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Conserved domains on  [gi|736655215|ref|WP_034662503|]
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glucosyl-3-phosphoglycerate synthase [Corynebacterium tuscaniense]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 1-236 1.22e-106

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.


The actual alignment was detected with superfamily member PRK13915:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 306  Bit Score: 309.93  E-value: 1.22e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVVKAARASCAS----EVIVVDSDSTDATAAVAREAGATVLNWGDIAPDIPVRPGKGEALWRG 76
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIRPLLMEplvdELIVIDSGSTDATAERAAAAGARVVSREEILPELPPRPGKGEALWRS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  77 VRAATGDVVVFLDADVTTVEPGWVDALAGEF-ADKRVQLVKATYRRTLDGED----HGGGRVTELTAKPLLKLLFPAIPA 151
Cdd:PRK13915 111 LAATTGDIVVFVDADLINFDPMFVPGLLGPLlTDPGVHLVKAFYRRPLRVSGgvdaTGGGRVTELVARPLLNLLRPELAG 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215 152 LEQPLAGEYAIRRDAALRLPFVTGYGVEVGLLIDVATAYGSGAITQVNLGVKTHRNRPLAELADMSDIVARTILSRARVA 231
Cdd:PRK13915 191 FVQPLGGEYAGRRELLESLPFVPGYGVEIGLLIDTLDRLGLDAIAQVDLGVRAHRNQPLRALGRMARQIIATALSRLGRP 270


                 ....*
gi 736655215 232 GTAVE 236
Cdd:PRK13915 271 DSGVG 275
 
Name Accession Description Interval E-value
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-236 1.22e-106

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 309.93  E-value: 1.22e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVVKAARASCAS----EVIVVDSDSTDATAAVAREAGATVLNWGDIAPDIPVRPGKGEALWRG 76
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIRPLLMEplvdELIVIDSGSTDATAERAAAAGARVVSREEILPELPPRPGKGEALWRS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  77 VRAATGDVVVFLDADVTTVEPGWVDALAGEF-ADKRVQLVKATYRRTLDGED----HGGGRVTELTAKPLLKLLFPAIPA 151
Cdd:PRK13915 111 LAATTGDIVVFVDADLINFDPMFVPGLLGPLlTDPGVHLVKAFYRRPLRVSGgvdaTGGGRVTELVARPLLNLLRPELAG 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215 152 LEQPLAGEYAIRRDAALRLPFVTGYGVEVGLLIDVATAYGSGAITQVNLGVKTHRNRPLAELADMSDIVARTILSRARVA 231
Cdd:PRK13915 191 FVQPLGGEYAGRRELLESLPFVPGYGVEIGLLIDTLDRLGLDAIAQVDLGVRAHRNQPLRALGRMARQIIATALSRLGRP 270


                 ....*
gi 736655215 232 GTAVE 236
Cdd:PRK13915 271 DSGVG 275
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-183 1.32e-28

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 107.48  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVVKAARA--SCASEVIVVDSDSTDATAAVAREAGATVlnwgdiaPDI-----PVRPGKGEAL 73
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAqtYPDFEIIVVDDGSTDGTAEILRELAAKD-------PRIrvirlERNRGKGAAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  74 WRGVRAATGDVVVFLDADvTTVEPGWVDALAGEFADKRVQLVKAtyRRTLDGEDHGGGRVTELTAKpLLKLLFPaipaLE 153
Cdd:COG0463   75 NAGLAAARGDYIAFLDAD-DQLDPEKLEELVAALEEGPADLVYG--SRLIREGESDLRRLGSRLFN-LVRLLTN----LP 146

                        170       180       190
                 ....*....|....*....|....*....|
gi 736655215 154 QPLAGEYAIRRDAALRLPFVTGYGVEVGLL 183
Cdd:COG0463  147 DSTSGFRLFRREVLEELGFDEGFLEDTELL 176
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 5-184 6.77e-23

