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Conserved domains on  [gi|446911495|ref|WP_000988751|]
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MULTISPECIES: glycosyltransferase [Bacillus]

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
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 ...
72-253 7.37e-66

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: 208.62  E-value: 7.37e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYPgKLTIYLLNDNSQDETPEIGDDFDKAYaHIRHIRVPPGEPKGKSRVLNYGLSISD 151
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALY-IRRVLVVRDKENGGKAGALNAGLRHAK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMQSGRWLLFQTGSLTGTN 231
Cdd:cd06423   79 GDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAF 158
                        170       180
                 ....*....|....*....|..
gi 446911495 232 MLLRRSALEELGGYDPYAIAED 253
Cdd:cd06423  159 GAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
40-377 1.94e-59

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: 196.12  E-value: 1.94e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  40 LLVYYSFLTIAGLIHRNSKRKDRTLEHYPSVDIFIPAHNEGVVIKDTLEAMAKIEYP-GKLTIYLLNDNSQDETPEIGDD 118
Cdd:COG1215    1 LLLLLALLALLYLLLLALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkEKLEVIVVDDGSTDETAEIARE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 119 FDKAYAHIRHIRVPPGepKGKSRVLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAETTEdaVGAvghvrtvnekrnw 198
Cdd:COG1215   81 LAAEYPRVRVIERPEN--GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG--VGA------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 199 ltrmislefqifqllmqsgrwllfqtgslTGTNMLLRRSALEELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQ 278
Cdd:COG1215  144 -----------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 279 EPEHLKILIKQRTRWLQGNLYILEKM-----FSSLSFFKGKLLVHSLQQVLVYVVFWLFLIISnVWFVIGLLGIFQIQYS 353
Cdd:COG1215  195 APETLRALFRQRRRWARGGLQLLLKHrpllrPRRLLLFLLLLLLPLLLLLLLLALLALLLLLL-PALLLALLLALRRRRL 273
                        330       340
                 ....*....|....*....|....
gi 446911495 354 IPLLFMWYVAYITYVSQLFSAQSV 377
Cdd:COG1215  274 LLPLLHLLYGLLLLLAALRGKKVV 297
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
72-253 7.37e-66

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: 208.62  E-value: 7.37e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYPgKLTIYLLNDNSQDETPEIGDDFDKAYaHIRHIRVPPGEPKGKSRVLNYGLSISD 151
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALY-IRRVLVVRDKENGGKAGALNAGLRHAK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMQSGRWLLFQTGSLTGTN 231
Cdd:cd06423   79 GDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAF 158
                        170       180
                 ....*....|....*....|..
gi 446911495 232 MLLRRSALEELGGYDPYAIAED 253
Cdd:cd06423  159 GAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
40-377 1.94e-59

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: 196.12  E-value: 1.94e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  40 LLVYYSFLTIAGLIHRNSKRKDRTLEHYPSVDIFIPAHNEGVVIKDTLEAMAKIEYP-GKLTIYLLNDNSQDETPEIGDD 118
Cdd:COG1215    1 LLLLLALLALLYLLLLALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkEKLEVIVVDDGSTDETAEIARE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 119 FDKAYAHIRHIRVPPGepKGKSRVLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAETTEdaVGAvghvrtvnekrnw 198
Cdd:COG1215   81 LAAEYPRVRVIERPEN--GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG--VGA------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 199 ltrmislefqifqllmqsgrwllfqtgslTGTNMLLRRSALEELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQ 278
Cdd:COG1215  144 -----------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 279 EPEHLKILIKQRTRWLQGNLYILEKM-----FSSLSFFKGKLLVHSLQQVLVYVVFWLFLIISnVWFVIGLLGIFQIQYS 353
Cdd:COG1215  195 APETLRALFRQRRRWARGGLQLLLKHrpllrPRRLLLFLLLLLLPLLLLLLLLALLALLLLLL-PALLLALLLALRRRRL 273
                        330       340
                 ....*....|....*....|....
gi 446911495 354 IPLLFMWYVAYITYVSQLFSAQSV 377
Cdd:COG1215  274 LLPLLHLLYGLLLLLAALRGKKVV 297
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
68-296 2.22e-32

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: 122.48  E-value: 2.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495   68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYPGkLTIYLLNDNSQDETPEIGDDFDKAY--AHIRHIRVP-PGEPKGKSRVLN 144
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPP-VEVVVVVNPSDAETLDVAEEIAARFpdVRLRVIRNArLLGPTGKSRGLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  145 YGLSISDGEYFCVYDADNQPEPHALRMLVEHAETteDAVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMqSGRWLLFQT 224
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDS--PKVGAVGTPVFSLNRSTMLSALGALEFALRHLRM-MSLRLALGV 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446911495  225 GSLTGTNMLLRRSALEELGGYDPY-AIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQG 296
Cdd:pfam13641 158 LPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
68-272 2.56e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 105.17  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYPGkLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPPGepKGKSRVLNYGL 147
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD-FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERN--RGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 148 SISDGEYFCVYDADNQPEPHALRMLVEHAEttEDAVGAVGHVRTVNEKRNWLTRMISLEFQIfqllmqsgRWLLFQTGSL 227
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALE--EGPADLVYGSRLIREGESDLRRLGSRLFNL--------VRLLTNLPDS 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446911495 228 TGTNMLLRRSALEELgGYDPyAIAEDAELtLRITQKGYLLPIVPE 272
Cdd:COG0463  149 TSGFRLFRREVLEEL-GFDE-GFLEDTEL-LRALRHGFRIAEVPV 190
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
66-367 4.48e-14

