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Conserved domains on  [gi|1084062691|gb|OGK67570|]
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hypothetical protein A2377_01855 [Candidatus Roizmanbacteria bacterium RIFOXYB1_FULL_41_27]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10118426)

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

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  9445404|12691742|10508766|12200473|10521532
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-232 6.15e-48

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: 158.22  E-value: 6.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   5 RITVVFQVKNEQAQIKEAIESARLLTNNIVVMDMRSSDDTALIAKKAGAKVIAIPsAIYVEPVRQYAFSKTNSDWVLILD 84
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRW-WDGFGAQRNFALELATNDWVLSLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691  85 ADERLTKAIAAEIKQTIASkSSHTHYYLSRLNTFNGQVFKHGGWWPDNQIRLIKKESFVKWPKNIHSTVQVTGKPGK-LD 163
Cdd:cd02511    80 ADERLTPELADEILALLAT-DDYDGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIvLK 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084062691 164 NCFLHYFHGDLTQMVNKTIKFEDIESELLFKAG--RAVNTATFFRKYFGELYRRLLKHQGWRDGSYGIIES 232
Cdd:cd02511   159 GDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGkkRSLLKGLLLGRPLLAFLKMYILKRGFLDGRAGFILA 229
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-232 6.15e-48

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: 158.22  E-value: 6.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   5 RITVVFQVKNEQAQIKEAIESARLLTNNIVVMDMRSSDDTALIAKKAGAKVIAIPsAIYVEPVRQYAFSKTNSDWVLILD 84
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRW-WDGFGAQRNFALELATNDWVLSLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691  85 ADERLTKAIAAEIKQTIASkSSHTHYYLSRLNTFNGQVFKHGGWWPDNQIRLIKKESFVKWPKNIHSTVQVTGKPGK-LD 163
Cdd:cd02511    80 ADERLTPELADEILALLAT-DDYDGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIvLK 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084062691 164 NCFLHYFHGDLTQMVNKTIKFEDIESELLFKAG--RAVNTATFFRKYFGELYRRLLKHQGWRDGSYGIIES 232
Cdd:cd02511   159 GDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGkkRSLLKGLLLGRPLLAFLKMYILKRGFLDGRAGFILA 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-139 7.60e-10

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 57.02  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   5 RITVVFQVKNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKKAGA-----KVIAIPSAIYVEPVRQYAFSKTN 76
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPdfeIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAAAR 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084062691  77 SDWVLILDADERLTKAIAAEIKQTIASKSSHtHYYLSRLNTFNGQVFKHGGWWPDNQIRLIKK 139
Cdd:COG0463    83 GDYIAFLDADDQLDPEKLEELVAALEEGPAD-LVYGSRLIREGESDLRRLGSRLFNLVRLLTN 144
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 2-57 1.77e-07

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 51.07  E-value: 1.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084062691   2 AKQ--RITVVFQVKNEQAQIKEAIESARLLTNN-----IVVMDMRSSDDTALIAKKAGAKVIA 57
Cdd:PRK13915   27 AKAgrTVSVVLPALNEEETVGKVVDSIRPLLMEplvdeLIVIDSGSTDATAERAAAAGARVVS 89
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-95 9.53e-07

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: 47.39  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   7 TVVFQVKNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKKA-----GAKVIAIPSAIYVEPVRQYAFSKTNSD 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPnfeIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|..
gi 1084062691  79 WVLILDAD-----ERLTKAIAA 95
Cdd:pfam00535  81 YIAFLDADdevppDWLEKLVEA 102
 
Name Accession Description Interval E-value
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-232 6.15e-48

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: 158.22  E-value: 6.15e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   5 RITVVFQVKNEQAQIKEAIESARLLTNNIVVMDMRSSDDTALIAKKAGAKVIAIPsAIYVEPVRQYAFSKTNSDWVLILD 84
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKWAVDEIIVVDSGSTDRTVEIAKEYGAKVYQRW-WDGFGAQRNFALELATNDWVLSLD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691  85 ADERLTKAIAAEIKQTIASkSSHTHYYLSRLNTFNGQVFKHGGWWPDNQIRLIKKESFVKWPKNIHSTVQVTGKPGK-LD 163
Cdd:cd02511    80 ADERLTPELADEILALLAT-DDYDGYYVPRRNFFLGRWIRHGGWYPDRQLRLFRRGKARFEDGRVHEQVVVDGGVGIvLK 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084062691 164 NCFLHYFHGDLTQMVNKTIKFEDIESELLFKAG--RAVNTATFFRKYFGELYRRLLKHQGWRDGSYGIIES 232
Cdd:cd02511   159 GDILHYGYKSLEEFLEKHNRYSSLEAKDLAAKGkkRSLLKGLLLGRPLLAFLKMYILKRGFLDGRAGFILA 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-139 7.60e-10