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: 91.87  E-value: 6.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARASCAS----EVIVVDSDSTDATAAVAREAGATVLNWGDIapDIPVRPGKGEALWRGVRAA 80
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEgydyEIIVVDDGSTDGTAEIARELAARVPRVRVI--RLSRNFGKGAAVRAGFKAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  81 TGDVVVFLDADVTTvEPGWVDALAGEFADKRVQLVKATyrRTLDGEDHGGGRVTELTAK----PLLKLLFPAIPAleqPL 156
Cdd:cd04179   79 RGDIVVTMDADLQH-PPEDIPKLLEKLLEGGADVVIGS--RFVRGGGAGMPLLRRLGSRlfnfLIRLLLGVRISD---TQ 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 736655215 157 AGEYAIRRDAALRL---PFVTGYGVEVGLLI 184
Cdd:cd04179  153 SGFRLFRREVLEALlslLESNGFEFGLELLV 183
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-169 9.92e-22

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: 88.22  E-value: 9.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215    4 SVVIPALNEEATVAGVVKAARASCAS--EVIVVDSDSTDATAAVAREAGATVLNWGDIApdIPVRPGKGEALWRGVRAAT 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPnfEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIR--LPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   82 GDVVVFLDADVtTVEPGWVDALAGEFADKRVQLVKATYRRTLDGEDHGGGRVTELTAKPLLKLLFPAIPALEQPLAGEYA 161
Cdd:pfam00535  79 GDYIAFLDADD-EVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 736655215  162 IRRDAALR 169
Cdd:pfam00535 158 LYRREALE 165
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-113 1.90e-19

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: 83.33  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215    3 VSVVIPALNEEATVAGVVKAARA-SCASEVIVVDSDSTDATAAVAREAGATVLNwgdiAPdipvrPGKGEALWRGVRAAT 81
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQAlRGDAEVIVVDGGSTDGTVEIARSLGAKVIH----SP-----KGRARQMNAGAALAK 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 736655215   82 GDVVVFLDADvTTVEPGWVDALAGEFADKRVQ 113
Cdd:TIGR04283  72 GDILLFLHAD-TRLPKDFLEAIRRALAKPGYV 102
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
4-108 2.27e-08

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 53.64  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   4 SVVIPALNEEATVAGVVKAARA-----SCASEVIVVDSDSTDATAAVAREAGAtvlNWgdiAPDIPVR----PGKGEAL- 73
Cdd:NF038302   4 TVAIPTYNGANRLPEVLERLRSqigteSLSWEIIVVDNNSTDNTAQVVQEYQK---NW---PSPYPLRycfePQQGAAFa 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 736655215  74 -WRGVRAATGDVVVFLDADvTTVEPGWVdALAGEFA 108
Cdd:NF038302  78 rQRAIQEAKGELIGFLDDD-NLPAPNWV-AAAYAFG 111
 
Name Accession Description Interval E-value
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-236 1.22e-106

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 309.93  E-value: 1.22e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVVKAARASCAS----EVIVVDSDSTDATAAVAREAGATVLNWGDIAPDIPVRPGKGEALWRG 76
Cdd:PRK13915  31 RTVSVVLPALNEEETVGKVVDSIRPLLMEplvdELIVIDSGSTDATAERAAAAGARVVSREEILPELPPRPGKGEALWRS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  77 VRAATGDVVVFLDADVTTVEPGWVDALAGEF-ADKRVQLVKATYRRTLDGED----HGGGRVTELTAKPLLKLLFPAIPA 151
Cdd:PRK13915 111 LAATTGDIVVFVDADLINFDPMFVPGLLGPLlTDPGVHLVKAFYRRPLRVSGgvdaTGGGRVTELVARPLLNLLRPELAG 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215 152 LEQPLAGEYAIRRDAALRLPFVTGYGVEVGLLIDVATAYGSGAITQVNLGVKTHRNRPLAELADMSDIVARTILSRARVA 231
Cdd:PRK13915 191 FVQPLGGEYAGRRELLESLPFVPGYGVEIGLLIDTLDRLGLDAIAQVDLGVRAHRNQPLRALGRMARQIIATALSRLGRP 270


                 ....*
gi 736655215 232 GTAVE 236
Cdd:PRK13915 271 DSGVG 275
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-183 1.32e-28

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 107.48  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVVKAARA--SCASEVIVVDSDSTDATAAVAREAGATVlnwgdiaPDI-----PVRPGKGEAL 73
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAqtYPDFEIIVVDDGSTDGTAEILRELAAKD-------PRIrvirlERNRGKGAAR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  74 WRGVRAATGDVVVFLDADvTTVEPGWVDALAGEFADKRVQLVKAtyRRTLDGEDHGGGRVTELTAKpLLKLLFPaipaLE 153
Cdd:COG0463   75 NAGLAAARGDYIAFLDAD-DQLDPEKLEELVAALEEGPADLVYG--SRLIREGESDLRRLGSRLFN-LVRLLTN----LP 146

