NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|501814207|ref|WP_012646473|]
View 

GPMC system family 4 glycosyltransferase [Geotalea daltonii]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 17609148)

glycosyltransferase family 4 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Glyco4_Geo_Pelo NF038229
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 2-340 2.68e-176

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


:

Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 492.19  E-value: 2.68e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   2 KLGIITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTAEEIGSEVDAARPELIHAFHGHSGGRVAYRLKEQYGI 81
Cdd:NF038229   1 RILIITPYYQPPVTGNAVTVRRIARHLEQLGHEVRVLELDALDAAEILAALRQFRPDIIHAFHAYRSGRVWLELARALGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  82 PYVITLTGTDIYEAIIDHRREETFRALNGAAGLVVFHESVRDRLLNHLSQLEANTVVIPQGVELPEEPCRRAREFPFSSD 161
Cdd:NF038229  81 PYLVTLTGTDVNEALDPDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLAAKLVVIPQGVELGGEPFPLRELGLFDSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 162 SFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEV 241
Cdd:NF038229 161 EFVFLLPAGLRPVKGVLFLLEMLAPLHAEDPRLRLAFAGPVLDEEYAAAFFAALARRPWARYLGEIPHDAMGALYRRADV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 242 VLNTSIFEgGMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLYQNERQFLQKAEQLVCRPDMRAAFGAAGRTLARER 321
Cdd:NF038229 241 VLNNSLFE-GMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLLYRDEAEFLRQARQLLQDPALRRRLGRPGRQLVRER 319

                        330
                 ....*....|....*....
gi 501814207 322 FAPEKEIAGYLQLYQGVLR 340
Cdd:NF038229 320 YSPEREAEAYLRLYRAVLA 338
 
Name Accession Description Interval E-value
Glyco4_Geo_Pelo NF038229
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 2-340 2.68e-176

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 492.19  E-value: 2.68e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   2 KLGIITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTAEEIGSEVDAARPELIHAFHGHSGGRVAYRLKEQYGI 81
Cdd:NF038229   1 RILIITPYYQPPVTGNAVTVRRIARHLEQLGHEVRVLELDALDAAEILAALRQFRPDIIHAFHAYRSGRVWLELARALGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  82 PYVITLTGTDIYEAIIDHRREETFRALNGAAGLVVFHESVRDRLLNHLSQLEANTVVIPQGVELPEEPCRRAREFPFSSD 161
Cdd:NF038229  81 PYLVTLTGTDVNEALDPDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLAAKLVVIPQGVELGGEPFPLRELGLFDSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 162 SFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEV 241
Cdd:NF038229 161 EFVFLLPAGLRPVKGVLFLLEMLAPLHAEDPRLRLAFAGPVLDEEYAAAFFAALARRPWARYLGEIPHDAMGALYRRADV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 242 VLNTSIFEgGMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLYQNERQFLQKAEQLVCRPDMRAAFGAAGRTLARER 321
Cdd:NF038229 241 VLNNSLFE-GMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLLYRDEAEFLRQARQLLQDPALRRRLGRPGRQLVRER 319

                        330
                 ....*....|....*....
gi 501814207 322 FAPEKEIAGYLQLYQGVLR 340
Cdd:NF038229 320 YSPEREAEAYLRLYRAVLA 338
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-336 4.08e-43

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 152.69  E-value: 4.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   2 KLGIITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTA---------------------------EEIGSEVDA 54
Cdd:cd03801    1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEppeeledgvivpllpslaallrarrllRELRPLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  55 ARPELIHAfHGHSGGRVAYRLKEQYGIPYVITLTGTDIYEAIIDHRREETF-----RALNGAAGLVVFHESVRDRLLNHL 129
Cdd:cd03801   81 RKFDVVHA-HGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLlaraeALLRRADAVIAVSEALRDELRALG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 130 SQLEANTVVIPQGVELPEEPCRRAREFPFSSDSFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGPvlDPAYAA 209
Cdd:cd03801  160 GIPPEKIVVIPNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG--DGPLRA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 210 QVMD-SLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEgGMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLY- 287
Cdd:cd03801  238 ELEElELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYE-GFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVp 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 501814207 288 -QNERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYLQLYQ 336
Cdd:cd03801  317 pDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 235-340 5.20e-19

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 81.58  E-value: 5.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 235 LYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLY--QNERQFLQKAEQLVCRPDMRAAFGA 312
Cdd:COG0438   17 LLAAADVFVLPSRSEG-FGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLEDPELRRRLGE 95

                         90       100
                 ....*....|....*....|....*...
gi 501814207 313 AGRTLARERFAPEKEIAGYLQLYQGVLR 340
Cdd:COG0438   96 AARERAEERFSWEAIAERLLALYEELLA 123
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 171-315 2.84e-15

