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Conserved domains on  [gi|1645985512|gb|QCP71979|]
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glycosyltransferase [Duncaniella sp. B8]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10157685)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  21205000|12691742|9445404
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-210 3.50e-80

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: 239.75  E-value: 3.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLyqgRLRYVSEPDRGIYDAMNKGIAMASGD 83
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDK---ITYWISEPDKGIYDAMNKGIALATGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  84 IIGILNSDDFFTADTIVATLAAELADQEIDAVYADVHYVDDSDlsRSVRYYSSRTFRPWMMKLGFQPAHPTFYCRKSVYD 163
Cdd:cd06433    78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENG--RVIGRRRPPPFLDKFLLYGMPICHQATFFRRSLFE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1645985512 164 RHGSFDINFRVAADFEHLLRLIYIQRIpTRYIPLDCVAMRTGGASTS 210
Cdd:cd06433   156 KYGGFDESYRIAADYDLLLRLLLAGKI-FKYLPEVLAAFRLGGVSST 201
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-210 3.50e-80

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: 239.75  E-value: 3.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLyqgRLRYVSEPDRGIYDAMNKGIAMASGD 83
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDK---ITYWISEPDKGIYDAMNKGIALATGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  84 IIGILNSDDFFTADTIVATLAAELADQEIDAVYADVHYVDDSDlsRSVRYYSSRTFRPWMMKLGFQPAHPTFYCRKSVYD 163
Cdd:cd06433    78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENG--RVIGRRRPPPFLDKFLLYGMPICHQATFFRRSLFE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1645985512 164 RHGSFDINFRVAADFEHLLRLIYIQRIpTRYIPLDCVAMRTGGASTS 210
Cdd:cd06433   156 KYGGFDESYRIAADYDLLLRLLLAGKI-FKYLPEVLAAFRLGGVSST 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-219 1.93e-36

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 128.28  E-value: 1.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   1 MKISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYqGRLRYVS-EPDRGIYDAMNKGIAM 79
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKD-PRIRVIRlERNRGKGAARNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  80 ASGDIIGILNSDDFFTADTIvATLAAELADQEIDAVYADVHYVDDSDLSRSVRYYSSRTFRpWMMKLGFQPAHPTFYcRK 159
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKL-EELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVR-LLTNLPDSTSGFRLF-RR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1645985512 160 SVYDRHGsFDINFRVAADFEHLLRLIY-IQRIPTRYIPldcvamrtgGASTSGLKSHLRIL 219
Cdd:COG0463   158 EVLEELG-FDEGFLEDTELLRALRHGFrIAEVPVRYRA---------GESKLNLRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-163 1.03e-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: 96.70  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYqGRLRYVSEP-DRGIYDAMNKGIAMASG 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKD-PRVRVIRLPeNRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  83 DIIGILNSDDFFTADTIvATLAAELADQEIDAVYADVHYVDDSD-------LSRSVRYYSSRTFRPWMMKLGFQPAHPTF 155
Cdd:pfam00535  80 DYIAFLDADDEVPPDWL-EKLVEALEEDGADVVVGSRYVIFGETgeyrrasRITLSRLPFFLGLRLLGLNLPFLIGGFAL 158


                  ....*...
gi 1645985512 156 YCRKSVYD 163
Cdd:pfam00535 159 YRREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-92 5.74e-14

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 70.46  E-value: 5.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   2 KISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYQgRLRYVSEPDRGIYDAMNKGIAMAS 81
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGLAVAT 85

                          90
                  ....*....|.
gi 1645985512  82 GDIIGILNSDD 92
Cdd:PRK10073   86 GKYVAFPDADD 96
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
9-91 1.27e-11

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 63.27  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   9 TYNSGATLRDTMESVLRQTYTQI---EHIIVDGASTDNTMDIVREleplYQ------GRLRYVSEPDRGIYDAMNKGIAM 79
Cdd:NF038302    9 TYNGANRLPEVLERLRSQIGTESlswEIIVVDNNSTDNTAQVVQE----YQknwpspYPLRYCFEPQQGAAFARQRAIQE 84

                          90
                  ....*....|..
gi 1645985512  80 ASGDIIGILNSD 91
Cdd:NF038302   85 AKGELIGFLDDD 96
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-168 1.41e-11