                        170       180       190
                 ....*....|....*....|....*....|
gi 736655215 154 QPLAGEYAIRRDAALRLPFVTGYGVEVGLL 183
Cdd:COG0463  147 DSTSGFRLFRREVLEELGFDEGFLEDTELL 176
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-123 3.18e-24

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: 97.89  E-value: 3.18e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVVKAARA----SCASEVIVVDSDSTDATAAVAREAGA-----TVLnwgdiapDIPVRPGKGE 71
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAqdypKEKLEVIVVDDGSTDETAEIARELAAeyprvRVI-------ERPENGGKAA 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 736655215  72 ALWRGVRAATGDVVVFLDADvTTVEPGWVDALAGEFADKRVQLVKAT--YRRTL 123
Cdd:COG1215  102 ALNAGLKAARGDIVVFLDAD-TVLDPDWLRRLVAAFADPGVGASGANlaFRREA 154
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 5-184 6.77e-23

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: 91.87  E-value: 6.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARASCAS----EVIVVDSDSTDATAAVAREAGATVLNWGDIapDIPVRPGKGEALWRGVRAA 80
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEEgydyEIIVVDDGSTDGTAEIARELAARVPRVRVI--RLSRNFGKGAAVRAGFKAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  81 TGDVVVFLDADVTTvEPGWVDALAGEFADKRVQLVKATyrRTLDGEDHGGGRVTELTAK----PLLKLLFPAIPAleqPL 156
Cdd:cd04179   79 RGDIVVTMDADLQH-PPEDIPKLLEKLLEGGADVVIGS--RFVRGGGAGMPLLRRLGSRlfnfLIRLLLGVRISD---TQ 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 736655215 157 AGEYAIRRDAALRL---PFVTGYGVEVGLLI 184
Cdd:cd04179  153 SGFRLFRREVLEALlslLESNGFEFGLELLV 183
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 3-114 4.79e-22

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: 90.32  E-value: 4.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   3 VSVVIPALNEEATVAGVVKAARASC--ASEVIVVDSDSTDATAAVAREAGATVlnwgdiapdIPVRPGKGEALWRGVRAA 80
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNplPLEIIVVDGGSTDGTVAIARSAGVVV---------ISSPKGRARQMNAGAAAA 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 736655215  81 TGDVVVFLDADvTTVEPGWVDALAGEFADKRVQL 114
Cdd:cd02522   72 RGDWLLFLHAD-TRLPPDWDAAIIETLRADGAVA 104
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-169 9.92e-22

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: 88.22  E-value: 9.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215    4 SVVIPALNEEATVAGVVKAARASCAS--EVIVVDSDSTDATAAVAREAGATVLNWGDIApdIPVRPGKGEALWRGVRAAT 81
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPnfEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIR--LPENRGKAGARNAGLRAAT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   82 GDVVVFLDADVtTVEPGWVDALAGEFADKRVQLVKATYRRTLDGEDHGGGRVTELTAKPLLKLLFPAIPALEQPLAGEYA 161
Cdd:pfam00535  79 GDYIAFLDADD-EVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFA 157


                  ....*...
gi 736655215  162 IRRDAALR 169
Cdd:pfam00535 158 LYRREALE 165
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 5-111 4.30e-20

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: 83.71  E-value: 4.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARAS--CASEVIVVDSDSTDATAAVAREAGATVLNWgdIAPDIPVRPGKGEALWRGVRAATG 82
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQtyPNFEVIVVDDGSTDGTLEILEEYAKKDPRV--IRVINEENQGLAAARNAGLKAARG 78

                         90       100
                 ....*....|....*....|....*....
gi 736655215  83 DVVVFLDADvTTVEPGWVDALAGEFADKR 111
Cdd:cd00761   79 EYILFLDAD-DLLLPDWLERLVAELLADP 106
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-113 1.90e-19

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: 83.33  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215    3 VSVVIPALNEEATVAGVVKAARA-SCASEVIVVDSDSTDATAAVAREAGATVLNwgdiAPdipvrPGKGEALWRGVRAAT 81
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQAlRGDAEVIVVDGGSTDGTVEIARSLGAKVIH----SP-----KGRARQMNAGAALAK 71

