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Conserved domains on  [gi|2540313737|ref|WP_296493301|]
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glycosyltransferase family 2 protein [uncultured Actinomyces sp.]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11440371)

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:  9445404|12691742

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
88-364 5.67e-32

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 120.87  E-value: 5.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMSIV-SASRPGLSRARNRGVLAARGEV 166
Cdd:COG1216     6 SVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGS-TDGTAELLAALAFPRVRVIrNPENLGFAAARNLGLRAAGGDY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 167 IVFTDDDAIVDPHWLTAMIDPFtaspyvaattgialpleerykaqrwfesrggfpkdmsprvwcvgdvpsglealgekgd 246
Cdd:COG1216    85 LLFLDDDTVVEPDWLERLLAAA---------------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 247 ggplfpittarvgagvCMAIRRDVLMEVGPFDPALGAgtstrGGEDLDMFARILATGDVIVHTPDALVHHRHRVDeAGLD 326
Cdd:COG1216   107 ----------------CLLIRREVFEEVGGFDERFFL-----YGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGAS-SGPL 164

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2540313737 327 KQIRGNGSGMAALLTKAIIDKPSVLGTLIGRVPAILNR 364
Cdd:COG1216   165 LRAYYLGRNRLLFLRKHGPRPLLRLALLRGLRLRLRGR 202
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
88-364 5.67e-32

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 120.87  E-value: 5.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMSIV-SASRPGLSRARNRGVLAARGEV 166
Cdd:COG1216     6 SVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGS-TDGTAELLAALAFPRVRVIrNPENLGFAAARNLGLRAAGGDY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 167 IVFTDDDAIVDPHWLTAMIDPFtaspyvaattgialpleerykaqrwfesrggfpkdmsprvwcvgdvpsglealgekgd 246
Cdd:COG1216    85 LLFLDDDTVVEPDWLERLLAAA---------------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 247 ggplfpittarvgagvCMAIRRDVLMEVGPFDPALGAgtstrGGEDLDMFARILATGDVIVHTPDALVHHRHRVDeAGLD 326
Cdd:COG1216   107 ----------------CLLIRREVFEEVGGFDERFFL-----YGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGAS-SGPL 164

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2540313737 327 KQIRGNGSGMAALLTKAIIDKPSVLGTLIGRVPAILNR 364
Cdd:COG1216   165 LRAYYLGRNRLLFLRKHGPRPLLRLALLRGLRLRLRGR 202
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 89-225 3.04e-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: 95.65  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  89 VIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNA--PHTGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEV 166
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGstDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2540313737 167 IVFTDDDAIVDPHWLTAMIDPFTASPYVAATTGIALPLeerYKAQRWFESRGGFPKDMS 225
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL---FRRELLEEIGGFDEALLS 136
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 88-224 1.16e-18

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: 82.83  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMS---IVSASRPGLSRARNRGVLAARG 164
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGS-TDGTVEIAEEYAKKDPRvrvIRLPENRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540313737 165 EVIVFTDDDAIVDPHWLTAMIDPFTASPYVAATTGIALPLEERY---KAQRWFESRGGFPKDM 224
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGeyrRASRITLSRLPFFLGL 142
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 19-340 7.30e-15

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 76.34  E-value: 7.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  19 VDRTARVSQLVSGDPT-----SPRALVLVRDNGRNSAFVeiegtdHPENDPRVLEV---EAACARGWEEGAGADiDATVI 90
Cdd:TIGR03965   7 VRRYGGGRVLLGGSPLrllrlAPAAARLLGGGRGGALEV------RDETSAALLRRlldSGVVHPRPALLPSPP-SVTVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  91 MCTVGSCDMLEEAVRAILAQDHQRFSL--VVVDNAPHTGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEVIV 168
Cdd:TIGR03965  80 VPVRNRPAGLARLLAALLALDYPRDRLevIVVDDGSEDPVPTRAARGARLPVRVIRHPRRQGPAAARNAGARAARTEFVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 169 FTDDDAIVDPHWLTAMIDPFtASPYVAATTGIALPLEERYKA-QRWFESRGgfPKDMSPRVwcvgdvpsglealGEKGDG 247
Cdd:TIGR03965 160 FTDSDVVPRPGWLRALLAHF-DDPGVALVAPRVVALPAADTRlARYEAVRS--SLDLGPEE-------------AVVRPR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 248 GPLFPITTARVgagvcmAIRRDVLMEVGPFDPALgagtstRGGEDLDMFARILATGDVIVHTPDALVHHRHRVDEAGLDK 327
Cdd:TIGR03965 224 GPVSYVPSAAL------LVRRRALLEVGGFDERL------EVGEDVDLCWRLCEAGGRVRYEPAAVVAHDHRTRLWPWLA 291

