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Conserved domains on  [gi|727016474|ref|WP_033592465|]
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glycosyltransferase family 2 protein [Helicobacter pylori]

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

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|9445404|10521532|12200473|10508766
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 ...
 5-208 6.59e-95

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: 277.12  E-value: 6.59e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   5 SVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIACVVSEKDKGIYDAMNKGIKRASGDIIA 84
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  85 LLNSDDFYKDEFVLEKVVHEFENKNCDSVYADLVFVKPDRLEKVVRYYESgeFNPKTLLYGVVPAHPTLFVKKEIYERYG 164
Cdd:cd06433   81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPP--FLDKFLLYGMPICHQATFFRRSLFEKYG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 727016474 165 LYKTDYKISADFEMIIRLFVVQKIsFSYLKEVLVMMRTGGVSAN 208
Cdd:cd06433  159 GFDESYRIAADYDLLLRLLLAGKI-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 ...
 5-208 6.59e-95

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: 277.12  E-value: 6.59e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   5 SVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIACVVSEKDKGIYDAMNKGIKRASGDIIA 84
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  85 LLNSDDFYKDEFVLEKVVHEFENKNCDSVYADLVFVKPDRLEKVVRYYESgeFNPKTLLYGVVPAHPTLFVKKEIYERYG 164
Cdd:cd06433   81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPP--FLDKFLLYGMPICHQATFFRRSLFEKYG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 727016474 165 LYKTDYKISADFEMIIRLFVVQKIsFSYLKEVLVMMRTGGVSAN 208
Cdd:cd06433  159 GFDESYRIAADYDLLLRLLLAGKI-FKYLPEVLAAFRLGGVSST 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-179 1.49e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 123.27  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   1 MLKVSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDK---IACVVSEKDKGIYDAMNKGIKR 77
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKdprIRVIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  78 ASGDIIALLNSDDFYKDEFvLEKVVHEFENKNCDSVYADLVFvkpDRLEKVVRYYESGEFNPKTLLYGVVPAHPTL-FVK 156
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEK-LEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRLFNLVRLLTNLPDSTSGFrLFR 156

                        170       180
                 ....*....|....*....|...
gi 727016474 157 KEIYERYGLyktDYKISADFEMI 179
Cdd:COG0463  157 REVLEELGF---DEGFLEDTELL 176
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-148 1.99e-29

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: 108.64  E-value: 1.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474    5 SVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDK---IACVVSEKDKGIYDAMNKGIKRASGD 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKdprVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727016474   82 IIALLNSDDFYKDEFvLEKVVHEFENKNCDSVYADLVFVKPDRLEKVVRYYESGEFNPKTLLYGVVP 148
Cdd:pfam00535  81 YIAFLDADDEVPPDW-LEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG 146
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-90 2.72e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 62.37  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   2 LKVSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIA--CVVSEKDKGIYDAMNKGIKRAS 79
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhvRLLHQANAGVSVARNTGLAVAT 85

                         90
                 ....*....|.
gi 727016474  80 GDIIALLNSDD 90
Cdd:PRK10073  86 GKYVAFPDADD 96
 
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 ...
 5-208 6.59e-95

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: 277.12  E-value: 6.59e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   5 SVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIACVVSEKDKGIYDAMNKGIKRASGDIIA 84
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  85 LLNSDDFYKDEFVLEKVVHEFENKNCDSVYADLVFVKPDRLEKVVRYYESgeFNPKTLLYGVVPAHPTLFVKKEIYERYG 164
Cdd:cd06433   81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPP--FLDKFLLYGMPICHQATFFRRSLFEKYG 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 727016474 165 LYKTDYKISADFEMIIRLFVVQKIsFSYLKEVLVMMRTGGVSAN 208
Cdd:cd06433  159 GFDESYRIAADYDLLLRLLLAGKI-FKYLPEVLAAFRLGGVSST 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-179 1.49e-34

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 123.27  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   1 MLKVSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDK---IACVVSEKDKGIYDAMNKGIKR 77
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKdprIRVIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  78 ASGDIIALLNSDDFYKDEFvLEKVVHEFENKNCDSVYADLVFvkpDRLEKVVRYYESGEFNPKTLLYGVVPAHPTL-FVK 156
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEK-LEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRLFNLVRLLTNLPDSTSGFrLFR 156

                        170       180
                 ....*....|....*....|...
gi 727016474 157 KEIYERYGLyktDYKISADFEMI 179
Cdd:COG0463  157 REVLEELGF---DEGFLEDTELL 176
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-137 4.47e-30

