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Conserved domains on  [gi|1249615387|dbj|BBA55699|]
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glycosyltransferase [Bifidobacterium bifidum]

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, ...
 4-260 5.39e-38

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: 136.41  E-value: 5.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPH--EVIVVNNRSTDRTCDIVEQFQRDHPeaPVILLQQNEDQGLIPTRNFGLN 81
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYPKEklEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  82 AATGDVLGRIDADCMLKPDWVEVVSGIFtEDPDamgatgpvvyydmpakgaglagddhirrhtyradndqVLLFGSNMAI 161
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPG-------------------------------------VGASGANLAF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387 162 RASAWHAISGEvcrdPEDVMHEDIDVSLHLLNHGFKTVYSQCMICgisARRMDTSFASFHRymQRFKNTFAAHPDHWREH 241
Cdd:COG1215   151 RREALEEVGGF----DEDTLGEDLDLSLRLLRAGYRIVYVPDAVV---YEEAPETLRALFR--QRRRWARGGLQLLLKHR 221

                         250
                  ....*....|....*....
gi 1249615387 242 HTERRLYALYPWLHMLYPI 260
Cdd:COG1215   222 PLLRPRRLLLFLLLLLLPL 240
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-260 5.39e-38

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: 136.41  E-value: 5.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPH--EVIVVNNRSTDRTCDIVEQFQRDHPeaPVILLQQNEDQGLIPTRNFGLN 81
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYPKEklEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  82 AATGDVLGRIDADCMLKPDWVEVVSGIFtEDPDamgatgpvvyydmpakgaglagddhirrhtyradndqVLLFGSNMAI 161
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPG-------------------------------------VGASGANLAF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387 162 RASAWHAISGEvcrdPEDVMHEDIDVSLHLLNHGFKTVYSQCMICgisARRMDTSFASFHRymQRFKNTFAAHPDHWREH 241
Cdd:COG1215   151 RREALEEVGGF----DEDTLGEDLDLSLRLLRAGYRIVYVPDAVV---YEEAPETLRALFR--QRRRWARGGLQLLLKHR 221

                         250
                  ....*....|....*....
gi 1249615387 242 HTERRLYALYPWLHMLYPI 260
Cdd:COG1215   222 PLLRPRRLLLFLLLLLLPL 240
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-124 1.05e-29

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: 110.29  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPeaPVILLQQNEDQGLIPTRNFGLNAATG 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDP--RVIRVINEENQGLAAARNAGLKAARG 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1249615387  86 DVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGATGPVVY 124
Cdd:cd00761    79 EYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL 117
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-165 1.28e-24

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: 97.08  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   5 SIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPeaPVILLQQNEDQGLIPTRNFGLNAAT 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  85 GDVLGRIDADCMLKPDWVEVVSGIFTEDPDAmGATGPVVYYDMPAKGAGLAGDDHIRRHTYRADNDQVL-----LFGSNM 159
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGAD-VVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGlnlpfLIGGFA 157


                  ....*.
gi 1249615387 160 AIRASA 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 1.28e-14

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: 71.39  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTvAPHEVIVVNNRSTDRTCDIVEQFqrdhpEAPVILLQQNedqgliptR----NFG 79
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALR-GDAEVIVVDGGSTDGTVEIARSL-----GAKVIHSPKG--------RarqmNAG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  80 LNAATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGatgpvvYYDMpakgaGLAGDDHIRRHTYRADN---------- 149
Cdd:TIGR04283  67 AALAKGDILLFLHADTRLPKDFLEAIRRALAKPGYVAG------AFDL-----RFDGPGLLLRLIEWGVNlrsrltgipy 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1249615387 150 -DQVLLfgsnmaIRASAWHAISGevcRDPEDVMhEDIDVSLHLLNHGFKTVYSQCMIcgISARR 212
Cdd:TIGR04283 136 gDQGLF------VRRSLFEQIGG---FPDIPLM-EDIELSRRLRRLGRLAILPAPVV--TSARR 187
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-100 5.34e-14

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 71.23  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVIlLQQNedQGLIPTRNFGLNAA 83
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL-HQAN--AGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1249615387  84 TGDVLGRIDADCMLKPD 100
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-102 4.59e-09

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 56.34  E-value: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   2 LNVSIIIPAWNEEERIA---DCLMNatrQTVAPH---EVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNEDQGLIPT 75
Cdd:NF038302    1 LDFTVAIPTYNGANRLPevlERLRS---QIGTESlswEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLRYCFEPQQGAAFA 77

