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Conserved domains on  [gi|2185637663|ref|WP_236608268|]
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glycosyltransferase family 2 protein [Dictyoglomus thermophilum]

Protein Classification

glycosyltransferase( domain architecture ID 11440269)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-309 3.82e-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: 102.51  E-value: 3.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTY--KPYEVIVVNDNSEDDTEGVGERNGARV--ISLYEEPPEGwvGKNWAIWNGYLESR 77
Cdd:COG1215    34 IIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYprVRVIERPENG--GKAAALNAGLKAAR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  78 GDILLFLDADVEPSSEFIEVMLSsyeryggliscwpyqrfekfyehlnfafnlvsvfsmAFLGKKEGAFGPAMMISRKDY 157
Cdd:COG1215   112 GDIVVFLDADTVLDPDWLRRLVA------------------------------------AFADPGVGASGANLAFRREAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663 158 ERIGGHKEvrNKIVEDMEFAKKCLEEGISVnNFLGGEYIKFRMyPHGIKDLFQGFSKNmAKGAFSINIVNFLLIFLYMTG 237
Cdd:COG1215   156 EEVGGFDE--DTLGEDLDLSLRLLRAGYRI-VYVPDAVVYEEA-PETLRALFRQRRRW-ARGGLQLLLKHRPLLRPRRLL 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2185637663 238 VYGSIFYFRNTIFNFLYILYAIQFSVIQRRLGDYKWYDFLFYPLHFLFFLLVFTYSILRVFFVKTVVWKGRK 309
Cdd:COG1215   231 LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTP 302
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-309 3.82e-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: 102.51  E-value: 3.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTY--KPYEVIVVNDNSEDDTEGVGERNGARV--ISLYEEPPEGwvGKNWAIWNGYLESR 77
Cdd:COG1215    34 IIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYprVRVIERPENG--GKAAALNAGLKAAR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  78 GDILLFLDADVEPSSEFIEVMLSsyeryggliscwpyqrfekfyehlnfafnlvsvfsmAFLGKKEGAFGPAMMISRKDY 157
Cdd:COG1215   112 GDIVVFLDADTVLDPDWLRRLVA------------------------------------AFADPGVGASGANLAFRREAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663 158 ERIGGHKEvrNKIVEDMEFAKKCLEEGISVnNFLGGEYIKFRMyPHGIKDLFQGFSKNmAKGAFSINIVNFLLIFLYMTG 237
Cdd:COG1215   156 EEVGGFDE--DTLGEDLDLSLRLLRAGYRI-VYVPDAVVYEEA-PETLRALFRQRRRW-ARGGLQLLLKHRPLLRPRRLL 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2185637663 238 VYGSIFYFRNTIFNFLYILYAIQFSVIQRRLGDYKWYDFLFYPLHFLFFLLVFTYSILRVFFVKTVVWKGRK 309
Cdd:COG1215   231 LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTP 302
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
2-184 2.06e-18

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: 80.63  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGERNGARVISLYEEPPEGWVGKNWAIWNGYLESRGDIL 81
Cdd:cd00761     2 IIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  82 LFLDADVEPSSEFIEVMLSSYERYGGLISCwpyqrfekfyehlnfafnlvsvfsmaflgkkegAFGPAMMISRKDYERIG 161
Cdd:cd00761    82 LFLDADDLLLPDWLERLVAELLADPEADAV---------------------------------GGPGNLLFRRELLEEIG 128
                         170       180
                  ....*....|....*....|...
gi 2185637663 162 GHKEVRNKIVEDMEFAKKCLEEG 184
Cdd:cd00761   129 GFDEALLSGEEDDDFLLRLLRGG 151
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
2-159 3.48e-16