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 57.02  E-value: 7.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   5 RITVVFQVKNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKKAGA-----KVIAIPSAIYVEPVRQYAFSKTN 76
Cdd:COG0463     3 LVSVVIPTYNEEEYLEEALESLLAQTYPdfeIIVVDDGSTDGTAEILRELAAkdpriRVIRLERNRGKGAARNAGLAAAR 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084062691  77 SDWVLILDADERLTKAIAAEIKQTIASKSSHtHYYLSRLNTFNGQVFKHGGWWPDNQIRLIKK 139
Cdd:COG0463    83 GDYIAFLDADDQLDPEKLEELVAALEEGPAD-LVYGSRLIREGESDLRRLGSRLFNLVRLLTN 144
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 5-91 4.01e-08

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: 52.82  E-value: 4.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   5 RITVVFQVKNEQAQIKEAIESARLLT-----NNIVVMDMRSSDDTALIAKKAGAKVIAIpSAIYVEP------VRQYAFS 73
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQDypkekLEVIVVDDGSTDETAEIARELAAEYPRV-RVIERPEnggkaaALNAGLK 108

                          90
                  ....*....|....*...
gi 1084062691  74 KTNSDWVLILDADERLTK 91
Cdd:COG1215   109 AARGDIVVFLDADTVLDP 126
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 2-57 1.77e-07

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 51.07  E-value: 1.77e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084062691   2 AKQ--RITVVFQVKNEQAQIKEAIESARLLTNN-----IVVMDMRSSDDTALIAKKAGAKVIA 57
Cdd:PRK13915   27 AKAgrTVSVVLPALNEEETVGKVVDSIRPLLMEplvdeLIVIDSGSTDATAERAAAAGARVVS 89
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-95 9.53e-07

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: 47.39  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   7 TVVFQVKNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKKA-----GAKVIAIPSAIYVEPVRQYAFSKTNSD 78
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPnfeIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100
                  ....*....|....*....|..
gi 1084062691  79 WVLILDAD-----ERLTKAIAA 95
Cdd:pfam00535  81 YIAFLDADdevppDWLEKLVEA 102
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 13-91 1.65e-06

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: 47.22  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691  13 KNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKKAGAKVIAIPSAIYVEPVR------QYAFSKTNSDWVLIL 83
Cdd:cd06423     6 YNEEAVIERTIESLLALDYPkleVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGgkagalNAGLRHAKGDIVVVL 85


                  ....*...
gi 1084062691  84 DADERLTK 91
Cdd:cd06423    86 DADTILEP 93
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-86 5.24e-06

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: 45.19  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   8 VVFQVKNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKKAGAKVIAIPSAIYVEP-----VRQYAFSKTNSDW 79
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPnfeVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENqglaaARNAGLKAARGEY 80


                  ....*..
gi 1084062691  80 VLILDAD 86
Cdd:cd00761    81 ILFLDAD 87
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 6-104 2.09e-05

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: 44.48  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   6 ITVVFQVKNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKKAGAKViaipsaIYVEPVR--Q--YAFSKTNSD 78
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLpleIIVVDGGSTDGTVAIARSAGVVV------ISSPKGRarQmnAGAAAARGD 74

                          90       100
                  ....*....|....*....|....*..
gi 1084062691  79 WVLILDADERLTK-AIAAEIKQTIASK 104
Cdd:cd02522    75 WLLFLHADTRLPPdWDAAIIETLRADG 101
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 8-86 2.87e-04

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: 40.63  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   8 VVFQVKNEQAQIKEAIESAR-----LLTNNIVVMDMRSSDDTALIAKKAGAKViaiPSAIYVEPVR--------QYAFSK 74
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLavleeGYDYEIIVVDDGSTDGTAEIARELAARV---PRVRVIRLSRnfgkgaavRAGFKA 77

                          90
                  ....*....|..
gi 1084062691  75 TNSDWVLILDAD 86
Cdd:cd04179    78 ARGDIVVTMDAD 89
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
5-90 7.61e-04

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 39.59  E-value: 7.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   5 RITVVFQVKNEQAQIKEAIESARLLTNN---IVVMDMRSSDDTALIAKK---AGAKVIAIPSAIYVEPVRQYAFSKTNSD 78
Cdd:COG1216     4 KVSVVIPTYNRPELLRRCLESLLAQTYPpfeVIVVDNGSTDGTAELLAAlafPRVRVIRNPENLGFAAARNLGLRAAGGD 83

                          90
                  ....*....|..
gi 1084062691  79 WVLILDADERLT 90
Cdd:COG1216    84 YLLFLDDDTVVE 95
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 6-89 5.89e-03

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: 36.75  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084062691   6 ITVVFqvkNEQAQIKEAIESARLLT-NNI--VVMDMRSSDDTALIAKKAGAKVIAIPSaiyvEPVR-QY-----AFSKTN 76
Cdd:cd06433     3 ITPTY---NQAETLEETIDSVLSQTyPNIeyIVIDGGSTDGTVDIIKKYEDKITYWIS----EPDKgIYdamnkGIALAT 75

                          90
                  ....*....|...
gi 1084062691  77 SDWVLILDADERL 89
Cdd:cd06433    76 GDIIGFLNSDDTL 88
 
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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