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Conserved domains on  [gi|740643789|ref|WP_038429237|]
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glycosyltransferase family 2 protein [Escherichia coli]

Protein Classification

glycosyltransferase( domain architecture ID 11440269)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-352 1.58e-35

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: 132.17  E-value: 1.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   4 LLFIFMTIAMLLWFLSTLRRKPCQKKGCIDAIIPAYNEGPCLAQSLDNLLRNPYFC---RVICVNDGSTDNTEAVMAEVK 80
Cdd:COG1215    3 LLLALLALLYLLLLALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKeklEVIVVDDGSTDETAEIARELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  81 RKWGDRFVAVTQKNTGKGGALMHGLKYATCDQVFLSDADTFVPPDndgmgyMLAEIERGADAvggipstalkgagllPHI 160
Cdd:COG1215   83 AEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPD------WLRRLVAAFAD---------------PGV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 161 RAtvklpmivmkrtlqqflggapfiiSGACGMFRTDVLRKFG-FSDRTKVEDLDLTWTLVANGYRIRQANRCIVYPQECN 239
Cdd:COG1215  142 GA------------------------SGANLAFRREALEEVGgFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPE 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 240 SPREEWRRWRRWIVGYAVCMRLHKRLLFSRFGIFSIFPMLLVVLYGVgiylttwfnefittgphgVVLAMSPLIWVGVVC 319
Cdd:COG1215  198 TLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLL------------------LLLALLALLLLLLPA 259
                        330       340       350
                 ....*....|....*....|....*....|...
gi 740643789 320 VIGAFSAWFHRCWLLVPLAPLSVVYVLLAYAIW 352
Cdd:COG1215  260 LLLALLLALRRRRLLLPLLHLLYGLLLLLAALR 292
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-352 1.58e-35

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: 132.17  E-value: 1.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   4 LLFIFMTIAMLLWFLSTLRRKPCQKKGCIDAIIPAYNEGPCLAQSLDNLLRNPYFC---RVICVNDGSTDNTEAVMAEVK 80
Cdd:COG1215    3 LLLALLALLYLLLLALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKeklEVIVVDDGSTDETAEIARELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  81 RKWGDRFVAVTQKNTGKGGALMHGLKYATCDQVFLSDADTFVPPDndgmgyMLAEIERGADAvggipstalkgagllPHI 160
Cdd:COG1215   83 AEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPD------WLRRLVAAFAD---------------PGV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 161 RAtvklpmivmkrtlqqflggapfiiSGACGMFRTDVLRKFG-FSDRTKVEDLDLTWTLVANGYRIRQANRCIVYPQECN 239
Cdd:COG1215  142 GA------------------------SGANLAFRREALEEVGgFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPE 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 240 SPREEWRRWRRWIVGYAVCMRLHKRLLFSRFGIFSIFPMLLVVLYGVgiylttwfnefittgphgVVLAMSPLIWVGVVC 319
Cdd:COG1215  198 TLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLL------------------LLLALLALLLLLLPA 259
                        330       340       350
                 ....*....|....*....|....*....|...
gi 740643789 320 VIGAFSAWFHRCWLLVPLAPLSVVYVLLAYAIW 352
Cdd:COG1215  260 LLLALLLALRRRRLLLPLLHLLYGLLLLLAALR 292
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
33-200 5.25e-30

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: 113.64  E-value: 5.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   33 DAIIPAYNEGPCLAQSLDNLLRNPY-FCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKNTGKGGALMHGLKYATCD 111
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYpNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  112 QVFLSDADTFVPPDNDGMGYMLAEIERGADAVGGIPSTALKGAGLLPHIRATVklpMIVMKRTLQQFLGGAPFIISGACG 191
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITL---SRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 740643789  192 MFRTDVLRK 200
Cdd:pfam00535 158 LYRREALEE 166
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
35-211 5.32e-27