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 72.31  E-value: 2.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  171 LRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEG 250
Cdd:pfam00534  11 LEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501814207  251 -GMAnsILEALAYGKAVLAADIEGNRSLIADGKTGFLYQ--NERQFLQKAEQLVCRPDMRAAFGAAGR 315
Cdd:pfam00534  91 fGIV--LLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLEDEELRERLGENAR 156
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 189-315 2.22e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 48.94  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 189 DQYPRIRLILAGpvlDPAYAAQVMDSLEGYPfAHYLGGIGHDEMGCLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLA 268
Cdd:PLN02871 286 ERLPGARLAFVG---DGPYREELEKMFAGTP-TVFTGMLQGDELSQAYASGDVFVMPSESET-LGFVVLEAMASGVPVVA 360

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501814207 269 ADIEGNRSLIAD---GKTGFLYQ--NERQFLQKAEQLVCRPDMRAAFGAAGR 315
Cdd:PLN02871 361 ARAGGIPDIIPPdqeGKTGFLYTpgDVDDCVEKLETLLADPELRERMGAAAR 412
 
Name Accession Description Interval E-value
Glyco4_Geo_Pelo NF038229
GPMC system family 4 glycosyltransferase; Members of this family are family 4 ...
 2-340 2.68e-176

GPMC system family 4 glycosyltransferase; Members of this family are family 4 glycosyltransferases of the GPMC (Geobacter/Pelobacter Mystery Cassette) system, in which the most distinctive signature is the TIGR04442 protein family.


Pssm-ID: 439530 [Multi-domain]  Cd Length: 338  Bit Score: 492.19  E-value: 2.68e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   2 KLGIITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTAEEIGSEVDAARPELIHAFHGHSGGRVAYRLKEQYGI 81
Cdd:NF038229   1 RILIITPYYQPPVTGNAVTVRRIARHLEQLGHEVRVLELDALDAAEILAALRQFRPDIIHAFHAYRSGRVWLELARALGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  82 PYVITLTGTDIYEAIIDHRREETFRALNGAAGLVVFHESVRDRLLNHLSQLEANTVVIPQGVELPEEPCRRAREFPFSSD 161
Cdd:NF038229  81 PYLVTLTGTDVNEALDPDRRPETLRVLRGAAAIVAFNPLVRERLGQHLPPLAAKLVVIPQGVELGGEPFPLRELGLFDSD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 162 SFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEV 241
Cdd:NF038229 161 EFVFLLPAGLRPVKGVLFLLEMLAPLHAEDPRLRLAFAGPVLDEEYAAAFFAALARRPWARYLGEIPHDAMGALYRRADV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 242 VLNTSIFEgGMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLYQNERQFLQKAEQLVCRPDMRAAFGAAGRTLARER 321
Cdd:NF038229 241 VLNNSLFE-GMANALLEAMALGRPVLARDIPGNRSVVRPGVTGLLYRDEAEFLRQARQLLQDPALRRRLGRPGRQLVRER 319

                        330
                 ....*....|....*....
gi 501814207 322 FAPEKEIAGYLQLYQGVLR 340
Cdd:NF038229 320 YSPEREAEAYLRLYRAVLA 338
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-336 4.08e-43

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 152.69  E-value: 4.08e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   2 KLGIITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTA---------------------------EEIGSEVDA 54
Cdd:cd03801    1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEppeeledgvivpllpslaallrarrllRELRPLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  55 ARPELIHAfHGHSGGRVAYRLKEQYGIPYVITLTGTDIYEAIIDHRREETF-----RALNGAAGLVVFHESVRDRLLNHL 129
Cdd:cd03801   81 RKFDVVHA-HGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLlaraeALLRRADAVIAVSEALRDELRALG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 130 SQLEANTVVIPQGVELPEEPCRRAREFPFSSDSFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGPvlDPAYAA 209
Cdd:cd03801  160 GIPPEKIVVIPNGVDLERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGG--DGPLRA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 210 QVMD-SLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEgGMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLY- 287
Cdd:cd03801  238 ELEElELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYE-GFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVp 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 501814207 288 -QNERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYLQLYQ 336
Cdd:cd03801  317 pDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 56-338 3.80e-23

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 98.61  E-value: 3.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  56 RPELIHAFHGHSGGRVAYRLKEQYGIPYVITLTGTDIYEaiidHRREETFRALNG-----AAGLVVFHESVRDRLLNHLS 130
Cdd:cd03798   95 PPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHGSDINV----FPPRSLLRKLLRwalrrAARVIAVSKALAEELVALGV 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 131 QLEaNTVVIPQGVEL----PEEPCRRAREfpfssdSFSFLLPAG-LRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDP 205
Cdd:cd03798  171 PRD-RVDVIPNGVDParfqPEDRGLGLPL------DAFVILFVGrLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPLR 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 206 AYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEgGMANSILEALAYGKAVLAADIEGNRSLIADGKTGF 285
Cdd:cd03798  244 EALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHE-GFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGL 322

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 501814207 286 LY--QNERQFLQKAEQLVCRPDMRAAfGAAGRTLARERFAPEKEIAGYLQLYQGV 338
Cdd:cd03798  323 LVppGDADALAAALRRALAEPYLREL-GEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 56-332 4.76e-21