                          90       100
                  ....*....|....*....|....*..
gi 1249615387  76 RNFGLNAATGDVLGRIDADCMLKPDWV 102
Cdd:NF038302   78 RQRAIQEAKGELIGFLDDDNLPAPNWV 104
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 4-260 5.39e-38

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: 136.41  E-value: 5.39e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPH--EVIVVNNRSTDRTCDIVEQFQRDHPeaPVILLQQNEDQGLIPTRNFGLN 81
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYPKEklEVIVVDDGSTDETAEIARELAAEYP--RVRVIERPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  82 AATGDVLGRIDADCMLKPDWVEVVSGIFtEDPDamgatgpvvyydmpakgaglagddhirrhtyradndqVLLFGSNMAI 161
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPG-------------------------------------VGASGANLAF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387 162 RASAWHAISGEvcrdPEDVMHEDIDVSLHLLNHGFKTVYSQCMICgisARRMDTSFASFHRymQRFKNTFAAHPDHWREH 241
Cdd:COG1215   151 RREALEEVGGF----DEDTLGEDLDLSLRLLRAGYRIVYVPDAVV---YEEAPETLRALFR--QRRRWARGGLQLLLKHR 221

                         250
                  ....*....|....*....
gi 1249615387 242 HTERRLYALYPWLHMLYPI 260
Cdd:COG1215   222 PLLRPRRLLLFLLLLLLPL 240
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-200 1.45e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 116.73  E-value: 1.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   1 MLNVSIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNedQGLIPTRNFGL 80
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERN--RGKGAARNAGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  81 NAATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMgatgpvVYYDMPAKGaglaGDDHIRRHTYRADNDQVLLF----- 155
Cdd:COG0463    79 AAARGDYIAFLDADDQLDPEKLEELVAALEEGPADL------VYGSRLIRE----GESDLRRLGSRLFNLVRLLTnlpds 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1249615387 156 -GSNMAIRASAWHAIsgevcrDPEDVMHEDIDVsLHLLNHGFKTVY 200
Cdd:COG0463   149 tSGFRLFRREVLEEL------GFDEGFLEDTEL-LRALRHGFRIAE 187
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-124 1.05e-29

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: 110.29  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPeaPVILLQQNEDQGLIPTRNFGLNAATG 85
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDP--RVIRVINEENQGLAAARNAGLKAARG 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1249615387  86 DVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGATGPVVY 124
Cdd:cd00761    79 EYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL 117
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-200 7.30e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 98.91  E-value: 7.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   1 MLNVSIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHpeapVILLQQNEDQGLIPTRNFGL 80
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPR----VRVIRNPENLGFAAARNLGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  81 NAATGDVLGRIDADCMLKPDWVEvvsgiftedpdamgatgpvvyydmpakgaglagddhirrhtyradndqVLLFGSNMA 160
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLE------------------------------------------------RLLAAACLL 109

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1249615387 161 IRASAWHAISGevcRDPE-DVMHEDIDVSLHLLNHGFKTVY 200
Cdd:COG1216   110 IRREVFEEVGG---FDERfFLYGEDVDLCLRLRKAGYRIVY 147
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-165 1.28e-24

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: 97.08  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   5 SIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPeaPVILLQQNEDQGLIPTRNFGLNAAT 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDP--RVRVIRLPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  85 GDVLGRIDADCMLKPDWVEVVSGIFTEDPDAmGATGPVVYYDMPAKGAGLAGDDHIRRHTYRADNDQVL-----LFGSNM 159
Cdd:pfam00535  79 GDYIAFLDADDEVPPDWLEKLVEALEEDGAD-VVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGlnlpfLIGGFA 157


                  ....*.
gi 1249615387 160 AIRASA 165
Cdd:pfam00535 158 LYRREA 163
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 6-171 3.43e-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: 93.83  E-value: 3.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEaPVILLQQNEDQG----LiptrNFGLN 81
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIR-RVLVVRDKENGGkagaL----NAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  82 AATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGATGPVVYYD----MPAKGAGL--AGDDHIRRHTYRADNDQVLLF 155
Cdd:cd06423    76 HAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNgsenLLTRLQAIeyLSIFRLGRRAQSALGGVLVLS 155