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: 74.74  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGV-----GERNGARVISLyeepPEGWvGKNWAIWNGYLES 76
Cdd:pfam00535   3 IIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIaeeyaKKDPRVRVIRL----PENR-GKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  77 RGDILLFLDADVEPSSEFIEVMLSSYERYG-GLISCWPYQRFEKFYE---HLNFAFNLVSVFSMAFLGKKEGAF--GPAM 150
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGaDVVVGSRYVIFGETGEyrrASRITLSRLPFFLGLRLLGLNLPFliGGFA 157

                  ....*....
gi 2185637663 151 MISRKDYER 159
Cdd:pfam00535 158 LYRREALEE 166
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
1-95 3.63e-11

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 62.63  E-value: 3.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEEENLGKLLSLLKKQTYKPY--EVIVVNDNSEDDTEGVGERNGARVIS----LYEEPPEGwvGKNWAIWNGYL 74
Cdd:PRK13915   35 VVLPALNEEETVGKVVDSIRPLLMEPLvdELIVIDSGSTDATAERAAAAGARVVSreeiLPELPPRP--GKGEALWRSLA 112
                          90       100
                  ....*....|....*....|..
gi 2185637663  75 ESRGDILLFLDAD-VEPSSEFI 95
Cdd:PRK13915  113 ATTGDIVVFVDADlINFDPMFV 134
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
2-179 1.75e-09

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 56.75  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYkPYEVIVVNDNSEDDTEGVGERNGARVISlyeEPPegwvGK----NWaiwnGYLESR 77
Cdd:TIGR04283   4 IIPVLNEAATLPELLADLQALRG-DAEVIVVDGGSTDGTVEIARSLGAKVIH---SPK----GRarqmNA----GAALAK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  78 GDILLFLDADVEPSSEFIEVM---LSSYERYGGliscwpyqRFE-KFYEHlNFAFNLVSvFSMAFLGKKEG-AFG-PAMM 151
Cdd:TIGR04283  72 GDILLFLHADTRLPKDFLEAIrraLAKPGYVAG--------AFDlRFDGP-GLLLRLIE-WGVNLRSRLTGiPYGdQGLF 141
                         170       180
                  ....*....|....*....|....*...
gi 2185637663 152 ISRKDYERIGGHKEVrnKIVEDMEFAKK 179
Cdd:TIGR04283 142 VRRSLFEQIGGFPDI--PLMEDIELSRR 167
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
2-309 3.82e-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: 102.51  E-value: 3.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTY--KPYEVIVVNDNSEDDTEGVGERNGARV--ISLYEEPPEGwvGKNWAIWNGYLESR 77
Cdd:COG1215    34 IIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYprVRVIERPENG--GKAAALNAGLKAAR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  78 GDILLFLDADVEPSSEFIEVMLSsyeryggliscwpyqrfekfyehlnfafnlvsvfsmAFLGKKEGAFGPAMMISRKDY 157
Cdd:COG1215   112 GDIVVFLDADTVLDPDWLRRLVA------------------------------------AFADPGVGASGANLAFRREAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663 158 ERIGGHKEvrNKIVEDMEFAKKCLEEGISVnNFLGGEYIKFRMyPHGIKDLFQGFSKNmAKGAFSINIVNFLLIFLYMTG 237
Cdd:COG1215   156 EEVGGFDE--DTLGEDLDLSLRLLRAGYRI-VYVPDAVVYEEA-PETLRALFRQRRRW-ARGGLQLLLKHRPLLRPRRLL 230
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2185637663 238 VYGSIFYFRNTIFNFLYILYAIQFSVIQRRLGDYKWYDFLFYPLHFLFFLLVFTYSILRVFFVKTVVWKGRK 309
Cdd:COG1215   231 LFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTP 302
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
2-178 2.63e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 84.37  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGERNGA-----RVISLyeeppEGWVGKNWAIWNGYLES 76
Cdd:COG0463     7 VIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAkdpriRVIRL-----ERNRGKGAARNAGLAAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  77 RGDILLFLDADVEPSSEFIEVMLSSYERYG-GLISCWPYQRF--EKFYEHLNFAFNLVSVFSmaflgKKEGAFGPAMMIS 153
Cdd:COG0463    82 RGDYIAFLDADDQLDPEKLEELVAALEEGPaDLVYGSRLIREgeSDLRRLGSRLFNLVRLLT-----NLPDSTSGFRLFR 156
                         170       180
                  ....*....|....*....|....*
gi 2185637663 154 RKDYERIGghkeVRNKIVEDMEFAK 178
Cdd:COG0463   157 REVLEELG----FDEGFLEDTELLR 177
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
2-184 2.06e-18