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: 4.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYR---DKIACVVSEKDKGIYDAMNKGIKRASGDI 82
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAkkdPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 727016474  83 IALLNSDDFYKDEFVLEKVVHEFENKNCDSVYAD-LVFVKPDRLEKVVRYYESGEF 137
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPgNLLFRRELLEEIGGFDEALLS 136
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-148 1.99e-29

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: 108.64  E-value: 1.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474    5 SVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDK---IACVVSEKDKGIYDAMNKGIKRASGD 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKdprVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727016474   82 IIALLNSDDFYKDEFvLEKVVHEFENKNCDSVYADLVFVKPDRLEKVVRYYESGEFNPKTLLYGVVP 148
Cdd:pfam00535  81 YIAFLDADDEVPPDW-LEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG 146
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 3-182 3.41e-24

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: 96.92  E-value: 3.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   3 KVSVITACFNSEKTIEDTILSVLHQTY--KNIEYIIIDGSSADSTLEIIQKYRDKIACV--VSEKDKGIYDAMNKGIKRA 78
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIrlIDNPKRIQSAGLNIGIRNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  79 SGDIIALLNSDDFYKDEFVLEkVVHEFENKNCDSVYADLVFVKPDRLEKVVRYYESGEFNPKTLLY-------GVVPAHP 151
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILE-LVEALKRTGADNVGGPMETIGESKFQKAIAVAQSSPLGSGGSAYrggavkiGYVDTVH 159

                        170       180       190
                 ....*....|....*....|....*....|.
gi 727016474 152 TLFVKKEIYERYGLYKTDYKISADFEMIIRL 182
Cdd:cd02525  160 HGAYRREVFEKVGGFDESLVRNEDAELNYRL 190
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-182 4.15e-23

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: 95.19  E-value: 4.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   1 MLKVSVITACFNSEKTIEDTILSVLHQTY--KNIEYIIIDGSSADSTLEIIQKYRDK---IACVVSEKDKGIYDAMNKGI 75
Cdd:COG1215   28 LPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEyprVRVIERPENGGKAAALNAGL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  76 KRASGDIIALLNSDDfykdefvlekvvhefenkncdsvyadlvFVKPDRLEKVVRYYEsgefNPKTLLYGvvpahPTLFV 155
Cdd:COG1215  108 KAARGDIVVFLDADT----------------------------VLDPDWLRRLVAAFA----DPGVGASG-----ANLAF 150

                        170       180
                 ....*....|....*....|....*..
gi 727016474 156 KKEIYERYGLYKTDyKISADFEMIIRL 182
Cdd:COG1215  151 RREALEEVGGFDED-TLGEDLDLSLRL 176
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-105 1.19e-20

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 86.59  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   1 MLKVSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYR-DKIACVVSEKDKGIYDAMNKGIKRAS 79
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAfPRVRVIRNPENLGFAAARNLGLRAAG 81

                         90       100
                 ....*....|....*....|....*.
gi 727016474  80 GDIIALLNSDDFYKDEFvLEKVVHEF 105
Cdd:COG1216   82 GDYLLFLDDDTVVEPDW-LERLLAAA 106
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-182 3.10e-20

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: 85.33  E-value: 3.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   3 KVSVITACFNS-EKTIEDTILSVLHQTYKNIEYIIIDG-SSADSTLEIIQKYR---DKIACVVSEKDKGIYDAMNKGIKR 77
Cdd:cd04184    2 LISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDaSTDPEVKRVLKKYAaqdPRIKVVFREENGGISAATNSALEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  78 ASGDIIALLNSDDFYKDEFVLEKVVHEFENKNCDSVYAD-----------LVFVKPDrlekvvryyesgeFNPKTLLYGV 146
Cdd:cd04184   82 ATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDedkideggkrsEPFFKPD-------------WSPDLLLSQN 148

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 727016474 147 VPAHPTLFvKKEIYERYGLYKTDYKISADFEMIIRL 182
Cdd:cd04184  149 YIGHLLVY-RRSLVRQVGGFREGFEGAQDYDLVLRV 183
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 3-161 1.43e-16

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 76.47  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   3 KVSVITACFNSEKTIEDTILSVLHQTYKN--IEYIIIDGSSADSTLEIIQKYRDKIACVVSEKD-KGIYDAMNKGIKRAS 79
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADKGVKLLRFPErRGKAAALNRALALAT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  80 GDIIALLNSDDFYKDEfVLEKVVHEFENKNCDSVYADLVFVKPD----------RLEKVVRYYESgefnpktLLYGVVPA 149
Cdd:cd06439  110 GEIVVFTDANALLDPD-ALRLLVRHFADPSVGAVSGELVIVDGGgsgsgeglywKYENWLKRAES-------RLGSTVGA 181

