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Conserved domains on  [gi|15833747|ref|NP_312520|]
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LPS(HepIII)-glucuronic acid glycosyltransferase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

glycosyltransferase( domain architecture ID 11484566)

glycosyltransferase that may be involved in cell wall biosynthesis; similar to Escherichia coli glycosyltransferase YibD

CAZY:  GT2
Gene Ontology:  GO:0016020|GO:0016757

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-327 0e+00

putative glycosyl transferase; Provisional


:

Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 635.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    1 MMNSTNKLSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQANAGASVARNRG 80
Cdd:PRK10073   1 MMNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   81 IEVATGKYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNADWSFRETGETWQSIPSDRLRSTGVLTGPDWLRMGLSSR 160
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRDTGETWQSIPSDRLRSTGVLSGPDWLRMALSSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  161 RWTHVVWMGVYRRDVIVKNNIKFIAGLHHQDIVWTTEFMFNALRARYTEQSLYKYYLHNTSVSRLHRQGNKNLNYQRHYI 240
Cdd:PRK10073 161 RWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHYI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  241 KITRLLEKLNRNYADKIMIYPEFHQQITYEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRLITNVRSVKVGYQALLWS 320
Cdd:PRK10073 241 KITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLWS 320


                 ....*..
gi 15833747  321 FRLWQWR 327
Cdd:PRK10073 321 FRLWQWR 327
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-327 0e+00

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 635.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    1 MMNSTNKLSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQANAGASVARNRG 80
Cdd:PRK10073   1 MMNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   81 IEVATGKYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNADWSFRETGETWQSIPSDRLRSTGVLTGPDWLRMGLSSR 160
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRDTGETWQSIPSDRLRSTGVLSGPDWLRMALSSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  161 RWTHVVWMGVYRRDVIVKNNIKFIAGLHHQDIVWTTEFMFNALRARYTEQSLYKYYLHNTSVSRLHRQGNKNLNYQRHYI 240
Cdd:PRK10073 161 RWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHYI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  241 KITRLLEKLNRNYADKIMIYPEFHQQITYEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRLITNVRSVKVGYQALLWS 320
Cdd:PRK10073 241 KITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLWS 320


                 ....*..
gi 15833747  321 FRLWQWR 327
Cdd:PRK10073 321 FRLWQWR 327
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 7-181 1.92e-38

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 135.60  E-value: 1.92e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   7 KLSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLL-HQANAGASVARNRGIEVAT 85
Cdd:COG0463   3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAAAR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  86 GKYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCnadWSFRETGETWQSIPSDRLRSTgvltgpdwlrMGLSSRRWTHV 165
Cdd:COG0463  83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG---SRLIREGESDLRRLGSRLFNL----------VRLLTNLPDST 149

                       170
                ....*....|....*.
gi 15833747 166 VWMGVYRRDVIVKNNI 181
Cdd:COG0463 150 SGFRLFRREVLEELGF 165
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 9-142 4.68e-38

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: 133.29  E-value: 4.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747     9 SVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQA-NAGASVARNRGIEVATGK 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15833747    88 YVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNADWSFRETGETWQSIPSDRLR 142
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSR 135
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 10-127 2.11e-35

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: 126.08  E-value: 2.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHV-RLLHQANAGASVARNRGIEVATGKY 88
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRViRVINEENQGLAAARNAGLKAARGEY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15833747  89 VAFVDADDEVYPTMYETLMTMALED-DLDVAQCNADWSFR 127
Cdd:cd00761  81 ILFLDADDLLLPDWLERLVAELLADpEADAVGGPGNLLFR 120
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
8-96 8.02e-13

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 67.90  E-value: 8.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    8 LSVIIPLYNAGDDFRTCMESLITQTWT---ALEIIIINDGSTDNSVEIAKHYAENYPH---VRLLHQANAGASVARNRGI 81
Cdd:NF038302   3 FTVAIPTYNGANRLPEVLERLRSQIGTeslSWEIIVVDNNSTDNTAQVVQEYQKNWPSpypLRYCFEPQQGAAFARQRAI 82

                         90
                 ....*....|....*
gi 15833747   82 EVATGKYVAFVDaDD 96
Cdd:NF038302  83 QEAKGELIGFLD-DD 96
 
Name Accession Description Interval E-value
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-327 0e+00