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: 80.63  E-value: 2.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGERNGARVISLYEEPPEGWVGKNWAIWNGYLESRGDIL 81
Cdd:cd00761     2 IIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  82 LFLDADVEPSSEFIEVMLSSYERYGGLISCwpyqrfekfyehlnfafnlvsvfsmaflgkkegAFGPAMMISRKDYERIG 161
Cdd:cd00761    82 LFLDADDLLLPDWLERLVAELLADPEADAV---------------------------------GGPGNLLFRRELLEEIG 128
                         170       180
                  ....*....|....*....|...
gi 2185637663 162 GHKEVRNKIVEDMEFAKKCLEEG 184
Cdd:cd00761   129 GFDEALLSGEEDDDFLLRLLRGG 151
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
2-176 1.91e-16

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 76.94  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKP--YEVIVVNDNSEDDT----EGVGERNGARVISLyEEPPEGWVGKNWAIWNGYLE 75
Cdd:cd04192     2 VIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTvqilEFAAAKPNFQLKIL-NNSRVSISGKKNALTTAIKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  76 SRGDILLFLDADVEPSSEFIEVMLSSYERY------GGLISCWPYQRFEKFyEHLNFAFNLVSVFSMAFLGKKEGAFGPA 149
Cdd:cd04192    81 AKGDWIVTTDADCVVPSNWLLTFVAFIQKEqiglvaGPVIYFKGKSLLAKF-QRLDWLSLLGLIAGSFGLGKPFMCNGAN 159
                         170       180
                  ....*....|....*....|....*..
gi 2185637663 150 MMISRKDYERIGGHKEVRNKIVEDMEF 176
Cdd:cd04192   160 MAYRKEAFFEVGGFEGNDHIASGDDEL 186
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
2-159 3.48e-16

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: 74.74  E-value: 3.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGV-----GERNGARVISLyeepPEGWvGKNWAIWNGYLES 76
Cdd:pfam00535   3 IIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIaeeyaKKDPRVRVIRL----PENR-GKAGARNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  77 RGDILLFLDADVEPSSEFIEVMLSSYERYG-GLISCWPYQRFEKFYE---HLNFAFNLVSVFSMAFLGKKEGAF--GPAM 150
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLVEALEEDGaDVVVGSRYVIFGETGEyrrASRITLSRLPFFLGLRLLGLNLPFliGGFA 157

                  ....*....
gi 2185637663 151 MISRKDYER 159
Cdd:pfam00535 158 LYRREALEE 166
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
2-173 7.27e-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: 74.19  E-value: 7.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGERNGARVIS--LYEEPPEGwVGKNWAIWNGYLESRGD 79
Cdd:cd06423     2 IVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRrvLVVRDKEN-GGKAGALNAGLRHAKGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  80 ILLFLDADVEPSSEFIEVMLSSYERYGGLI----SCWPYQRFEKFYEHLNFAFNLVSVFSM----AFLGKKEGAFGPAMM 151
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGavqgRVRVRNGSENLLTRLQAIEYLSIFRLGrraqSALGGVLVLSGAFGA 160
                         170       180
                  ....*....|....*....|..
gi 2185637663 152 ISRKDYERIGGHKEvrNKIVED 173
Cdd:cd06423   161 FRREALREVGGWDE--DTLTED 180
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
2-179 6.75e-14