                         170
                  ....*....|....*.
gi 1249615387 156 GSNMAIRASAWHAISG 171
Cdd:cd06423   156 GAFGAFRREALREVGG 171
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-201 7.36e-22

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: 91.66  E-value: 7.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNEDQGliPT-----RNF 78
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLG--PTgksrgLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  79 GLNAATGDVLGRIDADCMLKPDWVEVVSGIFtEDPDAMGATGPVVYYDMPAKGAGLAGDDHIRRHTYRADNDQVL----L 154
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRLALgvlpL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1249615387 155 FGSNMAIRASAWHAISGEvcrDPEDVMHEDIDVSLHLLNHGFKTVYS 201
Cdd:pfam13641 161 SGAGSAIRREVLKELGLF---DPFFLLGDDKSLGRRLRRHGWRVAYA 204
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 4-195 1.15e-18

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 82.62  E-value: 1.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQfqrdhpeAPVILLQQNedqgliPTR----NFG 79
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARS-------AGVVVISSP------KGRarqmNAG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  80 LNAATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGA-----TGPVVYYDMPAKGAGLAGddHIRRHTYradNDQVLL 154
Cdd:cd02522    68 AAAARGDWLLFLHADTRLPPDWDAAIIETLRADGAVAGAfrlrfDDPGPRLRLLELGANLRS--RLFGLPY---GDQGLF 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1249615387 155 fgsnmaIRASAWHAISGevcRDPEDVMhEDIDVSLHLLNHG 195
Cdd:cd02522   143 ------IRRELFEELGG---FPELPLM-EDVELVRRLRRRG 173
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 6-107 2.48e-17

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: 78.00  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCL--MNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNedQGLIPTRNFGLNAA 83
Cdd:cd04179     1 VVIPAYNEEENIPELVerLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRN--FGKGAAVRAGFKAA 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1249615387  84 TGDVLGRIDADC---------MLKPDW---VEVVSG 107
Cdd:cd04179    79 RGDIVVTMDADLqhppedipkLLEKLLeggADVVIG 114
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 4-260 4.32e-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: 78.81  E-value: 4.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTV--APHEVIVVNNRSTDRTCDIVEQFQrdhPEAPVILLQQNEDQGLIPTRNFGLN 81
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYA---AKDPRIRLIDNPKRIQSAGLNIGIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  82 AATGDVLGRIDADCMLKPDWV-EVVSGIFTEDPDAMGATGPVVYYDMPAKGAGLAGDDH----IRRHTYRADNDQVLLFG 156
Cdd:cd02525    79 NSRGDIIIRVDAHAVYPKDYIlELVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSPlgsgGSAYRGGAVKIGYVDTV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387 157 SNMAIRASAWHAISGevcRDPEDVMHEDIDVSLHLLNHGFKTVYSQCMICGISARrmdTSFASFHRymQRFKNTFaahpd 236
Cdd:cd02525   159 HHGAYRREVFEKVGG---FDESLVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPR---STLKKLAR--QYFRYGK----- 225

                         250       260
                  ....*....|....*....|....
gi 1249615387 237 hWReHHTERRLYALYPWLHMLYPI 260
Cdd:cd02525   226 -WR-ARTLRKHRKSLSLRHLLPLA 247
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-125 3.86e-16

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: 75.79  E-value: 3.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLmNATRQTVAPH---EVIVVNNRSTDRTCDIVEqFQRDHPEAPVILLQQneDQGLIPTRNFGLN- 81
Cdd:cd04192     1 VVIAARNEAENLPRLL-QSLSALDYPKekfEVILVDDHSTDGTVQILE-FAAAKPNFQLKILNN--SRVSISGKKNALTt 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1249615387  82 ---AATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGAtGPVVYY 125
Cdd:cd04192    77 aikAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVA-GPVIYF 122
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 4-200 6.10e-16

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: 75.70  E-value: 6.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTvAPH---EVIVVNNRSTDRTCDIVeqfqRDHPEAPVILLQQNEDQGLIPTRNFGL 80
Cdd:cd06439    31 VTIIIPAYNEEAVIEAKLENLLALD-YPRdrlEIIVVSDGSTDGTAEIA----REYADKGVKLLRFPERRGKAAALNRAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  81 NAATGDVLGRIDADCMLKPDWVEVVSGIFTeDPDAMGATGPVVYYDmpaKGAGLAGDDH-------IRRHTYRADNdqVL 153
Cdd:cd06439   106 ALATGEIVVFTDANALLDPDALRLLVRHFA-DPSVGAVSGELVIVD---GGGSGSGEGLywkyenwLKRAESRLGS--TV 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1249615387 154 LF-GSNMAIRASAWHAIsgevcrdPEDVMHEDIDVSLHLLNHGFKTVY 200
Cdd:cd06439   180 GAnGAIYAIRRELFRPL-------PADTINDDFVLPLRIARQGYRVVY 220
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 6-103 1.60e-15