                          90       100       110
                  ....*....|....*....|....*....|..
gi 736655215   82 GDVVVFLDADvTTVEPGWVDALAGEFADKRVQ 113
Cdd:TIGR04283  72 GDILLFLHAD-TRLPKDFLEAIRRALAKPGYV 102
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 5-112 2.34e-17

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 76.88  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARASCAS--EVIVVDSDSTDATAAVAREAGATVLNWGDIAPDiPVRPGKGEALWRGVRAATG 82
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPklEVIVVDDGSTDDTLEILEELAALYIRRVLVVRD-KENGGKAGALNAGLRHAKG 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 736655215  83 DVVVFLDADvTTVEPGWVDAL-AGEFADKRV 112
Cdd:cd06423   80 DIVVVLDAD-TILEPDALKRLvVPFFADPKV 109
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-120 2.73e-15

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


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 72.62  E-value: 2.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   2 RVSVVIPALNEEAtvagVVKAARASCAS--------EVIVVDSDSTDATAAVAREAGA---TVLnwgdiapDIPVRPGKG 70
Cdd:cd06439   30 TVTIIIPAYNEEA----VIEAKLENLLAldyprdrlEIIVVSDGSTDGTAEIAREYADkgvKLL-------RFPERRGKA 98

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 736655215  71 EALWRGVRAATGDVVVFLDADvTTVEPGWVDALAGEFADKRVQLVKATYR 120
Cdd:cd06439   99 AALNRALALATGEIVVFTDAN-ALLDPDALRLLVRHFADPSVGAVSGELV 147
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 2-91 7.73e-15

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: 71.17  E-value: 7.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   2 RVSVVIPALNEEATVAGVVKAARAsCASEVIVVDSDSTDATAAVAREAGATVLN--WGDIAPdipvrpgkgeALWRGVRA 79
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKW-AVDEIIVVDSGSTDRTVEIAKEYGAKVYQrwWDGFGA----------QRNFALEL 69

                         90
                 ....*....|..
gi 736655215  80 ATGDVVVFLDAD 91
Cdd:cd02511   70 ATNDWVLSLDAD 81
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-94 1.41e-14

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 69.90  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEE----ATVAGVVKAARASCAS--EVIVVDSDSTDATAAVAREAGA------TVLnwgdiapDIPVRPGKGEA 72
Cdd:cd04188    1 VVIPAYNEEkrlpPTLEEAVEYLEERPSFsyEIIVVDDGSKDGTAEVARKLARknpaliRVL-------TLPKNRGKGGA 73

                         90       100
                 ....*....|....*....|..
gi 736655215  73 LWRGVRAATGDVVVFLDADVTT 94
Cdd:cd04188   74 VRAGMLAARGDYILFADADLAT 95
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-108 4.38e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 68.48  E-value: 4.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVVKAARASCAS--EVIVVDSDSTDATAAVARE---AGATVLNWGDiapdipvRPGKGEALWR 75
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPpfEVIVVDNGSTDGTAELLAAlafPRVRVIRNPE-------NLGFAAARNL 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 736655215  76 GVRAATGDVVVFLDADvTTVEPGWVDALAGEFA 108
Cdd:COG1216   76 GLRAAGGDYLLFLDDD-TVVEPDWLERLLAAAC 107
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 5-108 5.91e-13

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: 64.93  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARA----SCASEVIVVDSDSTDATAAVAREAGATVLNWGDiapdiPVRPGKGEALWRGVR-- 78
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAqdypRELYRIFVVADNCTDDTAQVARAAGATVLERHD-----PERRGKGYALDFGFRhl 75

                         90       100       110
                 ....*....|....*....|....*....|...
gi 736655215  79 ---AATGDVVVFLDADvTTVEPGWVDALAGEFA 108
Cdd:cd06438   76 lnlADDPDAVVVFDAD-NLVDPNALEELNARFA 107
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 2-109 1.59e-11