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: 69.52  E-value: 6.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGERNGARVISlyeEPPegwvGK----NwaiwNGYLESR 77
Cdd:cd02522     4 IIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVVIS---SPK----GRarqmN----AGAAAAR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  78 GDILLFLDADVEPSSEFIEV---MLSSYERYGGlisCWPYqRFE------KFYEHLNFA-FNLVSVfsmaflgkkegAFG 147
Cdd:cd02522    73 GDWLLFLHADTRLPPDWDAAiieTLRADGAVAG---AFRL-RFDdpgprlRLLELGANLrSRLFGL-----------PYG 137
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2185637663 148 -PAMMISRKDYERIGGHKEVrnKIVEDMEFAKK 179
Cdd:cd02522   138 dQGLFIRRELFEELGGFPEL--PLMEDVELVRR 168
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
49-187 4.91e-13

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 66.15  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  49 ARVISLYEEPPEGWVGKNWAIWNGYLESRGDILLFLDADVEPSSEFIEVMLSSYERYG-GLISCWPY-QRFEKFYEHL-N 125
Cdd:pfam13506   2 SVRALVVGGPPVGVNPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKvGLVTSPPVgSDPKGLAAALeA 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2185637663 126 FAFNLVSVFSMAFLGKKEGAFGPAMMISRKDYERIGGHKEVRNKIVEDMEFAKKCLEEGISV 187
Cdd:pfam13506  82 AFFNTLAGVLQAALSGIGFAVGMSMAFRRADLERIGGFEALADYLAEDYALGKLLRAAGLKV 143
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
1-95 3.63e-11

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 62.63  E-value: 3.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEEENLGKLLSLLKKQTYKPY--EVIVVNDNSEDDTEGVGERNGARVIS----LYEEPPEGwvGKNWAIWNGYL 74
Cdd:PRK13915   35 VVLPALNEEETVGKVVDSIRPLLMEPLvdELIVIDSGSTDATAERAAAAGARVVSreeiLPELPPRP--GKGEALWRSLA 112
                          90       100
                  ....*....|....*....|..
gi 2185637663  75 ESRGDILLFLDAD-VEPSSEFI 95
Cdd:PRK13915  113 ATTGDIVVFVDADlINFDPMFV 134
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
2-87 6.03e-11

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: 60.28  E-value: 6.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEEN--LGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGERNGARVISLYEEPPEGWVGKNWAIWNGYLESRGD 79
Cdd:cd04179     2 VIPAYNEEENipELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARGD 81

                  ....*...
gi 2185637663  80 ILLFLDAD 87
Cdd:cd04179    82 IVVTMDAD 89
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
22-100 2.79e-10

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 58.85  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  22 QTYKPYEVIVVNDNSEDDT-EGVGERNGARVISLYEEPPEGWV-GKNWAIwngyLESRGDILLFLDADVEPSSEFIEVML 99
Cdd:COG1216    28 QTYPPFEVIVVDNGSTDGTaELLAALAFPRVRVIRNPENLGFAaARNLGL----RAAGGDYLLFLDDDTVVEPDWLERLL 103

                  .
gi 2185637663 100 S 100
Cdd:COG1216   104 A 104
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
2-179 1.75e-09

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 56.75  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYkPYEVIVVNDNSEDDTEGVGERNGARVISlyeEPPegwvGK----NWaiwnGYLESR 77
Cdd:TIGR04283   4 IIPVLNEAATLPELLADLQALRG-DAEVIVVDGGSTDGTVEIARSLGAKVIH---SPK----GRarqmNA----GAALAK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  78 GDILLFLDADVEPSSEFIEVM---LSSYERYGGliscwpyqRFE-KFYEHlNFAFNLVSvFSMAFLGKKEG-AFG-PAMM 151
Cdd:TIGR04283  72 GDILLFLHADTRLPKDFLEAIrraLAKPGYVAG--------AFDlRFDGP-GLLLRLIE-WGVNLRSRLTGiPYGdQGLF 141
                         170       180
                  ....*....|....*....|....*...
gi 2185637663 152 ISRKDYERIGGHKEVrnKIVEDMEFAKK 179
Cdd:TIGR04283 142 VRRSLFEQIGGFPDI--PLMEDIELSRR 167
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
1-176 3.73e-09

