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Conserved domains on  [gi|499293549|ref|WP_010984807|]
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MULTISPECIES: glycosyltransferase family 2 protein [Streptomyces]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

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:  16037492|18518825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-217 4.93e-40

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 139.45  E-value: 4.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   1 MVKLSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDT 80
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549  81 ARGEYLTFLDGDDWLAPGYFPQLLSAIEELGCDFVrtdhvqCTARartvnRVPHGRRGVVMNPRDAILPADRSTSVDYAY 160
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV------YGSR-----LIREGESDLRRLGSRLFNLVRLLTNLPDST 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499293549 161 AWAGIYHRRLVDRglLHFTDGLrtAEDRPWIWkLHREAESFATVgllGVFYRRGVAS 217
Cdd:COG0463  150 SGFRLFRREVLEE--LGFDEGF--LEDTELLR-ALRHGFRIAEV---PVRYRAGESK 198
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-217 4.93e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 139.45  E-value: 4.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   1 MVKLSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDT 80
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549  81 ARGEYLTFLDGDDWLAPGYFPQLLSAIEELGCDFVrtdhvqCTARartvnRVPHGRRGVVMNPRDAILPADRSTSVDYAY 160
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV------YGSR-----LIREGESDLRRLGSRLFNLVRLLTNLPDST 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499293549 161 AWAGIYHRRLVDRglLHFTDGLrtAEDRPWIWkLHREAESFATVgllGVFYRRGVAS 217
Cdd:COG0463  150 SGFRLFRREVLEE--LGFDEGF--LEDTELLR-ALRHGFRIAEV---PVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-115 2.02e-35

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: 126.36  E-value: 2.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549    5 SVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDTARGE 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 499293549   85 YLTFLDGDDWLAPGYFPQLLSAIEELGCDFV 115
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVV 111
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-109 2.75e-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: 109.90  E-value: 2.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDTARGEY 85
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80
                         90       100
                 ....*....|....*....|....
gi 499293549  86 LTFLDGDDWLAPGYFPQLLSAIEE 109
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLA 104
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-190 1.28e-27

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 109.75  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   3 KLSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPgAVHVRHEKNGGLATARNTGIDTAR 82
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGLAVAT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549  83 GEYLTFLDGDDWLAPGYFPQLLSAIEElgcdfVRTDHVQCTArartvNRVPHGRRgvvmnPRDAILPADR--STSV---- 156
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETLMTMALE-----DDLDVAQCNA-----DWCFRDTG-----ETWQSIPSDRlrSTGVlsgp 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 499293549 157 ---DYAYA--------WAGIYHRRLVDRGLLHFTDGLRtAEDRPW 190
Cdd:PRK10073 151 dwlRMALSsrrwthvvWLGVYRRDFIVKNNIKFEPGLH-HQDIPW 194
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-217 4.93e-40

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 139.45  E-value: 4.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   1 MVKLSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDT 80
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549  81 ARGEYLTFLDGDDWLAPGYFPQLLSAIEELGCDFVrtdhvqCTARartvnRVPHGRRGVVMNPRDAILPADRSTSVDYAY 160
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV------YGSR-----LIREGESDLRRLGSRLFNLVRLLTNLPDST 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 499293549 161 AWAGIYHRRLVDRglLHFTDGLrtAEDRPWIWkLHREAESFATVgllGVFYRRGVAS 217
Cdd:COG0463  150 SGFRLFRREVLEE--LGFDEGF--LEDTELLR-ALRHGFRIAEV---PVRYRAGESK 198
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-115 2.02e-35

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: 126.36  E-value: 2.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549    5 SVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDTARGE 84
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 499293549   85 YLTFLDGDDWLAPGYFPQLLSAIEELGCDFV 115
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVV 111
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-109 2.75e-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: 109.90  E-value: 2.75e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDTARGEY 85
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80
                         90       100
                 ....*....|....*....|....
gi 499293549  86 LTFLDGDDWLAPGYFPQLLSAIEE 109
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLA 104
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-190 1.28e-27

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 109.75  E-value: 1.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   3 KLSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPgAVHVRHEKNGGLATARNTGIDTAR 82
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYP-HVRLLHQANAGVSVARNTGLAVAT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549  83 GEYLTFLDGDDWLAPGYFPQLLSAIEElgcdfVRTDHVQCTArartvNRVPHGRRgvvmnPRDAILPADR--STSV---- 156
Cdd:PRK10073  86 GKYVAFPDADDVVYPTMYETLMTMALE-----DDLDVAQCNA-----DWCFRDTG-----ETWQSIPSDRlrSTGVlsgp 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 499293549 157 ---DYAYA--------WAGIYHRRLVDRGLLHFTDGLRtAEDRPW 190
Cdd:PRK10073 151 dwlRMALSsrrwthvvWLGVYRRDFIVKNNIKFEPGLH-HQDIPW 194
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-106 8.00e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 99.30  E-value: 8.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   1 MVKLSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILAraERELPGAVHVRHEKNGGLATARNTGIDT 80
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLA--ALAFPRVRVIRNPENLGFAAARNLGLRA 79
                         90       100
                 ....*....|....*....|....*.
gi 499293549  81 ARGEYLTFLDGDDWLAPGYFPQLLSA 106
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLERLLAA 105
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
3-115 8.65e-25