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: 62.25  E-value: 1.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   2 RVSVVIPALNEEATVAGVVKAARASC----ASEVIVVDSDSTDATAAVAREAgatvlnwgdIAPDIPVR----PGK--GE 71
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSypkdLIEIIVVDGGSTDGTREIVQEY---------AAKDPRIRlidnPKRiqSA 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 736655215  72 ALWRGVRAATGDVVVFLDADvTTVEPGWVDALAGEFAD 109
Cdd:cd02525   72 GLNIGIRNSRGDIIIRVDAH-AVYPKDYILELVEALKR 108
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 2-112 9.90e-10

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: 57.00  E-value: 9.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215    2 RVSVVIPALNEEATVAGVVKAARASC--ASEVIVVDSDSTDATAAVAREAGA---TVLNWGDIAPDIPVRPGKGEALWRG 76
Cdd:pfam13641   3 DVSVVVPAFNEDSVLGRVLEAILAQPypPVEVVVVVNPSDAETLDVAEEIAArfpDVRLRVIRNARLLGPTGKSRGLNHG 82

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 736655215   77 VRAATGDVVVFLDADvTTVEPGWVDALAGEFADKRV 112
Cdd:pfam13641  83 FRAVKSDLVVLHDDD-SVLHPGTLKKYVQYFDSPKV 117
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-91 1.46e-09

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: 55.56  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARASCAS-----EVIVVDSDSTDATAAVAREAGATvlnwgdiapDIPVRP-------GKGEA 72
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESlgydyEIIFVDDGSTDRTLEILRELAAR---------DPRVKVirlsrnfGQQAA 71

                         90
                 ....*....|....*....
gi 736655215  73 LWRGVRAATGDVVVFLDAD 91
Cdd:cd04187   72 LLAGLDHARGDAVITMDAD 90
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-93 3.79e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 55.47  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   1 MRVSVVIPALNEEATVAGVV----KAARASCASEVIVVDSDSTDATAAVAREAGATvlnWGDIAPDIPVRPGK---GEAL 73
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVylifKALQDVKDFEIIVVDDGSPDGTQDVVKQLQKV---YGEDRILLRPRPGKlglGTAY 85

                         90       100
                 ....*....|....*....|
gi 736655215  74 WRGVRAATGDVVVFLDADVT 93
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLS 105
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 5-91 4.98e-09

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 54.85  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARASCAS---EVIVVDSDSTDATAAVAREAGATVLNwgdiaPDIPVRPGK---GEALWRGVR 78
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGidyEIIVVDDNSPDGTAEIVRELAKEYPR-----VRLIVRPGKrglGSAYIEGFK 75

                         90
                 ....*....|...
gi 736655215  79 AATGDVVVFLDAD 91
Cdd:cd06442   76 AARGDVIVVMDAD 88
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 5-120 9.30e-09

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: 53.54  E-value: 9.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARA-SCASEVIVVDSDSTDATAAVAREA--GATVLNWGDIAPDipVRPGKGEALWRGV---- 77
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRnKPNFLVLVIDDASDDDTAGIVRLAitDSRVHLLRRHLPN--ARTGKGDALNAAYdqir 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 736655215  78 ------RAATGDVVV-FLDADvTTVEPGWVDALAGEFADKRVQLVKATYR 120
Cdd:cd06436   79 qilieeGADPERVIIaVIDAD-GRLDPNALEAVAPYFSDPRVAGTQSRVR 127
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
4-108 2.27e-08

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 53.64  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   4 SVVIPALNEEATVAGVVKAARA-----SCASEVIVVDSDSTDATAAVAREAGAtvlNWgdiAPDIPVR----PGKGEAL- 73
Cdd:NF038302   4 TVAIPTYNGANRLPEVLERLRSqigteSLSWEIIVVDNNSTDNTAQVVQEYQK---NW---PSPYPLRycfePQQGAAFa 77

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 736655215  74 -WRGVRAATGDVVVFLDADvTTVEPGWVdALAGEFA 108
Cdd:NF038302  78 rQRAIQEAKGELIGFLDDD-NLPAPNWV-AAAYAFG 111
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 4-94 1.52e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 51.31  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   4 SVVIPALNEEATVAGVVKAARA----------SCASEVIVVDSDSTDATAAVAREagatvLNWGDIAPDIPVR------- 66
Cdd:PTZ00260  73 SIVIPAYNEEDRLPKMLKETIKylesrsrkdpKFKYEIIIVNDGSKDKTLKVAKD-----FWRQNINPNIDIRllsllrn 147