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: 105.77  E-value: 5.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLRN--PYFcRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQK-NTGKGGALMHGLKYATCD 111
Cdd:cd06423    2 IVPAYNEEAVIERTIESLLALdyPKL-EVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKeNGGKAGALNAGLRHAKGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 112 QVFLSDADTFVPPDNdgMGYMLAEIER--GADAVGGIPSTALKGAGLLPHIrATVKLPMIVMKRTLQQFLGGAPFIISGA 189
Cdd:cd06423   81 IVVVLDADTILEPDA--LKRLVVPFFAdpKVGAVQGRVRVRNGSENLLTRL-QAIEYLSIFRLGRRAQSALGGVLVLSGA 157
                        170       180
                 ....*....|....*....|...
gi 740643789 190 CGMFRTDVLRKFG-FSDRTKVED 211
Cdd:cd06423  158 FGAFRREALREVGgWDEDTLTED 180
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
35-145 1.39e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 58.17  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEG---PCLAQSLDNLLRNPYFCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQ--KNTGKGGALMHGLKYAT 109
Cdd:PLN02726  14 IVPTYNERlniALIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPrpGKLGLGTAYIHGLKHAS 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 740643789 110 CDQVFLSDAD-----TFVPpdndgmGYMLAEIERGADAVGG 145
Cdd:PLN02726  94 GDFVVIMDADlshhpKYLP------SFIKKQRETGADIVTG 128
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
35-233 4.11e-09

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


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 56.37  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   35 IIPAYNEGPCLAQSLDNLLRNPYFCRVICVNDGSTDNTeavmAEVKRKWGDRfVAVTQKntGKGGALMHGLKYATCDQVF 114
Cdd:TIGR04283   4 IIPVLNEAATLPELLADLQALRGDAEVIVVDGGSTDGT----VEIARSLGAK-VIHSPK--GRARQMNAGAALAKGDILL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  115 LSDADTFVPPDNDgmgymlAEIER---GADAVGGIPSTALKGAG-LLPHIRATVKLpmivmkRTLqqfLGGAPFiisGAC 190
Cdd:TIGR04283  77 FLHADTRLPKDFL------EAIRRalaKPGYVAGAFDLRFDGPGlLLRLIEWGVNL------RSR---LTGIPY---GDQ 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 740643789  191 GMF-RTDVLRKF-GFSDRTKVEDLDLTWTLVANGyRIRQANRCIV 233
Cdd:TIGR04283 139 GLFvRRSLFEQIgGFPDIPLMEDIELSRRLRRLG-RLAILPAPVV 182
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-352 1.58e-35

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: 132.17  E-value: 1.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   4 LLFIFMTIAMLLWFLSTLRRKPCQKKGCIDAIIPAYNEGPCLAQSLDNLLRNPYFC---RVICVNDGSTDNTEAVMAEVK 80
Cdd:COG1215    3 LLLALLALLYLLLLALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKeklEVIVVDDGSTDETAEIARELA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  81 RKWGDRFVAVTQKNTGKGGALMHGLKYATCDQVFLSDADTFVPPDndgmgyMLAEIERGADAvggipstalkgagllPHI 160
Cdd:COG1215   83 AEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPD------WLRRLVAAFAD---------------PGV 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 161 RAtvklpmivmkrtlqqflggapfiiSGACGMFRTDVLRKFG-FSDRTKVEDLDLTWTLVANGYRIRQANRCIVYPQECN 239
Cdd:COG1215  142 GA------------------------SGANLAFRREALEEVGgFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPE 197
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 240 SPREEWRRWRRWIVGYAVCMRLHKRLLFSRFGIFSIFPMLLVVLYGVgiylttwfnefittgphgVVLAMSPLIWVGVVC 319
Cdd:COG1215  198 TLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLLLLLLPLLLLL------------------LLLALLALLLLLLPA 259
                        330       340       350
                 ....*....|....*....|....*....|...
gi 740643789 320 VIGAFSAWFHRCWLLVPLAPLSVVYVLLAYAIW 352
Cdd:COG1215  260 LLLALLLALRRRRLLLPLLHLLYGLLLLLAALR 292
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
33-200 5.25e-30

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: 113.64  E-value: 5.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   33 DAIIPAYNEGPCLAQSLDNLLRNPY-FCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKNTGKGGALMHGLKYATCD 111
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYpNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  112 QVFLSDADTFVPPDNDGMGYMLAEIERGADAVGGIPSTALKGAGLLPHIRATVklpMIVMKRTLQQFLGGAPFIISGACG 191
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITL---SRLPFFLGLRLLGLNLPFLIGGFA 157

                  ....*....
gi 740643789  192 MFRTDVLRK 200
Cdd:pfam00535 158 LYRREALEE 166
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
35-211 5.32e-27

