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Conserved domains on  [gi|1802059242|gb|QHP50913|]
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glycosyltransferase [Bifidobacterium breve]

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
PubMed:  9334165|16037492|12691742|10521532
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, ...
 4-261 2.73e-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: 129.48  E-value: 2.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQT--VMPYEVLVVDNRSTDDTCAIVERFIAEHPeaPVKLLHQNDEQGLIPTRNFGLN 81
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  82 AATGDVLGRFDADCMIRPDWVEVVSGIFtEDPGAMgatgpvmyydmpsrhfglrsdnslrkrmykadgdqplLFGSNMAL 161
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVG-------------------------------------ASGANLAF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242 162 RASAWyqiaNEVCRDKADVMHEDIDISLHLLGKDLKTVYSPRMIAAMSARrmdTSLSSFLN-YMRRFKNTFDAHPQHWRK 240
Cdd:COG1215   151 RREAL----EEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAP---ETLRALFRqRRRWARGGLQLLLKHRPL 223

                         250       260
                  ....*....|....*....|..
gi 1802059242 241 HKPESLFTAMYP-AMHLFYPVW 261
Cdd:COG1215   224 LRPRRLLLFLLLlLLPLLLLLL 245
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-261 2.73e-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: 129.48  E-value: 2.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQT--VMPYEVLVVDNRSTDDTCAIVERFIAEHPeaPVKLLHQNDEQGLIPTRNFGLN 81
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  82 AATGDVLGRFDADCMIRPDWVEVVSGIFtEDPGAMgatgpvmyydmpsrhfglrsdnslrkrmykadgdqplLFGSNMAL 161
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVG-------------------------------------ASGANLAF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242 162 RASAWyqiaNEVCRDKADVMHEDIDISLHLLGKDLKTVYSPRMIAAMSARrmdTSLSSFLN-YMRRFKNTFDAHPQHWRK 240
Cdd:COG1215   151 RREAL----EEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAP---ETLRALFRqRRRWARGGLQLLLKHRPL 223

                         250       260
                  ....*....|....*....|..
gi 1802059242 241 HKPESLFTAMYP-AMHLFYPVW 261
Cdd:COG1215   224 LRPRRLLLFLLLlLLPLLLLLL 245
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-121 1.53e-28

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 107.59  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPeaPVKLLHQNDEQGLIPTRNFGLNAATG 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDP--RVIRVINEENQGLAAARNAGLKAARG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1802059242  86 DVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGATGP 121
Cdd:cd00761    79 EYILFLDADDLLLPDWLERLVAELLADPEADAVGGP 114
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-165 1.58e-28

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: 107.87  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   5 SIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPeaPVKLLHQNDEQGLIPTRNFGLNAAT 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  85 GDVLGRFDADCMIRPDWVEVVSGIFtEDPGAMGATGPVMYYDMPSRHFGLRSDNSLRKRMYKADGDQ-----PLLFGSNM 159
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEAL-EEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLlglnlPFLIGGFA 157


                  ....*.
gi 1802059242 160 ALRASA 165
Cdd:pfam00535 158 LYRREA 163
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 4-212 5.34e-13

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: 66.77  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTvMPYEVLVVDNRSTDDTCAIVErfiaehpEAPVKLLHQndEQGliptR----NFG 79
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALR-GDAEVIVVDGGSTDGTVEIAR-------SLGAKVIHS--PKG----RarqmNAG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  80 LNAATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGAtgpvmyydmpsrhFGLRSDNSlrKRMYKadgdqplLFGSNM 159
Cdd:TIGR04283  67 AALAKGDILLFLHADTRLPKDFLEAIRRALAKPGYVAGA-------------FDLRFDGP--GLLLR-------LIEWGV 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242 160 ALRaSAWYQIANE-----VCRD---------KADVMhEDIDISlhllgKDLKTVYSPRMIAA---MSARR 212
Cdd:TIGR04283 125 NLR-SRLTGIPYGdqglfVRRSlfeqiggfpDIPLM-EDIELS-----RRLRRLGRLAILPApvvTSARR 187
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-100 5.43e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 65.45  E-value: 5.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHQnDEQGLIPTRNFGLNAA 83
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLLHQ-ANAGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1802059242  84 TGDVLGRFDADCMIRPD 100
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-102 6.74e-10

