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Conserved domains on  [gi|727185834|ref|WP_033647723|]
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MULTISPECIES: glycosyltransferase family A protein [Serratia]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

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

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-181 2.26e-23

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 95.15  E-value: 2.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   1 MDFSIVIPIYNSSRYLPKTLKRIFNAcQGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTKL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQ-TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834  81 AQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAEVSGDSvrdfnFHYKSGSSGEDF--LFLEMGDIRSSTISM 158
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES-----DLRRLGSRLFNLvrLLTNLPDSTSGFRLF 155
                        170       180
                 ....*....|....*....|...
gi 727185834 159 RKKSDRRFLFPEFLnkHQDWGFL 181
Cdd:COG0463  156 RREVLEELGFDEGF--LEDTELL 176
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-181 2.26e-23

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 95.15  E-value: 2.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   1 MDFSIVIPIYNSSRYLPKTLKRIFNAcQGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTKL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQ-TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834  81 AQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAEVSGDSvrdfnFHYKSGSSGEDF--LFLEMGDIRSSTISM 158
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES-----DLRRLGSRLFNLvrLLTNLPDSTSGFRLF 155
                        170       180
                 ....*....|....*....|...
gi 727185834 159 RKKSDRRFLFPEFLnkHQDWGFL 181
Cdd:COG0463  156 RREVLEELGFDEGF--LEDTELL 176
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-118 6.33e-23

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: 92.57  E-value: 6.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIFNacQGF-DYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTKLAQS 83
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLA--QTYpNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 727185834  84 EIVFFLDSDDYFTTNYIIRRMKK-HEDRQIDIIFGN 118
Cdd:cd00761   79 EYILFLDADDLLLPDWLERLVAElLADPEADAVGGP 114
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 4.35e-19

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: 82.44  E-value: 4.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834    4 SIVIPIYNSSRYLPKTLKRIFNACqGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTKLAQS 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQT-YPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   84 EIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAEVSGDSVRD-----FNFHYKSGSSGEDFLFLEMGDIRSSTISM 158
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYrrasrITLSRLPFFLGLRLLGLNLPFLIGGFALY 159

                  ....*..
gi 727185834  159 RKKSDRR 165
Cdd:pfam00535 160 RREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
4-93 4.33e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.43  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIFnACQGFDYQVILVDDCSDEDDIKSIRQIAATNSNV-MLHEKKQksNAAVSRNLGTKLAQ 82
Cdd:PRK10073   9 SIIIPLYNAGKDFRAFMESLI-AQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVrLLHQANA--GVSVARNTGLAVAT 85
                         90
                 ....*....|.
gi 727185834  83 SEIVFFLDSDD 93
Cdd:PRK10073  86 GKYVAFPDADD 96
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-181 2.26e-23

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 95.15  E-value: 2.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   1 MDFSIVIPIYNSSRYLPKTLKRIFNAcQGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTKL 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQ-TYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834  81 AQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAEVSGDSvrdfnFHYKSGSSGEDF--LFLEMGDIRSSTISM 158
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGES-----DLRRLGSRLFNLvrLLTNLPDSTSGFRLF 155
                        170       180
                 ....*....|....*....|...
gi 727185834 159 RKKSDRRFLFPEFLnkHQDWGFL 181
Cdd:COG0463  156 RREVLEELGFDEGF--LEDTELL 176
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-118 6.33e-23

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: 92.57  E-value: 6.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIFNacQGF-DYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTKLAQS 83
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLA--QTYpNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 727185834  84 EIVFFLDSDDYFTTNYIIRRMKK-HEDRQIDIIFGN 118
Cdd:cd00761   79 EYILFLDADDLLLPDWLERLVAElLADPEADAVGGP 114
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-165 4.35e-19

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: 82.44  E-value: 4.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834    4 SIVIPIYNSSRYLPKTLKRIFNACqGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTKLAQS 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQT-YPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   84 EIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAEVSGDSVRD-----FNFHYKSGSSGEDFLFLEMGDIRSSTISM 158
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYrrasrITLSRLPFFLGLRLLGLNLPFLIGGFALY 159

                  ....*..
gi 727185834  159 RKKSDRR 165
Cdd:pfam00535 160 RREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-145 2.27e-15

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: 74.78  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   1 MDFSIVIPIYNSSRYLPKTLKRIFNA-CQGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKSNAAVSRNLGTK 79
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQdYPKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLK 108
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 727185834  80 LAQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAeVSGDSVRDFNfHYKSGSSGEDFLF 145
Cdd:COG1215  109 AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANLA-FRREALEEVG-GFDEDTLGEDLDL 172
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-100 1.12e-14