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: 73.00  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPeAPVILLQQnEDQG--LIPTRNFGLNAA 83
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFP-IPIKHVWQ-EDEGfrKAKIRNKAIAAA 78

                          90       100
                  ....*....|....*....|
gi 1249615387  84 TGDVLGRIDADCMLKPDWVE 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 1.28e-14

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: 71.39  E-value: 1.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTvAPHEVIVVNNRSTDRTCDIVEQFqrdhpEAPVILLQQNedqgliptR----NFG 79
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALR-GDAEVIVVDGGSTDGTVEIARSL-----GAKVIHSPKG--------RarqmNAG 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  80 LNAATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGatgpvvYYDMpakgaGLAGDDHIRRHTYRADN---------- 149
Cdd:TIGR04283  67 AALAKGDILLFLHADTRLPKDFLEAIRRALAKPGYVAG------AFDL-----RFDGPGLLLRLIEWGVNlrsrltgipy 135

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1249615387 150 -DQVLLfgsnmaIRASAWHAISGevcRDPEDVMhEDIDVSLHLLNHGFKTVYSQCMIcgISARR 212
Cdd:TIGR04283 136 gDQGLF------VRRSLFEQIGG---FPDIPLM-EDIELSRRLRRLGRLAILPAPVV--TSARR 187
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 6-169 4.47e-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: 69.52  E-value: 4.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIaDCLMNATRQTVA-----PHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVIL-LQQNEDQGLIPTRnfG 79
Cdd:cd04188     1 VVIPAYNEEKRL-PPTLEEAVEYLEerpsfSYEIIVVDDGSKDGTAEVARKLARKNPALIRVLtLPKNRGKGGAVRA--G 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  80 LNAATGDVLGRIDADCMLKP-DWVEVVSGIFTEDPDAmgATGpvvyydmpaKGAGLAGDDHIRRHTYRadndQVLLFGSN 158
Cdd:cd04188    78 MLAARGDYILFADADLATPFeELEKLEEALKTSGYDI--AIG---------SRAHLASAAVVKRSWLR----NLLGRGFN 142

                         170
                  ....*....|.
gi 1249615387 159 MAIRASAWHAI 169
Cdd:cd04188   143 FLVRLLLGLGI 153
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 4-100 5.34e-14

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 71.23  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVIlLQQNedQGLIPTRNFGLNAA 83
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLL-HQAN--AGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1249615387  84 TGDVLGRIDADCMLKPD 100
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-200 4.92e-13

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 65.66  E-value: 4.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDhpeapVILLQQNEDQGLIPTRNFGLNAATG 85
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPE-----VRLIRNGENLGFGAGNNQGIREAKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  86 DVLGRIDADCMLKPDWVEVVSGIFTEDPDAmGATGPvvyydmpakgaglagddhirrhtyradndqvLLFGSNMAIRASA 165
Cdd:cd04186    76 DYVLLLNPDTVVEPGALLELLDAAEQDPDV-GIVGP-------------------------------KVSGAFLLVRREV 123

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1249615387 166 WHAISGevcRDPEDVM-HEDIDVSLHLLNHGFKTVY 200
Cdd:cd04186   124 FEEVGG---FDEDFFLyYEDVDLCLRARLAGYRVLY 156
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-94 7.76e-13

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: 66.54  E-value: 7.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   3 NVSIIIPAWNEEERIADCLmnatrQTVAPH--EVIVVNNRSTDRTCDIVEQFQrdhpeAPVIllqQNEDQGLIPTRNFGL 80
Cdd:cd02511     1 TLSVVIITKNEERNIERCL-----ESVKWAvdEIIVVDSGSTDRTVEIAKEYG-----AKVY---QRWWDGFGAQRNFAL 67

                          90
                  ....*....|....*
gi 1249615387  81 NAATGD-VLgRIDAD 94
Cdd:cd02511    68 ELATNDwVL-SLDAD 81
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 6-94 3.03e-12