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: 62.14  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   3 ISIITATYNSGATLRDTMESVLRQTYTqIEHIIVDGASTDNTMDIVRELeplyqGRLRYVSEPDRGIydAMNKGIAMASG 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGD-AEVIVVDGGSTDGTVEIARSL-----GAKVIHSPKGRAR--QMNAGAALAKG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  83 DIIGILNSDDFFTADTIVAtLAAELADQEIDAVYADVHyVDDSDLSRSVRYyssrtfrpWMMKL---------GFQpahp 153
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEA-IRRALAKPGYVAGAFDLR-FDGPGLLLRLIE--------WGVNLrsrltgipyGDQ---- 138

                         170
                  ....*....|....*
gi 1645985512 154 TFYCRKSVYDRHGSF 168
Cdd:TIGR04283 139 GLFVRRSLFEQIGGF 153
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-210 3.50e-80

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: 239.75  E-value: 3.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLyqgRLRYVSEPDRGIYDAMNKGIAMASGD 83
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDK---ITYWISEPDKGIYDAMNKGIALATGD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  84 IIGILNSDDFFTADTIVATLAAELADQEIDAVYADVHYVDDSDlsRSVRYYSSRTFRPWMMKLGFQPAHPTFYCRKSVYD 163
Cdd:cd06433    78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENG--RVIGRRRPPPFLDKFLLYGMPICHQATFFRRSLFE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1645985512 164 RHGSFDINFRVAADFEHLLRLIYIQRIpTRYIPLDCVAMRTGGASTS 210
Cdd:cd06433   156 KYGGFDESYRIAADYDLLLRLLLAGKI-FKYLPEVLAAFRLGGVSST 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-219 1.93e-36

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 128.28  E-value: 1.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   1 MKISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYqGRLRYVS-EPDRGIYDAMNKGIAM 79
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKD-PRIRVIRlERNRGKGAARNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  80 ASGDIIGILNSDDFFTADTIvATLAAELADQEIDAVYADVHYVDDSDLSRSVRYYSSRTFRpWMMKLGFQPAHPTFYcRK 159
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKL-EELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVR-LLTNLPDSTSGFRLF-RR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1645985512 160 SVYDRHGsFDINFRVAADFEHLLRLIY-IQRIPTRYIPldcvamrtgGASTSGLKSHLRIL 219
Cdd:COG0463   158 EVLEELG-FDEGFLEDTELLRALRHGFrIAEVPVRYRA---------GESKLNLRDLLRLL 208
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 5-117 2.64e-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: 105.67  E-value: 2.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYQGRLRYVSEPDRGIYDAMNKGIAMASGDI 84
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1645985512  85 IGILNSDDFFTADTIVATLAAELADQEIDAVYA 117
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGG 113
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-239 7.25e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 97.76  E-value: 7.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   1 MKISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPlyqGRLRYV-SEPDRGIYDAMNKGIAM 79
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAF---PRVRVIrNPENLGFAAARNLGLRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  80 ASGDIIGILNSDDFFTADTIVATLAAeladqeidavyadvhyvddsdlsrsvryyssrtfrpWMMklgfqpahptfYCRK 159
Cdd:COG1216    80 AGGDYLLFLDDDTVVEPDWLERLLAA------------------------------------ACL-----------LIRR 112

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512 160 SVYDRHGSFDINFRVAA-DFEHLLRLIYiQRIPTRYIPlDCVAMRTGGASTSGLKSHLRILSDHLKAYRKNGVNSNLFLD 238
Cdd:COG1216   113 EVFEEVGGFDERFFLYGeDVDLCLRLRK-AGYRIVYVP-DAVVYHLGGASSGPLLRAYYLGRNRLLFLRKHGPRPLLRLA 190


                  .
gi 1645985512 239 A 239
Cdd:COG1216   191 L 191
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-163 1.03e-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: 96.70  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYqGRLRYVSEP-DRGIYDAMNKGIAMASG 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKD-PRVRVIRLPeNRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  83 DIIGILNSDDFFTADTIvATLAAELADQEIDAVYADVHYVDDSD-------LSRSVRYYSSRTFRPWMMKLGFQPAHPTF 155
Cdd:pfam00535  80 DYIAFLDADDEVPPDWL-EKLVEALEEDGADVVVGSRYVIFGETgeyrrasRITLSRLPFFLGLRLLGLNLPFLIGGFAL 158