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: 105.77  E-value: 5.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLRN--PYFcRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQK-NTGKGGALMHGLKYATCD 111
Cdd:cd06423    2 IVPAYNEEAVIERTIESLLALdyPKL-EVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKeNGGKAGALNAGLRHAKGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 112 QVFLSDADTFVPPDNdgMGYMLAEIER--GADAVGGIPSTALKGAGLLPHIrATVKLPMIVMKRTLQQFLGGAPFIISGA 189
Cdd:cd06423   81 IVVVLDADTILEPDA--LKRLVVPFFAdpKVGAVQGRVRVRNGSENLLTRL-QAIEYLSIFRLGRRAQSALGGVLVLSGA 157
                        170       180
                 ....*....|....*....|...
gi 740643789 190 CGMFRTDVLRKFG-FSDRTKVED 211
Cdd:cd06423  158 FGAFRREALREVGgWDEDTLTED 180
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
32-227 5.50e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.01  E-value: 5.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  32 IDAIIPAYNEGPCLAQSLDNLLRNPYF-CRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKNTGKGGALMHGLKYATC 110
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESLLAQTYPdFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAARG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 111 DQVFLSDADTFVPPDNdgMGYMLAEIER-GADAVGGipsTALKGAGLLPHIRATVKLpmivmkRTLQQFLGGAPFIISGa 189
Cdd:COG0463   84 DYIAFLDADDQLDPEK--LEELVAALEEgPADLVYG---SRLIREGESDLRRLGSRL------FNLVRLLTNLPDSTSG- 151
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 740643789 190 CGMFRTDVLRKFGFSDRtKVEDLDLTWtLVANGYRIRQ 227
Cdd:COG0463  152 FRLFRREVLEELGFDEG-FLEDTELLR-ALRHGFRIAE 187
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
34-152 6.26e-22

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: 91.41  E-value: 6.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  34 AIIPAYNEGPCLAQSLDNLLRNPY-FCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKNTGKGGALMHGLKYATCDQ 112
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYpNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 740643789 113 VFLSDADTFVPPDNDGMGYMLAEIERGADAVGGIPSTALK 152
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLLFR 120
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
35-201 2.56e-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: 87.63  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLA---QSLDNLLRNPYFCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKNTGKGGALMHGLKYATCD 111
Cdd:cd04179    2 VIPAYNEEENIPelvERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 112 QVFLSDADTFVPPDNdgMGYMLAEI-ERGADAVGGIPsTALKGAGLLPHIRatvKLPMIVMKRTLQQFLGGApfIISGAC 190
Cdd:cd04179   82 IVVTMDADLQHPPED--IPKLLEKLlEGGADVVIGSR-FVRGGGAGMPLLR---RLGSRLFNFLIRLLLGVR--ISDTQS 153
                        170
                 ....*....|...
gi 740643789 191 GM--FRTDVLRKF 201
Cdd:cd04179  154 GFrlFRREVLEAL 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
32-234 5.93e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.80  E-value: 5.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  32 IDAIIPAYNEGPCLAQSLDNLLRNPYF-CRVICVNDGSTDNTEAVMAEVKRKwGDRFVAvTQKNTGKGGALMHGLKYATC 110
Cdd:COG1216    5 VSVVIPTYNRPELLRRCLESLLAQTYPpFEVIVVDNGSTDGTAELLAALAFP-RVRVIR-NPENLGFAAARNLGLRAAGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 111 DQVFLSDADTFVPPDndgmgyMLAEiergadavggipstalkgagllphiratvklpmivmkrtlqqflggapfIISGAC 190
Cdd:COG1216   83 DYLLFLDDDTVVEPD------WLER-------------------------------------------------LLAAAC 107
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 740643789 191 GMFRTDVLRKFG-FSDRTKV--EDLDLTWTLVANGYRIRQANRCIVY 234
Cdd:COG1216  108 LLIRREVFEEVGgFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVY 154
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
35-146 1.27e-15