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 101.74  E-value: 8.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   3 KLSVIVPFYNVQQYAPDTLKSLRAN--AGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDT 80
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQdyPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKA 109
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499293549  81 ARGEYLTFLDGDDWLAPGYFPQLLSAIEELGCDFV 115
Cdd:COG1215  110 ARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
6-115 2.96e-24

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: 97.26  E-value: 2.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRA--NAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDTARG 83
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 499293549  84 EYLTFLDGDDWLAPGYFPQLLSAIEELGCDFV 115
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVV 112
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
5-218 2.08e-18

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: 81.82  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   5 SVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELpgaVHVRHEKNGGLATARNTGIDTARGE 84
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKI---TYWISEPDKGIYDAMNKGIALATGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549  85 YLTFLDGDDWLAPGYFPQLLSAIEEL-GCDFVrtdhvqCtarARTVNRVPHGRRGVVMNPRdailpaDRSTSVDYAYAW- 162
Cdd:cd06433   78 IIGFLNSDDTLLPGALLAVVAAFAEHpEVDVV------Y---GDVLLVDENGRVIGRRRPP------PFLDKFLLYGMPi 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499293549 163 ---AGIYHRRLVDRGLLHFTDgLRTAEDRPWIWKLHREAESFATVGLLGVFYRRGVASS 218
Cdd:cd06433  143 chqATFFRRSLFEKYGGFDES-YRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSS 200
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-119 6.12e-18

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: 80.71  E-value: 6.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   3 KLSVIVPFYNV-QQYAPDTLKSLRANAGDDFEFILVDDCSRD-ETPDILAR-AERELPGAVHVRhEKNGGLATARNTGID 79
Cdd:cd04184    2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDpEVKRVLKKyAAQDPRIKVVFR-EENGGISAATNSALE 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 499293549  80 TARGEYLTFLDGDDWLAPGYFPQLLSAI-EELGCDFVRTDH 119
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALnEHPDADLIYSDE 121
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-109 1.33e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 76.06  E-value: 1.33e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILaraERELPGAVHVRHEKNGGLATARNTGIDTARGEY 85
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELL---RELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77
                         90       100
                 ....*....|....*....|....
gi 499293549  86 LTFLDGDDWLAPGYFPQLLSAIEE 109
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAAEQ 101
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
6-131 1.55e-16

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: 76.11  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAVH-VRHEKNGGLATARNTGIDTARGE 84
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLvVRDKENGGKAGALNAGLRHAKGD 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499293549  85 YLTFLDGDDWLAPGyfpqllsAIEELGCDFVR-TDHVQCTARARTVNR 131
Cdd:cd06423   81 IVVVLDADTILEPD-------ALKRLVVPFFAdPKVGAVQGRVRVRNG 121
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
5-115 2.86e-15

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: 74.19  E-value: 2.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   5 SVIVPFYNVQQYAPDTLKSLRANA--GDDFEFILVDDCSRDETPDILARAERELPgavHVRHEKNGG--LATARNTGIDT 80
Cdd:cd02525    3 SIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYAAKDP---RIRLIDNPKriQSAGLNIGIRN 79
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499293549  81 ARGEYLTFLDGDDWLAPGYFPQLLSAIEELGCDFV 115
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDYILELVEALKRTGADNV 114
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-115 1.33e-14

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


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 70.97  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRA---NAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDTAR 82
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAvleSLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 499293549  83 GEYLTFLDGDdwL--APGYFPQLLSAIEElGCDFV 115
Cdd:cd04187   81 GDAVITMDAD--LqdPPELIPEMLAKWEE-GYDVV 112
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
6-115 5.02e-14

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: 70.25  E-value: 5.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSL-RANAGDDFEFILVDDCSRDETPDILARAERELPGAVHVRHEKNGGLATARNTGIDTARGE 84
Cdd:cd06442    1 IIIPTYNERENIPELIERLdAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499293549  85 YLTFLDGDDWLAPGYFPQLLSAIEELGCDFV 115
Cdd:cd06442   81 VIVVMDADLSHPPEYIPELLEAQLEGGADLV 111
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
6-115 2.78e-13