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 92.27  E-value: 4.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  56 RPELIHAFHGHSG--GRVAYRLKeqyGIPYVI-TLTG---TDIYEAIIDH--RREEtFRALNGAAGLVVFHESVRDRLLN 127
Cdd:cd03808   81 KPDIVHCHTPKPGilGRLAARLA---GVPKVIyTVHGlgfVFTEGKLLRLlyLLLE-KLALLFTDKVIFVNEDDRDLAIK 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 128 HLSQLEANTVVIPqGVELPEEPCRRaREFPFSSDSFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGP-VLDPA 206
Cdd:cd03808  157 KGIIKKKKTVLIP-GSGVDLDRFQY-SPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDgELENP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 207 YAAQVMD-SLEGYpfAHYLGGIghDEMGCLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRSLIADGKTGF 285
Cdd:cd03808  235 SEILIEKlGLEGR--IEFLGFR--SDVPELLAESDVFVLPSYREG-LPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGF 309

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 501814207 286 LYQ--NERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYL 332
Cdd:cd03808  310 LVPpgDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKLL 358
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 235-340 5.20e-19

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 81.58  E-value: 5.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 235 LYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLY--QNERQFLQKAEQLVCRPDMRAAFGA 312
Cdd:COG0438   17 LLAAADVFVLPSRSEG-FGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLEDPELRRRLGE 95

                         90       100
                 ....*....|....*....|....*...
gi 501814207 313 AGRTLARERFAPEKEIAGYLQLYQGVLR 340
Cdd:COG0438   96 AARERAEERFSWEAIAERLLALYEELLA 123
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 56-335 1.73e-16

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 79.28  E-value: 1.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  56 RPELIHAFHGHSG--GRVAYRLKEqyGIPYVITLTGTDIYE-AIIDHRREETFRALNGAAGLVVFHESVRDRLLNHLSQl 132
Cdd:cd03807   79 NPDVVHTWMYHADliGGLAAKLAG--GVKVIWSVRSSNIPQrLTRLVRKLCLLLSKFSPATVANSSAVAEFHQEQGYAK- 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 133 eANTVVIPQGVEL----PEEPCRR--AREFPFSSDSFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPA 206
Cdd:cd03807  156 -NKIVVIYNGIDLfklsPDDASRAraRRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERP 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 207 YAAQVMD--SLEGYpfAHYLGGIGHdeMGCLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNrSLIADGKTG 284
Cdd:cd03807  235 NLERLLLelGLEDR--VHLLGERSD--VPALLPAMDIFVLSSRTEG-FPNALLEAMACGLPVVATDVGGA-AELVDDGTG 308

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 501814207 285 FLYQNER--QFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYLQLY 335
Cdd:cd03807  309 FLVPAGDpqALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYETLY 361
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 3-287 2.88e-16

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 77.06  E-value: 2.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   3 LGIITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTAEEIGSEVDAARPELIHAFHGHSGGRVAYRLKEQYGIP 82
Cdd:cd01635    1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLALRRILKKLLELKPDVVHAHSPHAAALAALLAARLLGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  83 YVITLTGTDIYeaiiDHRREETFRALNGAAGLVVFHEsvrdrllnhlsqleantvvipqgvelpeepcrrarefpfssds 162
Cdd:cd01635   81 IVVTVHGPDSL----ESTRSELLALARLLVSLPLADK------------------------------------------- 113

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 163 fsfLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVMDSLEGYPFAHYLGGIGHDE-MGCLYNKAEV 241
Cdd:cd01635  114 ---VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEvLELLLAAADV 190

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 501814207 242 VLNTSIFEGgMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLY 287
Cdd:cd01635  191 FVLPSRSEG-FGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 6-319 2.60e-15

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 75.85  E-value: 2.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   6 ITPHYYPlmrGNAVT-VRRIEKNLANAGVEVAVYSLD---AMTAEEIGSEVDAA---------------------RPELI 60
Cdd:cd03819    4 LTPALEI---GGAETyILDLARALAERGHRVLVVTAGgplLPRLRQIGIGLPGLkvpllrallgnvrlarlirreRIDLI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  61 HAfhgHSGG--RVAYRLKEQYGIPYVITLTGTDI-YEAIIDHRREETFRALNGAAGLvvfhESVRDRLLNHLSQLEANTV 137
Cdd:cd03819   81 HA---HSRApaWLGWLASRLTGVPLVTTVHGSYLaTYHPKDFALAVRARGDRVIAVS----ELVRDHLIEALGVDPERIR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 138 VIPQGVEL----PEEPCRRAREFPFSSDSFSFLLPAGLRPVKNVLFPLGPLAALHDQyPRIRLILAGpvlDPAYAAQVMD 213
Cdd:cd03819  154 VIPNGVDTdrfpPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDE-PDFRLLVAG---DGPERDEIRR 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 214 SLEGYPFAHYLGGIGHDE-MGCLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRSLIADGKTGFL---YQN 289
Cdd:cd03819  230 LVERLGLRDRVTFTGFREdVPAALAASDVVVLPSLHEE-FGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLvppGDA 308