                         90       100
                 ....*....|....*....|....*...
gi 736655215  67 PGKGEALWRGVRAATGDVVVFLDADVTT 94
Cdd:PTZ00260 148 KGKGGAVRIGMLASRGKYILMVDADGAT 175
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 3-115 1.88e-07

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: 50.33  E-value: 1.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   3 VSVVIPALNEEATV-AGVVKAARASCASEVIVVdsdsTDATAAVAREAGATVLNWGDIAPDIPVRPGKGEALWRGVRAAT 81
Cdd:cd06434    2 VTVIIPVYDEDPDVfRECLRSILRQKPLEIIVV----TDGDDEPYLSILSQTVKYGGIFVITVPHPGKRRALAEGIRHVT 77

                         90       100       110
                 ....*....|....*....|....*....|....
gi 736655215  82 GDVVVFLDADVTTVEPGWVDALAGeFADKRVQLV 115
Cdd:cd06434   78 TDIVVLLDSDTVWPPNALPEMLKP-FEDPKVGGV 110
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-115 3.62e-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: 49.59  E-value: 3.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKAARA----SCASEVIVVDSDSTDATAA-VAREAGATVLNWGDIAPDIPVRPGKGEALWRGVRA 79
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSAldypKEKFEVILVDDHSTDGTVQiLEFAAAKPNFQLKILNNSRVSISGKKNALTTAIKA 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 736655215  80 ATGDVVVFLDADVtTVEPGWVDALAGEFADKRVQLV 115
Cdd:cd04192   81 AKGDWIVTTDADC-VVPSNWLLTFVAFIQKEQIGLV 115
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-91 8.26e-07

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: 47.93  E-value: 8.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   4 SVVIPALNEEATVAGVVKaaraSCAS------EVIVVDSDSTDATAAVAREAGATVLNWgDIAPDipvrpgKG--EALWR 75
Cdd:cd06433    1 SIITPTYNQAETLEETID----SVLSqtypniEYIVIDGGSTDGTVDIIKKYEDKITYW-ISEPD------KGiyDAMNK 69

                         90
                 ....*....|....*.
gi 736655215  76 GVRAATGDVVVFLDAD 91
Cdd:cd06433   70 GIALATGDIIGFLNSD 85
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 2-92 1.03e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 48.58  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   2 RVSVVIPALNEEATVAGVVKAARASCAS-----EVIVVDSDSTDATAAVAREAGAtvlnwgdiAPDIPV-------RPGK 69
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTTAACESlgkeyEILLIDDGSSDNSAEMLVEAAQ--------APDSHIvaillnrNYGQ 78

                         90       100
                 ....*....|....*....|...
gi 736655215  70 GEALWRGVRAATGDVVVFLDADV 92
Cdd:PRK10714  79 HSAIMAGFSHVTGDLIITLDADL 101
Osmo_MPGsynth pfam09488
Mannosyl-3-phosphoglycerate synthase (osmo_MPGsynth); This family consists of examples of ...
 2-194 2.53e-06

Mannosyl-3-phosphoglycerate synthase (osmo_MPGsynth); This family consists of examples of mannosyl-3-phosphoglycerate synthase (MPGS), which together with mannosyl-3-phosphoglycerate phosphatase (MPGP) EC:2.4.1.217, comprises a two-step pathway for mannosylglycerate biosynthesis. Mannosylglycerate is a compatible solute that tends to be restricted to extreme thermophiles of archaea and bacteria. Note that in Rhodothermus marinus, this pathway is one of two; the other is condensation of GDP-mannose with D-glycerate by mannosylglycerate synthase.


Pssm-ID: 401440  Cd Length: 380  Bit Score: 47.63  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215    2 RVSVVIPALNEE-ATVAGVVKAARASCAseVIVVdSDST-------------------------------DATAAVA-RE 48
Cdd:pfam09488  50 QMAIVVPCKNEDlKLLEGVLSGIPHDCL--VIVV-SNSSrgpvdrfkmevdllkqfcrltgrpaiiihqkDPALAEAfKA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   49 AGAtvlnwgdiaPDI------PVRPGKGEALWRGV---RAATGDVVVFLDADVTTvePG----WVDALAGEFADKR---- 111
Cdd:pfam09488 127 AGY---------PEIldedggLIRSGKGEGMILGIllaKLLGRRYVGFIDADNYV--PGavneYCKAFAAGFAMAKspya 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  112 -VQLV----------KATYRRTldgedhggGRVTELTAKPLLKLLfPAIPALEQPL-----AGEYAIRRDAALRLPFVTG 175
Cdd:pfam09488 196 mVRIKwrskpkvrndELYFRKW--------GRVSEVTNRWLNKLL-SAITGFETDIiktgnAGEHAMTMELALKLRFASG 266