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 59.04  E-value: 6.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   2 LNVSIIIPAWNESERI---LDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEA-PVKLLHQnDEQGLIPTRN 77
Cdd:NF038302    1 LDFTVAIPTYNGANRLpevLERLRSQIGTESLSWEIIVVDNNSTDNTAQVVQEYQKNWPSPyPLRYCFE-PQQGAAFARQ 79

                          90       100
                  ....*....|....*....|....*
gi 1802059242  78 FGLNAATGDVLGRFDADCMIRPDWV 102
Cdd:NF038302   80 RAIQEAKGELIGFLDDDNLPAPNWV 104
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-261 2.73e-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: 129.48  E-value: 2.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQT--VMPYEVLVVDNRSTDDTCAIVERFIAEHPeaPVKLLHQNDEQGLIPTRNFGLN 81
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  82 AATGDVLGRFDADCMIRPDWVEVVSGIFtEDPGAMgatgpvmyydmpsrhfglrsdnslrkrmykadgdqplLFGSNMAL 161
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVG-------------------------------------ASGANLAF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242 162 RASAWyqiaNEVCRDKADVMHEDIDISLHLLGKDLKTVYSPRMIAAMSARrmdTSLSSFLN-YMRRFKNTFDAHPQHWRK 240
Cdd:COG1215   151 RREAL----EEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAP---ETLRALFRqRRRWARGGLQLLLKHRPL 223

                         250       260
                  ....*....|....*....|..
gi 1802059242 241 HKPESLFTAMYP-AMHLFYPVW 261
Cdd:COG1215   224 LRPRRLLLFLLLlLLPLLLLLL 245
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-121 1.53e-28

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


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 107.59  E-value: 1.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPeaPVKLLHQNDEQGLIPTRNFGLNAATG 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDP--RVIRVINEENQGLAAARNAGLKAARG 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1802059242  86 DVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGATGP 121
Cdd:cd00761    79 EYILFLDADDLLLPDWLERLVAELLADPEADAVGGP 114
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-165 1.58e-28

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: 107.87  E-value: 1.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   5 SIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPeaPVKLLHQNDEQGLIPTRNFGLNAAT 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  85 GDVLGRFDADCMIRPDWVEVVSGIFtEDPGAMGATGPVMYYDMPSRHFGLRSDNSLRKRMYKADGDQ-----PLLFGSNM 159
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEAL-EEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLlglnlPFLIGGFA 157


                  ....*.
gi 1802059242 160 ALRASA 165
Cdd:pfam00535 158 LYRREA 163
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-148 4.75e-28

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 107.48  E-value: 4.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   1 MLNVSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHQNDEQGLIPTRNFGL 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPR--IRVIRLERNRGKGAARNAGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  81 NAATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAM------GATGPVMYYDMPSRHFGLRS------DNSLRKRMYKAD 148
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLvygsrlIREGESDLRRLGSRLFNLVRlltnlpDSTSGFRLFRRE 158
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 6-165 2.53e-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: 94.22  E-value: 2.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEaPVKLLHQNDEQG----LiptrNFGLN 81
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIR-RVLVVRDKENGGkagaL----NAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  82 AATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGATGPVMYYDmpsRHFGL---------RSDNSLRKRMYKADGDQP 152
Cdd:cd06423    76 HAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRN---GSENLltrlqaieyLSIFRLGRRAQSALGGVL 152

                         170
                  ....*....|...
gi 1802059242 153 LLFGSNMALRASA 165
Cdd:cd06423   153 VLSGAFGAFRREA 165
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-103 1.72e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 92.75  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   1 MLNVSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFiaEHPEapVKLLHQNDEQGLIPTRNFGL 80
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPR--VRVIRNPENLGFAAARNLGL 77

                          90       100
                  ....*....|....*....|...
gi 1802059242  81 NAATGDVLGRFDADCMIRPDWVE 103
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLE 100
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 4-122 2.19e-17