                        330       340       350
                 ....*....|....*....|....*....|
gi 501814207 290 ERqFLQKAEQLVCRPDMRAAFGAAGRTLAR 319
Cdd:cd03819  309 EA-LADAIRAAKLLPEAREKLQAAAALTEA 337
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 171-315 2.84e-15

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 72.31  E-value: 2.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  171 LRPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEG 250
Cdd:pfam00534  11 LEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501814207  251 -GMAnsILEALAYGKAVLAADIEGNRSLIADGKTGFLYQ--NERQFLQKAEQLVCRPDMRAAFGAAGR 315
Cdd:pfam00534  91 fGIV--LLEAMACGLPVIASDVGGPPEVVKDGETGFLVKpnNAEALAEAIDKLLEDEELRERLGENAR 156
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 56-333 1.90e-14

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 73.43  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  56 RPELIHAFHGHSGgRVAYRLKEQYGIPYVIT-----------LTGTDIYEaiIDHRREETFRALNGAAGLVVFHESVRDR 124
Cdd:cd03800  101 RYDLIHSHYWDSG-LVGALLARRLGVPLVHTfhslgrvkyrhLGAQDTYH--PSLRITAEEQILEAADRVIASTPQEADE 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 125 LLNHLSQLEANTVVIPQGVEL----PEEPCRRAREFPFSSDSFSFLLPAG-LRPVKNVLFPLGPLAALHDQYPRIRLILA 199
Cdd:cd03800  178 LISLYGADPSRINVVPPGVDLerffPVDRAEARRARLLLPPDKPVVLALGrLDPRKGIDTLVRAFAQLPELRELANLVLV 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 200 G-----PVLDPAYAAQVMDSLEG----YpfaHYLGGIGHDEMGCLYNKAEVVLNTSIFEG-GManSILEALAYGKAVLAA 269
Cdd:cd03800  258 GgpsddPLSMDREELAELAEELGlidrV---RFPGRVSRDDLPELYRAADVFVVPSLYEPfGL--TAIEAMACGTPVVAT 332

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501814207 270 DIEGNRSLIADGKTGFLY--QNERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYLQ 333
Cdd:cd03800  333 AVGGLQDIVRDGRTGLLVdpHDPEALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQLLT 398
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 5-328 4.07e-14

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 72.76  E-value: 4.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   5 IITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYS-----LDAMTAEEIGSEVDAA------------------------ 55
Cdd:cd03794    4 LISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTpspnyPLGRIFAGATETKDGIrvirvklgpikknglirrllnyls 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  56 --------------RPELIHAFHG-HSGGRVAYRLKEQYGIPYVITLTgtDIY-EAIID--HRREETF---------RAL 108
Cdd:cd03794   84 falaallkllvreeRPDVIIAYSPpITLGLAALLLKKLRGAPFILDVR--DLWpESLIAlgVLKKGSLlkllkklerKLY 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 109 NGAAGLVVFHESVRDRLLNHlSQLEANTVVIPQGVELPE--EPCRRAREFPFSSDSFSFLLPAGLRPVKNVLFPLGPLAA 186
Cdd:cd03794  162 RLADAIIVLSPGLKEYLLRK-GVPKEKIIVIPNWADLEEfkPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAAE 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 187 LHDQYPRIRLILAGPVlDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVL----NTSIFEGGMANSILEALAY 262
Cdd:cd03794  241 RLKRRPDIRFLFVGDG-DEKERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLvplkDNPANRGSSPSKLFEYMAA 319

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501814207 263 GKAVLAADIEGNRSLIADGKTGFLYQNER--QFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEI 328
Cdd:cd03794  320 GKPILASDDGGSDLAVEINGCGLVVEPGDpeALADAILELLDDPELRRAMGENGRELAEEKFSREKLA 387
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 100-271 3.50e-13

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 69.70  E-value: 3.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 100 RREETFRALNGAAGLVVFHESVRDRLLNHLSQLEANTVVIPQGVELPEEPCRRAREFPFSSDSFSF--LLPAGLRPVKNV 177
Cdd:cd03809  128 YRLLLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPEPyfLYVGTLEPRKNH 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 178 LFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVM-DSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEG-GManS 255
Cdd:cd03809  208 ERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLvKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGfGL--P 285

                        170
                 ....*....|....*.
gi 501814207 256 ILEALAYGKAVLAADI 271
Cdd:cd03809  286 VLEAMACGTPVIASNI 301
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 2-335 1.09e-12