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 635.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    1 MMNSTNKLSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQANAGASVARNRG 80
Cdd:PRK10073   1 MMNSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   81 IEVATGKYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNADWSFRETGETWQSIPSDRLRSTGVLTGPDWLRMGLSSR 160
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDDLDVAQCNADWCFRDTGETWQSIPSDRLRSTGVLSGPDWLRMALSSR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  161 RWTHVVWMGVYRRDVIVKNNIKFIAGLHHQDIVWTTEFMFNALRARYTEQSLYKYYLHNTSVSRLHRQGNKNLNYQRHYI 240
Cdd:PRK10073 161 RWTHVVWLGVYRRDFIVKNNIKFEPGLHHQDIPWTTEVMFNALRVRYTEQSLYKYYLHDTSVSRLPRQGNKNLNYQRHYI 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  241 KITRLLEKLNRNYADKIMIYPEFHQQITYEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRLITNVRSVKVGYQALLWS 320
Cdd:PRK10073 241 KITRMLEKLNRRYADKIKIYPAFHQQITKEALRVCHAVRKEPDILTRQRMIAEIFTSGMYKRIWKNARSVKLGYQLLLWS 320


                 ....*..
gi 15833747  321 FRLWQWR 327
Cdd:PRK10073 321 FRLWQWR 327
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 7-181 1.92e-38

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 135.60  E-value: 1.92e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   7 KLSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLL-HQANAGASVARNRGIEVAT 85
Cdd:COG0463   3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIrLERNRGKGAARNAGLAAAR 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  86 GKYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCnadWSFRETGETWQSIPSDRLRSTgvltgpdwlrMGLSSRRWTHV 165
Cdd:COG0463  83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG---SRLIREGESDLRRLGSRLFNL----------VRLLTNLPDST 149

                       170
                ....*....|....*.
gi 15833747 166 VWMGVYRRDVIVKNNI 181
Cdd:COG0463 150 SGFRLFRREVLEELGF 165
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 9-142 4.68e-38

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: 133.29  E-value: 4.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747     9 SVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQA-NAGASVARNRGIEVATGK 87
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15833747    88 YVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNADWSFRETGETWQSIPSDRLR 142
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSR 135
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 10-127 2.11e-35

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: 126.08  E-value: 2.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHV-RLLHQANAGASVARNRGIEVATGKY 88
Cdd:cd00761   1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRViRVINEENQGLAAARNAGLKAARGEY 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15833747  89 VAFVDADDEVYPTMYETLMTMALED-DLDVAQCNADWSFR 127
Cdd:cd00761  81 ILFLDADDLLLPDWLERLVAELLADpEADAVGGPGNLLFR 120
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
4-110 1.87e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 101.22  E-value: 1.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   4 STNKLSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKhyAENYPHVRLLHQ-ANAGASVARNRGIE 82
Cdd:COG1216   1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLA--ALAFPRVRVIRNpENLGFAAARNLGLR 78

                        90       100
                ....*....|....*....|....*...
gi 15833747  83 VATGKYVAFVDADDEVYPTMYETLMTMA 110
Cdd:COG1216  79 AAGGDYLLFLDDDTVVEPDWLERLLAAA 106
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 7-122 2.08e-25

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 103.67  E-value: 2.08e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   7 KLSVIIPLYNAGDDFRTCMESLITQTWTA--LEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQ-ANAGASVARNRGIEV 83
Cdd:COG1215  30 RVSVIIPAYNEEAVIEETLRSLLAQDYPKekLEVIVVDDGSTDETAEIARELAAEYPRVRVIERpENGGKAAALNAGLKA 109

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15833747  84 ATGKYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNA 122
Cdd:COG1215 110 ARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL 148
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 10-178 2.42e-23

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: 94.99  E-value: 2.42e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENY--PHVRLLHQANAGASVARNRGIEVATGK 87
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYirRVLVVRDKENGGKAGALNAGLRHAKGD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  88 YVAFVDADDEVYPTMYETLMTMALEDDlDVAQCNADWSFRETGETW----QSIpsDRLRSTGVLTGPDWLRMGLSsrrwt 163
Cdd:cd06423  81 IVVVLDADTILEPDALKRLVVPFFADP-KVGAVQGRVRVRNGSENLltrlQAI--EYLSIFRLGRRAQSALGGVL----- 152