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: 64.04  E-value: 3.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADC---LMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLqqnedqglipTRNFG--- 79
Cdd:cd04187     1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRL----------SRNFGqqa 70

                          90       100
                  ....*....|....*....|
gi 1249615387  80 -----LNAATGDVLGRIDAD 94
Cdd:cd04187    71 allagLDHARGDAVITMDAD 90
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-154 4.24e-11

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 61.64  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   1 MLNVSIIIPAWNEEERIADC--LMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNEDQGLIPTRNF 78
Cdd:PLN02726    8 AMKYSIIVPTYNERLNIALIvyLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKLGLGTAYIH 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1249615387  79 GLNAATGDVLGRIDADCMLKPDWV-EVVSGIFTEDPDAMGATGPVvyydmpaKGAGLAGDDHIRRHTYRADN--DQVLL 154
Cdd:PLN02726   88 GLKHASGDFVVIMDADLSHHPKYLpSFIKKQRETGADIVTGTRYV-------KGGGVHGWDLRRKLTSRGANvlAQTLL 159
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 5-168 1.22e-09

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


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 56.78  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   5 SIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHpeapvILLQQNEDQGL---IptrNFGLN 81
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKI-----TYWISEPDKGIydaM---NKGIA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  82 AATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGATGPVVYYDmpakgaglAGDDHIRRHTYRADNDQVLLFGSNMAI 161
Cdd:cd06433    73 LATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVD--------ENGRVIGRRRPPPFLDKFLLYGMPICH 144


                  ....*..
gi 1249615387 162 RASAWHA 168
Cdd:cd06433   145 QATFFRR 151
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
2-102 4.59e-09

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 56.34  E-value: 4.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   2 LNVSIIIPAWNEEERIA---DCLMNatrQTVAPH---EVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNEDQGLIPT 75
Cdd:NF038302    1 LDFTVAIPTYNGANRLPevlERLRS---QIGTESlswEIIVVDNNSTDNTAQVVQEYQKNWPSPYPLRYCFEPQQGAAFA 77

                          90       100
                  ....*....|....*....|....*..
gi 1249615387  76 RNFGLNAATGDVLGRIDADCMLKPDWV 102
Cdd:NF038302   78 RQRAIQEAKGELIGFLDDDNLPAPNWV 104
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 6-94 7.32e-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: 54.85  E-value: 7.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADC---LMNATRQtvAPHEVIVVNNRSTDRTCDIVEQFQRDHPEapVILLQQNEDQGLIPTRNFGLNA 82
Cdd:cd06442     1 IIIPTYNERENIPELierLDAALKG--IDYEIIVVDDNSPDGTAEIVRELAKEYPR--VRLIVRPGKRGLGSAYIEGFKA 76

                          90
                  ....*....|..
gi 1249615387  83 ATGDVLGRIDAD 94
Cdd:cd06442    77 ARGDVIVVMDAD 88
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 5-119 1.56e-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: 53.86  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   5 SIIIPAWNEE--ERIADCLMNATRQTVAPHEVIVV-NNRSTDRTCDIVEQFQRDHPeAPVILLQQNedQGLIPTRNFGLN 81
Cdd:cd04195     1 SVLMSVYIKEkpEFLREALESILKQTLPPDEVVLVkDGPVTQSLNEVLEEFKRKLP-LKVVPLEKN--RGLGKALNEGLK 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1249615387  82 AATGDVLGRIDADCMLKPDWVEVVSGIFTEDP--DAMGAT 119
Cdd:cd04195    78 HCTYDWVARMDTDDISLPDRFEKQLDFIEKNPeiDIVGGG 117
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-192 1.18e-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: 51.89  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   5 SIIIPAWNEEER--IADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQrdhpEAPVILLQQNEDQ---GLIPTRNFG 79
Cdd:pfam10111   1 SVVIPVYNGEKThwIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIK----DHNLQVYYPNAPDttySLAASRNRG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  80 LNAATGDVLGRIDADCMLKPDWVEVVSGIFT-----EDPDAMGATgPVVYYDMPA-----KGAGLAGDDHIRRHTYRADN 149
Cdd:pfam10111  77 TSHAIGEYISFIDGDCLWSPDKFEKQLKIATslalqENIQAAVVL-PVTDLNDESsnflrRGGDLTASGDVLRDLLVFYS 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1249615387 150 DQVLLF---GSNMAIRASAWHAISG--EVCRDPEdvmHEDIDVSLHLL 192
Cdd:pfam10111 156 PLAIFFapnSSNALINRQAFIEVGGfdESFRGHG---AEDFDIFLRLA 200
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 3-94 4.06e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 47.42  E-value: 4.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   3 NVSIIIPAWNEEERIADCL---MNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDhPEAPVILLQQNEDQGLIPTRNFG 79
Cdd:PRK10714    7 KVSVVIPVYNEQESLPELIrrtTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQA-PDSHIVAILLNRNYGQHSAIMAG 85