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 74.29  E-value: 4.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  66 HYPSVDIFIPAHNEGV-VIKDTLEAMAKIEYPG-KLTIYLLNDNSQDETPEIGDDfdkayAHIRHIRVPPGEpKGKSRVL 143
Cdd:PRK11498 258 LWPTVDIFVPTYNEDLnVVKNTIYASLGIDWPKdKLNIWILDDGGREEFRQFAQE-----VGVKYIARPTHE-HAKAGNI 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 144 NYGLSISDGEYFCVYDADNQPEPHALRMlvehaettedAVG------AVGHVRTVNE-------KRNwLT--RMISLEFQ 208
Cdd:PRK11498 332 NNALKYAKGEFVAIFDCDHVPTRSFLQM----------TMGwflkdkKLAMMQTPHHffspdpfERN-LGrfRKTPNEGT 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 209 IFQLLMQSGR--W-LLFQTGSLTgtnmLLRRSALEELGGYDPYAIAEDAELTLRITQKGY---LLPIvPESVTWeqEPEH 282
Cdd:PRK11498 401 LFYGLVQDGNdmWdATFFCGSCA----VIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYtsaYMRI-PQAAGL--ATES 473
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 283 LKILIKQRTRWLQGNLYIlekmFSSLSFFKGKLLvhSLQQVLVYVVFWL-FLiiSNVWFVIGLLGifqiqysiPLLFMWY 361
Cdd:PRK11498 474 LSAHIGQRIRWARGMVQI----FRLDNPLTGKGL--KLAQRLCYANAMLhFL--SGIPRLIFLTA--------PLAFLLL 537

                 ....*.
gi 446911495 362 VAYITY 367
Cdd:PRK11498 538 HAYIIY 543
 
Name Accession Description Interval E-value
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
72-253 7.37e-66

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: 208.62  E-value: 7.37e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYPgKLTIYLLNDNSQDETPEIGDDFDKAYaHIRHIRVPPGEPKGKSRVLNYGLSISD 151
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYP-KLEVIVVDDGSTDDTLEILEELAALY-IRRVLVVRDKENGGKAGALNAGLRHAK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMQSGRWLLFQTGSLTGTN 231
Cdd:cd06423   79 GDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAF 158
                        170       180
                 ....*....|....*....|..
gi 446911495 232 MLLRRSALEELGGYDPYAIAED 253
Cdd:cd06423  159 GAFRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
40-377 1.94e-59

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: 196.12  E-value: 1.94e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  40 LLVYYSFLTIAGLIHRNSKRKDRTLEHYPSVDIFIPAHNEGVVIKDTLEAMAKIEYP-GKLTIYLLNDNSQDETPEIGDD 118
Cdd:COG1215    1 LLLLLALLALLYLLLLALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkEKLEVIVVDDGSTDETAEIARE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 119 FDKAYAHIRHIRVPPGepKGKSRVLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAETTEdaVGAvghvrtvnekrnw 198
Cdd:COG1215   81 LAAEYPRVRVIERPEN--GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG--VGA------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 199 ltrmislefqifqllmqsgrwllfqtgslTGTNMLLRRSALEELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQ 278
Cdd:COG1215  144 -----------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 279 EPEHLKILIKQRTRWLQGNLYILEKM-----FSSLSFFKGKLLVHSLQQVLVYVVFWLFLIISnVWFVIGLLGIFQIQYS 353
Cdd:COG1215  195 APETLRALFRQRRRWARGGLQLLLKHrpllrPRRLLLFLLLLLLPLLLLLLLLALLALLLLLL-PALLLALLLALRRRRL 273
                        330       340
                 ....*....|....*....|....
gi 446911495 354 IPLLFMWYVAYITYVSQLFSAQSV 377
Cdd:COG1215  274 LLPLLHLLYGLLLLLAALRGKKVV 297
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
68-296 4.32e-46

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: 159.34  E-value: 4.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYP-GKLTIYLLNDNSQDETPEIGDDFDKAyAHIRHIRVPPGEPKGKSRVLNYG 146
Cdd:cd06427    1 PVYTILVPLYKEAEVLPQLIASLSALDYPrSKLDVKLLLEEDDEETIAAARALRLP-SIFRVVVVPPSQPRTKPKACNYA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 147 LSISDGEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAV-GHVRTVNEKRNWLTRMISLEF-QIFQLL---MQSGRWLL 221
Cdd:cd06427   80 LAFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDKLACVqAPLNYYNARENWLTRMFALEYaAWFDYLlpgLARLGLPI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446911495 222 fqtgSLTGTNMLLRRSALEELGGYDPYAIAEDAELTLRITQKGYLLPIVPeSVTWEQEPEHLKILIKQRTRWLQG 296
Cdd:cd06427  160 ----PLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLN-STTLEEANNALGNWIRQRSRWIKG 229
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
68-301 2.25e-39

