-EGTLELSVFNDASTDKSAEIIEKWRKKLEdsgvIVLVGSHNSPSP-KGVGYAKNQ 78

                         90       100
                 ....*....|....*....|...
gi 515927832 129 GLKASTGDVICVYDADN--MPEK 149
Cdd:cd06913   79 AIAQSSGRYLCFLDSDDvmMPQR 101
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 50-144 2.69e-05

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: 45.36  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  50 TVSILIPAHNEEVVIRQTLKamvqlSYPKHLLEIIVINDNSSDRTGEIVQSFSeqyDHVHmietkpPFAGKGKSTALNGG 129
Cdd:cd02511    1 TLSVVIITKNEERNIERCLE-----SVKWAVDEIIVVDSGSTDRTVEIAKEYG---AKVY------QRWWDGFGAQRNFA 66

                         90
                 ....*....|....*
gi 515927832 130 LKASTGDVICVYDAD 144
Cdd:cd02511   67 LELATNDWVLSLDAD 81
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 52-182 3.42e-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: 44.54  E-value: 3.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  52 SILIPAHNEEVVIRQTLKAMVQLSYPkhLLEIIVINDNSSDRTGEIVQSFSEQYDHVHMIetkpPFAGKGKSTALN--GG 129
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYK--NDELIISDDGSTDGTVEIIKEYIDKDPFIIIL----IRNGKNLGVARNfeSL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515927832 130 LKASTGDVICVYDADN--MPEKKAVyhLVLGLLNDPKAGAVVGKFRVINAAKNLL 182
Cdd:cd04196   75 LQAADGDYVFFCDQDDiwLPDKLER--LLKAFLKDDKPLLVYSDLELVDENGNPI 127
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 52-243 9.48e-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: 9.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832  52 SILIPAHNEE-VVIRQTLKAMVQLSyPKHLL-EIIVINDNSSDrtGEIVQSFSEQYDH----VHMIETKPPfagKGKSTA 125
Cdd:cd02510    1 SVIIIFHNEAlSTLLRTVHSVINRT-PPELLkEIILVDDFSDK--PELKLLLEEYYKKylpkVKVLRLKKR---EGLIRA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515927832 126 LNGGLKASTGDVICVYDAdnmpekkavyH----------LVLGLLNDPKAgAVVGKFRVINAAKNLLTKFINIETICFQW 195
Cdd:cd02510   75 RIAGARAATGDVLVFLDS----------HcevnvgwlepLLARIAENRKT-VVCPIIDVIDADTFEYRGSSGDARGGFDW 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515927832 196 maqGGRWKWFGI----------------ATIPGTNFAIRRHILEELGGWDVHAL---AEDTELTIRV 243
Cdd:cd02510  144 ---SLHFKWLPLpeeerrresptapirsPTMAGGLFAIDREWFLELGGYDEGMDiwgGENLELSFKV 207
 
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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