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 68.07  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   2 KLGIITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTAE-----------------------------EIGSEV 52
Cdd:cd03817    1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEdeeevvryrsfsipirkyhrqhipfpfkkAVIDRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  53 DAARPELIHAFHGHSGGRVAYRLKEQYGIPYVITL-TgtdIYEAIIDHRREETFRALNGAAGLVVFH-----------ES 120
Cdd:cd03817   81 KELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYhT---MYEDYLHYIPKGKLLVKAVVRKLVRRFynhtdaviapsEK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 121 VRDRLLNHLsqLEANTVVIPQGVEL---PEEPCRRAREFPFSSDSFSFLLPAG-LRPVKNVLFPLGPLAALHDQYPrIRL 196
Cdd:cd03817  158 IKDTLREYG--VKGPIEVIPNGIDLdkfEKPLNTEERRKLGLPPDEPILLYVGrLAKEKNIDFLLRAFAELKKEPN-IKL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 197 ILAGPVLDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRS 276
Cdd:cd03817  235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTET-QGLVYLEAMAAGLPVVAAKDPAASE 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 277 LIADGKTGFLYQNERQFLQKA-EQLVCRPDMRAAFGAAGRtLARERFAPEKEIAGYLQLY 335
Cdd:cd03817  314 LVEDGENGFLFEPNDETLAEKlLHLRENLELLRKLSKNAE-ISAREFAFAKSVEKLYEEV 372
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 228-326 2.35e-11

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 63.86  E-value: 2.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 228 GHDEMGCLYNKAEVVLNTSIFEG-GMANsiLEALAYGKAVLAADIE-GNRSLIADGKTGFL--YQNERQFLQKAEQLVCR 303
Cdd:cd04949  224 YHSNLDQEYQDAYLSLLTSQMEGfGLTL--MEAIGHGLPVVSYDVKyGPSELIEDGENGYLieKNNIDALADKIIELLND 301

                         90       100
                 ....*....|....*....|...
gi 501814207 304 PDMRAAFGAAGRTLArERFAPEK 326
Cdd:cd04949  302 PEKLQQFSEESYKIA-EKYSTEN 323
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 56-322 3.37e-11

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 63.63  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  56 RPELIHAFHGHsGGRVAYRLKEQYGIPYVITLTGTDIYeaiIDHRREETFRALNG------------AAGLVVFHESVRD 123
Cdd:cd05844   81 APALVHAHFGR-DGVYALPLARALGVPLVVTFHGFDIT---TSRAWLAASPGWPSqfqrhrralqrpAALFVAVSGFIRD 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 124 RLLnHLSQLEANTVVIPQGVEL----PEEPCRRARefpfssdsfSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIRLILA 199
Cdd:cd05844  157 RLL-ARGLPAERIHVHYIGIDPakfaPRDPAERAP---------TILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 200 GpvlDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEG-----GMANSILEALAYGKAVLAADIEGN 274
Cdd:cd05844  227 G---DGPLRPALQALAAALGRVRFLGALPHAEVQDWMRRAEIFCLPSVTAAsgdseGLGIVLLEAAACGVPVVSSRHGGI 303

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501814207 275 RSLIADGKTGFLYQnERQFLQKAEQ---LVCRPDMRAAFGAAGRTLARERF 322
Cdd:cd05844  304 PEAILDGETGFLVP-EGDVDALADAlqaLLADRALADRMGGAARAFVCEQF 353
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
172-300 8.65e-11

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 59.06  E-value: 8.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  172 RPVKNVLFPLGPLAALHDQYPRIRLILAGPVLDPAYAAQVMDSLEGypfAHYLGGIghDEMGCLYNKAEVVLNTSIFEGg 251
Cdd:pfam13692  12 PNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAAGLEDR---VIFTGFV--EDLAELLAAADVFVLPSLYEG- 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 501814207  252 MANSILEALAYGKAVLAADIEGNRSLIaDGKTGFL--YQNERQFLQKAEQL 300
Cdd:pfam13692  86 FGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLvpPGDPEALAEAILRL 135
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 48-321 9.27e-11

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 62.31  E-value: 9.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  48 IGSEVDAARPELIHA----FHGHSGGRVAYRLkeqyGIPYVITLTgTDIYEAIidHRREETFRALNGAAGLVVFH----- 118
Cdd:cd03814   76 VRRLIKEFQPDIIHIatpgPLGLAALRAARRL----GLPVVTSYH-TDFPEYL--SYYTLGPLSWLAWAYLRWFHnpfdt 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 119 -----ESVRDRLLNHLSQleaNTVVIPQGVEL----PEEPCRRAREFPFSSDSFSfLLPAG-LRPVKNVLFPLGPLAALH 188
Cdd:cd03814  149 tlvpsPSIARELEGHGFE---RVRLWPRGVDTelfhPSRRDAALRRRLGPPGRPL-LLYVGrLAPEKNLEALLDADLPLA 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 189 DQyPRIRLILAGpvlDPAYAAQVMdslEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFE--GgmaNSILEALAYGKAV 266
Cdd:cd03814  225 AS-PPVRLVVVG---DGPARAELE---ARGPDVIFTGFLTGEELARAYASADVFVFPSRTEtfG---LVVLEAMASGLPV 294

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 501814207 267 LAADIEGNRSLIADGKTGFLY--QNERQFLQKAEQLVCRPDMRAAFGAAGRTLARER 321
Cdd:cd03814  295 VAADAGGPRDIVRPGGTGALVepGDAAAFAAALRALLEDPELRRRMAARARAEAERY 351
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 55-287 4.03e-10