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 71.18  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   1 MDFSIVIPIYNSSRYLPKTLKRIFNACQGfDYQVILVDDCSDEDDIKSIRQIAAtnSNVMLHEKKQKSNAAVSRNLGTKL 80
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYP-PFEVIVVDNGSTDGTAELLAALAF--PRVRVIRNPENLGFAAARNLGLRA 79
                         90       100
                 ....*....|....*....|
gi 727185834  81 AQSEIVFFLDSDDYFTTNYI 100
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWL 99
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
5-118 9.93e-14

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: 67.98  E-value: 9.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIFNAC-QGFDYQVILVDDCSDEDDIKSIRQIAATNSNVML--HEKKQKSNAAVSRnlGTKLA 81
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLeEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVirLSRNFGKGAAVRA--GFKAA 78
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 727185834  82 QSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGN 118
Cdd:cd04179   79 RGDIVVTMDADLQHPPEDIPKLLEKLLEGGADVVIGS 115
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
4-119 7.28e-12

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: 64.18  E-value: 7.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIFNacQGF---DYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKsNAAVSRNLGTKL 80
Cdd:cd02525    3 SIIIPVRNEEKYIEELLESLLN--QSYpkdLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKR-IQSAGLNIGIRN 79
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 727185834  81 AQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNY 119
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPM 118
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-193 1.68e-10

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 59.52  E-value: 1.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   3 FSIVIPIYNSS-RYLPKTLKRIFNacQGFDY-QVILVDDCSDEDDIKSI-RQIAATNSNVMLHEKKQKSNAAVSRNLGTK 79
Cdd:cd04184    3 ISIVMPVYNTPeKYLREAIESVRA--QTYPNwELCIADDASTDPEVKRVlKKYAAQDPRIKVVFREENGGISAATNSALE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834  80 LAQSEIVFFLDSDDYFTTN--YIIrrMKKH-EDRQIDIIFGNYAEVSGDSVRdFNFHYKSGSSGEDFL----FLEMGDIR 152
Cdd:cd04184   81 LATGEFVALLDHDDELAPHalYEV--VKALnEHPDADLIYSDEDKIDEGGKR-SEPFFKPDWSPDLLLsqnyIGHLLVYR 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 727185834 153 SSTIsmrkksDRRFLFPEFLNKHQDWGFLVNATNLGAQVAH 193
Cdd:cd04184  158 RSLV------RQVGGFREGFEGAQDYDLVLRVSEHTDRIAH 192
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-92 2.45e-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: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIFNACQ--GFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLhekkqksnaaV--SRNLGT-- 78
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLEslGYDYEIIFVDDGSTDRTLEILRELAARDPRVKV----------IrlSRNFGQqa 70
                         90       100
                 ....*....|....*....|
gi 727185834  79 ------KLAQSEIVFFLDSD 92
Cdd:cd04187   71 allaglDHARGDAVITMDAD 90
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
5-144 3.61e-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: 56.00  E-value: 3.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIFNACQGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKS--NAAVSRnlGTKLAQ 82
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRglGSAYIE--GFKAAR 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727185834  83 SEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGN-YaeVSGDSVRDFNFHYKSGSSGEDFL 144
Cdd:cd06442   79 GDVIVVMDADLSHPPEYIPELLEAQLEGGADLVIGSrY--VEGGGVEGWGLKRKLISRGANLL 139
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-98 1.73e-08

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 54.59  E-value: 1.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834    4 SIVIPIYNSSRYlPKTLKRIFNACQGFD--YQVILVDDCSDEDDIKSIRQIAATNSNVML-HEKKQKSNAAVSRNLGTKL 80
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFQYDpeFELIIINDGSTDKTLEEVSSIKDHNLQVYYpNAPDTTYSLAASRNRGTSH 79
                          90
                  ....*....|....*...
gi 727185834   81 AQSEIVFFLDSDDYFTTN 98
Cdd:pfam10111  80 AIGEYISFIDGDCLWSPD 97
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
4-135 3.21e-08

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


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 53.75  E-value: 3.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSR-YLPKTLKRIFNACQGFDY-QVILVDDCSDEDDIKS--IRQIAATNSNVMLHEKKQKSNAAVSRNLGTK 79
Cdd:cd02510    1 SVIIIFHNEALsTLLRTVHSVINRTPPELLkEIILVDDFSDKPELKLllEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834  80 LAQSEIVFFLDSDDYFTTNY---IIRRMKkhEDRQ------IDII-FGNYAEVSGDSVR----DFNFHYK 135
Cdd:cd02510   81 AATGDVLVFLDSHCEVNVGWlepLLARIA--ENRKtvvcpiIDVIdADTFEYRGSSGDArggfDWSLHFK 148
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-119 3.62e-08