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 55.30  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEEENLGKLLSLLKKQTYKP--YEVIVVNDNSEDDTEGVGERNGARVISlYEEPPEgwVGKNWAI-WN-GYLES 76
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPRelYRIFVVADNCTDDTAQVARAAGATVLE-RHDPER--RGKGYALdFGfRHLLN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  77 RG---DILLFLDADVEPSSEFIEVM----------LSSYERY----GGLIScwpyqrfeKFYEHLNFAFNLVSVFSMAFL 139
Cdd:cd06438    78 LAddpDAVVVFDADNLVDPNALEELnarfaagarvVQAYYNSknpdDSWIT--------RLYAFAFLVFNRLRPLGRSNL 149
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2185637663 140 GKKEGAFGPAMMISRKDYERIG--GHkevrnKIVEDMEF 176
Cdd:cd06438   150 GLSCQLGGTGMCFPWAVLRQAPwaAH-----SLTEDLEF 183
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
2-87 3.40e-08

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: 52.95  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEE----NLGKLLSLLKKQTYKPYEVIVVNDNSEDDT----EGVGERNGA--RVISLyeeppEGWVGKNWAIWN 71
Cdd:cd04188     2 VIPAYNEEKrlppTLEEAVEYLEERPSFSYEIIVVDDGSKDGTaevaRKLARKNPAliRVLTL-----PKNRGKGGAVRA 76
                          90
                  ....*....|....*.
gi 2185637663  72 GYLESRGDILLFLDAD 87
Cdd:cd04188    77 GMLAARGDYILFADAD 92
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
2-124 1.17e-07

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: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLL---SLLKKQTYKPYEVIVVNDNSEDDTEGV-----GERNGARVISL---YeeppegwvGKNWAIW 70
Cdd:cd04187     2 VVPVYNEEENLPELYerlKAVLESLGYDYEIIFVDDGSTDRTLEIlrelaARDPRVKVIRLsrnF--------GQQAALL 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2185637663  71 NGYLESRGDILLFLDADVEPSSEFIEVMLSSYE------------RYGGLISCWPYQRFEKFYEHL 124
Cdd:cd04187    74 AGLDHARGDAVITMDADLQDPPELIPEMLAKWEegydvvygvrknRKESWLKRLTSKLFYRLINKL 139
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-106 3.46e-07

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: 50.31  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTY--KPYEVIVVNDNSEDDTEGVGERNGAR--VISLYEEP----PEGWvgkNWAIwngy 73
Cdd:cd02525     5 IIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKdpRIRLIDNPkriqSAGL---NIGI---- 77
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2185637663  74 LESRGDILLFLDADVEPSSEFIEVMLSSYERYG 106
Cdd:cd02525    78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRTG 110
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
1-87 5.97e-07

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: 49.89  E-value: 5.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEEENLGKLLSLLKKQTYKP--YEVIVVNDNSEDDTEGVGERNGARVISLYEEPPEGwvGKNWAIWNGYLESRG 78
Cdd:cd06439    33 IIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADKGVKLLRFPERR--GKAAALNRALALATG 110