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: 141.17  E-value: 2.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGV-VIKDTLEAMAKIEYPG-KLTIYLLNDNSQDETPEIGDDFdkAYAHIRHIRVPPGEPKGKSRVLNY 145
Cdd:cd06421    1 PTVDVFIPTYNEPLeIVRKTLRAALAIDYPHdKLRVYVLDDGRRPELRALAAEL--GVEYGYRYLTRPDNRHAKAGNLNN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 146 GLSISDGEYFCVYDADNQPEPHALRMLVEHAETtEDAVGAVG--HVRTVNEKRNWLTRMISLEFQIFQLLMQSGRwLLFQ 223
Cdd:cd06421   79 ALAHTTGDFVAILDADHVPTPDFLRRTLGYFLD-DPKVALVQtpQFFYNPDPFDWLADGAPNEQELFYGVIQPGR-DRWG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446911495 224 TGSLTGTNMLLRRSALEELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQGNLYIL 301
Cdd:cd06421  157 AAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
68-296 2.22e-32

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: 122.48  E-value: 2.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495   68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYPGkLTIYLLNDNSQDETPEIGDDFDKAY--AHIRHIRVP-PGEPKGKSRVLN 144
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPP-VEVVVVVNPSDAETLDVAEEIAARFpdVRLRVIRNArLLGPTGKSRGLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  145 YGLSISDGEYFCVYDADNQPEPHALRMLVEHAETteDAVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMqSGRWLLFQT 224
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDS--PKVGAVGTPVFSLNRSTMLSALGALEFALRHLRM-MSLRLALGV 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446911495  225 GSLTGTNMLLRRSALEELGGYDPY-AIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQG 296
Cdd:pfam13641 158 LPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
71-241 1.10e-29

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: 113.26  E-value: 1.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495   71 DIFIPAHNEGVVIKDTLEAMAKIEYPgKLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPpgEPKGKSRVLNYGLSIS 150
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP-NFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLP--ENRGKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  151 DGEYFCVYDADNQPEPHALRMLVEHAEtTEDAVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMQSgRWLLFQTGSLTGT 230
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALE-EDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGL-RLLGLNLPFLIGG 155
                         170
                  ....*....|.
gi 446911495  231 NMLLRRSALEE 241
Cdd:pfam00535 156 FALYRREALEE 166
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
72-303 1.19e-28

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: 112.49  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEG-VVIKDTLEAMAKIEYPgKLTIYLLNDNSQDET---------PEIGDDFdkayahiRHIRVPPgEPKGKSR 141
Cdd:cd06435    2 IHVPCYEEPpEMVKETLDSLAALDYP-NFEVIVIDNNTKDEAlwkpveahcAQLGERF-------RFFHVEP-LPGAKAG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 142 VLNYGLSI--SDGEYFCVYDADNQPEPHALRMLVEHAETTEdavgaVGHVRTVNEKRNW----LTRMISLEFQIF---QL 212
Cdd:cd06435   73 ALNYALERtaPDAEIIAVIDADYQVEPDWLKRLVPIFDDPR-----VGFVQAPQDYRDGeeslFKRMCYAEYKGFfdiGM 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 213 LMQSGRWLLFQTGSLTgtnmLLRRSALEELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTR 292
Cdd:cd06435  148 VSRNERNAIIQHGTMC----LIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFR 223
                        250
                 ....*....|.
gi 446911495 293 WLQGNLYILEK 303
Cdd:cd06435  224 WAYGAVQILKK 234
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
68-296 4.97e-28

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: 110.86  E-value: 4.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYPG-KLTIYLLnDNSQDETPEIGDDFDKAYA----HIRHIRvpPGEPKG-KSR 141
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAACALDYPKdRLEIQVL-DDSTDETVRLAREIVEEYAaqgvNIKHVR--RADRTGyKAG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 142 VLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAETTEdavgaVGHVRT----VNEKRNWLTRMISLEFQIFQLLMQSG 217
Cdd:cd06437   78 ALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFADPK-----LGFVQTrwghINANYSLLTRVQAMSLDYHFTIEQVA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446911495 218 RWLLFQTGSLTGTNMLLRRSALEELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQG 296
Cdd:cd06437  153 RSSTGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
68-272 2.56e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 105.17  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYPGkLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPPGepKGKSRVLNYGL 147
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD-FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERN--RGKGAARNAGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 148 SISDGEYFCVYDADNQPEPHALRMLVEHAEttEDAVGAVGHVRTVNEKRNWLTRMISLEFQIfqllmqsgRWLLFQTGSL 227
Cdd:COG0463   79 AAARGDYIAFLDADDQLDPEKLEELVAALE--EGPADLVYGSRLIREGESDLRRLGSRLFNL--------VRLLTNLPDS 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446911495 228 TGTNMLLRRSALEELgGYDPyAIAEDAELtLRITQKGYLLPIVPE 272
Cdd:COG0463  149 TSGFRLFRREVLEEL-GFDE-GFLEDTEL-LRALRHGFRIAEVPV 190
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
40-298 1.04e-25