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: 74.44  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPC---LAQSLDNLLRNP-YFCRVICVNDGSTDNTEAVMAEVKRKWgDRFVAVT-QKNTGKGGALMHGLKYAT 109
Cdd:cd04187    2 VVPVYNEEENlpeLYERLKAVLESLgYDYEIIFVDDGSTDRTLEILRELAARD-PRVKVIRlSRNFGQQAALLAGLDHAR 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 740643789 110 CDQVFLSDADTFVPPDNdgMGYMLAEIERGADAVGGI 146
Cdd:cd04187   81 GDAVITMDADLQDPPEL--IPEMLAKWEEGYDVVYGV 115
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
12-125 1.41e-14

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: 73.00  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  12 AMLLWFLSTLRRKPCQKKGC----IDAIIPAYNEGPCLAQSLDNLLRNPY---FCRVICVNDGSTDNTeavmAEVKRKWG 84
Cdd:cd06439    7 LLLKLLARLRPKPPSLPDPAylptVTIIIPAYNEEAVIEAKLENLLALDYprdRLEIIVVSDGSTDGT----AEIAREYA 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 740643789  85 DRFVAVTQK--NTGKGGALMHGLKYATCDQVFLSDADTFVPPD 125
Cdd:cd06439   83 DKGVKLLRFpeRRGKAAALNRALALATGEIVVFTDANALLDPD 125
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
34-240 2.47e-14

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 71.90  E-value: 2.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  34 AIIPAYNEGP-CLAQSLDNLLRN-PYfcRVICVNDGStDNTEAVMAEVKRKWGDRFVaVTQKNTGKGGALMHGLKYATCD 111
Cdd:cd06434    4 VIIPVYDEDPdVFRECLRSILRQkPL--EIIVVTDGD-DEPYLSILSQTVKYGGIFV-ITVPHPGKRRALAEGIRHVTTD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 112 QVFLSDADTFVPPDNdgMGYMLAEIErgADAVGGIpST---ALKGAGLLPHIRATVKLPMIVMKRTLQQFLGGAPFIISG 188
Cdd:cd06434   80 IVVLLDSDTVWPPNA--LPEMLKPFE--DPKVGGV-GTnqrILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740643789 189 ACGMFRTDVLRKFGFSDRTKVE-----------DLDLTWTLVANGYRIR-QANR-CIVYPQECNS 240
Cdd:cd06434  155 RTAAYRTEILKDFLFLEEFTNEtfmgrrlnagdDRFLTRYVLSHGYKTVyQYTSeAYTETPENYK 219
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
35-119 6.55e-14

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: 70.29  E-value: 6.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLL-----RNPYFCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQ-KNTGKGGALMHGLKYA 108
Cdd:cd04188    2 VIPAYNEEKRLPPTLEEAVeyleeRPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLpKNRGKGGAVRAGMLAA 81
                         90
                 ....*....|.
gi 740643789 109 TCDQVFLSDAD 119
Cdd:cd04188   82 RGDYILFADAD 92
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
35-234 5.90e-13

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: 68.03  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLRNPYFC---RVICVNDGSTDNTEAVMAEVKRKwgDRFVAVT---QKNTGKGgaLMHGLKYA 108
Cdd:cd02525    5 IIPVRNEEKYIEELLESLLNQSYPKdliEIIVVDGGSTDGTREIVQEYAAK--DPRIRLIdnpKRIQSAG--LNIGIRNS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 109 TCDQVFLSDADTFVPPDndgmgYML----AEIERGADAVGG----IPSTALKGAgllphIRATVKLPMIVmkrtlqqflG 180
Cdd:cd02525   81 RGDIIIRVDAHAVYPKD-----YILelveALKRTGADNVGGpmetIGESKFQKA-----IAVAQSSPLGS---------G 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740643789 181 GAPF---------IISGACGMFRTDVLRKFGFSDRTKV--EDLDLTWTLVANGYRIRQANRCIVY 234
Cdd:cd02525  142 GSAYrggavkigyVDTVHHGAYRREVFEKVGGFDESLVrnEDAELNYRLRKAGYKIWLSPDIRVY 206
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
35-226 2.79e-11

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 61.42  E-value: 2.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLRNPYF-CRVICVNDGSTDNTEAvmaEVKRKWGDRFVAVTQKNTGKGGALMHGLKYATCDQV 113
Cdd:cd04186    2 IIVNYNSLEYLKACLDSLLAQTYPdFEVIVVDNASTDGSVE---LLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 114 FLSDADTFVppDNDGMGYMLAEIERGADAVggipstalkgagllphiratvklpmIVMKRtlqqflggapfiISGACGMF 193
Cdd:cd04186   79 LLLNPDTVV--EPGALLELLDAAEQDPDVG-------------------------IVGPK------------VSGAFLLV 119
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 740643789 194 RTDVLRKFG-FSDRTKV--EDLDLTWTLVANGYRIR 226
Cdd:cd04186  120 RREVFEEVGgFDEDFFLyyEDVDLCLRARLAGYRVL 155
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
35-225 5.05e-11