                         330
                  ....*....|...
gi 2540313737 328 QIRGNGSGMAALL 340
Cdd:TIGR03965 292 RRAFYGTSAAPLA 304
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 98-178 1.62e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 43.50  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  98 DMLEEAVRAILAQDHQRFSLVVVDNAP--HTGQTREKLAGiTDTRMSIVSASRPGLSRARNRGVLAARGEVIVFTDDDAI 175
Cdd:PRK10073   19 KDFRAFMESLIAQTWTALEIIIVNDGStdNSVEIAKHYAE-NYPHVRLLHQANAGVSVARNTGLAVATGKYVAFPDADDV 97


                  ...
gi 2540313737 176 VDP 178
Cdd:PRK10073   98 VYP 100
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
88-364 5.67e-32

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 120.87  E-value: 5.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMSIV-SASRPGLSRARNRGVLAARGEV 166
Cdd:COG1216     6 SVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGS-TDGTAELLAALAFPRVRVIrNPENLGFAAARNLGLRAAGGDY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 167 IVFTDDDAIVDPHWLTAMIDPFtaspyvaattgialpleerykaqrwfesrggfpkdmsprvwcvgdvpsglealgekgd 246
Cdd:COG1216    85 LLFLDDDTVVEPDWLERLLAAA---------------------------------------------------------- 106

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 247 ggplfpittarvgagvCMAIRRDVLMEVGPFDPALGAgtstrGGEDLDMFARILATGDVIVHTPDALVHHRHRVDeAGLD 326
Cdd:COG1216   107 ----------------CLLIRREVFEEVGGFDERFFL-----YGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGAS-SGPL 164

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2540313737 327 KQIRGNGSGMAALLTKAIIDKPSVLGTLIGRVPAILNR 364
Cdd:COG1216   165 LRAYYLGRNRLLFLRKHGPRPLLRLALLRGLRLRLRGR 202
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 88-342 4.27e-26

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: 107.52  E-value: 4.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQD--HQRFSLVVVDNAPhTGQTREKL--AGITDTRMSIVS-ASRPGLSRARNRGVLAA 162
Cdd:COG1215    32 SVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGS-TDETAEIAreLAAEYPRVRVIErPENGGKAAALNAGLKAA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 163 RGEVIVFTDDDAIVDPHWLTAMIDPFtASPYVAATtgialpleerykaqrwfesrggfpkdmsprvwcvgdvpsglealg 242
Cdd:COG1215   111 RGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGAS--------------------------------------------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 243 ekgdggplfpittarvgaGVCMAIRRDVLMEVGPFDPalgagtsTRGGEDLDMFARILATGDVIVHTPDALVHHRHRVDE 322
Cdd:COG1215   145 ------------------GANLAFRREALEEVGGFDE-------DTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETL 199

                         250       260
                  ....*....|....*....|
gi 2540313737 323 AGLDKQIRGNGSGMAALLTK 342
Cdd:COG1215   200 RALFRQRRRWARGGLQLLLK 219
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 89-225 3.04e-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: 95.65  E-value: 3.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  89 VIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNA--PHTGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEV 166
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGstDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2540313737 167 IVFTDDDAIVDPHWLTAMIDPFTASPYVAATTGIALPLeerYKAQRWFESRGGFPKDMS 225
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL---FRRELLEEIGGFDEALLS 136
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 89-318 4.43e-21

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: 89.54  E-value: 4.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  89 VIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEVIV 168
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNAS-TDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 169 FTDDDAIVDPHWLTAMIDPFTASPYVAATTgialpleerykaqrwfesrggfpkdmsPRVWcvgdvpsglealgekgdgg 248
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAEQDPDVGIVG---------------------------PKVS------------------- 113

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 249 plfpittarvgaGVCMAIRRDVLMEVGPFDPALGAgtstrGGEDLDMFARILATGDVIVHTPDALVHHRH 318
Cdd:cd04186   114 ------------GAFLLVRREVFEEVGGFDEDFFL-----YYEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 88-330 1.39e-20