                          90
                  ....*....|....*
gi 1249615387  80 LNAATGDVLGRIDAD 94
Cdd:PRK10714   86 FSHVTGDLIITLDAD 100
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 77-228 4.11e-06

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: 46.80  E-value: 4.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  77 NFGLNAATGDVLGRIDADCMLKPDWVEVVSGIFTEDPD-AMGATgPVVYYDMP-----AKGAGLAGDDHIRRHTYRADND 150
Cdd:cd06421    77 NNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKvALVQT-PQFFYNPDpfdwlADGAPNEQELFYGVIQPGRDRW 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387 151 QVLLF-GSNMAIRASAWHAISGEvcrdPEDVMHEDIDVSLHLLNHGFKTVY-SQCMICGISArrmdTSFASFHryMQRFK 228
Cdd:cd06421   156 GAAFCcGSGAVVRREALDEIGGF----PTDSVTEDLATSLRLHAKGWRSVYvPEPLAAGLAP----ETLAAYI--KQRLR 225
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 27-165 7.15e-06

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 46.08  E-value: 7.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  27 QTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEaPVILLQQNEDQGliPTRNF--GLNAATGDVLGRIDADCMLKPDWVEV 104
Cdd:cd04196    23 QTYKNDELIISDDGSTDGTVEIIKEYIDKDPF-IIILIRNGKNLG--VARNFesLLQAADGDYVFFCDQDDIWLPDKLER 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387 105 VSGIFtedpdaMGATGPVVYYD----MPAKGAGLAGDDHIRRHTYRADNDQVLLF-----GSNMAIRASA 165
Cdd:cd04196   100 LLKAF------LKDDKPLLVYSdlelVDENGNPIGESFFEYQKIKPGTSFNNLLFqnvvtGCTMAFNREL 163
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 2-94 9.49e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 46.30  E-value: 9.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   2 LNVSIIIPAWNEEERIADCLMNA-----TRQTVAP---HEVIVVNNRSTDRTCDIVEQFQRDHPEAP----VILLQQNED 69
Cdd:PTZ00260   70 VDLSIVIPAYNEEDRLPKMLKETikyleSRSRKDPkfkYEIIIVNDGSKDKTLKVAKDFWRQNINPNidirLLSLLRNKG 149

                          90       100
                  ....*....|....*....|....*
gi 1249615387  70 QGLIPTRnfGLNAATGDVLGRIDAD 94
Cdd:PTZ00260  150 KGGAVRI--GMLASRGKYILMVDAD 172
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-133 1.83e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 45.29  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   1 MLNVSIIIPAWNEEERIADCLMNATRQTVAP--HEVIVVNNRSTDRTCDIVEQFQrdhpeAPVIllqqNEDQGL--IPTR 76
Cdd:PRK13915   30 GRTVSVVLPALNEEETVGKVVDSIRPLLMEPlvDELIVIDSGSTDATAERAAAAG-----ARVV----SREEILpeLPPR 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1249615387  77 N-------FGLNAATGDVLGRIDADcmLK---PDWVEVVSGIFTEDPDAMGATGpvvYYDMPAKGAG 133
Cdd:PRK13915  101 PgkgealwRSLAATTGDIVVFVDAD--LInfdPMFVPGLLGPLLTDPGVHLVKA---FYRRPLRVSG 162
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 6-103 2.11e-05

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 44.76  E-value: 2.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQTV-APHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNED----QGLIPTRNFGL 80
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFeGTLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNspspKGVGYAKNQAI 80

                          90       100
                  ....*....|....*....|...
gi 1249615387  81 NAATGDVLGRIDADCMLKPDWVE 103
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIR 103
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 6-118 2.29e-05