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: 79.97  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNES---ERILDCLLNATRQTVmPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHqnDEQGLIPT-RNFG 79
Cdd:cd02525     2 VSIIIPVRNEEkyiEELLESLLNQSYPKD-LIEIIVVDGGSTDGTREIVQEYAAKDPR--IRLID--NPKRIQSAgLNIG 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1802059242  80 LNAATGDVLGRFDADCMIRPDWVEVVSGIFtEDPGAMGATGPV 122
Cdd:cd02525    77 IRNSRGDIIIRVDAHAVYPKDYILELVEAL-KRTGADNVGGPM 118
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-230 2.24e-17

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: 79.34  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEAPVKLLHQNDEQGliPT-----RNF 78
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLG--PTgksrgLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  79 GLNAATGDVLGRFDADCMIRPDWVEVVSGIFtEDPGAMGATGPVmYYDMPSR--------HFGLRSDNSLRKRmykADGD 150
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTPV-FSLNRSTmlsalgalEFALRHLRMMSLR---LALG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242 151 QPLLFGSNMALRASAWYQIANEvcrDKADVMHEDIDISLHLLGKDLKTVYSPRmIAAMSARRmdTSLSSFLNYMRRFKNT 230
Cdd:pfam13641 157 VLPLSGAGSAIRREVLKELGLF---DPFFLLGDDKSLGRRLRRHGWRVAYAPD-AAVRTVFP--TYLAASIKQRARWVYG 230
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 6-107 3.46e-16

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: 74.92  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCL--LNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHQNDEQGLIPTRNFGLNAA 83
Cdd:cd04179     1 VVIPAYNEEENIPELVerLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPR--VRVIRLSRNFGKGAAVRAGFKAA 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1802059242  84 TGDVLGRFDADC---------MIRPDW---VEVVSG 107
Cdd:cd04179    79 RGDIVVTMDADLqhppedipkLLEKLLeggADVVIG 114
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 4-212 3.12e-15

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: 73.37  E-value: 3.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERfiaehpeAPVKLLHQNdeqgliPTR----NFG 79
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARS-------AGVVVISSP------KGRarqmNAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  80 LNAATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGA-----TGPVMYYDMPSRHFGLRSDnsLRKRMYkadGDQPLL 154
Cdd:cd02522    68 AAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAfrlrfDDPGPRLRLLELGANLRSR--LFGLPY---GDQGLF 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802059242 155 FgsnmalRASAWYQIA--NEVcrdkaDVMhEDIDISlhllgKDLKTVYSPRMI---AAMSARR 212
Cdd:cd02522   143 I------RRELFEELGgfPEL-----PLM-EDVELV-----RRLRRRGRPALLpspVTTSARR 188
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-125 4.46e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 73.09  E-value: 4.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCLlNATRQTVMP---YEVLVVDNRSTDDTCAIVErFIAEHPEAPVKLLhQNDEQGLIPTRN---FG 79
Cdd:cd04192     1 VVIAARNEAENLPRLL-QSLSALDYPkekFEVILVDDHSTDGTVQILE-FAAAKPNFQLKIL-NNSRVSISGKKNaltTA 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1802059242  80 LNAATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGAtGPVMYY 125
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVA-GPVIYF 122
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 6-103 4.11e-14

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: 69.14  E-value: 4.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFiAEHPEAPVKLLHQNDEqG--LIPTRNFGLNAA 83
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEF-KSQFPIPIKHVWQEDE-GfrKAKIRNKAIAAA 78

                          90       100
                  ....*....|....*....|
gi 1802059242  84 TGDVLGRFDADCMIRPDWVE 103
Cdd:cd06420    79 KGDYLIFIDGDCIPHPDFIA 98
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 4-212 5.34e-13