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 89.38  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKL--AGITDTRMSIVSASR-PGLSRARNRGVLAARG 164
Cdd:COG0463     5 SVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGS-TDGTAEILreLAAKDPRIRVIRLERnRGKGAARNAGLAAARG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 165 EVIVFTDDDAIVDPHWLTAMIDPFTASPYVAATtgialpleerykAQRWFESRGGFPKDMSPRVWCVGDVpsglealgek 244
Cdd:COG0463    84 DYIAFLDADDQLDPEKLEELVAALEEGPADLVY------------GSRLIREGESDLRRLGSRLFNLVRL---------- 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 245 gdggpLFPITTArvgAGVCMAIRRDVLMEVGpFDPALgagtstrgGEDLDMFaRILATGDVIVHTPdalVHHRHRVDEAG 324
Cdd:COG0463   142 -----LTNLPDS---TSGFRLFRREVLEELG-FDEGF--------LEDTELL-RALRHGFRIAEVP---VRYRAGESKLN 200


                  ....*.
gi 2540313737 325 LDKQIR 330
Cdd:COG0463   201 LRDLLR 206
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 88-224 1.16e-18

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: 82.83  E-value: 1.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMS---IVSASRPGLSRARNRGVLAARG 164
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGS-TDGTVEIAEEYAKKDPRvrvIRLPENRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2540313737 165 EVIVFTDDDAIVDPHWLTAMIDPFTASPYVAATTGIALPLEERY---KAQRWFESRGGFPKDM 224
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGeyrRASRITLSRLPFFLGL 142
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 98-279 1.09e-16

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


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 77.65  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  98 DMLEEAVRAILAQDHQRFSLVVVDNA--PHTGQTREKLAGITDTRMSIVSASRPGL-SRARNRGVLAARGEVIVFTDDDA 174
Cdd:cd06423    10 AVIERTIESLLALDYPKLEVIVVDDGstDDTLEILEELAALYIRRVLVVRDKENGGkAGALNAGLRHAKGDIVVVLDADT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 175 IVDPHWLTAMIDPFTASPYVAATTGIALPLEERY----KAQRWfESRGGFpkdmsprvwcvgdvpsGLEALGEKGDGGPL 250
Cdd:cd06423    90 ILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSEnlltRLQAI-EYLSIF----------------RLGRRAQSALGGVL 152

                         170       180
                  ....*....|....*....|....*....
gi 2540313737 251 FPittarvgAGVCMAIRRDVLMEVGPFDP 279
Cdd:cd06423   153 VL-------SGAFGAFRREALREVGGWDE 174
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 100-342 1.01e-15

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: 76.50  E-value: 1.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 100 LEEAVRAILAQD--HQRFSLVVVDnAPHTGQTREKLAGITDTRMSIVSASRPG--LSRARNRGVLAARGEVIVFTDDDAI 175
Cdd:cd02525    15 IEELLESLLNQSypKDLIEIIVVD-GGSTDGTREIVQEYAAKDPRIRLIDNPKriQSAGLNIGIRNSRGDIIIRVDAHAV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 176 VDPHWLTAMIDPFTASPyVAATTGIALPLEErykaqrwfesrggfpkdmSPRVWCVGDVPSGLEALGEKGDGGPLFPITT 255
Cdd:cd02525    94 YPKDYILELVEALKRTG-ADNVGGPMETIGE------------------SKFQKAIAVAQSSPLGSGGSAYRGGAVKIGY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 256 ARVGAGVCMaiRRDVLMEVGPFDPALGAgtstrgGEDLDMFARILATGDVIVHTPDALVHHRHRVDEAGLDKQIRGNGSG 335
Cdd:cd02525   155 VDTVHHGAY--RREVFEKVGGFDESLVR------NEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKW 226


                  ....*..
gi 2540313737 336 MAALLTK 342
Cdd:cd02525   227 RARTLRK 233
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 19-340 7.30e-15