                  ....*...
gi 1645985512 156 YCRKSVYD 163
Cdd:pfam00535 159 YRREALEE 166
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 2-185 8.20e-22

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


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 90.75  E-value: 8.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   2 KISIITATYNSGATLRDTMESVLRQTY--TQIEHIIVDGASTDNTMDIVRELEPLYQgRLRYVSEPDRGIYDAMNKGIAM 79
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDP-RIRLIDNPKRIQSAGLNIGIRN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  80 ASGDIIGILNSDDFFTADTIvATLAAELADQEIDAVYADVHYVDDSDLSRSVRY-YSSR------TFRPWMMKLGF-QPA 151
Cdd:cd02525    80 SRGDIIIRVDAHAVYPKDYI-LELVEALKRTGADNVGGPMETIGESKFQKAIAVaQSSPlgsggsAYRGGAVKIGYvDTV 158

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1645985512 152 HPTFYcRKSVYDRHGSFDINFRVAADFEHLLRLI 185
Cdd:cd02525   159 HHGAY-RREVFEKVGGFDESLVRNEDAELNYRLR 191
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-132 3.19e-21

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: 90.57  E-value: 3.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   1 MKISIITATYNSGATLRDTMESVLRQTY--TQIEHIIVDGASTDNTMDIVRELEPLYqGRLRYVSEPDR-GIYDAMNKGI 77
Cdd:COG1215    29 PRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEY-PRVRVIERPENgGKAAALNAGL 107

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1645985512  78 AMASGDIIGILNSDDFFTADTIvATLAAELADQEIDAV----------------YADVHYVDDSDLSRSVR 132
Cdd:COG1215   108 KAARGDIVVFLDADTVLDPDWL-RRLVAAFADPGVGASganlafrrealeevggFDEDTLGEDLDLSLRLL 177
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 5-169 4.48e-21

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: 87.28  E-value: 4.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYQGRLRYV-SEPDRGIYDAMNKGIAMASGD 83
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVrDKENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  84 IIGILNSDDFFTADTIVATLAAELADQEIDAVYADVHYVDDSD--LSR--SVRYYSS-RTFRPWMMKLG--FQPAHPTFY 156
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSEnlLTRlqAIEYLSIfRLGRRAQSALGgvLVLSGAFGA 160

                         170
                  ....*....|...
gi 1645985512 157 CRKSVYDRHGSFD 169
Cdd:cd06423   161 FRREALREVGGWD 173
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 2-191 2.58e-19

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: 83.02  E-value: 2.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   2 KISIITATYNS-GATLRDTMESVLRQTYTQIEHIIVDGASTDntmDIVRELEPLYQ---GRLRYV-SEPDRGIYDAMNKG 76
Cdd:cd04184     2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTD---PEVKRVLKKYAaqdPRIKVVfREENGGISAATNSA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  77 IAMASGDIIGILNSDDFFTADTIVATLAAELADQEIDAVYADVHYVDDSdlsrSVRYysSRTFRPwmmklGFQPahPTFY 156
Cdd:cd04184    79 LELATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEG----GKRS--EPFFKP-----DWSP--DLLL 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1645985512 157 C----------RKSVYDRHGSFDINFRVAADFEHLLRLI----YIQRIP 191
Cdd:cd04184   146 SqnyighllvyRRSLVRQVGGFREGFEGAQDYDLVLRVSehtdRIAHIP 194
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-134 4.92e-15

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: 72.62  E-value: 4.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   2 KISIITATYNSGATLRDTMESVLRQTY--TQIEHIIVDGASTDNTMDIVRELEPlyQGRLRYVSEPDRGIYDAMNKGIAM 79
Cdd:cd06439    30 TVTIIIPAYNEEAVIEAKLENLLALDYprDRLEIIVVSDGSTDGTAEIAREYAD--KGVKLLRFPERRGKAAALNRALAL 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1645985512  80 ASGDIIGILNSDDFFTADTIVAtLAAELADQEIDAVYADVHYVDDSDLSRSVRYY 134
Cdd:cd06439   108 ATGEIVVFTDANALLDPDALRL-LVRHFADPSVGAVSGELVIVDGGGSGSGEGLY 161
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 4-142 5.17e-15