                       170
                ....*....|....*..
gi 15833747 164 hVVW--MGVYRRDVIVK 178
Cdd:cd06423 153 -VLSgaFGAFRREALRE 168
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 9-176 1.05e-22

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: 94.99  E-value: 1.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   9 SVIIPLYNAGDDFRTCMESLITQTW--TALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQANAGASVARNRGIEVATG 86
Cdd:cd02525   3 SIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRNSRG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  87 KYVAFVDAdDEVYPTMY-ETLMTMALEDDLDVaqCNADWSFRETGETWQSIP---SDRLRSTGVLtgpdwLRMGLSSRRW 162
Cdd:cd02525  83 DIIIRVDA-HAVYPKDYiLELVEALKRTGADN--VGGPMETIGESKFQKAIAvaqSSPLGSGGSA-----YRGGAVKIGY 154

                       170
                ....*....|....
gi 15833747 163 THVVWMGVYRRDVI 176
Cdd:cd02525 155 VDTVHHGAYRREVF 168
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 10-118 5.08e-20

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: 86.09  E-value: 5.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESL--ITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLL-HQANAGASVARNRGIEVATG 86
Cdd:cd04179   1 VVIPAYNEEENIPELVERLlaVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIrLSRNFGKGAAVRAGFKAARG 80

                        90       100       110
                ....*....|....*....|....*....|..
gi 15833747  87 KYVAFVDADDEVYPTMYETLMTMALEDDLDVA 118
Cdd:cd04179  81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 9-142 5.15e-20

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 86.45  E-value: 5.15e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   9 SVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENypHVRLLHQANAGASVARNRGIEVATGKY 88
Cdd:cd06433   1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDK--ITYWISEPDKGIYDAMNKGIALATGDI 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15833747  89 VAFVDADDEVYP-TMYETLMTMALEDDLDVAQCNADWSFRETGETWQSIPSDRLR 142
Cdd:cd06433  79 IGFLNSDDTLLPgALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLD 133
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-118 3.30e-19

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: 83.38  E-value: 3.30e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKhyaENYPHVRLLHQA-NAGASVARNRGIEVATGKY 88
Cdd:cd04186   1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLR---ELFPEVRLIRNGeNLGFGAGNNQGIREAKGDY 77

                        90       100       110
                ....*....|....*....|....*....|
gi 15833747  89 VAFVDADDEVYPTMYETLMTmALEDDLDVA 118
Cdd:cd04186  78 VLLLNPDTVVEPGALLELLD-AAEQDPDVG 106
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 7-117 7.46e-17

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: 77.63  E-value: 7.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   7 KLSVIIPLYNAGDDF-RTCMESLITQTWTALEIIIINDGSTDNSV-EIAKHYAENYPHVRLLHQA-NAGASVARNRGIEV 83
Cdd:cd04184   2 LISIVMPVYNTPEKYlREAIESVRAQTYPNWELCIADDASTDPEVkRVLKKYAAQDPRIKVVFREeNGGISAATNSALEL 81

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15833747  84 ATGKYVAFVDADDEVYPT-MYETLMTMALEDDLDV 117
Cdd:cd04184  82 ATGEFVALLDHDDELAPHaLYEVVKALNEHPDADL 116
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 10-118 1.99e-15

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: 74.14  E-value: 1.99e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLI-------TQTWtalEIIIINDGSTDNSVEIAKHYAENYP-HVRLLHQ-ANAGASVARNRG 80
Cdd:cd04188   1 VVIPAYNEEKRLPPTLEEAVeyleerpSFSY---EIIVVDDGSKDGTAEVARKLARKNPaLIRVLTLpKNRGKGGAVRAG 77

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15833747  81 IEVATGKYVAFVDADDEVYPTMYETLMTMALEDDLDVA 118
Cdd:cd04188  78 MLAARGDYILFADADLATPFEELEKLEEALKTSGYDIA 115
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 9-96 4.08e-15