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 60.45  E-value: 4.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  55 ARPELIHAFHGHSggRVAYRLKEQYGIPYVITLTGTDIYEAIIDHRREETFRALNGAAGLVVFHESVRDRLLNHLSQLEA 134
Cdd:cd03811   82 AKPDVVISFLGFA--TYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPE 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 135 NTVVIPQGVELPEEPCRRAREFPFSSDSFSFLLPAG-LRPVKNVLFPLGPLAALHDQYPRIRLILAGP-VLDPAYAAQVM 212
Cdd:cd03811  160 KIEVIYNPIDIDRIRALAKEPILNEPEDGPVILAVGrLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDgPLREELEKLAK 239

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 213 DS-LEGY---------PFAhylggighdemgcLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRSLIADGK 282
Cdd:cd03811  240 ELgLAERviflgfqsnPYP-------------YLKKADLFVLSSRYEG-FPNVLLEAMALGTPVVSTDCPGPREILDDGE 305


                 ....*
gi 501814207 283 TGFLY 287
Cdd:cd03811  306 NGLLV 310
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 184-336 6.60e-10

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 59.65  E-value: 6.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 184 LAALH--DQYPRIRLILAGPvLDPayaaqvmdSLEGYPFAH-YLGGIGHDE-MGCLYNKAEVVLNTSIFEGgMANSILEA 259
Cdd:cd03825  214 IEALKllATKDDLLLVVFGK-NDP--------QIVILPFDIiSLGYIDDDEqLVDIYSAADLFVHPSLADN-LPNTLLEA 283

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501814207 260 LAYGKAVLAADIEGNRSLIADGKTGFLYQN-ERQFLQKA-EQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYLQLYQ 336
Cdd:cd03825  284 MACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAiEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYK 362
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 1-336 1.61e-09

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 58.52  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   1 MKLGIITphyYPLMRGNAVTVRRIEKNLANAG-------------------------VEVAVYSL------DAMTAEEIG 49
Cdd:cd04962    1 MKIGIVC---YPSYGGSGVVATELGLELAERGhevhfissaipfrlnlysgniffheVEVPNYPLfeyppyTLALASKIV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  50 SEVDAARPELIHAFHGHSGGRVAYRLKEQYG--IPYVITLTGTDIYEAIIDHRREETFR-ALNGAAGLVVFHESVRDRLL 126
Cdd:cd04962   78 EVAKEHKLDVLHAHYAIPHASCAYLAREILGekIPIVTTLHGTDITLVGYDPSLQPAVRfSINKSDRVTAVSSSLRQETY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 127 NHLsQLEANTVVIPQGVElpeepCRRAREFPFSSDSFSFLLPAG---------LRPVKNVLFPLGPLAALHDQYP-RIRL 196
Cdd:cd04962  158 ELF-DVDKDIEVIHNFID-----EDVFKRKPAGALKRRLLAPPDekvvihvsnFRPVKRIDDVVRVFARVRRKIPaKLLL 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 197 ILAGPVLDPAYAAQVMDSLEGYpfAHYLGGIghDEMGCLYNKAEVVLNTSIFEG-GMAnsILEALAYGKAVLAADIEGNR 275
Cdd:cd04962  232 VGDGPERVPAEELARELGVEDR--VLFLGKQ--DDVEELLSIADLFLLPSEKESfGLA--ALEAMACGVPVVSSNAGGIP 305

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 501814207 276 SLIADGKTGFLYQ--NERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYLQLYQ 336
Cdd:cd04962  306 EVVKHGETGFLSDvgDVDAMAKSALSILEDDELYNRMGRAARKRAAERFDPERIVPQYEAYYR 368
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 188-334 5.09e-09

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 56.95  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 188 HDQYPRIRLILAG--PVLDPAYA---AQVMDSLEGYPFAHYLG-GIGHDEMGCLYNKAEVVLNTSIFEG-GManSILEAL 260
Cdd:cd03792  223 KRRAEEPQLVICGhgAVDDPEGSvvyEEVMEYAGDDHDIHVLRlPPSDQEINALQRAATVVLQLSTREGfGL--TVSEAL 300

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501814207 261 AYGKAVLAADIEGNRSLIADGKTGFLYQNERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYLQL 334
Cdd:cd03792  301 WKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVRILRLLTDPELRRKMGLAAREHVRDNFLITGNLRAWLYL 374
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 193-338 8.42e-09

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 56.14  E-value: 8.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 193 RIRLILAGPVLDPAYAaQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEGGMANSILEALAYGKAVLAADIE 272
Cdd:cd03802  195 GLPLKIAGKVRDEDYF-YYLQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRG 273

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501814207 273 GNRSLIADGKTGFLYQNERQFLQKAEQL--VCRPDMRAAfgaagrtlARERFAPEKEIAGYLQLYQGV 338
Cdd:cd03802  274 GLPEVIQHGETGFLVDSVEEMAEAIANIdrIDRAACRRY--------AEDRFSAARMADRYEALYRKV 333
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 52-335 9.01e-09