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: 62.00  E-value: 5.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   35 IIPAYNEGPCLAQSLDNLLRNPYF-CRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKN-----TGKGGALMHGLKYA 108
Cdd:pfam13641   7 VVPAFNEDSVLGRVLEAILAQPYPpVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNArllgpTGKSRGLNHGFRAV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  109 TCDQVFLSDADTFVPPDNDGMGYMLAEIErGADAVGGIP-STALKGAGLLPHIR--ATVKLPMIVMKRTlqqflGGAPFi 185
Cdd:pfam13641  87 KSDLVVLHDDDSVLHPGTLKKYVQYFDSP-KVGAVGTPVfSLNRSTMLSALGALefALRHLRMMSLRLA-----LGVLP- 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 740643789  186 ISGACGMFRTDVLRKFGFSDR--TKVEDLDLTWTLVANGYRI 225
Cdd:pfam13641 160 LSGAGSAIRREVLKELGLFDPffLLGDDKSLGRRLRRHGWRV 201
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
35-145 1.39e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 58.17  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEG---PCLAQSLDNLLRNPYFCRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQ--KNTGKGGALMHGLKYAT 109
Cdd:PLN02726  14 IVPTYNERlniALIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPrpGKLGLGTAYIHGLKHAS 93
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 740643789 110 CDQVFLSDAD-----TFVPpdndgmGYMLAEIERGADAVGG 145
Cdd:PLN02726  94 GDFVVIMDADlshhpKYLP------SFIKKQRETGADIVTG 128
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
35-225 2.07e-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: 2.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEG---PCLAQSLDNLLRNPYFcRVICVNDGSTDNTEAVMAEVKRKWGDRFVAVTQKNTGKGGALMHGLKYATCD 111
Cdd:cd06442    2 IIPTYNEReniPELIERLDAALKGIDY-EIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 112 QVFLSDAD-----TFVPPdndgmgyML-AEIERGADAVGG---IPSTALKGAGLLPHI--RATVKLPMIVMKRTLQQFLG 180
Cdd:cd06442   81 VIVVMDADlshppEYIPE-------LLeAQLEGGADLVIGsryVEGGGVEGWGLKRKLisRGANLLARLLLGRKVSDPTS 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 740643789 181 GapFIisgacgMFRTDVLRKFGFSDRTK--VEDLDLTWTLVANGYRI 225
Cdd:cd06442  154 G--FR------AYRREVLEKLIDSLVSKgyKFQLELLVRARRLGYRI 192
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
35-233 4.11e-09

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


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 56.37  E-value: 4.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   35 IIPAYNEGPCLAQSLDNLLRNPYFCRVICVNDGSTDNTeavmAEVKRKWGDRfVAVTQKntGKGGALMHGLKYATCDQVF 114
Cdd:TIGR04283   4 IIPVLNEAATLPELLADLQALRGDAEVIVVDGGSTDGT----VEIARSLGAK-VIHSPK--GRARQMNAGAALAKGDILL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  115 LSDADTFVPPDNDgmgymlAEIER---GADAVGGIPSTALKGAG-LLPHIRATVKLpmivmkRTLqqfLGGAPFiisGAC 190
Cdd:TIGR04283  77 FLHADTRLPKDFL------EAIRRalaKPGYVAGAFDLRFDGPGlLLRLIEWGVNL------RSR---LTGIPY---GDQ 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 740643789  191 GMF-RTDVLRKF-GFSDRTKVEDLDLTWTLVANGyRIRQANRCIV 233
Cdd:TIGR04283 139 GLFvRRSLFEQIgGFPDIPLMEDIELSRRLRRLG-RLAILPAPVV 182
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
39-224 8.00e-08