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: 52.23  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKrifnACQGFDY---QVILVDDCSDEDDIKSIRQIAAT-NSNVMLHEKKQKSNAAVSRNLGTKL 80
Cdd:cd06423    1 IIVPAYNEEAVIERTIE----SLLALDYpklEVIVVDDGSTDDTLEILEELAALyIRRVLVVRDKENGGKAGALNAGLRH 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 727185834  81 AQSEIVFFLDSDDYFTTNYIIRRMKKH-EDRQIDIIFGNY 119
Cdd:cd06423   77 AKGDIVVVLDADTILEPDALKRLVVPFfADPKVGAVQGRV 116
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
4-125 9.51e-08

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: 51.39  E-value: 9.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIFNacQGF-DYQVILVDDCSDEDDIKsirqIAATNSNVMLHekkqksnaAVSR-------- 74
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLS--QTYpNIEYIVIDGGSTDGTVD----IIKKYEDKITY--------WISEpdkgiyda 66
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 727185834  75 -NLGTKLAQSEIVFFLDSDDYFTTNYIIRRMKK-HEDRQIDIIFGNYAEVSGD 125
Cdd:cd06433   67 mNKGIALATGDIIGFLNSDDTLLPGALLAVVAAfAEHPEVDVVYGDVLLVDEN 119
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
4-178 3.52e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 49.94  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIFNacQ-GFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEKKQKsNAAVSRN--LGTKL 80
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILA--QtYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGK-NLGVARNfeSLLQA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834  81 AQSEIVFFLDSDDYFTTNYIIRRMKK-HEDRQIDIIFGNYAEV--SGDSVRDFNFHYKSGSSGEDFLFLEMGDIRS-STI 156
Cdd:cd04196   78 ADGDYVFFCDQDDIWLPDKLERLLKAfLKDDKPLLVYSDLELVdeNGNPIGESFFEYQKIKPGTSFNNLLFQNVVTgCTM 157
                        170       180
                 ....*....|....*....|...
gi 727185834 157 SMRKKSDRRFL-FPEFLNKHQDW 178
Cdd:cd04196  158 AFNRELLELALpFPDADVIMHDW 180
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-92 3.92e-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: 49.09  E-value: 3.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIFNAcQGFDYQVILVDDCSDEDDIKSIRQiaaTNSNVMLHEKKQKSNAAVSRNLGTKLAQSE 84
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQ-TYPDFEVIVVDNASTDGSVELLRE---LFPEVRLIRNGENLGFGAGNNQGIREAKGD 76

                 ....*...
gi 727185834  85 IVFFLDSD 92
Cdd:cd04186   77 YVLLLNPD 84
PRK10073 PRK10073
putative glycosyl transferase; Provisional
4-93 4.33e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.43  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIFnACQGFDYQVILVDDCSDEDDIKSIRQIAATNSNV-MLHEKKQksNAAVSRNLGTKLAQ 82
Cdd:PRK10073   9 SIIIPLYNAGKDFRAFMESLI-AQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVrLLHQANA--GVSVARNTGLAVAT 85
                         90
                 ....*....|.
gi 727185834  83 SEIVFFLDSDD 93
Cdd:PRK10073  86 GKYVAFPDADD 96
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
1-117 4.36e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 50.54  E-value: 4.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   1 MDFSIVIPIYNSSRYLPKTLKRIFNACQG-------FDYQVILVDDCSDEDDIKS----IRQIAATNSNVMLHEKKQKSN 69
Cdd:PTZ00260  70 VDLSIVIPAYNEEDRLPKMLKETIKYLESrsrkdpkFKYEIIIVNDGSKDKTLKVakdfWRQNINPNIDIRLLSLLRNKG 149
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 727185834  70 AAVSRNLGTKLAQSEIVFFLDSD---DYFTTNYIIRRMKKHEDRQIDIIFG 117
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDADgatDIDDFDKLEDIMLKIEQNGLGIVFG 200
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-127 5.18e-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: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   3 FSIVIPIYNSSRYLPKTLKRIFNacqgFDY-----QVILVDDCSD--EDDIksIRQIAAtnSNVMLHEKKQKSNAAVSRN 75
Cdd:cd06439   31 VTIIIPAYNEEAVIEAKLENLLA----LDYprdrlEIIVVSDGSTdgTAEI--AREYAD--KGVKLLRFPERRGKAAALN 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 727185834  76 LGTKLAQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAEVSGDSV 127
Cdd:cd06439  103 RALALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVDGGGS 154
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
5-92 1.44e-06