                  ....*....
gi 2185637663  79 DILLFLDAD 87
Cdd:cd06439   111 EIVVFTDAN 119
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
22-162 6.18e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 48.71  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  22 QTYKPYEVIVVNDNSEDDTEGVGERNGARVISLYEEPPEGW-VGKNWAIwngyLESRGDILLFLDADVEPSSEFIEVMLS 100
Cdd:cd04186    22 QTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFgAGNNQGI----REAKGDYVLLLNPDTVVEPGALLELLD 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2185637663 101 SYERYggliscwpyqrfekfyehlnfafnlvsvfsmaflgKKEGAFGP-----AMMISRKDYERIGG 162
Cdd:cd04186    98 AAEQD-----------------------------------PDVGIVGPkvsgaFLLVRREVFEEVGG 129
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
1-87 7.21e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 47.07  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEE--------ENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGER---------NGARVISLYEEppegwV 63
Cdd:PTZ00260   74 IVIPAYNEEdrlpkmlkETIKYLESRSRKDPKFKYEIIIVNDGSKDKTLKVAKDfwrqninpnIDIRLLSLLRN-----K 148
                          90       100
                  ....*....|....*....|....
gi 2185637663  64 GKNWAIWNGYLESRGDILLFLDAD 87
Cdd:PTZ00260  149 GKGGAVRIGMLASRGKYILMVDAD 172
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
22-188 1.32e-05

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


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 45.28  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  22 QTYKPYEVIVVNDNSEDD-----TEGVGERNGARVISLYEEPPEGWVGKNWAIWNGYLESRGDILLFLDADVEPSSEFIE 96
Cdd:cd02520    26 QDYPKYEILFCVQDEDDPaipvvRKLIAKYPNVDARLLIGGEKVGINPKVNNLIKGYEEARYDILVISDSDISVPPDYLR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  97 VMLSSYERYG-GLISCWPyqrfekfyehlnfafnlvsvfsmaflgkkegAFGPAMMISRKDYERIGGHKEVRNKIVEDME 175
Cdd:cd02520   106 RMVAPLMDPGvGLVTCLC-------------------------------AFGKSMALRREVLDAIGGFEAFADYLAEDYF 154
                         170
                  ....*....|...
gi 2185637663 176 FAKKCLEEGISVN 188
Cdd:cd02520   155 LGKLIWRLGYRVV 167
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
2-100 4.70e-05

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: 43.90  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEEENLGKLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGE-------RNGARVISLYEEPpeGWVGKNWAIWNGYL 74
Cdd:pfam13641   7 VVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEeiaarfpDVRLRVIRNARLL--GPTGKSRGLNHGFR 84
                          90       100
                  ....*....|....*....|....*.
gi 2185637663  75 ESRGDILLFLDADVEPSSEFIEVMLS 100
Cdd:pfam13641  85 AVKSDLVVLHDDDSVLHPGTLKKYVQ 110
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
2-128 9.75e-05

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 42.37  E-value: 9.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   2 IIPARNEE---ENLGKLLSLLKKQTYkpyeVIVVNDNSEDDTEGV--GERNGARVISLYEEPPEGWVGK----NWAIwnG 72
Cdd:cd06436     2 LVPCLNEEaviQRTLASLLRNKPNFL----VLVIDDASDDDTAGIvrLAITDSRVHLLRRHLPNARTGKgdalNAAY--D 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2185637663  73 YLESRGD---------ILLFLDADVEPSSEFIEVMLSSYE--RYGGL-ISCWPYQRFEKFYEHL-NFAF 128
Cdd:cd06436    76 QIRQILIeegadpervIIAVIDADGRLDPNALEAVAPYFSdpRVAGTqSRVRMYNRHKNLLTILqDLEF 144
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
1-116 3.20e-04

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: 41.36  E-value: 3.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEEENLGKLLSLLKKQTYKP-YEVIVVNDNSEDDTEGV-----GERNGARVISLYEEPpegwvGKNWAIWNGYL 74
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGIdYEIIVVDDNSPDGTAEIvrelaKEYPRVRLIVRPGKR-----GLGSAYIEGFK 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2185637663  75 ESRGDILLFLDADVEPSSEFIEVMLSSYE----------RY--GGLISCWPYQR 116
Cdd:cd06442    76 AARGDVIVVMDADLSHPPEYIPELLEAQLeggadlvigsRYveGGGVEGWGLKR 129
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
24-223 9.03e-04