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: 66.77  E-value: 5.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTvMPYEVLVVDNRSTDDTCAIVErfiaehpEAPVKLLHQndEQGliptR----NFG 79
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALR-GDAEVIVVDGGSTDGTVEIAR-------SLGAKVIHS--PKG----RarqmNAG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  80 LNAATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGAtgpvmyydmpsrhFGLRSDNSlrKRMYKadgdqplLFGSNM 159
Cdd:TIGR04283  67 AALAKGDILLFLHADTRLPKDFLEAIRRALAKPGYVAGA-------------FDLRFDGP--GLLLR-------LIEWGV 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242 160 ALRaSAWYQIANE-----VCRD---------KADVMhEDIDISlhllgKDLKTVYSPRMIAA---MSARR 212
Cdd:TIGR04283 125 NLR-SRLTGIPYGdqglfVRRSlfeqiggfpDIPLM-EDIELS-----RRLRRLGRLAILPApvvTSARR 187
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-141 4.30e-12

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: 64.62  E-value: 4.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   3 NVSIIIPAWNESERILDCLlnatrQTVMPY--EVLVVDNRSTDDTCAIVERFIAEhpeapvklLHQNDEQGLIPTRNFGL 80
Cdd:cd02511     1 TLSVVIITKNEERNIERCL-----ESVKWAvdEIIVVDSGSTDRTVEIAKEYGAK--------VYQRWWDGFGAQRNFAL 67

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802059242  81 NAATGD-VLgRFDADCMIRPDWVEVVSGIFTEDPGAmGATGPV--MYYDMPSRHFGLRSDNSLR 141
Cdd:cd02511    68 ELATNDwVL-SLDADERLTPELADEILALLATDDYD-GYYVPRrnFFLGRWIRHGGWYPDRQLR 129
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-100 5.43e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 65.45  E-value: 5.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHQnDEQGLIPTRNFGLNAA 83
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPH--VRLLHQ-ANAGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1802059242  84 TGDVLGRFDADCMIRPD 100
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 4-100 8.16e-12

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: 64.14  E-value: 8.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTvmpY-----EVLVVDNRSTDDTCAIVERFIAEhpeaPVKLLHQNDEQGLIPTRNF 78
Cdd:cd06439    31 VTIIIPAYNEEAVIEAKLENLLALD---YprdrlEIIVVSDGSTDGTAEIAREYADK----GVKLLRFPERRGKAAALNR 103

                          90       100
                  ....*....|....*....|..
gi 1802059242  79 GLNAATGDVLGRFDADCMIRPD 100
Cdd:cd06439   104 ALALATGEIVVFTDANALLDPD 125
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 6-94 1.52e-11

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: 62.58  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERIlDCLLNATRQTVM-----PYEVLVVDNRSTDDTCAIVERFIAEHPeAPVKLLHQNDEQGliptRNFGL 80
Cdd:cd04188     1 VVIPAYNEEKRL-PPTLEEAVEYLEerpsfSYEIIVVDDGSKDGTAEVARKLARKNP-ALIRVLTLPKNRG----KGGAV 74

                          90
                  ....*....|....*...
gi 1802059242  81 N----AATGDVLGRFDAD 94
Cdd:cd04188    75 RagmlAARGDYILFADAD 92
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-121 2.01e-10

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 58.34  E-value: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEhpeapVKLLHQNDEQGLIPTRNFGLNAATG 85
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE-----VRLIRNGENLGFGAGNNQGIREAKG 75

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1802059242  86 DVLGRFDADCMIRPDWVEVVSGIFTEDPGAmGATGP 121
Cdd:cd04186    76 DYVLLLNPDTVVEPGALLELLDAAEQDPDV-GIVGP 110
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 6-94 2.10e-10

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: 59.47  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESE-------RILDCLLNAtrqtvmPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHQNDEQGLIPTRNF 78
Cdd:cd06442     1 IIIPTYNEREnipelieRLDAALKGI------DYEIIVVDDNSPDGTAEIVRELAKEYPR--VRLIVRPGKRGLGSAYIE 72

                          90
                  ....*....|....*.
gi 1802059242  79 GLNAATGDVLGRFDAD 94
Cdd:cd06442    73 GFKAARGDVIVVMDAD 88
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-102 6.74e-10