                         250
                  ....*....|....*....
gi 736655215  176 YGVEVGLLIDVATAYGSGA 194
Cdd:pfam09488 267 YAIEPFQLIDILERFGGLL 285
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-103 3.24e-06

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 46.01  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   5 VVIPALNEEATVAGVVKA--ARASCASEVIVVDSDSTDATAAVAREAGATVLnwgDIAPDIPVrpGKGEALWRGVRAATG 82
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSllAQTYPDFEVIVVDNASTDGSVELLRELFPEVR---LIRNGENL--GFGAGNNQGIREAKG 75

                         90       100
                 ....*....|....*....|.
gi 736655215  83 DVVVFLDADvTTVEPGWVDAL 103
Cdd:cd04186   76 DYVLLLNPD-TVVEPGALLEL 95
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 2-117 4.45e-04

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 40.37  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   2 RVSVVIPALNEEATVAGVVKAARA----SCASEVIVVDsDSTDATaavAREAGATVLNWGDIAPDI-----PVRPG-KGE 71
Cdd:cd06437    2 MVTVQLPVFNEKYVVERLIEAACAldypKDRLEIQVLD-DSTDET---VRLAREIVEEYAAQGVNIkhvrrADRTGyKAG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 736655215  72 ALWRGVRAATGDVVVFLDADVTTvEPGWVDALAGEFADKRVQLVKA 117
Cdd:cd06437   78 ALAEGMKVAKGEYVAIFDADFVP-PPDFLQKTPPYFADPKLGFVQT 122
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 30-127 7.69e-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: 39.69  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215  30 EVIVVDSDSTDATAAVAREAGATVLNWGDIAPDIPVRPG-KGEALWRGVRAATGD--VVVFLDADVTtVEPGWVDALAGE 106
Cdd:cd06435   30 EVIVIDNNTKDEALWKPVEAHCAQLGERFRFFHVEPLPGaKAGALNYALERTAPDaeIIAVIDADYQ-VEPDWLKRLVPI 108

                         90       100
                 ....*....|....*....|...
gi 736655215 107 FADKRVQLVKAT--YRrtlDGED 127
Cdd:cd06435  109 FDDPRVGFVQAPqdYR---DGEE 128
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-98 1.06e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 39.64  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   2 RVSVVIPALNEEATVAGVVKA--ARASCASEVIVVDSDSTDATAAVAReagatvlNWGDIAPDIPV----RPGKGEALWR 75
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESliAQTWTALEIIIVNDGSTDNSVEIAK-------HYAENYPHVRLlhqaNAGVSVARNT 79

                         90       100
                 ....*....|....*....|...
gi 736655215  76 GVRAATGDVVVFLDADvTTVEPG 98
Cdd:PRK10073  80 GLAVATGKYVAFPDAD-DVVYPT 101
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 75-120 4.45e-03

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: 36.88  E-value: 4.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 736655215   75 RGVRAATGDVVVFLDADVtTVEPGWVDALAGEFADKRVQLVKATYR 120
Cdd:pfam13506  24 QGLEAAKYDLLVISDSDI-RVPPDYLRDLLAPLADPKVGLVTSPPV 68
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 2-115 6.51e-03

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 36.78  E-value: 6.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 736655215   2 RVSVVIPALNEE-ATVAGVVKAARA----SCASEVIVVDSDSTDATAAVAREAGATvlnWGDIAPDIPVRPG-KGEALWR 75
Cdd:cd06421    2 TVDVFIPTYNEPlEIVRKTLRAALAidypHDKLRVYVLDDGRRPELRALAAELGVE---YGYRYLTRPDNRHaKAGNLNN 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 736655215  76 GVRAATGDVVVFLDADvTTVEPGWVDALAGEFAD-KRVQLV 115
Cdd:cd06421   79 ALAHTTGDFVAILDAD-HVPTPDFLRRTLGYFLDdPKVALV 118
 
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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