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


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 40.08  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  24 YKPYEVIVVNDNSEDDT-----EGVGERNGARVISLYEEPPEGWVGK--NWAIwnGYLESRGDILLFLDADVEPSSEFIE 96
Cdd:cd06435    26 YPNFEVIVIDNNTKDEAlwkpvEAHCAQLGERFRFFHVEPLPGAKAGalNYAL--ERTAPDAEIIAVIDADYQVEPDWLK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  97 VMLSSYE--RYGGLISCWPYQRFEK--FYEHLNFAFNLVSVFSMAFLGKKEGAF--GPAMMISRKDYERIGGHKEvrNKI 170
Cdd:cd06435   104 RLVPIFDdpRVGFVQAPQDYRDGEEslFKRMCYAEYKGFFDIGMVSRNERNAIIqhGTMCLIRRSALDDVGGWDE--WCI 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2185637663 171 VEDMEFAKKCLEEGISvnnflgGEYIKFRmYPHG-IKDLFQGFSKNM---AKGAFSI 223
Cdd:cd06435   182 TEDSELGLRMHEAGYI------GVYVAQS-YGHGlIPDTFEAFKKQRfrwAYGAVQI 231
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-116 2.83e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 38.53  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEEENLG--KLLSLLKKQTYKPYEVIVVNDNSEDDTEGVGErngaRVISLYEE------PPEGWVGKNWAIWNG 72
Cdd:PLN02726   13 IIVPTYNERLNIAliVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVK----QLQKVYGEdrillrPRPGKLGLGTAYIHG 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2185637663  73 YLESRGDILLFLDADV--EPS--SEFIEVMLS------SYERY--GGLISCWPYQR 116
Cdd:PLN02726   89 LKHASGDFVVIMDADLshHPKylPSFIKKQREtgadivTGTRYvkGGGVHGWDLRR 144
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
25-107 3.31e-03

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: 38.39  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  25 KPYEVIVV-NDNSEDDTEGVG--ERNGARVISLYEEPpegwvGKNWAIWNGYLESRGDILLFLDADVEPSSEFIEVMLSS 101
Cdd:cd06434    27 KPLEIIVVtDGDDEPYLSILSqtVKYGGIFVITVPHP-----GKRRALAEGIRHVTTDIVVLLDSDTVWPPNALPEMLKP 101

                  ....*...
gi 2185637663 102 YE--RYGG 107
Cdd:cd06434   102 FEdpKVGG 109
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
22-87 3.84e-03

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 38.00  E-value: 3.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663  22 QTYKPYEVIVVNDNSEDDT----EGVGERNGARVISLYEEPPEGWVgKNWaiWNGYLESRGDILLFLDAD 87
Cdd:cd04196    23 QTYKNDELIISDDGSTDGTveiiKEYIDKDPFIIILIRNGKNLGVA-RNF--ESLLQAADGDYVFFCDQD 89
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
1-95 6.10e-03

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 37.79  E-value: 6.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2185637663   1 MIIPARNEEENLGKLLSLLK---KQTYKPYEVIVVNDNSEDDTegvgerngARVISLYEEPPEGWV---------GKNWA 68
Cdd:PRK10714   10 VVIPVYNEQESLPELIRRTTaacESLGKEYEILLIDDGSSDNS--------AEMLVEAAQAPDSHIvaillnrnyGQHSA 81
                          90       100
                  ....*....|....*....|....*..
gi 2185637663  69 IWNGYLESRGDILLFLDADVEPSSEFI 95
Cdd:PRK10714   82 IMAGFSHVTGDLIITLDADLQNPPEEI 108
 
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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