                        170
                 ....*....|...
gi 727016474 150 HPTLF-VKKEIYE 161
Cdd:cd06439  182 NGAIYaIRRELFR 194
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 6-109 1.75e-15

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: 72.26  E-value: 1.75e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIAC----VVSEKDKGIYDAMNKGIKRASGD 81
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRrvlvVRDKENGGKAGALNAGLRHAKGD 80

                         90       100
                 ....*....|....*....|....*...
gi 727016474  82 IIALLNSDDFYKDEFVLEKVVHEFENKN 109
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADPK 108
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-143 5.50e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 68.81  E-value: 5.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   5 SVITACFNSEKTIEDTILSVLHQTYKNIEyIII--DGSSaDSTLEIIQKYRDK----IACVVSEKDKGIYDAMNKGIKRA 78
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDE-LIIsdDGST-DGTVEIIKEYIDKdpfiIILIRNGKNLGVARNFESLLQAA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 727016474  79 SGDIIALLNSDD-FYKDEfvLEKVV-HEFENKNCDSVYADLVFVKPDRLEKVVRYYESGEFNPKTLL 143
Cdd:cd04196   79 DGDYVFFCDQDDiWLPDK--LERLLkAFLKDDKPLLVYSDLELVDENGNPIGESFFEYQKIKPGTSF 143
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-109 3.35e-13

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 65.66  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIACVVSEKDKGIYDAMNKGIKRASGDIIAL 85
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLL 80

                         90       100
                 ....*....|....*....|....
gi 727016474  86 LNSDDFYKDEFVLEKVVHEFENKN 109
Cdd:cd04186   81 LNPDTVVEPGALLELLDAAEQDPD 104
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 6-115 3.88e-13

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: 65.67  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDT---ILSVLHQTYkNIEYIIIDGSSADSTLEIIQKYRDK---IACVVSEKDKGIYDAMNKGIKRAS 79
Cdd:cd04179    1 VVIPAYNEEENIPELverLLAVLEEGY-DYEIIVVDDGSTDGTAEIARELAARvprVRVIRLSRNFGKGAAVRAGFKAAR 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 727016474  80 GDIIALLNSDDFYKDEFvLEKVVHEFENKNCDSVYA 115
Cdd:cd04179   80 GDIVVTMDADLQHPPED-IPKLLEKLLEGGADVVIG 114
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 4-182 1.42e-12

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: 64.90  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   4 VSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIacVVSEKDKGIydAMNKGIKRASGDII 83
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVV--ISSPKGRAR--QMNAGAAAARGDWL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  84 ALLNSDDFYKDEFVlEKVVHEFENKNCDSVYADLVFVKPDRLekvVRYYESGEF---NPKTLLYGvvpaHPTLFVKKEIY 160
Cdd:cd02522   77 LFLHADTRLPPDWD-AAIIETLRADGAVAGAFRLRFDDPGPR---LRLLELGANlrsRLFGLPYG----DQGLFIRRELF 148

                        170       180
                 ....*....|....*....|..
gi 727016474 161 ERYGLYKTDYkISADFEMIIRL 182
Cdd:cd02522  149 EELGGFPELP-LMEDVELVRRL 169
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-90 2.72e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 62.37  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   2 LKVSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIA--CVVSEKDKGIYDAMNKGIKRAS 79
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhvRLLHQANAGVSVARNTGLAVAT 85

                         90
                 ....*....|.
gi 727016474  80 GDIIALLNSDD 90
Cdd:PRK10073  86 GKYVAFPDADD 96
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 6-89 6.90e-08

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: 50.94  E-value: 6.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDT---ILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIACVvsekdKGI--------YDAMNKG 74
Cdd:cd04187    1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRV-----KVIrlsrnfgqQAALLAG 75

                         90
                 ....*....|....*
gi 727016474  75 IKRASGDIIALLNSD 89
Cdd:cd04187   76 LDHARGDAVITMDAD 90
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-182 1.31e-07

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: 50.83  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474    4 VSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQ----KYRD-KIACVVSEKDKGIY---DAMNKGI 75
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEeiaaRFPDvRLRVIRNARLLGPTgksRGLNHGF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   76 KRASGDIIALLNSDDFYKDEFvLEKVVHEFENKNCDSVYADlVFVK--------PDRLEKVVRYyesGEFNPKTLLYGVV 147
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGT-LKKYVQYFDSPKVGAVGTP-VFSLnrstmlsaLGALEFALRH---LRMMSLRLALGVL 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 727016474  148 PAHPTLFV-KKEIYERYGLYKTDYKISADFEMIIRL 182
Cdd:pfam13641 159 PLSGAGSAiRREVLKELGLFDPFFLLGDDKSLGRRL 194
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-89 1.63e-07