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 76.34  E-value: 7.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  19 VDRTARVSQLVSGDPT-----SPRALVLVRDNGRNSAFVeiegtdHPENDPRVLEV---EAACARGWEEGAGADiDATVI 90
Cdd:TIGR03965   7 VRRYGGGRVLLGGSPLrllrlAPAAARLLGGGRGGALEV------RDETSAALLRRlldSGVVHPRPALLPSPP-SVTVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  91 MCTVGSCDMLEEAVRAILAQDHQRFSL--VVVDNAPHTGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEVIV 168
Cdd:TIGR03965  80 VPVRNRPAGLARLLAALLALDYPRDRLevIVVDDGSEDPVPTRAARGARLPVRVIRHPRRQGPAAARNAGARAARTEFVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 169 FTDDDAIVDPHWLTAMIDPFtASPYVAATTGIALPLEERYKA-QRWFESRGgfPKDMSPRVwcvgdvpsglealGEKGDG 247
Cdd:TIGR03965 160 FTDSDVVPRPGWLRALLAHF-DDPGVALVAPRVVALPAADTRlARYEAVRS--SLDLGPEE-------------AVVRPR 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 248 GPLFPITTARVgagvcmAIRRDVLMEVGPFDPALgagtstRGGEDLDMFARILATGDVIVHTPDALVHHRHRVDEAGLDK 327
Cdd:TIGR03965 224 GPVSYVPSAAL------LVRRRALLEVGGFDERL------EVGEDVDLCWRLCEAGGRVRYEPAAVVAHDHRTRLWPWLA 291

                         330
                  ....*....|...
gi 2540313737 328 QIRGNGSGMAALL 340
Cdd:TIGR03965 292 RRAFYGTSAAPLA 304
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 86-328 2.03e-13

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: 69.32  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  86 DATVIMCTVGSCDMLEEAVRAILAQDHQRFSLVVVDNaPHTGQTREKLAGIT----DTRMSIVSASRP----GLSRARNR 157
Cdd:pfam13641   3 DVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVN-PSDAETLDVAEEIAarfpDVRLRVIRNARLlgptGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 158 GVLAARGEVIVFTDDDAIVDPHWLTAMIDPFTASPYVAATTgialpleerykaQRWFESRGGfpkdmsprvwcvgdVPSG 237
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGT------------PVFSLNRST--------------MLSA 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 238 LEALGEKGDGGPlFPITTARVGA----GVCMAIRRDVLMEVGPFDPALGAgtstrgGEDLDMFARILATGDVIVHTPDAL 313
Cdd:pfam13641 136 LGALEFALRHLR-MMSLRLALGVlplsGAGSAIRREVLKELGLFDPFFLL------GDDKSLGRRLRRHGWRVAYAPDAA 208

                         250
                  ....*....|....*
gi 2540313737 314 VHHRHRVDEAGLDKQ 328
Cdd:pfam13641 209 VRTVFPTYLAASIKQ 223
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 166-315 2.06e-06

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 48.10  E-value: 2.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 166 VIVFTDDDAIVDPHWLtAMIDPFTASPYVAATTGIALPLEERYKAQRWFesrggfpkDMSPRVWCVGDVPSGlEALGEkg 245
Cdd:pfam13632   1 WILLLDADTVLPPDCL-LGIANEMASPEVAIIQGPILPMNVGNYLEELA--------ALFFADDHGKSIPVR-MALGR-- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 246 dggPLFPittarvgAGVCMAIRRDVLMEVGPFDPalgagTSTrgGEDLDMFARILATGDVIVHTPDALVH 315
Cdd:pfam13632  69 ---VLPF-------VGSGAFLRRSALQEVGGWDD-----GSV--SEDFDFGLRLQRAGYRVRFAPYSAVY 121
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 106-315 2.58e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 48.44  E-value: 2.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 106 AILAQD--HQRFSLVVVDNAPhTGQTREKLAGITDT---RMSIVSASRPGLSR---ARNRGVLAARGEVIVFTDDDAIVD 177
Cdd:cd04192    18 SLSALDypKEKFEVILVDDHS-TDGTVQILEFAAAKpnfQLKILNNSRVSISGkknALTTAIKAAKGDWIVTTDADCVVP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 178 PHWLTAMIDPFTASPYvaatTGIALPLEErYKAQRWFESRGGFPkdmsprvWCvgdVPSGLeALGEKGDGGPLFpittar 257
Cdd:cd04192    97 SNWLLTFVAFIQKEQI----GLVAGPVIY-FKGKSLLAKFQRLD-------WL---SLLGL-IAGSFGLGKPFM------ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2540313737 258 vGAGVCMAIRRDVLMEVGPFdpalgAGTSTRGGEDLDMFARILATGDVIVH---TPDALVH 315
Cdd:cd04192   155 -CNGANMAYRKEAFFEVGGF-----EGNDHIASGDDELLLAKVASKYPKVAylkNPEALVT 209
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 88-199 2.71e-06

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: 48.35  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  88 TVIMCTVGSCDMLEEAVRAILAQD--HQRFSLVVVDNAPhTGQTREKLAGITDTRMSIVSAS-RPGLSRARNRGVLAARG 164
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENLLALDypRDRLEIIVVSDGS-TDGTAEIAREYADKGVKLLRFPeRRGKAAALNRALALATG 110