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: 104.97  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  40 LLVYYSFLTIAGLIHRNSKRKDRTlEHYPSVDIFIPAHNEGVVIKDTLEAMAKIEYPG-KLTIYLLNDNSQDETPEIGDD 118
Cdd:cd06439    2 YFGYPLLLKLLARLRPKPPSLPDP-AYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRdRLEIIVVSDGSTDGTAEIARE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 119 FDKAyaHIRHIRVPPGepKGKSRVLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAetTEDAVGAV-GHVRTVNekRN 197
Cdd:cd06439   81 YADK--GVKLLRFPER--RGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHF--ADPSVGAVsGELVIVD--GG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 198 WLTRMISLEFQIFQLL--MQSgrwllfQTGSLTGTN---MLLRRSALEELggyDPYAIAEDAELTLRITQKGYLLPIVPE 272
Cdd:cd06439  153 GSGSGEGLYWKYENWLkrAES------RLGSTVGANgaiYAIRRELFRPL---PADTINDDFVLPLRIARQGYRVVYEPD 223
                        250       260
                 ....*....|....*....|....*.
gi 446911495 273 SVTWEQEPEHLKILIKQRTRWLQGNL 298
Cdd:cd06439  224 AVAYEEVAEDGSEEFRRRVRIAAGNL 249
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
72-296 3.91e-24

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: 100.06  E-value: 3.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYP-GKLTIYLLNDNSQDETPEIGDD-FDKAYAHIRHIRVPPGEPKGKSRVLNYGLSI 149
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPkEKFEVILVDDHSTDGTVQILEFaAAKPNFQLKILNNSRVSISGKKNALTTAIKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 150 SDGEYFCVYDADNQPEPHALRMLVEHAETTEDA--VGAVghvrTVNEKRNWLTRMISLEFqiFQLLMQSGRWLLFQ---T 224
Cdd:cd04192   81 AKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGlvAGPV----IYFKGKSLLAKFQRLDW--LSLLGLIAGSFGLGkpfM 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446911495 225 GSltGTNMLLRRSALEELGGYD--PYAIAEDAELTLRITQKGYL---LPIVPESVTWEQEPEHLKILIKQRTRWLQG 296
Cdd:cd04192  155 CN--GANMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYPkvaYLKNPEALVTTQPVTSWKELLNQRKRWASK 229
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
72-256 1.34e-23

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: 96.90  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYP-GKLTIYLLNDNSQDETPEIGddfdKAYAHIRHIRVPPgEPKGKSRVLNYGLSIS 150
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYPrELYRIFVVADNCTDDTAQVA----RAAGATVLERHDP-ERRGKGYALDFGFRHL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 151 -----DGEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAvgHVRTVNEKRNWLTRMISLEFQIFQLLMQSGRWLLFQTG 225
Cdd:cd06438   76 lnladDPDAVVVFDADNLVDPNALEELNARFAAGARVVQA--YYNSKNPDDSWITRLYAFAFLVFNRLRPLGRSNLGLSC 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446911495 226 SLTGTNMLLRRSALEElGGYDPYAIAEDAEL 256
Cdd:cd06438  154 QLGGTGMCFPWAVLRQ-APWAAHSLTEDLEF 183
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
159-345 2.00e-21

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: 91.24  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  159 DADNQPEPHALRMLVEHAETTEdaVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMQSGRWLLFQTGSLTGTNMLLRRSA 238
Cdd:pfam13632   6 DADTVLPPDCLLGIANEMASPE--VAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFLRRSA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  239 LEELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQGNLYIlekMFSSLSFFKGKLLVH 318
Cdd:pfam13632  84 LQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLI---LLIRLLGYLGTLLWS 160
                         170       180
                  ....*....|....*....|....*..
gi 446911495  319 SLqqVLVYVVFWLFLIISNVWFVIGLL 345
Cdd:pfam13632 161 GL--PLALLLLLLFSISSLALVLLLLA 185
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
68-315 6.11e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 90.05  E-value: 6.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYPGkLTIYLLNDNSQDETPEIGDDFDkaYAHIRHIRVPpgEPKGKSRVLNYGL 147
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPP-FEVIVVDNGSTDGTAELLAALA--FPRVRVIRNP--ENLGFAAARNLGL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 148 SISDGEYFCVYDADNQPEPHALRMLVEHAettedavgavghvrtvnekrnwltrmislefqifqllmqsgrwllfqtgsl 227
Cdd:COG1216   78 RAAGGDYLLFLDDDTVVEPDWLERLLAAA--------------------------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 228 tgtNMLLRRSALEELGGYDP--YAIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRtRWLQGNLYILEKMF 305
Cdd:COG1216  107 ---CLLIRREVFEEVGGFDErfFLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY-YLGRNRLLFLRKHG 182
                        250
                 ....*....|
gi 446911495 306 SSLSFFKGKL 315
Cdd:COG1216  183 PRPLLRLALL 192
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
72-266 2.01e-19