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 59.04  E-value: 6.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   2 LNVSIIIPAWNESERI---LDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEA-PVKLLHQnDEQGLIPTRN 77
Cdd:NF038302    1 LDFTVAIPTYNGANRLpevLERLRSQIGTESLSWEIIVVDNNSTDNTAQVVQEYQKNWPSPyPLRYCFE-PQQGAAFARQ 79

                          90       100
                  ....*....|....*....|....*
gi 1802059242  78 FGLNAATGDVLGRFDADCMIRPDWV 102
Cdd:NF038302   80 RAIQEAKGELIGFLDDDNLPAPNWV 104
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 6-94 1.24e-09

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: 56.72  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDC---LLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHqndeqgLipTRNFG--- 79
Cdd:cd04187     1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPR--VKVIR------L--SRNFGqqa 70

                          90       100
                  ....*....|....*....|
gi 1802059242  80 -----LNAATGDVLGRFDAD 94
Cdd:cd04187    71 allagLDHARGDAVITMDAD 90
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 18-86 2.65e-08

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: 53.40  E-value: 2.65e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802059242  18 LDCLLNatrQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEapvKLLHQNDEQGLIPTRNF--GLNAATGD 86
Cdd:cd04196    17 LDSILA---QTYKNDELIISDDGSTDGTVEIIKEYIDKDPF---IIILIRNGKNLGVARNFesLLQAADGD 81
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-94 1.42e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 51.62  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   1 MLNVSIIIPAWNESERI--LDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEAPVKLLHQNDEQGLIPTRNF 78
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIalIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAYIH 87

                          90
                  ....*....|....*.
gi 1802059242  79 GLNAATGDVLGRFDAD 94
Cdd:PLN02726   88 GLKHASGDFVVIMDAD 103
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-150 3.35e-07

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 50.74  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   5 SIIIPAWNESER--ILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEapVKLLHQNDEQ-GLIPTRNFGLN 81
Cdd:pfam10111   1 SVVIPVYNGEKThwIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQ--VYYPNAPDTTySLAASRNRGTS 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  82 AATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGATGPVMYydmPSRHFGLRSDNSLRKRMYK-ADGD 150
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFEKQLKIATSLALQENIQAAVVL---PVTDLNDESSNFLRRGGDLtASGD 145
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 5-115 3.57e-07

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: 49.62  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   5 SIIIPAW-NES-ERILDCLLNATRQTVMPYE-VLVVDNRSTDDTCAIVERFIAEHPEAPVKLlHQNdeQGLIPTRNFGLN 81
Cdd:cd04195     1 SVLMSVYiKEKpEFLREALESILKQTLPPDEvVLVKDGPVTQSLNEVLEEFKRKLPLKVVPL-EKN--RGLGKALNEGLK 77

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1802059242  82 AATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGA 115
Cdd:cd04195    78 HCTYDWVARMDTDDISLPDRFEKQLDFIEKNPEI 111
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 5-103 1.49e-06

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: 48.74  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   5 SIIIPAWNESE----RILDCLLNATRqtvmPY---EVLVVDNRSTDDTCAIVERFIAEHPEAPVKLLHQNDEQGLIPTRN 77
Cdd:cd02510     1 SVIIIFHNEALstllRTVHSVINRTP----PEllkEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARI 76

                          90       100
                  ....*....|....*....|....*.
gi 1802059242  78 FGLNAATGDVLGRFDADCMIRPDWVE 103
Cdd:cd02510    77 AGARAATGDVLVFLDSHCEVNVGWLE 102
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 3-94 1.90e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 48.58  E-value: 1.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   3 NVSIIIPAWNESE---RILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERfIAEHPEAPVKLLHQNDEQGLIPTRNFG 79
Cdd:PRK10714    7 KVSVVIPVYNEQEslpELIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPDSHIVAILLNRNYGQHSAIMAG 85

                          90
                  ....*....|....*
gi 1802059242  80 LNAATGDVLGRFDAD 94
Cdd:PRK10714   86 FSHVTGDLIITLDAD 100
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 5-144 2.34e-06