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 50.75  E-value: 1.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDTILSVLHQTY--KNIEYIIIDGSSADSTLEIIQKYRDK------IACVVSEKDKGIYDAMNKGIKR 77
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAKpnfqlkILNNSRVSISGKKNALTTAIKA 80

                         90
                 ....*....|..
gi 727016474  78 ASGDIIALLNSD 89
Cdd:cd04192   81 AKGDWIVTTDAD 92
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 6-90 5.20e-07

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: 48.99  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDTILSVLHQTYKN-IEYIIIDGSSADSTLEIIQKYRDK-----IACVVSEKD----KGIYDAMNKGI 75
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKledsgVIVLVGSHNspspKGVGYAKNQAI 80

                         90
                 ....*....|....*
gi 727016474  76 KRASGDIIALLNSDD 90
Cdd:cd06913   81 AQSSGRYLCFLDSDD 95
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 6-94 1.43e-06

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: 47.19  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIACVVS---EKDKGIYDA--MNKGIKRASG 80
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKhvwQEDEGFRKAkiRNKAIAAAKG 80

                         90
                 ....*....|....*....
gi 727016474  81 DIIALLNSD-----DFYKD 94
Cdd:cd06420   81 DYLIFIDGDciphpDFIAD 99
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 6-113 1.63e-06

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: 47.56  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIE---DTILSVLHQTYK-NIEYIIIDGSSADSTLEIIQKYRDK----IACVVSEKDKGIYDAMNKGIKR 77
Cdd:cd04188    1 VVIPAYNEEKRLPptlEEAVEYLEERPSfSYEIIVVDDGSKDGTAEVARKLARKnpalIRVLTLPKNRGKGGAVRAGMLA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 727016474  78 ASGDIIALLNSD---DFykDEFvlEKVVHEFENKNCDSV 113
Cdd:cd04188   81 ARGDYILFADADlatPF--EEL--EKLEEALKTSGYDIA 115
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 5-201 4.32e-06

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: 46.15  E-value: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   5 SVITACFNSEKT--IEDTILSVLHQTYKNIEYIII-DGSSADSTLEIIQKYRDK--IACVVSEKDKGIYDAMNKGIKRAS 79
Cdd:cd04195    1 SVLMSVYIKEKPefLREALESILKQTLPPDEVVLVkDGPVTQSLNEVLEEFKRKlpLKVVPLEKNRGLGKALNEGLKHCT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  80 GDIIALLNSDDFYkdefvlekvvhefenkncdsvyadlvfvKPDRLEKVVRYYESG-------------EFNPKTLLYGV 146
Cdd:cd04195   81 YDWVARMDTDDIS----------------------------LPDRFEKQLDFIEKNpeidivgggvlefDSDGNDIGKRR 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 727016474 147 VPA----------------HPTLFVKKEIYERYGLYKTDYKISaDFEMIIRLfVVQKISFSYLKEVLVMMR 201
Cdd:cd04195  133 LPTshddilkfarrrspfnHPTVMFRKSKVLAVGGYQDLPLVE-DYALWARM-LANGARFANLPEILVKAR 201
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 3-99 1.51e-05

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: 44.97  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   3 KVSVITACFNSEKTIEDTILSVLHQTyknIEYIIIDGSSADSTLEIIQKYRDKiacVVSEKDKGIYDAMNKGIKRASGDI 82
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAV---DEIIVVDSGSTDRTVEIAKEYGAK---VYQRWWDGFGAQRNFALELATNDW 74

                         90
                 ....*....|....*..
gi 727016474  83 IALLNSDDFYKDEFVLE 99
Cdd:cd02511   75 VLSLDADERLTPELADE 91
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-193 1.62e-05

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 44.55  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITacFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSADSTLEII--QKYRDKIACVVSEKDKGIYDAMNKGIKRA--SG- 80
Cdd:cd04185    3 VVT--YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLtsLGDLDNIVYLRLPENLGGAGGFYEGVRRAyeLGy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  81 DIIALLNsDDFYKDEFVLEKVVHEFENKNCDsvyadlvFVKPDrlekvvRYYESGEFNpktllyGVvpahptlFVKKEIY 160
Cdd:cd04185   81 DWIWLMD-DDAIPDPDALEKLLAYADKDNPQ-------FLAPL------VLDPDGSFV------GV-------LISRRVV 133