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: 84.48  E-value: 2.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYPgKLTIYLLNDNSQDETPEIGDDFDKAYahIRHIRVPPGEPKGKSRVLNYGLSISD 151
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYP-NFEVIVVDDGSTDGTLEILEEYAKKD--PRVIRVINEENQGLAAARNAGLKAAR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAVGHvrtvnekrnwltrmislefqifqllmqsgrwllfqtgsltgTN 231
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGP-----------------------------------------GN 116
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446911495 232 MLLRRSALEELGGYDP--YAIAEDAELTLRITQKGYL 266
Cdd:cd00761  117 LLFRRELLEEIGGFDEalLSGEEDDDFLLRLLRGGKV 153
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
72-253 6.60e-17

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: 78.58  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIeyPGKLTIYLLNDNSQDETPEIGDDF--DKAYAHIRhiRVPPGEPKGKSRVLNYGLS- 148
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRN--KPNFLVLVIDDASDDDTAGIVRLAitDSRVHLLR--RHLPNARTGKGDALNAAYDq 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 149 -----ISDG-----EYFCVYDADNQPEPHALRMLvehAETTEDA--VGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMQS 216
Cdd:cd06436   77 irqilIEEGadperVIIAVIDADGRLDPNALEAV---APYFSDPrvAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQS 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 446911495 217 GRWLLfQTGSLTGTNMLLRRSALEELGGYDPY--AIAED 253
Cdd:cd06436  154 LRALT-GTVGLGGNGQFMRLSALDGLIGEEPWsdSLLED 191
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
125-293 1.66e-16

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: 76.94  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  125 HIRHIRVPPGEPKGKSRV--LNYGLSISDGEYFCVYDADNQPEPHALRMLVEHaeTTEDAVGAVGHVRTVNEKRNWLTRM 202
Cdd:pfam13506   2 SVRALVVGGPPVGVNPKVnnLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAP--LADPKVGLVTSPPVGSDPKGLAAAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  203 ISLEFQIFQLLMQSGrWLLFQTGslTGTNMLLRRSALEELGGYDPYA--IAEDAELTLRITQKGYLLPIVPESVTWE--Q 278
Cdd:pfam13506  80 EAAFFNTLAGVLQAA-LSGIGFA--VGMSMAFRRADLERIGGFEALAdyLAEDYALGKLLRAAGLKVVLSPRPILQTsgP 156
                         170
                  ....*....|....*
gi 446911495  279 EPEHLKILIKQRTRW 293
Cdd:pfam13506 157 RRTSFRAFMARQLRW 171
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
69-311 3.22e-16

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 78.04  E-value: 3.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  69 SVDIFIPAHNEGVVIKDTLEAMAKIEYP-GKLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIrvpPGEPKGKSRVLNYGL 147
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYPkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLI---DNPKRIQSAGLNIGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 148 SISDGEYFCVYDADNQPEPHALRMLVEHAETTeDAVGAVGHVRTVNEKrnwltrmislEFQIFQLLMQSGRWL----LFQ 223
Cdd:cd02525   78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRT-GADNVGGPMETIGES----------KFQKAIAVAQSSPLGsggsAYR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 224 TGSL------TGTNMLLRRSALEELGGYDP-YAIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQG 296
Cdd:cd02525  147 GGAVkigyvdTVHHGAYRREVFEKVGGFDEsLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKW 226
                        250
                 ....*....|....*
gi 446911495 297 NLYILEKMFSSLSFF 311
Cdd:cd02525  227 RARTLRKHRKSLSLR 241
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
72-259 3.61e-15

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: 73.38  E-value: 3.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKI-EYPGKLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPPGepKGKSRVLNYGLSIS 150
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRN--FGKGAAVRAGFKAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 151 DGEYFCVYDADNQPEPHALRMLVEHAETTE-DAVGAVGHVRTVNEKRNWLTRMISlefQIFQLLMqsgRWLLFQTGSLTG 229
Cdd:cd04179   79 RGDIVVTMDADLQHPPEDIPKLLEKLLEGGaDVVIGSRFVRGGGAGMPLLRRLGS---RLFNFLI---RLLLGVRISDTQ 152
                        170       180       190
                 ....*....|....*....|....*....|....
gi 446911495 230 TNM-LLRRSALEELGGY---DPYAIaeDAELTLR 259
Cdd:cd04179  153 SGFrLFRREVLEALLSLlesNGFEF--GLELLVG 184
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
66-367 4.48e-14

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 74.29  E-value: 4.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  66 HYPSVDIFIPAHNEGV-VIKDTLEAMAKIEYPG-KLTIYLLNDNSQDETPEIGDDfdkayAHIRHIRVPPGEpKGKSRVL 143
Cdd:PRK11498 258 LWPTVDIFVPTYNEDLnVVKNTIYASLGIDWPKdKLNIWILDDGGREEFRQFAQE-----VGVKYIARPTHE-HAKAGNI 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 144 NYGLSISDGEYFCVYDADNQPEPHALRMlvehaettedAVG------AVGHVRTVNE-------KRNwLT--RMISLEFQ 208
Cdd:PRK11498 332 NNALKYAKGEFVAIFDCDHVPTRSFLQM----------TMGwflkdkKLAMMQTPHHffspdpfERN-LGrfRKTPNEGT 400
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 209 IFQLLMQSGR--W-LLFQTGSLTgtnmLLRRSALEELGGYDPYAIAEDAELTLRITQKGY---LLPIvPESVTWeqEPEH 282
Cdd:PRK11498 401 LFYGLVQDGNdmWdATFFCGSCA----VIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYtsaYMRI-PQAAGL--ATES 473
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 283 LKILIKQRTRWLQGNLYIlekmFSSLSFFKGKLLvhSLQQVLVYVVFWL-FLiiSNVWFVIGLLGifqiqysiPLLFMWY 361
Cdd:PRK11498 474 LSAHIGQRIRWARGMVQI----FRLDNPLTGKGL--KLAQRLCYANAMLhFL--SGIPRLIFLTA--------PLAFLLL 537