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 56.18  E-value: 9.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  52 VDAARPELIHaFHGHSG-GRVAYRLKEQYGIPYVITLTgtDIYeaIIDHRreeTFRALNGAAGLVVFHESVRDRLLNHLs 130
Cdd:cd03823   92 LEDFRPDVVH-THNLSGlGASLLDAARDLGIPVVHTLH--DYW--LLCPR---QFLFKKGGDAVLAPSRFTANLHEANG- 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 131 QLEANTVVIPQGVELPEEPCRRAREFpfssdsfsfllpaglRPVKNVLFpLGPL-----------AALHDQYPRIRLILA 199
Cdd:cd03823  163 LFSARISVIPNAVEPDLAPPPRRRPG---------------TERLRFGY-IGRLteekgidllveAFKRLPREDIELVIA 226

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 200 GPVLDPAYAAQvmdslEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEGGMANSILEALAYGKAVLAADIEGNRSLIA 279
Cdd:cd03823  227 GHGPLSDERQI-----EGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLGGIAELIQ 301

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501814207 280 DGKTGFLYQNErqflqKAEQLVCRPDMRAAFGAAGRTL---ARERFAPEKEIAGYLQLY 335
Cdd:cd03823  302 PGVNGLLFAPG-----DAEDLAAAMRRLLTDPALLERLragAEPPRSTESQAEEYLKLY 355
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 6-333 1.05e-08

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 56.22  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   6 ITPHYYPLMRGNAVTVRRIEKNLANAGVEVAVYSLDAmTAEEIGSEVDAARPELIHAFHGH-----SGGRVAYRLK---- 76
Cdd:cd03821    5 VTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGD-GYESLVVEENGRYIPPQDGFASIpllrqGAGRTDFSPGlpnw 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  77 ----------------------------EQYGIPYVITLTGT---------DIYEAIIDHRREEtfRALNGAAGLVVFHE 119
Cdd:cd03821   84 lrrnlreydvvhihgvwtytslaacklaRRRGIPYVVSPHGMldpwalqqkHWKKRIALHLIER--RNLNNAALVHFTSE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 120 SVRDRLlnHLSQLEANTVVIPQGVELPE-EPCRRAREFPFSSDSFSFLLPAG-LRPVKNVLFPLGPLAALHDQYPRIRLI 197
Cdd:cd03821  162 QEADEL--RRFGLEPPIAVIPNGVDIPEfDPGLRDRRKHNGLEDRRIILFLGrIHPKKGLDLLIRAARKLAEQGRDWHLV 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 198 LAGP-VLDPAYAAQVMDSLEGYPFAHYLGGIGHDEMGCLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRS 276
Cdd:cd03821  240 IAGPdDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSEN-FGNVVAEALACGLPVVITDKCGLSE 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 501814207 277 LIADGKTGFLYQNERQFLQKAEQLVCRPDMRAAFGAAGR--TLARERFApEKEIAGYLQ 333
Cdd:cd03821  319 LVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARraRQVEENFS-WEAVAGQLG 376
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
241-322 7.39e-08

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 49.52  E-value: 7.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  241 VVLNTSIFEGGMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLYQNERQFLQKAEQLVCRPDMRAAFGAAGRTLARE 320
Cdd:pfam13524   1 IVLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVLA 80


                  ..
gi 501814207  321 RF 322
Cdd:pfam13524  81 EH 82
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 59-335 7.39e-08

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 53.88  E-value: 7.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  59 LIHAFHGHSGGRVAYRLKEQYGIPYVITLTGtdIYeaiidHR-REETFRALNGAAG-----LVVFHESV-------RDRL 125
Cdd:cd03813  176 LYHSVSTGYAGLLGALARHRRGIPFLLTEHG--IY-----TReRKIEILQSTWIMGyikklWIRFFERLgklayqqADKI 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 126 L-----NHLSQLE-----ANTVVIPQGVELpeEPCRRAREFPFSSDSFSFLLPAGLRPVKNVLFPLGPLAALHDQYPRIR 195
Cdd:cd03813  249 IslyegNRRRQIRlgadpDKTRVIPNGIDI--QRFAPAREERPEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMPDAE 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 196 LILAGPVL-DPAYAAQVMDSLEGypfahyLGGIGH------DEMGCLYNKAEVVLNTSIFEgGMANSILEALAYGKAVLA 268
Cdd:cd03813  327 GWLIGPEDeDPEYAQECKRLVAS------LGLENKvkflgfQNIKEYYPKLGLLVLTSISE-GQPLVILEAMASGVPVVA 399

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501814207 269 ADIEGNRSLIADGKTGFLYQNE----RQFLQKAEQLV--CR-PDMRAAFGAAGRTLARERFAPEKEIAGYLQLY 335
Cdd:cd03813  400 TDVGSCRELIYGADDALGQAGLvvppADPEALAEALIklLRdPELRQAFGEAGRKRVEKYYTLEGMIDSYRKLY 473
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 235-326 1.07e-07

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 53.01  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 235 LYNKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIE-GNRSLIADGKTGFL--YQNERQFLQKAEQLVCRPDMRAAFG 311
Cdd:cd03820  252 EYANSSIFVLSSRYEG-FPMVLLEAMAYGLPIISFDCPtGPSEIIEDGENGLLvpNGDVDALAEALLRLMEDEELRKKMG 330