                        170       180       190
                 ....*....|....*....|....*....|....
gi 727016474 161 ERYGLYKTDYKISA-DFEMIIRLfvvQKISFSYL 193
Cdd:cd04185  134 EKIGLPDKEFFIWGdDTEYTLRA---SKAGPGIY 164
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
4-184 2.98e-05

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 44.21  E-value: 2.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   4 VSVITACFNSEKTIEDTILSVLHQTYKNIEYIIIDGSSadSTLEIIQKYRD-----KIACVVSEKDKGIYDAMNKGIKRA 78
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCS--TSWEQLQQYVTalndpRITYIHNDINSGACAVRNQAIMLA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474  79 SGDIIALLNSDDFYKDE----FVLEK---VVHEFENKNcDSVYADLVFVKPDRLEkvvryyesgefnpktlLYGVVPAHP 151
Cdd:PRK10018  85 QGEYITGIDDDDEWTPNrlsvFLAHKqqlVTHAFLYAN-DYVCQGEVYSQPASLP----------------LYPKSPYSR 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 727016474 152 TLFVKKEIYE----------RYGLYKTDYKISADFEMIIRLFV 184
Cdd:PRK10018 148 RLFYKRNIIGnqvftwawrfKECLFDTELKAAQDYDIFLRMVV 190
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 5-91 3.41e-05

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: 44.19  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474    5 SVITACFNSEKT--IEDTILSVLHQTYKNIEYIIIDGSSADSTLEIIQKYRDKIACV----VSEKDKGIYDAMNKGIKRA 78
Cdd:pfam10111   1 SVVIPVYNGEKThwIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVyypnAPDTTYSLAASRNRGTSHA 80

                          90
                  ....*....|...
gi 727016474   79 SGDIIALLNSDDF 91
Cdd:pfam10111  81 IGEYISFIDGDCL 93
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 6-113 5.36e-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: 43.29  E-value: 5.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   6 VITACFNSEKTIEDtILSVLHQTYKNIEY--IIIDGSSADSTLEIIQKYR---DKIACVVSEKDKGIYDAMNKGIKRASG 80
Cdd:cd06442    1 IIIPTYNERENIPE-LIERLDAALKGIDYeiIVVDDNSPDGTAEIVRELAkeyPRVRLIVRPGKRGLGSAYIEGFKAARG 79

                         90       100       110
                 ....*....|....*....|....*....|...
gi 727016474  81 DIIALLNSdDFYKDEFVLEKVVHEFENKNCDSV 113
Cdd:cd06442   80 DVIVVMDA-DLSHPPEYIPELLEAQLEGGADLV 111
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-89 1.30e-04

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 41.99  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   1 MLKVSVITACFNSEKTIEdTILSVLHQT---YKNIEYIIIDGSSADSTLEIIQKYR-----DKIACVVSEKDKGIYDAMN 72
Cdd:PLN02726   8 AMKYSIIVPTYNERLNIA-LIVYLIFKAlqdVKDFEIIVVDDGSPDGTQDVVKQLQkvygeDRILLRPRPGKLGLGTAYI 86

                         90
                 ....*....|....*..
gi 727016474  73 KGIKRASGDIIALLNSD 89
Cdd:PLN02726  87 HGLKHASGDFVVIMDAD 103
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 5-88 1.85e-04

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 41.81  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   5 SVITACFNSEK-TIEDTILSVLHQTYKN--IEYIIIDGSSADSTL-----EIIQKYRDKIACVVSEKDKGIYDAMNKGIK 76
Cdd:cd02510    1 SVIIIFHNEALsTLLRTVHSVINRTPPEllKEIILVDDFSDKPELkllleEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80

                         90
                 ....*....|..
gi 727016474  77 RASGDIIALLNS 88
Cdd:cd02510   81 AATGDVLVFLDS 92
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-89 1.61e-03

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 39.13  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727016474   1 MLKVSVITACFNSEKTIEDTILSVLHQTYKNI--EYIIIDGSSADSTLEIIqkyRDKIACVVSEKD----------KGiy 68
Cdd:PRK13915  30 GRTVSVVLPALNEEETVGKVVDSIRPLLMEPLvdELIVIDSGSTDATAERA---AAAGARVVSREEilpelpprpgKG-- 104

                         90       100
                 ....*....|....*....|.
gi 727016474  69 DAMNKGIKRASGDIIALLNSD 89
Cdd:PRK13915 105 EALWRSLAATTGDIVVFVDAD 125
 
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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