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


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 47.78  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   5 SIIIPAWNESERILDCLLNATRQTVMP-YEVLVVDNRSTDDTC-AIVERFIAEHPEApVKLLHQNDEQGLIP-TRNFGLN 81
Cdd:cd06435     1 SIHVPCYEEPPEMVKETLDSLAALDYPnFEVIVIDNNTKDEALwKPVEAHCAQLGER-FRFFHVEPLPGAKAgALNYALE 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1802059242  82 AATGD--VLGRFDADCMIRPDWVEVVSGIFtEDPGAMGATGPVMYYDmpsrhfglrSDNSLRKRM 144
Cdd:cd06435    80 RTAPDaeIIAVIDADYQVEPDWLKRLVPIF-DDPRVGFVQAPQDYRD---------GEESLFKRM 134
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 6-124 7.08e-06

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: 45.84  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNES---ERILDCLLNATRQTVmpyeVLVVDNRSTDDTCAIVErfIAEHPEApVKLLHQ---NDEQGliptRNFG 79
Cdd:cd06436     1 VLVPCLNEEaviQRTLASLLRNKPNFL----VLVIDDASDDDTAGIVR--LAITDSR-VHLLRRhlpNARTG----KGDA 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1802059242  80 LNAATG--------------DVL-GRFDADCMIRPDWVEVVSGIFtEDPGAMGATGPV-MY 124
Cdd:cd06436    70 LNAAYDqirqilieegadpeRVIiAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVrMY 129
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 5-145 7.33e-06

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: 46.00  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   5 SIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIverfIAEHPEAPVKLLHQNDeQGL---IptrNFGLN 81
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDI----IKKYEDKITYWISEPD-KGIydaM---NKGIA 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802059242  82 AATGDVLGRFDADCMIRPDWVEVVSGIFTEDPGAMGATGPVMYYD-----MPSRHFGLRSDNSLRKRMY 145
Cdd:cd06433    73 LATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDengrvIGRRRPPPFLDKFLLYGMP 141
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 2-94 8.27e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 46.68  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   2 LNVSIIIPAWNESERILDCLLNA--------TRQTVMPYEVLVVDNRSTDDTCAIVERFIAEH--PEAPVKLLHQNDEQG 71
Cdd:PTZ00260   70 VDLSIVIPAYNEEDRLPKMLKETikylesrsRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNinPNIDIRLLSLLRNKG 149

                          90       100
                  ....*....|....*....|...
gi 1802059242  72 LIPTRNFGLNAATGDVLGRFDAD 94
Cdd:PTZ00260  150 KGGAVRIGMLASRGKYILMVDAD 172
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-133 9.58e-06

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 46.45  E-value: 9.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   1 MLNVSIIIPAWNESERILDcLLNATRQTVM---PYEVLVVDNRSTDDTCAIVERFIAEhpeapvkLLHQNDEQGLIPTRN 77
Cdd:PRK13915   30 GRTVSVVLPALNEEETVGK-VVDSIRPLLMeplVDELIVIDSGSTDATAERAAAAGAR-------VVSREEILPELPPRP 101

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802059242  78 -------FGLNAATGDVLGRFDADCM-IRPDWVEVVSGIFTEDPGAMGATGpvmYYDMPSRHFG 133
Cdd:PRK13915  102 gkgealwRSLAATTGDIVVFVDADLInFDPMFVPGLLGPLLTDPGVHLVKA---FYRRPLRVSG 162
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 4-222 6.12e-05

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: 43.33  E-value: 6.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNES-ERILDCLLNATRQTV--MPYEVLVVDnrstDDTCAIVERFIAEH-PEAPVKLLHQNDEQG-----Lip 74
Cdd:cd06421     3 VDVFIPTYNEPlEIVRKTLRAALAIDYphDKLRVYVLD----DGRRPELRALAAELgVEYGYRYLTRPDNRHakagnL-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  75 trNFGLNAATGDVLGRFDADCMIRPDWVEVVSGIFTEDPgAMG-ATGPVMYYDMPSRHFGLRSDNSLRKRMY------KA 147
Cdd:cd06421    77 --NNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDP-KVAlVQTPQFFYNPDPFDWLADGAPNEQELFYgviqpgRD 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1802059242 148 DGDQPLLFGSNMALRASAWYQIAN----EVCrdkadvmhEDIDISLHLLGKDLKTVYSPRMIAAMSARrmdTSLSSFLN 222
Cdd:cd06421   154 RWGAAFCCGSGAVVRREALDEIGGfptdSVT--------EDLATSLRLHAKGWRSVYVPEPLAAGLAP---ETLAAYIK 221
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 4-115 1.31e-04