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: 44.30  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQTVAPHeVIVVNNRSTDRTCDIVEQFQRDhpeAPVILLQQ---NEDQGliptRNFGLNA 82
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNKPNFL-VLVIDDASDDDTAGIVRLAITD---SRVHLLRRhlpNARTG----KGDALNA 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1249615387  83 ATG--------------DVL-GRIDADCMLKPDWVEVVSGIFtEDPDAMGA 118
Cdd:cd06436    73 AYDqirqilieegadpeRVIiAVIDADGRLDPNALEAVAPYF-SDPRVAGT 122
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 32-103 1.06e-04

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: 42.96  E-value: 1.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1249615387  32 HEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNEDQGLIPTRNFGLNAATGDVLGRIDADCMLKPDWVE 103
Cdd:cd02510    31 KEIILVDDFSDKPELKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDSHCEVNVGWLE 102
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 5-233 2.42e-04

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: 41.62  E-value: 2.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   5 SIIIPAWNEEERIADCLMNATRQTVAPH-EVIVVNNRSTDRTC-DIVEQFQRDHPEAPVILlqqnEDQGLIPTR----NF 78
Cdd:cd06435     1 SIHVPCYEEPPEMVKETLDSLAALDYPNfEVIVIDNNTKDEALwKPVEAHCAQLGERFRFF----HVEPLPGAKagalNY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387  79 GLNAATGD--VLGRIDADCMLKPDWVEVVSGIFtEDPDAMGATGPVVYYD------MPAKGAGLAGDDHIRRHTyRADND 150
Cdd:cd06435    77 ALERTAPDaeIIAVIDADYQVEPDWLKRLVPIF-DDPRVGFVQAPQDYRDgeeslfKRMCYAEYKGFFDIGMVS-RNERN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387 151 QVLLFGSNMAIRASAWHAISGEvcrdPEDVMHEDIDVSLHLLNHGFKTVY-SQCMICGIsarrMDTSFASFHRymQRFKN 229
Cdd:cd06435   155 AIIQHGTMCLIRRSALDDVGGW----DEWCITEDSELGLRMHEAGYIGVYvAQSYGHGL----IPDTFEAFKK--QRFRW 224


                  ....
gi 1249615387 230 TFAA 233
Cdd:cd06435   225 AYGA 228
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 6-127 7.07e-04

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: 39.89  E-value: 7.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   6 IIIPAWNEEERIADCLMNATRQtVAPHE---VIVVNNRSTDRTCDIVEQFqrdhpEAPVILLQQNEDQGliptRNFGLN- 81
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQ-DYPRElyrIFVVADNCTDDTAQVARAA-----GATVLERHDPERRG----KGYALDf 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1249615387  82 --------AATGDVLGRIDADCMLKPDWVEVVSGIFTEDPDAMGAtgpvvYYDM 127
Cdd:cd06438    71 gfrhllnlADDPDAVVVFDADNLVDPNALEELNARFAAGARVVQA-----YYNS 119
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 26-71 2.05e-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: 38.39  E-value: 2.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1249615387  26 RQTVAPHEVIVVNNRSTDRTCDIVEQFqrdHPEAPVILLQQNEDQG 71
Cdd:cd04185    21 AQTRPPDHIIVIDNASTDGTAEWLTSL---GDLDNIVYLRLPENLG 63
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 4-100 2.18e-03

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: 38.35  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWNEEERIADCLMNATRQTVAPHEVIVVNNRSTDRTCDIVEQFQRDHPEAPVILLQQNEDQGLIPTRNF---GL 80
Cdd:cd02520     3 VSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKVNNlikGY 82

                          90       100
                  ....*....|....*....|
gi 1249615387  81 NAATGDVLGRIDADCMLKPD 100
Cdd:cd02520    83 EEARYDILVISDSDISVPPD 102
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 4-115 7.77e-03

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: 36.80  E-value: 7.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1249615387   4 VSIIIPAWN-EEERIADCLMNATRQTVAPHEVIVVNNRSTDR-TCDIVEQFQRDHPEAPVILLQQNedQGLIPTRNFGLN 81
Cdd:cd04184     3 ISIVMPVYNtPEKYLREAIESVRAQTYPNWELCIADDASTDPeVKRVLKKYAAQDPRIKVVFREEN--GGISAATNSALE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1249615387  82 AATGDVLGRIDADCMLKPDWV-EVVSgIFTEDPDA 115
Cdd:cd04184    81 LATGEFVALLDHDDELAPHALyEVVK-ALNEHPDA 114
 
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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