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: 67.59  E-value: 2.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAP----DTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAV-HVRHEKNGGLATARNTGIDT 80
Cdd:cd04188    1 VVIPAYNEEKRLPptleEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIrVLTLPKNRGKGGAVRAGMLA 80
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499293549  81 ARGEYLTFLDGDdwLA--PGYFPQLLSAIEELGCDFV 115
Cdd:cd04188   81 ARGDYILFADAD--LAtpFEELEKLEEALKTSGYDIA 115
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
3-113 4.17e-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: 67.70  E-value: 4.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   3 KLSVIVPFYNVQQYAPDTLKSLRaNAGDdfEFILVDDCSRDETPDIlARAERelpgaVHVRHEKNGGLATARNTGIDTAR 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVK-WAVD--EIIVVDSGSTDRTVEI-AKEYG-----AKVYQRWWDGFGAQRNFALELAT 71
                         90       100       110
                 ....*....|....*....|....*....|.
gi 499293549  83 GEYLTFLDGDDWLAPGYFPQLLSAIEELGCD 113
Cdd:cd02511   72 NDWVLSLDADERLTPELADEILALLATDDYD 102
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
6-114 1.10e-12

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: 65.29  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPGAV-HVRHEKNG-GLATARNTGIDTARG 83
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIkHVWQEDEGfRKAKIRNKAIAAAKG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499293549  84 EYLTFLDGD-----DWLA-------PGYF--------PQLLSAIEELGCDF 114
Cdd:cd06420   81 DYLIFIDGDciphpDFIAdhielaePGVFlsgsrvllNEKLTERGIRGCNM 131
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
4-100 8.04e-11

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: 61.05  E-value: 8.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   4 LSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAerelpGAVHVRHEKngGLATARNTGIDTARG 83
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSA-----GVVVISSPK--GRARQMNAGAAAARG 73
                         90
                 ....*....|....*..
gi 499293549  84 EYLTFLDGDDWLAPGYF 100
Cdd:cd02522   74 DWLLFLHADTRLPPDWD 90
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
5-109 1.25e-10

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: 61.45  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   5 SVIVPFYN-------------VQQYAPDTLKslranagddfEFILVDDCS-RDETPDILARAERELPGAVHV-RHEKNGG 69
Cdd:cd02510    1 SVIIIFHNealstllrtvhsvINRTPPELLK----------EIILVDDFSdKPELKLLLEEYYKKYLPKVKVlRLKKREG 70
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 499293549  70 LATARNTGIDTARGEYLTFLDG-----DDWLAPgyfpqLLSAIEE 109
Cdd:cd02510   71 LIRARIAGARAATGDVLVFLDShcevnVGWLEP-----LLARIAE 110
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
5-110 4.37e-10

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: 59.60  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549    5 SVIVPFYNVQQ--YAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAeRELPGAVHVRHE--KNGGLATARNTGIDT 80
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSI-KDHNLQVYYPNApdTTYSLAASRNRGTSH 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 499293549   81 ARGEYLTFLDGDDWLAPGYFPQLLSAIEEL 110
Cdd:pfam10111  80 AIGEYISFIDGDCLWSPDKFEKQLKIATSL 109
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-110 9.26e-10

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 58.47  E-value: 9.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   4 LSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSrdETPDILARAEREL--PGAVHVRHEKNGGLATARNTGIDTA 81
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCS--TSWEQLQQYVTALndPRITYIHNDINSGACAVRNQAIMLA 84
                         90       100
                 ....*....|....*....|....*....
gi 499293549  82 RGEYLTFLDGDDWLAPGYFPQLLSAIEEL 110
Cdd:PRK10018  85 QGEYITGIDDDDEWTPNRLSVFLAHKQQL 113
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-115 1.57e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 57.40  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   1 MVKLSVIVPFYN-------VQQYAPDTLKSLranagDDFEFILVDDCSRDETPDIlARAERELPGAVHV----RHEKNGg 69
Cdd:PLN02726   8 AMKYSIIVPTYNerlnialIVYLIFKALQDV-----KDFEIIVVDDGSPDGTQDV-VKQLQKVYGEDRIllrpRPGKLG- 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499293549  70 LATARNTGIDTARGEYLTFLDGDDWLAPGYFPQLLSAIEELGCDFV 115
Cdd:PLN02726  81 LGTAYIHGLKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIV 126
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-95 1.16e-08

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 54.60  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRA-NAGDD-FEFILVDDCSRDETPDILARAERElpGAVHVRH-----EKNGGLATARNTGI 78
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSAlDYPKEkFEVILVDDHSTDGTVQILEFAAAK--PNFQLKIlnnsrVSISGKKNALTTAI 78
                         90       100
                 ....*....|....*....|..
gi 499293549  79 DTARGEYLTFLDGD-----DWL 95
Cdd:cd04192   79 KAAKGDWIVTTDADcvvpsNWL 100
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-95 1.42e-08