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: 42.19  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTVMPY-EVLVVDNRSTDDTCAIVERFIAEHpEAPVKLLHQNDEQGLIPTRNFGLNA 82
Cdd:cd04184     3 ISIVMPVYNTPEKYLREAIESVRAQTYPNwELCIADDASTDPEVKRVLKKYAAQ-DPRIKVVFREENGGISAATNSALEL 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1802059242  83 ATGDVLGRFDADCMIRPDWV-EVVSgIFTEDPGA 115
Cdd:cd04184    82 ATGEFVALLDHDDELAPHALyEVVK-ALNEHPDA 114
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 4-125 1.91e-04

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 41.81  E-value: 1.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTDDTCAIVERFIAEHPEAPVKLLHQNDEQGLIPTRNF---GL 80
Cdd:cd02520     3 VSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNlikGY 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1802059242  81 NAATGDVLGRFDADCMIRPDWV-EVVSGIFTEDPG---AMGATGPVMYY 125
Cdd:cd02520    83 EEARYDILVISDSDISVPPDYLrRMVAPLMDPGVGlvtCLCAFGKSMAL 131
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-94 1.53e-03

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 39.59  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESERILDCLLNATRQTVMPYEVLVVDNRSTddTCAIVERFIAEHPEAPVKLLHQNDEQGLIPTRNFGLNAA 83
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTALNDPRITYIHNDINSGACAVRNQAIMLA 84

                          90
                  ....*....|.
gi 1802059242  84 TGDVLGRFDAD 94
Cdd:PRK10018   85 QGEYITGIDDD 95
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 15-66 2.02e-03

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: 38.77  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1802059242  15 ERILDCLLNatrQTVMPYEVLVVDNRSTDDTCAIVERFiaeHPEAPVKLLHQ 66
Cdd:cd04185    13 KECLDALLA---QTRPPDHIIVIDNASTDGTAEWLTSL---GDLDNIVYLRL 58
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 4-101 2.95e-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: 38.45  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   4 VSIIIPAWNESErILDCLLNATRQTVMP---YEVLVVDNrSTDDTCAIVERFIAEHPEA--PVKLLHQNDEQGliptrnF 78
Cdd:cd06437     3 VTVQLPVFNEKY-VVERLIEAACALDYPkdrLEIQVLDD-STDETVRLAREIVEEYAAQgvNIKHVRRADRTG------Y 74

                          90       100       110
                  ....*....|....*....|....*....|
gi 1802059242  79 -------GLNAATGDVLGRFDADCMIRPDW 101
Cdd:cd06437    75 kagalaeGMKVAKGEYVAIFDADFVPPPDF 104
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 6-164 7.12e-03

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: 36.81  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242   6 IIIPAWNESERILDCLLNATRQTVMP--YEVLVV-DNrSTDDTCAIVERFIAEHPEapvkllHQNDEQgliPTRNFGLN- 81
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPRelYRIFVVaDN-CTDDTAQVARAAGATVLE------RHDPER---RGKGYALDf 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802059242  82 --------AATGDVLGRFDADCMIRPDWVEVVSGIFTEdpGAMGATGpvmYYDM--P-------SRHFGLRSDNSLRKRM 144
Cdd:cd06438    71 gfrhllnlADDPDAVVVFDADNLVDPNALEELNARFAA--GARVVQA---YYNSknPddswitrLYAFAFLVFNRLRPLG 145

                         170       180
                  ....*....|....*....|
gi 1802059242 145 YKADGDQPLLFGSNMALRAS 164
Cdd:cd06438   146 RSNLGLSCQLGGTGMCFPWA 165
 
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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