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 71.89  E-value: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYQGRLRYVS-EPDRGIYDAMNKGIAMASG 82
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRnGKNLGVARNFESLLQAADG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  83 DIIGILNSDDFFTADTIVATLAAELADQEIDAVYADVHYVDDSDLSRSVRYYSSRTFRPW 142
Cdd:cd04196    81 DYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGESFFEYQKIKPG 140
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-115 1.68e-14

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: 69.13  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPlyqgRLRYVSEPD-RGIYDAMNKGIAMASGD 83
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFP----EVRLIRNGEnLGFGAGNNQGIREAKGD 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1645985512  84 IIGILNSDDFFTADTIVATLAAELADQEIDAV 115
Cdd:cd04186    77 YVLLLNPDTVVEPGALLELLDAAEQDPDVGIV 108
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-92 5.74e-14

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 70.46  E-value: 5.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   2 KISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYQgRLRYVSEPDRGIYDAMNKGIAMAS 81
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGLAVAT 85

                          90
                  ....*....|.
gi 1645985512  82 GDIIGILNSDD 92
Cdd:PRK10073   86 GKYVAFPDADD 96
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 3-169 6.54e-13

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


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 66.05  E-value: 6.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   3 ISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELeplyqGRLRYVSEPDRGIydAMNKGIAMASG 82
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSA-----GVVVISSPKGRAR--QMNAGAAAARG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  83 DIIGILNSDDFFTADTIvATLAAELADQEIDAVYADVHYVDDSDLSRSVRY----YSSRTFRPWmmklGFQpahpTFYCR 158
Cdd:cd02522    74 DWLLFLHADTRLPPDWD-AAIIETLRADGAVAGAFRLRFDDPGPRLRLLELganlRSRLFGLPY----GDQ----GLFIR 144

                         170
                  ....*....|.
gi 1645985512 159 KSVYDRHGSFD 169
Cdd:cd02522   145 RELFEELGGFP 155
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 5-184 1.93e-12

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: 64.13  E-value: 1.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLR--QTYTQIEHIIVDGASTDNTMDIVRELEPLYQGRLRYVSEPDRGIYDAMNKGIAMASG 82
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  83 DIIGILNSDDFFTADTIVAtLAAELADQEIDAVYAdVHYVDDSDLSRS-VRYYSSRTFRPWMMKLGFQPAHPTFYC---- 157
Cdd:cd04179    81 DIVVTMDADLQHPPEDIPK-LLEKLLEGGADVVIG-SRFVRGGGAGMPlLRRLGSRLFNFLIRLLLGVRISDTQSGfrlf 158

                         170       180
                  ....*....|....*....|....*..
gi 1645985512 158 RKSVYDRHGSFDINFRVAADFEHLLRL 184
Cdd:cd04179   159 RREVLEALLSLLESNGFEFGLELLVGA 185
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
9-91 1.27e-11

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 63.27  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   9 TYNSGATLRDTMESVLRQTYTQI---EHIIVDGASTDNTMDIVREleplYQ------GRLRYVSEPDRGIYDAMNKGIAM 79
Cdd:NF038302    9 TYNGANRLPEVLERLRSQIGTESlswEIIVVDNNSTDNTAQVVQE----YQknwpspYPLRYCFEPQQGAAFARQRAIQE 84

                          90
                  ....*....|..
gi 1645985512  80 ASGDIIGILNSD 91
Cdd:NF038302   85 AKGELIGFLDDD 96
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-168 1.41e-11

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: 62.14  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   3 ISIITATYNSGATLRDTMESVLRQTYTqIEHIIVDGASTDNTMDIVRELeplyqGRLRYVSEPDRGIydAMNKGIAMASG 82
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALRGD-AEVIVVDGGSTDGTVEIARSL-----GAKVIHSPKGRAR--QMNAGAALAKG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  83 DIIGILNSDDFFTADTIVAtLAAELADQEIDAVYADVHyVDDSDLSRSVRYyssrtfrpWMMKL---------GFQpahp 153
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEA-IRRALAKPGYVAGAFDLR-FDGPGLLLRLIE--------WGVNLrsrltgipyGDQ---- 138

                         170
                  ....*....|....*
gi 1645985512 154 TFYCRKSVYDRHGSF 168
Cdd:TIGR04283 139 GLFVRRSLFEQIGGF 153
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 5-91 8.90e-10