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 54.17  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   5 SVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILAR-AERELPGAVHVRHEKNGGLatARN--TGIDTA 81
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEyIDKDPFIIILIRNGKNLGV--ARNfeSLLQAA 78
                         90
                 ....*....|....*
gi 499293549  82 RGEYLTFLDGDD-WL 95
Cdd:cd04196   79 DGDYVFFCDQDDiWL 93
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-118 2.87e-08

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: 53.53  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549    4 LSVIVPFYNVQQYAPDTLKSLRANAGDDFEFILVDDCSRDETPDILARAERELPG-----AVHVRHEKNGGLATARNTGI 78
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDvrlrvIRNARLLGPTGKSRGLNHGF 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 499293549   79 DTARGEYLTFLDGDDWLAPGYFPQLLSAIEELGCDFVRTD 118
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTP 123
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-98 2.96e-08

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: 53.74  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   3 KLSVIVPFYNVQQYAPDTLKSLRANA--GDDFEFILVDDCSRDETPDIlarAERELPGAVHV-RHEKNGGLATARNTGID 79
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKLENLLALDypRDRLEIIVVSDGSTDGTAEI---AREYADKGVKLlRFPERRGKAAALNRALA 106
                         90
                 ....*....|....*....
gi 499293549  80 TARGEYLTFLDGDDWLAPG 98
Cdd:cd06439  107 LATGEIVVFTDANALLDPD 125
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-117 1.32e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 52.43  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   3 KLSVIVPFYNVQQYAPDTLKSLRA---NAGDDFEFILVDDCSRDETPDILARAErELPGA--VHVRHEKNGGLATARNTG 77
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAaceSLGKEYEILLIDDGSSDNSAEMLVEAA-QAPDShiVAILLNRNYGQHSAIMAG 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499293549  78 IDTARGEYLTFLDGDDWLAPGYFPQLLSAIEElGCDFVRT 117
Cdd:PRK10714  86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADE-GYDVVGT 124
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
2-92 1.38e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 52.46  E-value: 1.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   2 VKLSVIVPFYNVQQYAPDTLKS----LRANAGDD----FEFILVDDCSRDETPDILARAERELPGAVH----VRHEKNGG 69
Cdd:PTZ00260  70 VDLSIVIPAYNEEDRLPKMLKEtikyLESRSRKDpkfkYEIIIVNDGSKDKTLKVAKDFWRQNINPNIdirlLSLLRNKG 149
                         90       100
                 ....*....|....*....|...
gi 499293549  70 LATARNTGIDTARGEYLTFLDGD 92
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDAD 172
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
6-133 1.07e-06

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: 48.61  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   6 VIVPFYNVQQYAPDTLKSLRANagdDF----EFILVDDCSRDETPDILARAERELPGA---VHVRHEKNG---GLATARN 75
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQ---DFegtlELSVFNDASTDKSAEIIEKWRKKLEDSgviVLVGSHNSPspkGVGYAKN 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499293549  76 TGIDTARGEYLTFLDGDDWLAPGYFP-QLLSAIEE----LGCDFVRtDHVQCTAR-ARTVNRVP 133
Cdd:cd06913   78 QAIAQSSGRYLCFLDSDDVMMPQRIRlQYEAALQHpnsiIGCQVRR-IPEDSTERyTRWINTLT 140
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
4-109 7.92e-04

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 40.32  E-value: 7.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549   4 LSVIVPFYN-VQQYAPDTLKSLRANAGDdfEFILVDDCSRDETPDILARAERelPGAVHVRHEKNGGLATARNTGIDTAR 82
Cdd:cd06434    2 VTVIIPVYDeDPDVFRECLRSILRQKPL--EIIVVTDGDDEPYLSILSQTVK--YGGIFVITVPHPGKRRALAEGIRHVT 77
                         90       100
                 ....*....|....*....|....*..
gi 499293549  83 GEYLTFLDGDDWLAPGYFPQLLSAIEE 109
Cdd:cd06434   78 TDIVVLLDSDTVWPPNALPEMLKPFED 104
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
19-104 2.49e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 38.80  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499293549  19 DTLKSLRANAGddfEFILVDDCSRdetPDILARAERELPGAVHVRHEKNGGLATARNTGIDTARG---EYLTFLDGDDWL 95
Cdd:cd02526   15 ELLAALAEQVD---KVVVVDNSSG---NDIELRLRLNSEKIELIHLGENLGIAKALNIGIKAALEngaDYVLLFDQDSVP 88

                 ....*....
gi 499293549  96 APGYFPQLL 104
Cdd:cd02526   89 PPDMVEKLL 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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