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: 52.32  E-value: 8.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  39 YNEGPC-LAQSLDNLLRN---PyfCRVICVNDGS-TDNTEAVMAEVKRKWGDRFVAVtQKNTGKGGALMHGLKYATCDQV 113
Cdd:cd04195    8 IKEKPEfLREALESILKQtlpP--DEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPL-EKNRGLGKALNEGLKHCTYDWV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 114 FLSDADTFVPPDndgmgymlaEIERGADAVGGIPSTALKGAGLL-----PHIRATVKLPMivMKRTLQQFLGGA-PFIis 187
Cdd:cd04195   85 ARMDTDDISLPD---------RFEKQLDFIEKNPEIDIVGGGVLefdsdGNDIGKRRLPT--SHDDILKFARRRsPFN-- 151
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 740643789 188 GACGMFRTD-VLRKFGFSDRTKVEDLDLTWTLVANGYR 224
Cdd:cd04195  152 HPTVMFRKSkVLAVGGYQDLPLVEDYALWARMLANGAR 189
PRK10073 PRK10073
putative glycosyl transferase; Provisional
35-125 1.29e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 52.74  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLR-NPYFCRVICVNDGSTDNTeavmAEVKRKWGDRFVAVT---QKNTGKGGALMHGLKYATC 110
Cdd:PRK10073  11 IIPLYNAGKDFRAFMESLIAqTWTALEIIIVNDGSTDNS----VEIAKHYAENYPHVRllhQANAGVSVARNTGLAVATG 86
                         90
                 ....*....|....*
gi 740643789 111 DQVFLSDADTFVPPD 125
Cdd:PRK10073  87 KYVAFPDADDVVYPT 101
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
35-119 1.33e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 52.85  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLL--------RNPYF-CRVICVNDGSTDNTEAV----MAEVKRKWGDRFVAVTQKNTGKGGAL 101
Cdd:PTZ00260  75 VIPAYNEEDRLPKMLKETIkylesrsrKDPKFkYEIIIVNDGSKDKTLKVakdfWRQNINPNIDIRLLSLLRNKGKGGAV 154
                         90
                 ....*....|....*...
gi 740643789 102 MHGLKYATCDQVFLSDAD 119
Cdd:PTZ00260 155 RIGMLASRGKYILMVDAD 172
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
34-125 1.56e-07

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: 51.91  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  34 AIIPAYNEGPCLAQSLDNLLRnpyFC-RVICVNDGSTDNTEAV----MAEVKRKWGDRFVAvtQKNtgkggalmHGLKYA 108
Cdd:cd02511    4 VVIITKNEERNIERCLESVKW---AVdEIIVVDSGSTDRTVEIakeyGAKVYQRWWDGFGA--QRN--------FALELA 70
                         90
                 ....*....|....*..
gi 740643789 109 TCDQVFLSDADTFVPPD 125
Cdd:cd02511   71 TNDWVLSLDADERLTPE 87
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
35-214 2.07e-07

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: 50.68  E-value: 2.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLL-----RNPYfcRVICVNDGSTDNTeavmAEVKRKWG----DRFvavTQKNTGKGGALMHGL 105
Cdd:cd06438    2 LIPAHNEEAVIGNTVRSLKaqdypRELY--RIFVVADNCTDDT----AQVARAAGatvlERH---DPERRGKGYALDFGF 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 106 KYA-----TCDQVFLSDADTFVppDNDGMGYMLAEIERGADAVGGIPSTALKGAGLLPHIRATVklpMIVMKRTLQqfLG 180
Cdd:cd06438   73 RHLlnladDPDAVVVFDADNLV--DPNALEELNARFAAGARVVQAYYNSKNPDDSWITRLYAFA---FLVFNRLRP--LG 145
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 740643789 181 ----GAPFIISGAcGM-FRTDVLRKFGFSDRTKVEDLDL 214
Cdd:cd06438  146 rsnlGLSCQLGGT-GMcFPWAVLRQAPWAAHSLTEDLEF 183
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
36-215 2.18e-07