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: 56.43  E-value: 8.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYQGRLRYVSEPDRGIYDA--MNKGIAMASG 82
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVWQEDEGFRKAkiRNKAIAAAKG 80


                  ....*....
gi 1645985512  83 DIIGILNSD 91
Cdd:cd06420    81 DYLIFIDGD 89
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-196 4.01e-09

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: 55.45  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   3 ISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYQ-GRLRYVSEPD----RGIYDAMNKGI 77
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdVRLRVIRNARllgpTGKSRGLNHGF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  78 AMASGDIIGILNSDDFFTADTIVATLAAeLADQEIDAVYADVHYV-DDSDLSRSVRYYSSRTFRPWMM---KLGFQPAHP 153
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQY-FDSPKVGAVGTPVFSLnRSTMLSALGALEFALRHLRMMSlrlALGVLPLSG 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1645985512 154 TFYC-RKSVYDRHGSFDINFRVAADFEHLLRLIyIQRIPTRYIP 196
Cdd:pfam13641 163 AGSAiRREVLKELGLFDPFFLLGDDKSLGRRLR-RHGWRVAYAP 205
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-184 4.66e-08

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: 52.66  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYNSGATlRDTMESVLRQTY---TQIEHIIVDGASTDNTMDIVRELEPLyQGRLRYVSEPDR--GIYDAMNKGIA 78
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFqydPEFELIIINDGSTDKTLEEVSSIKDH-NLQVYYPNAPDTtySLAASRNRGTS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  79 MASGDIIGILNSDDFFTADTI--VATLAAELADQE-IDA--VYADVHYVD-DSDLSRSVRY--YSSRTFRPWMMKLG--- 147
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFekQLKIATSLALQEnIQAavVLPVTDLNDeSSNFLRRGGDltASGDVLRDLLVFYSpla 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1645985512 148 --FQPAHPTFYCRKSVYDRHGSFDINFRV--AADFEHLLRL 184
Cdd:pfam10111 159 ifFAPNSSNALINRQAFIEVGGFDESFRGhgAEDFDIFLRL 199
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-91 7.44e-08

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 52.01  E-value: 7.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   1 MKISIITATYNSGAT-------LRDTMESVLRqtytqIEHIIVDGASTDNTMDIVRELEPLY-QGRLRYVSEPDR-GIYD 71
Cdd:PLN02726    9 MKYSIIVPTYNERLNialivylIFKALQDVKD-----FEIIVVDDGSPDGTQDVVKQLQKVYgEDRILLRPRPGKlGLGT 83

                          90       100
                  ....*....|....*....|
gi 1645985512  72 AMNKGIAMASGDIIGILNSD 91
Cdd:PLN02726   84 AYIHGLKHASGDFVVIMDAD 103
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-91 1.16e-06

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 47.47  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTME---SVLRQTYTQIEHIIVDGASTDNTMDIVRELEPLYqGRLRYVSEpDR--GIYDAMNKGIAM 79
Cdd:cd04187     1 IVVPVYNEEENLPELYErlkAVLESLGYDYEIIFVDDGSTDRTLEILRELAARD-PRVKVIRL-SRnfGQQAALLAGLDH 78

                          90
                  ....*....|..
gi 1645985512  80 ASGDIIGILNSD 91
Cdd:cd04187    79 ARGDAVITMDAD 90
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 9-109 1.17e-06

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 48.02  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   9 TYNSGATLRDTMESVLRQTYtQIEHI-IVDGASTDNTMDIVRELEPLYQGRLRYVSE---PDRGIYDAMnkGIAMASG-D 83
Cdd:cd04185     5 TYNRLDLLKECLDALLAQTR-PPDHIiVIDNASTDGTAEWLTSLGDLDNIVYLRLPEnlgGAGGFYEGV--RRAYELGyD 81