                 ....*.
gi 446911495 362 VAYITY 367
Cdd:PRK11498 538 HAYIIY 543
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
72-276 1.42e-13

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: 68.35  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYPGkLTIYLLNDNSQDETPEIgddFDKAYAHIRHIRvpPGEPKGKSRVLNYGLSISD 151
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPD-FEVIVVDNASTDGSVEL---LRELFPEVRLIR--NGENLGFGAGNNQGIREAK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHALRMLVEHAETTEDaVGAVGhvrtvnekrnwltrmislefqifqllmqsgrwllfqtGSLTGTN 231
Cdd:cd04186   75 GDYVLLLNPDTVVEPGALLELLDAAEQDPD-VGIVG-------------------------------------PKVSGAF 116
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446911495 232 MLLRRSALEELGGYDP-YAIA-EDAELTLRITQKGYLLPIVPESVTW 276
Cdd:cd04186  117 LLVRREVFEEVGGFDEdFFLYyEDVDLCLRARLAGYRVLYVPQAVIY 163
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
72-279 2.57e-13

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: 68.75  E-value: 2.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEyPGKLTIYLLNDNSQDETPEIGDDfdkayAHIRHIRvppgEPKGKSRVLNYGLSISD 151
Cdd:cd02522    3 IIIPTLNEAENLPRLLASLRRLN-PLPLEIIVVDGGSTDGTVAIARS-----AGVVVIS----SPKGRARQMNAGAAAAR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAvghvrtvnekrnwltrmislefqiFQLLMQSGRWLLFQT--GSLTG 229
Cdd:cd02522   73 GDWLLFLHADTRLPPDWDAAIIETLRADGAVAGA------------------------FRLRFDDPGPRLRLLelGANLR 128
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446911495 230 TN----------MLLRRSALEELGGYDPYAIAEDAELTLRITQKGyLLPIVPESVT-----WEQE 279
Cdd:cd02522  129 SRlfglpygdqgLFIRRELFEELGGFPELPLMEDVELVRRLRRRG-RPALLPSPVTtsarrWERN 192
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
72-280 1.45e-10

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: 60.66  E-value: 1.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAM-----AKIEYPGKLTIylLNDNSQDETPEIGDDFDKAY-AHIRHIRVPpgEPKGKSRVLNY 145
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAveyleERPSFSYEIIV--VDDGSKDGTAEVARKLARKNpALIRVLTLP--KNRGKGGAVRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 146 GLSISDGEYFCVYDADNQPEPHALRMLVEHAETTEDAVgAVG----HVRTVNEKRNWLTRMISLefqIFQLLMqsgrWLL 221
Cdd:cd04188   77 GMLAARGDYILFADADLATPFEELEKLEEALKTSGYDI-AIGsrahLASAAVVKRSWLRNLLGR---GFNFLV----RLL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446911495 222 FQTGsLTGTN---MLLRRSALEELGGY---DPYAIaeDAELTLRITQKGYllPIVPESVTWEQEP 280
Cdd:cd04188  149 LGLG-IKDTQcgfKLFTRDAARRLFPRlhlERWAF--DVELLVLARRLGY--PIEEVPVRWVEIP 208
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
107-276 9.06e-09

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: 55.24  E-value: 9.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 107 NSQDETPEIGddfdKAYAHIRHIRVppGEP-KGKSRVLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAETTEDAVGA 185
Cdd:cd06433   36 GSTDGTVDII----KKYEDKITYWI--SEPdKGIYDAMNKGIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 186 VGHVRTVNEKRNWLTRMISLEFQIFQLLMqsgRWLLFQTGsltgtnMLLRRSALEELGGYDP-YAIAEDAELTLRITQKG 264
Cdd:cd06433  110 YGDVLLVDENGRVIGRRRPPPFLDKFLLY---GMPICHQA------TFFRRSLFEKYGGFDEsYRIAADYDLLLRLLLAG 180
                        170
                 ....*....|..
gi 446911495 265 YLLPIVPESVTW 276
Cdd:cd06433  181 KIFKYLPEVLAA 192
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
103-264 6.50e-07