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: 51.54  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  36 IPAYNEGPCLAQSLDN--LLRNPYFCRVICVNDGSTDNT-EAVMAEVKRKWGD----RFVAVTQKNTGKGGALMHGLKYA 108
Cdd:cd06437    7 LPVFNEKYVVERLIEAacALDYPKDRLEIQVLDDSTDETvRLAREIVEEYAAQgvniKHVRRADRTGYKAGALAEGMKVA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 109 TCDQVFLSDADtFVPPDNdgmgYMLAEIERGADAVGGIPSTALK----GAGLLPHIRATvklpMIVMKRTLQQFLG---G 181
Cdd:cd06437   87 KGEYVAIFDAD-FVPPPD----FLQKTPPYFADPKLGFVQTRWGhinaNYSLLTRVQAM----SLDYHFTIEQVARsstG 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 740643789 182 APFIISGACGMFRTDVLRKFG-FSDRTKVEDLDLT 215
Cdd:cd06437  158 LFFNFNGTAGVWRKECIEDAGgWNHDTLTEDLDLS 192
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
35-126 2.18e-07

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: 51.52  E-value: 2.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEG---PCLAQSLDNLLRNPYFCRVICVNDGSTDNTEAVMAEVKRKwGDRFVAVTQ----KNTGKGGALMHGLKY 107
Cdd:cd04192    2 VIAARNEAenlPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAK-PNFQLKILNnsrvSISGKKNALTTAIKA 80
                         90
                 ....*....|....*....
gi 740643789 108 ATCDQVFLSDADTFVPPDN 126
Cdd:cd04192   81 AKGDWIVTTDADCVVPSNW 99
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
35-144 3.37e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 51.66  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLD------NLLRNPYfcRVICVNDGSTDNTEAVMAEVKRKWGDRFVAV-TQKNTGKGGALMHGLKY 107
Cdd:PRK10714  11 VIPVYNEQESLPELIRrttaacESLGKEY--EILLIDDGSSDNSAEMLVEAAQAPDSHIVAIlLNRNYGQHSAIMAGFSH 88
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 740643789 108 ATCDQVFLSDADTFVPPDNdgMGYMLAEIERGADAVG 144
Cdd:PRK10714  89 VTGDLIITLDADLQNPPEE--IPRLVAKADEGYDVVG 123
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
97-233 1.33e-06

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


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 48.05  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789   97 KGGALMHGLKYATCDQVFLSDADTFVPPdnDGMGYMLAEIERGADA-VGGIP--------STALKGAGLLPHiratvklp 167
Cdd:pfam13506  18 KVNNLLQGLEAAKYDLLVISDSDIRVPP--DYLRDLLAPLADPKVGlVTSPPvgsdpkglAAALEAAFFNTL-------- 87
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  168 mivmKRTLQQFLGGAPFIIsGACGMFRTDVLRKFG----FSDrTKVEDLDLTWTLVANGYRIRQANRCIV 233
Cdd:pfam13506  88 ----AGVLQAALSGIGFAV-GMSMAFRRADLERIGgfeaLAD-YLAEDYALGKLLRAAGLKVVLSPRPIL 151
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
35-142 8.58e-06

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: 46.41  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLR-NPYFCRVICVNDGSTDNTEAVmAEVKRkwgdrfVAVTQKNTGKGGALMHGLKYATCDQV 113
Cdd:cd02522    4 IIPTLNEAENLPRLLASLRRlNPLPLEIIVVDGGSTDGTVAI-ARSAG------VVVISSPKGRARQMNAGAAAARGDWL 76
                         90       100
                 ....*....|....*....|....*....
gi 740643789 114 FLSDADTFVPPDNDGMGYMLAeIERGADA 142
Cdd:cd02522   77 LFLHADTRLPPDWDAAIIETL-RADGAVA 104
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
35-119 1.70e-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: 45.31  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLRNPYF-CRVICVNDGSTDNTEAVMAEVKRKWGDRFvaVTQKNTGKGGA---LMHGLKYATC 110
Cdd:cd04196    3 LMATYNGEKYLREQLDSILAQTYKnDELIISDDGSTDGTVEIIKEYIDKDPFII--ILIRNGKNLGVarnFESLLQAADG 80

                 ....*....
gi 740643789 111 DQVFLSDAD 119
Cdd:cd04196   81 DYVFFCDQD 89
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
31-237 1.46e-04