                          90       100
                  ....*....|....*....|....*.
gi 1645985512  84 IIGILNSDDFFTADTIVATLAAELAD 109
Cdd:cd04185    82 WIWLMDDDAIPDPDALEKLLAYADKD 107
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-196 2.27e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 47.28  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLRQTYTQ--IEHIIVDGASTDNTMDIV--RELEPLYQGR-LRYVSEPDRGIYDAMNKGIAM 79
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQILefAAAKPNFQLKiLNNSRVSISGKKNALTTAIKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  80 ASGDIIgilnsddFFT-ADTIVAT--LaaeladQEIDAVYADvhyVDDSDLSRSVRYYSSRTFRP------WM----MKL 146
Cdd:cd04192    81 AKGDWI-------VTTdADCVVPSnwL------LTFVAFIQK---EQIGLVAGPVIYFKGKSLLAkfqrldWLsllgLIA 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1645985512 147 GFQPAHPTFYC-------RKSVYDRHGSFD-INFRVAADFEhLLRLIYIQRIP-TRYIP 196
Cdd:cd04192   145 GSFGLGKPFMCnganmayRKEAFFEVGGFEgNDHIASGDDE-LLLAKVASKYPkVAYLK 202
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 2-107 2.27e-06

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: 47.28  E-value: 2.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   2 KISIITATYNSGATLRDTMESVLRQTytqIEHIIVDGASTDNTMDIVRELeplyqgRLRYVSEPDRGIYDAMNKGIAMAS 81
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAV---DEIIVVDSGSTDRTVEIAKEY------GAKVYQRWWDGFGAQRNFALELAT 71

                          90       100
                  ....*....|....*....|....*.
gi 1645985512  82 GDIIGILNSDDFFTADtivatLAAEL 107
Cdd:cd02511    72 NDWVLSLDADERLTPE-----LADEI 92
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
3-185 9.95e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 45.75  E-value: 9.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   3 ISIITATYNSGATLRDTMESVLRQTYTQIEHIIVDGASTdNTMDIVRELEPLYQGRLRYV-SEPDRGIYDAMNKGIAMAS 81
Cdd:PRK10018    7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST-SWEQLQQYVTALNDPRITYIhNDINSGACAVRNQAIMLAQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512  82 GDIIGILNSDDFFTADTIVATLAAELADQEIDAVYADvHYVDDSDLsrsvryYSSRTFRPwmmklgFQPAHPtfYCRKSV 161
Cdd:PRK10018   86 GEYITGIDDDDEWTPNRLSVFLAHKQQLVTHAFLYAN-DYVCQGEV------YSQPASLP------LYPKSP--YSRRLF 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1645985512 162 YDRH--GS-------------FDINFRVAADFEHLLRLI 185
Cdd:PRK10018  151 YKRNiiGNqvftwawrfkeclFDTELKAAQDYDIFLRMV 189
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 5-107 5.12e-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: 43.22  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLRQTYTQ-IEHIIVDGASTDNTMDIVRELEPLYQGRLRYV------SEPDRGIYDAMNKGI 77
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVlvgshnSPSPKGVGYAKNQAI 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1645985512  78 AMASGDIIGILNSDDFFTADTIVATLAAEL 107
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAAL 110
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 5-91 6.43e-05

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: 42.91  E-value: 6.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITATYNSGATLRDTMESVLRQTYT-QIEHIIVDGASTDNTMDIVRELEPLYQGRLRYVSEPDRGIYDAMNKGIAMASGD 83
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80


                  ....*...
gi 1645985512  84 IIGILNSD 91
Cdd:cd06442    81 VIVVMDAD 88
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-91 1.29e-04

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: 41.78  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   5 IITAtYNSGATLRDTMESVL-----RQTYTqIEHIIVDGASTDNTMDIVRELEPLYQGRLRYVSEP-DRGIYDAMNKGIA 78
Cdd:cd04188     2 VIPA-YNEEKRLPPTLEEAVeyleeRPSFS-YEIIVVDDGSKDGTAEVARKLARKNPALIRVLTLPkNRGKGGAVRAGML 79

                          90
                  ....*....|...
gi 1645985512  79 MASGDIIGILNSD 91
Cdd:cd04188    80 AARGDYILFADAD 92
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 4-115 3.43e-03

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: 37.68  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1645985512   4 SIITATYN--SGATLRDTMESVLRQTYTQIEHIIV-DGASTDNTMDIVRELEPLYQGRlRYVSEPDRGIYDAMNKGIAMA 80
Cdd:cd04195     1 SVLMSVYIkeKPEFLREALESILKQTLPPDEVVLVkDGPVTQSLNEVLEEFKRKLPLK-VVPLEKNRGLGKALNEGLKHC 79

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1645985512  81 SGDIIGILNSDDFFTADTIVATLAAELADQEIDAV 115
Cdd:cd04195    80 TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIV 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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