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: 49.51  E-value: 6.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 103 LLNDNSQDetPEIGDDFDKAYAHIRHIRVP-PGEPKGKSRVLNYGLSISDGEYFCVYDADNQPEPHALRMLV-EHAE--- 177
Cdd:cd04184   36 IADDASTD--PEVKRVLKKYAAQDPRIKVVfREENGGISAATNSALELATGEFVALLDHDDELAPHALYEVVkALNEhpd 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 178 -----TTEDAVGAVGHVRTVNEKRNWltrmiSLEfqifqllmqsgrwlLFQTGSLTGTNMLLRRSALEELGGYDP-YAIA 251
Cdd:cd04184  114 adliySDEDKIDEGGKRSEPFFKPDW-----SPD--------------LLLSQNYIGHLLVYRRSLVRQVGGFREgFEGA 174
                        170
                 ....*....|...
gi 446911495 252 EDAELTLRITQKG 264
Cdd:cd04184  175 QDYDLVLRVSEHT 187
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
72-265 8.34e-07

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 49.84  E-value: 8.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYPGKLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRvPPGEpKGKSRVLNYGLSISD 151
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIV-RPGK-RGLGSAYIEGFKAAR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHAL-RMLVEHAETTEDAVgaVG--HVRTVN-EKRNWLTRMISLEFQIFqllmqsGRWLLFQTGS- 226
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIpELLEAQLEGGADLV--IGsrYVEGGGvEGWGLKRKLISRGANLL------ARLLLGRKVSd 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446911495 227 LTGTNMLLRRSALEELGGYDP---YAIAEdaELTLRITQKGY 265
Cdd:cd06442  151 PTSGFRAYRREVLEKLIDSLVskgYKFQL--ELLVRARRLGY 190
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
72-246 1.05e-06

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: 48.63  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKI--EYPGKLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVppgepkgkSRvlNYG--- 146
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVleSLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRL--------SR--NFGqqa 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 147 -----LSISDGEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAvghVRTvNEKRNWLTRMISlefQIFQLLMqsgrwll 221
Cdd:cd04187   71 allagLDHARGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYG---VRK-NRKESWLKRLTS---KLFYRLI------- 136
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446911495 222 fqtGSLTGTNM--------LLRRSALEELGGYD 246
Cdd:cd04187  137 ---NKLSGVDIpdnggdfrLMDRKVVDALLLLP 166
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
68-295 3.18e-06

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: 47.59  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGVVIKDTLEAMAKIEYPgKLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPPGEPKG---KSRVLN 144
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYP-KYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGinpKVNNLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 145 YGLSISDGEYFCVYDADNQPEPHALRMLVEHAETTEdaVGAVGHvrtvnekrnwltrmislefqifqllmqsgrwlLFQT 224
Cdd:cd02520   80 KGYEEARYDILVISDSDISVPPDYLRRMVAPLMDPG--VGLVTC--------------------------------LCAF 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446911495 225 GSLtgtnMLLRRSALEELGGYDPYA--IAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQ 295
Cdd:cd02520  126 GKS----MALRREVLDAIGGFEAFAdyLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
72-176 5.43e-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: 47.07  E-value: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  72 IFIPAHNEGVVIKDTLEAMAKIEYPGKLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPPG----EPKGKSRVLNYGL 147
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGShnspSPKGVGYAKNQAI 80
                         90       100
                 ....*....|....*....|....*....
gi 446911495 148 SISDGEYFCVYDADNQPEPHALRMLVEHA 176
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAA 109
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
22-278 7.01e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 47.84  E-value: 7.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  22 ITFSIKYVLIFTAFLFSGL-LVYYSFL-----------TIAGLIHRNSKRKD----RTLEHYPS---VDIFIPAHNEGVV 82
Cdd:PTZ00260   5 WKVIFKHRMLIVLGLVVGLaLLFYPYIswpdddkvirqVKSSVIHEKSKEVDkenyINNILKDSdvdLSIVIPAYNEEDR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  83 IKDTLEAM-----AKIEYPGKLT--IYLLNDNSQDETPEIGDDFDKAYAH----IRHIRVppGEPKGKSRVLNYGLSISD 151
Cdd:PTZ00260  85 LPKMLKETikyleSRSRKDPKFKyeIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSL--LRNKGKGGAVRIGMLASR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 152 GEYFCVYDADNQPEPHALRMLVEHAETTED-----AVGAVGHVR--TVNEKRNWLTRMISLEFQIFQllmqsgrWLLFQT 224
Cdd:PTZ00260 163 GKYILMVDADGATDIDDFDKLEDIMLKIEQnglgiVFGSRNHLVdsDVVAKRKWYRNILMYGFHFIV-------NTICGT 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446911495 225 G---SLTGTNMLLRRSALEELGGYDPYAIAEDAELtLRITQKgYLLPIVPESVTWEQ 278
Cdd:PTZ00260 236 NlkdTQCGFKLFTRETARIIFPSLHLERWAFDIEI-VMIAQK-LNLPIAEVPVNWTE 290
PRK10073 PRK10073
putative glycosyl transferase; Provisional
68-178 1.23e-05