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: 73.05  E-value: 4.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   9 SVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQANAGASVARN--RGIEVATG 86
Cdd:cd04196   1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNfeSLLQAADG 80

                        90
                ....*....|
gi 15833747  87 KYVAFVDADD 96
Cdd:cd04196  81 DYVFFCDQDD 90
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 7-126 8.63e-15

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: 72.71  E-value: 8.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   7 KLSVIIPLYNAGDDFRTCMESLItqtWTALEIIIINDGSTDNSVEIAKHYAenyphVRLLHQANAGASVARNRGIEVATG 86
Cdd:cd02511   1 TLSVVIITKNEERNIERCLESVK---WAVDEIIVVDSGSTDRTVEIAKEYG-----AKVYQRWWDGFGAQRNFALELATN 72

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15833747  87 KYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNADWSF 126
Cdd:cd02511  73 DWVLSLDADERLTPELADEILALLATDDYDGYYVPRRNFF 112
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 10-117 1.50e-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: 70.97  E-value: 1.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESL---ITQTWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQA-NAGASVARNRGIEVAT 85
Cdd:cd04187   1 IVVPVYNEEENLPELYERLkavLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSrNFGQQAALLAGLDHAR 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15833747  86 GKYVAFVDAD--D--EVYPTMYEtlmtmALEDDLDV 117
Cdd:cd04187  81 GDAVITMDADlqDppELIPEMLA-----KWEEGYDV 111
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-175 9.88e-14

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: 69.71  E-value: 9.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747     6 NKLSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYPH--VRLLHQANA----GASVARNR 79
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDvrLRVIRNARLlgptGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    80 GIEVATGKYVAFVDADDEVYPTMYETLMTMALEDDLDVAQCNADWSFRetgETWQSiPSDRLRSTgvLTGPDWLRMGLSS 159
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNR---STMLS-ALGALEFA--LRHLRMMSLRLAL 155

                         170
                  ....*....|....*.
gi 15833747   160 RRWTHVVWMGVYRRDV 175
Cdd:pfam13641 156 GVLPLSGAGSAIRREV 171
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 10-95 3.31e-13

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 67.22  E-value: 3.31e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHYAENYP----HVRllhQANAG--ASVARNRGIEV 83
Cdd:cd06420   1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPipikHVW---QEDEGfrKAKIRNKAIAA 77

                        90
                ....*....|..
gi 15833747  84 ATGKYVAFVDAD 95
Cdd:cd06420  78 AKGDYLIFIDGD 89
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-95 4.64e-13

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: 67.99  E-value: 4.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   3 NSTNKLSVIIPLYNAGDDFRTCMESLITQTWTA--LEIIIINDGSTDNSVEIAKHYAENypHVRLLHQ-ANAGASVARNR 79
Cdd:cd06439  26 AYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADK--GVKLLRFpERRGKAAALNR 103

                        90
                ....*....|....*.
gi 15833747  80 GIEVATGKYVAFVDAD 95
Cdd:cd06439 104 ALALATGEIVVFTDAN 119
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
8-96 8.02e-13

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 67.90  E-value: 8.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    8 LSVIIPLYNAGDDFRTCMESLITQTWT---ALEIIIINDGSTDNSVEIAKHYAENYPH---VRLLHQANAGASVARNRGI 81
Cdd:NF038302   3 FTVAIPTYNGANRLPEVLERLRSQIGTeslSWEIIVVDNNSTDNTAQVVQEYQKNWPSpypLRYCFEPQQGAAFARQRAI 82

                         90
                 ....*....|....*
gi 15833747   82 EVATGKYVAFVDaDD 96
Cdd:NF038302  83 QEAKGELIGFLD-DD 96
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-108 2.87e-12

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 65.39  E-value: 2.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWTA--LEIIIINDGSTDNSVEI-AKHYAENYPHVRLLHQA---NAGASVARNRGIEV 83
Cdd:cd04192   1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQIlEFAAAKPNFQLKILNNSrvsISGKKNALTTAIKA 80

                        90       100
                ....*....|....*....|....*
gi 15833747  84 ATGKYVAFVDADDEVYPTMYETLMT 108
Cdd:cd04192  81 AKGDWIVTTDADCVVPSNWLLTFVA 105
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 10-100 1.44e-11