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: 42.94  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  31 CIDAIIPAYNEGP---------CLAqsldnlLRNPYFC-RVICVNDGSTDNTEAVMAEVKRKWGDRFVAvTQKNTG-KGG 99
Cdd:cd06421    2 TVDVFIPTYNEPLeivrktlraALA------IDYPHDKlRVYVLDDGRRPELRALAAELGVEYGYRYLT-RPDNRHaKAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 100 ALMHGLKYATCDQVFLSDADtFVP-PD--NDGMGYMLAEiergadavggiPSTALKGAgllPH----------IRATVKL 166
Cdd:cd06421   75 NLNNALAHTTGDFVAILDAD-HVPtPDflRRTLGYFLDD-----------PKVALVQT---PQffynpdpfdwLADGAPN 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 740643789 167 PMIVMKRTLQQFL--GGAPFIIsGACGMFRTDVLRKFG-FSDRTKVEDLDLTWTLVANGYRIRQANRCIVYPQE 237
Cdd:cd06421  140 EQELFYGVIQPGRdrWGAAFCC-GSGAVVRREALDEIGgFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLA 212
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
34-125 2.98e-04

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: 41.47  E-value: 2.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  34 AIIPAYNEGPCLAQSLDNLLRNPY-FCRVICVNDGSTDNTEAVmaeVKRKWGDRFVAV--TQKNTGKGGALMHGLKYAT- 109
Cdd:cd04185    1 AVVVTYNRLDLLKECLDALLAQTRpPDHIIVIDNASTDGTAEW---LTSLGDLDNIVYlrLPENLGGAGGFYEGVRRAYe 77
                         90
                 ....*....|....*...
gi 740643789 110 --CDQVFLSDADTFVPPD 125
Cdd:cd04185   78 lgYDWIWLMDDDAIPDPD 95
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
113-294 4.72e-04

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: 40.78  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  113 VFLSDADTFVPPDNdgMGYMLAEIERGADAVGGIPSTALKGAGLL-PHIRATVKLPMIVMKRtlQQFLGGAPFIISGACG 191
Cdd:pfam13632   2 ILLLDADTVLPPDC--LLGIANEMASPEVAIIQGPILPMNVGNYLeELAALFFADDHGKSIP--VRMALGRVLPFVGSGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  192 MFRTDVLRK-FGFSDRTKVEDLDLTWTLVANGYRIRQANRCIVYpqeCNSPREEWRRW---RRWIVGYAVCMRLHKRLLF 267
Cdd:pfam13632  78 FLRRSALQEvGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVY---EKSPLTFRDFLrqrRRWAYGCLLILLIRLLGYL 154
                         170       180
                  ....*....|....*....|....*..
gi 740643789  268 SRFGIFSIFPMLLVVLYGVGIYLTTWF 294
Cdd:pfam13632 155 GTLLWSGLPLALLLLLLFSISSLALVL 181
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
35-119 2.13e-03

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: 38.90  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  35 IIPAYNEGPCLAQSLDNLLRNPYFCRVICVNDGSTDNTeAVMAEVKRKwGDRFVAVTQK----NTGKGGALMHGLkYATC 110
Cdd:cd06436    2 LVPCLNEEAVIQRTLASLLRNKPNFLVLVIDDASDDDT-AGIVRLAIT-DSRVHLLRRHlpnaRTGKGDALNAAY-DQIR 78

                 ....*....
gi 740643789 111 DQVFLSDAD 119
Cdd:cd06436   79 QILIEEGAD 87
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
34-234 4.63e-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: 4.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789  34 AIIPAYNegPCLAQSLDNLLRNPYFCRVICVNDGSTDNTEAVMAEVKRkwGDRFVAVTQKNTGKGGALMHGLKYAT---C 110
Cdd:cd02526    1 AVVVTYN--PDLSKLKELLAALAEQVDKVVVVDNSSGNDIELRLRLNS--EKIELIHLGENLGIAKALNIGIKAALengA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740643789 111 DQVFLSDADTFVPPDndgmgyMLAE-IERGADAVGGIPstalkgAGLL-PHIRATVKL----PMIVMKRTLQQFLGG--- 181
Cdd:cd02526   77 DYVLLFDQDSVPPPD------MVEKlLAYKILSDKNSN------IGAVgPRIIDRRTGenspGVRKSGYKLRIQKEGeeg 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740643789 182 ---APFIISGACgMFRTDVLRKFGFSDrtkvEDL-----DLTWTL--VANGYRIRQANRCIVY 234
Cdd:cd02526  145 lkeVDFLITSGS-LISLEALEKVGGFD----EDLfidyvDTEWCLraRSKGYKIYVVPDAVLK 202
 
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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