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 46.96  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEG--------VVIKDTLEAmakieypgkLTIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPPGepkGK 139
Cdd:PRK10073   6 PKLSIIIPLYNAGkdfrafmeSLIAQTWTA---------LEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANA---GV 73
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446911495 140 SRVLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAET 178
Cdd:PRK10073  74 SVARNTGLAVATGKYVAFPDADDVVYPTMYETLMTMALE 112
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
68-271 1.88e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 45.84  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  68 PSVDIFIPAHNEGV-------VIKDTLEAMAKIEypgkltIYLLNDNSQDETPEIGDDFDKAYAHIRHIRVPPGEPKGKS 140
Cdd:PLN02726   9 MKYSIIVPTYNERLnialivyLIFKALQDVKDFE------IIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 141 RVLNYGLSISDGEYFCVYDADNQPEPHALR-MLVEHAETTEDAVGAV-----GHVRTVNEKRNWLTRMISLefqIFQLLM 214
Cdd:PLN02726  83 TAYIHGLKHASGDFVVIMDADLSHHPKYLPsFIKKQRETGADIVTGTryvkgGGVHGWDLRRKLTSRGANV---LAQTLL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446911495 215 QSGrwllfqTGSLTGTNMLLRRSALEEL------GGYdpyaiAEDAELTLRITQKGYLLPIVP 271
Cdd:PLN02726 160 WPG------VSDLTGSFRLYKRSALEDLvssvvsKGY-----VFQMEIIVRASRKGYRIEEVP 211
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
147-296 2.83e-05

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: 45.38  E-value: 2.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 147 LSISDGEYFCVYDADNQPEPHALRMLVEHAETTEDAVGAVGHVRTVNEKRNWLTRMISLEFQIFQLLMQS---------- 216
Cdd:cd04190   69 LFPDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVMYQVFEYAISHWLDKAfesvfgfvtc 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 217 --GRWLLFQTGSLTGTNMLLR--------RSALEELGGYDPYAIAEDAELTLRITQKGY--LLPIVPESVTWEQEPEHLK 284
Cdd:cd04190  149 lpGCFSMYRIEALKGDNGGKGplldyaylTNTVDSLHKKNNLDLGEDRILCTLLLKAGPkrKYLYVPGAVAETDVPETFV 228
                        170
                 ....*....|..
gi 446911495 285 ILIKQRTRWLQG 296
Cdd:cd04190  229 ELLSQRRRWINS 240
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
69-299 8.79e-05

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: 43.78  E-value: 8.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495  69 SVDIFIPAHNEGV-VIKDTLEAMAKIEyPGKltIYLLNDNSQDETPEIGDDfDKAYAHIRHIRVPPGepkGKSRVLNYGL 147
Cdd:cd06434    1 DVTVIIPVYDEDPdVFRECLRSILRQK-PLE--IIVVTDGDDEPYLSILSQ-TVKYGGIFVITVPHP---GKRRALAEGI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 148 SISDGEYFCVYDADNQ-PEPHALRMLvehAETTEDAVGAVG-HVRTVNEKRNWLTRMISLEFQIFQLLMQSGRWLLFQTG 225
Cdd:cd06434   74 RHVTTDIVVLLDSDTVwPPNALPEML---KPFEDPKVGGVGtNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVP 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 226 SLTGTNMLLRRSAL----------EELGGYDPYAIAEDAELTLRITQKGYLLPIVPESVTWEQEPEHLKILIKQRTRWLQ 295
Cdd:cd06434  151 CLSGRTAAYRTEILkdflfleeftNETFMGRRLNAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSR 230

                 ....
gi 446911495 296 GNLY 299
Cdd:cd06434  231 SNWR 234
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
100-242 9.70e-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: 43.39  E-value: 9.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 100 TIYLLNDNSQDETPEIGDDFDKAYAHIRHIrVPPGEPKGKSRVLNYGLSISDGEYFCVYDADNQPEPHALRMLVEHAETT 179
Cdd:cd04196   29 ELIISDDGSTDGTVEIIKEYIDKDPFIIIL-IRNGKNLGVARNFESLLQAADGDYVFFCDQDDIWLPDKLERLLKAFLKD 107
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446911495 180 EDAVGAVGHVRTVNE------KRNWLTRMISLEFQIFQLLMQSGRwllfqtgslTGTNMLLRRSALEEL 242
Cdd:cd04196  108 DKPLLVYSDLELVDEngnpigESFFEYQKIKPGTSFNNLLFQNVV---------TGCTMAFNRELLELA 167
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
106-274 4.38e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 38.42  E-value: 4.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 106 DNSQDETPEIGDDFDKAYAHIrhirVPPGEPKGKSRVLNYGLS--ISDG-EYFCVYDADNQPEPHALRMLVEHAETTEDA 182
Cdd:cd02526   31 DNSSGNDIELRLRLNSEKIEL----IHLGENLGIAKALNIGIKaaLENGaDYVLLFDQDSVPPPDMVEKLLAYKILSDKN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446911495 183 --VGAVG-HVRTVNEKRNwltrmislefqiFQLLMQSGRWLLFQTGSLTG---------TNMLLRRSALEELGGYDpyai 250
Cdd:cd02526  107 snIGAVGpRIIDRRTGEN------------SPGVRKSGYKLRIQKEGEEGlkevdflitSGSLISLEALEKVGGFD---- 170
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446911495 251 aE-------DAELTLRITQKGYLLPIVPESV 274
Cdd:cd02526  171 -EdlfidyvDTEWCLRARSKGYKIYVVPDAV 200
 
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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