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


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 47.95  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIF---NACQGFDYQVILVDDCSDEDDIKSIRQIAATNSNVMLHEkKQKSN----AAVsrNLG 77
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVeylEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVL-TLPKNrgkgGAV--RAG 77
                         90
                 ....*....|....*
gi 727185834  78 TKLAQSEIVFFLDSD 92
Cdd:cd04188   78 MLAARGDYILFADAD 92
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-144 4.67e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 47.00  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   1 MDFSIVIPIYNSSRYLPKTLKRIFNACQGF-DYQVILVDDCSDEDDIKSIRQIAAT--NSNVMLHEKKQKSNAAVSRNLG 77
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKALQDVkDFEIIVVDDGSPDGTQDVVKQLQKVygEDRILLRPRPGKLGLGTAYIHG 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 727185834  78 TKLAQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGN-YaeVSGDSVRDFNFHYKSGSSGEDFL 144
Cdd:PLN02726  89 LKHASGDFVVIMDADLSHHPKYLPSFIKKQRETGADIVTGTrY--VKGGGVHGWDLRRKLTSRGANVL 154
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
4-92 5.36e-06

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: 46.41  E-value: 5.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIfNACQGFDYQVILVDdcSDEDDikSIRQIAATNSNVMLHEKKqksNAAVSRNLGTKLAQS 83
Cdd:cd02522    2 SIIIPTLNEAENLPRLLASL-RRLNPLPLEIIVVD--GGSTD--GTVAIARSAGVVVISSPK---GRARQMNAGAAAARG 73

                 ....*....
gi 727185834  84 EIVFFLDSD 92
Cdd:cd02522   74 DWLLFLHAD 82
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
4-44 1.25e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 45.88  E-value: 1.25e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIFNACQ--GFDYQVILVDDCSDED 44
Cdd:PRK10714   9 SVVIPVYNEQESLPELIRRTTAACEslGKEYEILLIDDGSSDN 51
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-126 1.40e-05

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 45.36  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIfnACQgfDY-----QVILVDDCSdEDDIKSIRQIAA--TNSNVMLHEKKQKSNA--AVSRN 75
Cdd:cd04192    1 VVIAARNEAENLPRLLQSL--SAL--DYpkekfEVILVDDHS-TDGTVQILEFAAakPNFQLKILNNSRVSISgkKNALT 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 727185834  76 LGTKLAQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQIDIIFGNYAEVSGDS 126
Cdd:cd04192   76 TAIKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKS 126
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
4-116 3.00e-05

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 44.20  E-value: 3.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   4 SIVIPIYNSSRYLPKTLKRIFNACQgfdyQVILVDDCSdEDDIKSIrqiaATNSNVMLHEKKQKSNAAvSRNLGTKLAQS 83
Cdd:cd02511    3 SVVIITKNEERNIERCLESVKWAVD----EIIVVDSGS-TDRTVEI----AKEYGAKVYQRWWDGFGA-QRNFALELATN 72
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 727185834  84 EIVFFLDSDDYFTTNYI--IRRMKKHEDRQIDIIF 116
Cdd:cd02511   73 DWVLSLDADERLTPELAdeILALLATDDYDGYYVP 107
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
2-112 7.10e-04

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 40.32  E-value: 7.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   2 DFSIVIPIYNSSR-YLPKTLKRIFnacQGFDYQVILVDDCSDEDDIKSIRQIAATN-SNVMLHEKKQKSNAAVsrnLGTK 79
Cdd:cd06434    1 DVTVIIPVYDEDPdVFRECLRSIL---RQKPLEIIVVTDGDDEPYLSILSQTVKYGgIFVITVPHPGKRRALA---EGIR 74
                         90       100       110
                 ....*....|....*....|....*....|...
gi 727185834  80 LAQSEIVFFLDSDDYFTTNYIIRRMKKHEDRQI 112
Cdd:cd06434   75 HVTTDIVVLLDSDTVWPPNALPEMLKPFEDPKV 107
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
5-92 1.21e-03

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 39.10  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727185834   5 IVIPIYNSSRYLPKTLKRIFNACQgFDYQVILVDDCSDEDDIKSIRQIAATnSNVMLHEKKQKSN---AAVSRNLGTKLA 81
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSI-LPFEVIIADDGSTEETKELIEEFKSQ-FPIPIKHVWQEDEgfrKAKIRNKAIAAA 78
                         90
                 ....*....|.
gi 727185834  82 QSEIVFFLDSD 92
Cdd:cd06420   79 KGDYLIFIDGD 89
 
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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