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: 63.25  E-value: 1.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWT-ALEIIIINDGSTDNSVEIAKHYA---ENYPHVRLLHQANA----GASVARNRGI 81
Cdd:cd06913   1 IILPVHNGEQWLDECLESVLQQDFEgTLELSVFNDASTDKSAEIIEKWRkklEDSGVIVLVGSHNSpspkGVGYAKNQAI 80

                        90
                ....*....|....*....
gi 15833747  82 EVATGKYVAFVDADDEVYP 100
Cdd:cd06913  81 AQSSGRYLCFLDSDDVMMP 99
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 8-152 2.28e-10

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: 59.51  E-value: 2.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   8 LSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEIAKHyaenyPHVRLLHqANAGASVARNRGIEVATGK 87
Cdd:cd02522   1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARS-----AGVVVIS-SPKGRARQMNAGAAAARGD 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15833747  88 YVAFVDADDEVyPTMYETLMTMALEDDLDVAqcnadWSFRetgetwQSIPSDRLRSTGVLTGPDW 152
Cdd:cd02522  75 WLLFLHADTRL-PPDWDAAIIETLRADGAVA-----GAFR------LRFDDPGPRLRLLELGANL 127
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 9-105 6.48e-10

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 58.10  E-value: 6.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   9 SVIIPLYNaGDD---FRTCMESLITQTWTALEIIIINDGSTDNSV-EIAKHYAENYPHVRLLHQANAGASVARNRGIEVA 84
Cdd:cd04195   1 SVLMSVYI-KEKpefLREALESILKQTLPPDEVVLVKDGPVTQSLnEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHC 79

                        90       100
                ....*....|....*....|.
gi 15833747  85 TGKYVAFVDADDEVYPTMYET 105
Cdd:cd04195  80 TYDWVARMDTDDISLPDRFEK 100
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 8-95 9.20e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 59.01  E-value: 9.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    8 LSVIIPLYNAGDDFRTCMESLI--------TQTWTALEIIIINDGSTDNSVEIAKHYAENYPH----VRLL-HQANAGAS 74
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKETIkylesrsrKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLsLLRNKGKG 151

                         90       100
                 ....*....|....*....|.
gi 15833747   75 VARNRGIEVATGKYVAFVDAD 95
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDAD 172
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 9-110 1.37e-09

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: 58.06  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747     9 SVIIPLYNaGDDFRTCMESLITQTW---TALEIIIINDGSTDNSVEIAKHYAENYPHVRLLH--QANAGASVARNRGIEV 83
Cdd:pfam10111   1 SVVIPVYN-GEKTHWIQERILNQTFqydPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNapDTTYSLAASRNRGTSH 79

                          90       100
                  ....*....|....*....|....*..
gi 15833747    84 ATGKYVAFVDADDEVYPTMYETLMTMA 110
Cdd:pfam10111  80 AIGEYISFIDGDCLWSPDKFEKQLKIA 106
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 10-118 1.61e-09

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: 57.16  E-value: 1.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQ-TWTALEIIIINDGSTDNSVEIAKHYAENYPHVRLLHQAN-AGASVARNRGIEVATGK 87
Cdd:cd06442   1 IIIPTYNERENIPELIERLDAAlKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGkRGLGSAYIEGFKAARGD 80

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15833747  88 YVAFVDAD----DEVYPTMYETlmtmALEDDLDVA 118
Cdd:cd06442  81 VIVVMDADlshpPEYIPELLEA----QLEGGADLV 111
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-117 1.80e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 51.24  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    2 MNSTNKLSVIIPLYNAGDDFRTCMEsLITQTWTAL---EIIIINDGSTDNSVEIAKHYAENYPHVRLLHQANA---GASV 75
Cdd:PLN02726   5 GEGAMKYSIIVPTYNERLNIALIVY-LIFKALQDVkdfEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPgklGLGT 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15833747   76 ARNRGIEVATGKYVAFVDADDEVYPTMYETLMTMALEDDLDV 117
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADI 125
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 9-98 2.71e-07