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2540313737 165 EVIVFTDDDAIVDPHWLTAMIDPFtASPYVAATTG 199
Cdd:cd06439   111 EIVVFTDANALLDPDALRLLVRHF-ADPSVGAVSG 144
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 147-316 5.24e-06

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: 47.97  E-value: 5.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 147 SRPGLSRARNRGVLAARGEVIVFTDDDAIVDPHWLTAMIDPFTASPYVaattgIALPL-----EERYKAQRWFE-SRGGF 220
Cdd:cd02510    67 KREGLIRARIAGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKT-----VVCPIidvidADTFEYRGSSGdARGGF 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 221 pkDMSprVWCVGDVPSgleaLGEKGDGGPLFPITTARVGAGVcMAIRRDVLMEVGPFDPALgagtSTRGGEDLDMFARIL 300
Cdd:cd02510   142 --DWS--LHFKWLPLP----EEERRRESPTAPIRSPTMAGGL-FAIDREWFLELGGYDEGM----DIWGGENLELSFKVW 208

                         170
                  ....*....|....*.
gi 2540313737 301 ATGDVIVHTPDALVHH 316
Cdd:cd02510   209 QCGGSIEIVPCSRVGH 224
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 86-188 5.46e-06

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: 47.25  E-value: 5.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  86 DATVIMCTVGSC-DMLEEAVRAILAQdhQRFSLVVVDNAPHTGQtREKLAG-ITDTRMSIVSASRPGLSRARNRGVLAAR 163
Cdd:cd06434     1 DVTVIIPVYDEDpDVFRECLRSILRQ--KPLEIIVVTDGDDEPY-LSILSQtVKYGGIFVITVPHPGKRRALAEGIRHVT 77

                          90       100
                  ....*....|....*....|....*
gi 2540313737 164 GEVIVFTDDDAIVDPHWLTAMIDPF 188
Cdd:cd06434    78 TDIVVLLDSDTVWPPNALPEMLKPF 102
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 100-301 6.67e-06

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: 47.66  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 100 LEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMSIVSASRP----GLSRARNRGVLAARGEVIVFTDDDAI 175
Cdd:pfam10111  15 IQERILNQTFQYDPEFELIIINDGS-TDKTLEEVSSIKDHNLQVYYPNAPdttySLAASRNRGTSHAIGEYISFIDGDCL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 176 VDPHWLTAMIDPFTASPYVA-ATTGIALPLEERYKAQRWFESRGGfpkDMSprvwCVGDVPSGLEALGEkgdggplfPIT 254
Cdd:pfam10111  94 WSPDKFEKQLKIATSLALQEnIQAAVVLPVTDLNDESSNFLRRGG---DLT----ASGDVLRDLLVFYS--------PLA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2540313737 255 TARVGAGVCMAIRRDVLMEVGPFDPALGAgtstRGGEDLDMFARILA 301
Cdd:pfam10111 159 IFFAPNSSNALINRQAFIEVGGFDESFRG----HGAEDFDIFLRLAA 201
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 100-192 9.97e-06

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: 46.04  E-value: 9.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 100 LEEAVRAILAQDHQRFSLVVVDNA---PHTGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEVIVFTDDDAIV 176
Cdd:cd04184    17 LREAIESVRAQTYPNWELCIADDAstdPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALELATGEFVALLDHDDEL 96

                          90
                  ....*....|....*.
gi 2540313737 177 DPHWLTAMIDPFTASP 192
Cdd:cd04184    97 APHALYEVVKALNEHP 112
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 100-317 1.20e-05

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: 46.00  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 100 LEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEVIVFT-DDDAIVDP 178
Cdd:cd06433    13 LEETIDSVLSQTYPNIEYIVIDGGS-TDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIGFLnSDDTLLPG 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 179 HwLTAMIDPFTASPYVAATTGIALPLEERYKAQRWFESRGGFPKDMsprvwcvgdvpsglealgekgdggplfpittaRV 258
Cdd:cd06433    92 A-LLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFL--------------------------------LY 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2540313737 259 GAGVC---MAIRRDVLMEVGPFDpalgagTSTRGGEDLDMFARILATGDVIVHTPDALVHHR 317
Cdd:cd06433   139 GMPIChqaTFFRRSLFEKYGGFD------ESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFR 194
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 98-178 1.62e-04