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: 51.44  E-value: 2.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   9 SVIIPLYNAGDDF--RTcMESLITQTWTAL--EIIIINDGSTDNSVEIA-KHYAENYPH-VRLLH-QANAGASVARNRGI 81
Cdd:cd02510   1 SVIIIFHNEALSTllRT-VHSVINRTPPELlkEIILVDDFSDKPELKLLlEEYYKKYLPkVKVLRlKKREGLIRARIAGA 79

                        90
                ....*....|....*..
gi 15833747  82 EVATGKYVAFVDADDEV 98
Cdd:cd02510  80 RAATGDVLVFLDSHCEV 96
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 8-114 5.79e-07

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 49.95  E-value: 5.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   8 LSVIIPLYNA-GDDFRTCMESLITQTwtALEIIIINDGSTDNSVEIAKHyAENYPHVRLLHQANAGASVARNRGIEVATG 86
Cdd:cd06434   2 VTVIIPVYDEdPDVFRECLRSILRQK--PLEIIVVTDGDDEPYLSILSQ-TVKYGGIFVITVPHPGKRRALAEGIRHVTT 78

                        90       100
                ....*....|....*....|....*...
gi 15833747  87 KYVAFVDaDDEVYPTMYETLMTMALEDD 114
Cdd:cd06434  79 DIVVLLD-SDTVWPPNALPEMLKPFEDP 105
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
8-100 1.34e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 49.22  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    8 LSVIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTdnSVEIAKHYAE--NYPHVRLLHQA-NAGASVARNRGIEVA 84
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTalNDPRITYIHNDiNSGACAVRNQAIMLA 84

                         90
                 ....*....|....*.
gi 15833747   85 TGKYVAFVDADDEVYP 100
Cdd:PRK10018  85 QGEYITGIDDDDEWTP 100
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 10-126 2.48e-06

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 47.63  E-value: 2.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747  10 VIIPLYNAGDDFRTCMESLITQTWTALEIIIINDGSTDNSVEI--AKHYAENYPHVRLlhQANAGASVARNRGIEVA--T 85
Cdd:cd04185   1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWltSLGDLDNIVYLRL--PENLGGAGGFYEGVRRAyeL 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15833747  86 G-KYVAFVDADDEVYPTMYETLMTMALEDDLDVAQ---CNADWSF 126
Cdd:cd04185  79 GyDWIWLMDDDAIPDPDALEKLLAYADKDNPQFLAplvLDPDGSF 123
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 6-95 3.95e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 44.73  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    6 NKLSVIIPLYNAGDDFRTCMESLIT---QTWTALEIIIINDGSTDNSVEIAKHYAE--NYPHVRLLHQANAGASVARNRG 80
Cdd:PRK10714   6 KKVSVVIPVYNEQESLPELIRRTTAaceSLGKEYEILLIDDGSSDNSAEMLVEAAQapDSHIVAILLNRNYGQHSAIMAG 85

                         90
                 ....*....|....*
gi 15833747   81 IEVATGKYVAFVDAD 95
Cdd:PRK10714  86 FSHVTGDLIITLDAD 100
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 7-95 4.67e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.44  E-value: 4.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747    7 KLSVIIPLYN----AGDDFRTC----MESLItqtwtaLEIIIINDGSTDNSVEIAkhyaenyphvrllhqANAGASV-AR 77
Cdd:PRK13915  32 TVSVVLPALNeeetVGKVVDSIrpllMEPLV------DELIVIDSGSTDATAERA---------------AAAGARVvSR 90

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15833747   78 N-----------------RGIEVATGKYVAFVDAD 95
Cdd:PRK13915  91 EeilpelpprpgkgealwRSLAATTGDIVVFVDAD 125
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 9-95 1.83e-03

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: 39.22  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15833747   9 SVIIPLYNAGDDFRTCMESLITQTWTA--LEIIIINDgSTDNSVEIAKHYAENYP----HVRLLHQAN-----AGASVAr 77
Cdd:cd06437   4 TVQLPVFNEKYVVERLIEAACALDYPKdrLEIQVLDD-STDETVRLAREIVEEYAaqgvNIKHVRRADrtgykAGALAE- 81

                        90
                ....*....|....*...
gi 15833747  78 nrGIEVATGKYVAFVDAD 95
Cdd:cd06437  82 --GMKVAKGEYVAIFDAD 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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