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 43.50  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  98 DMLEEAVRAILAQDHQRFSLVVVDNAP--HTGQTREKLAGiTDTRMSIVSASRPGLSRARNRGVLAARGEVIVFTDDDAI 175
Cdd:PRK10073   19 KDFRAFMESLIAQTWTALEIIIVNDGStdNSVEIAKHYAE-NYPHVRLLHQANAGVSVARNTGLAVATGKYVAFPDADDV 97


                  ...
gi 2540313737 176 VDP 178
Cdd:PRK10073   98 VYP 100
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 140-289 3.52e-04

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: 41.11  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 140 RMSIVSASRPGLSRARN---RGVLAARGEVIVFTDDDAIVDPHWLTAMIDPFTaSPYVAATTGIalpleerykaqrwfes 216
Cdd:pfam13506   4 RALVVGGPPVGVNPKVNnllQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLA-DPKVGLVTSP---------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 217 rggfpkdmsPRvwcVGDvPSGLEALGEKGDGGPLFPITTARVGA-----GVCMAIRRDVLMEVGPFDP---------ALG 282
Cdd:pfam13506  67 ---------PV---GSD-PKGLAAALEAAFFNTLAGVLQAALSGigfavGMSMAFRRADLERIGGFEAladylaedyALG 133


                  ....*..
gi 2540313737 283 AGTSTRG 289
Cdd:pfam13506 134 KLLRAAG 140
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 98-193 8.92e-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: 40.25  E-value: 8.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737  98 DMLEEAVRAILA--QDHQRFSLVVVDNAPhTGQTREKL--AGITDTRMSIVSASRP-GLSRARNRGVLAARGEVIVFTDD 172
Cdd:cd04179    10 ENIPELVERLLAvlEEGYDYEIIVVDDGS-TDGTAEIAreLAARVPRVRVIRLSRNfGKGAAVRAGFKAARGDIVVTMDA 88

                          90       100
                  ....*....|....*....|.
gi 2540313737 173 DAIVDPHWLTAMIDPFTASPY 193
Cdd:cd04179    89 DLQHPPEDIPKLLEKLLEGGA 109
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
103-185 1.34e-03

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 40.36  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 103 AVRAILAQDHQRFSLVVVDNAPHTGQTREK-LAGITDTRMSIV-SASRPGLSRARNRGVLAARGEVIVFTDDDAIVDPHW 180
Cdd:PRK10018   23 AIKSVLRQDYSNWEMIIVDDCSTSWEQLQQyVTALNDPRITYIhNDINSGACAVRNQAIMLAQGEYITGIDDDDEWTPNR 102


                  ....*
gi 2540313737 181 LTAMI 185
Cdd:PRK10018  103 LSVFL 107
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 151-180 2.84e-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: 38.71  E-value: 2.84e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2540313737 151 LSRARNRGVLAARGEVIVFTDDDAIVDPHW 180
Cdd:cd06420    67 KAKIRNKAIAAAKGDYLIFIDGDCIPHPDF 96
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 99-173 3.17e-03

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: 38.70  E-value: 3.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2540313737  99 MLEEAVRAILAQDHQRFSLVVVDNAPhTGQTREKLAGITDTRMSIV----SASRPGLSRARNRGVLAARGEVIVFTDDD 173
Cdd:cd04188    15 TLEEAVEYLEERPSFSYEIIVVDDGS-KDGTAEVARKLARKNPALIrvltLPKNRGKGGAVRAGMLAARGDYILFADAD 92
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 100-196 4.87e-03

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: 38.32  E-value: 4.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 100 LEEAVRAILAQDHQRFSLVVVDnAPHTGQTREKLAGITDTRMSivsaSRPGlsRAR--NRGVLAARGEVIVFTDDDAIVD 177
Cdd:cd02522    14 LPRLLASLRRLNPLPLEIIVVD-GGSTDGTVAIARSAGVVVIS----SPKG--RARqmNAGAAAARGDWLLFLHADTRLP 86

                          90
                  ....*....|....*....
gi 2540313737 178 PHWLTAMIDPFTASPYVAA 196
Cdd:cd02522    87 PDWDAAIIETLRADGAVAG 105
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 117-185 9.53e-03

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: 37.51  E-value: 9.53e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2540313737 117 LVVVDNAPH-TGQTREKLAGITDTRMSIVSASRPGLSRARNRGVLAARGEVIVFTDDDAIVDPHWLTAMI 185
Cdd:cd06442    31 IVVDDNSPDgTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGDVIVVMDADLSHPPEYIPELL 100
 
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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