                         90
                 ....*....|....*
gi 501814207 312 AAGRTLArERFAPEK 326
Cdd:cd03820  331 KNARKNA-ERFSIEK 344
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
13-319 3.37e-07

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 51.09  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  13 LMRGNAVTVRRIEKNLANAGVEVAVYSLDAMTAEEIGSE--VDAARPELIHAFHGHSGGRVAyrlkEQYGIPYVITLTgt 90
Cdd:COG4641    4 LWNGHATYYRGLLRALAALGHEVTFLEPDDPWHDPLYAAelLDAFRPDLVLVISGVELVAAL----RARGIPTVFWDT-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  91 diyEAIIDHRReeTFRALNGAAGLVVFHESVRDRLLNHLSQleaNTVVIPQGVElPE--EPCRRARefpfssdsfsfllp 168
Cdd:COG4641   78 ---DDPVTLDR--FRELLPLYDLVFTFDGDCVEEYRALGAR---RVFYLPFAAD-PElhRPVPPEA-------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 169 aglRPVKNVLFpLG--------PLAALHDQYPRIRLILAGP-VLDPAYAAQVmdslegypfaHYLGGIGHDEMGCLYNKA 239
Cdd:COG4641  135 ---RFRYDVAF-VGnyypdrraRLEELLLAPAGLRLKIYGPgWPKLALPANV----------RRGGHLPGEEHPAAYASS 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 240 EVVLN---TSIFEGGMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLYQNERQFLQKAEQLVCRPDMRAAFGAAG-- 314
Cdd:COG4641  201 KITLNvnrMAASPDSPTRRTFEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGrr 280


                 ....*
gi 501814207 315 RTLAR 319
Cdd:COG4641  281 RVLAE 285
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 189-315 2.22e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 48.94  E-value: 2.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 189 DQYPRIRLILAGpvlDPAYAAQVMDSLEGYPfAHYLGGIGHDEMGCLYNKAEVVLNTSIFEGgMANSILEALAYGKAVLA 268
Cdd:PLN02871 286 ERLPGARLAFVG---DGPYREELEKMFAGTP-TVFTGMLQGDELSQAYASGDVFVMPSESET-LGFVVLEAMASGVPVVA 360

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501814207 269 ADIEGNRSLIAD---GKTGFLYQ--NERQFLQKAEQLVCRPDMRAAFGAAGR 315
Cdd:PLN02871 361 ARAGGIPDIIPPdqeGKTGFLYTpgDVDDCVEKLETLLADPELRERMGAAAR 412
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
166-285 6.13e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 47.48  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 166 LLPAG-LRPVKNVLFPLGPLAALHDQYPRIRLILAGpvlDP---------AYAAQVMDSLEGY-PFAHYLGGIGHDEMGC 234
Cdd:PRK15484 196 LLYAGrISPDKGILLLMQAFEKLATAHSNLKLVVVG---DPtasskgekaAYQKKVLEAAKRIgDRCIMLGGQPPEKMHN 272

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501814207 235 LYNKAEVVLNTSIFEGGMANSILEALAYGKAVLAADIEGNRSLIADGKTGF 285
Cdd:PRK15484 273 YYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGY 323
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 66-326 1.83e-05

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 45.91  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  66 HSGGRVAYRLKEQYGIPYVITLT-GTDIYEAIIDH----RREETFRALNGaaglvVF--HESVRDRLLNHLSQLEANTVV 138
Cdd:cd04946  131 NHTALGLGLLKDEYYRDVVISRAhRYDLYEDQYGSyylpLREYLVSYLDA-----VFliSKEGKDYLQKCYPAYKEKIFV 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 139 IPQGVELPEEPCRRAREFPFSSDSFsfllpAGLRPVKNVLFPLGPLAALHDQYPRIRL----ILAGPVLdpayaaQVMDS 214
Cdd:cd04946  206 SRLGVSDKEQYSKVKKEGDLRLVSC-----SSIVPVKRIDLIIETLNSLCVAHPSICIswthIGGGPLK------ERLEK 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 215 L-EGYP---FAHYLGGIGHDEMGCLY--NKAEVVLNTSIFEGgMANSILEALAYGKAVLAADIEGNRSLIADGKTGFLYQ 288
Cdd:cd04946  275 LaENKLenvKVNFTGEVSNKEVKQLYkeNDVDVFVNVSESEG-IPVSIMEAISFGIPVIATNVGGTREIVENETNGLLLD 353

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 501814207 289 NERQFLQKAE---QLVCRPDMRAAFGAAGRTLARERFAPEK 326
Cdd:cd04946  354 KDPTPNEIVSsimKFYLDGGDYKTMKISARECWEERFNAEV 394
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 52-281 7.32e-05

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 44.30  E-value: 7.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207  52 VDAARPELIHAFH-----GHSGGRVAYRLKEQYGIPYVITLTgtDIYEAIIDHRREETFRALNGAAGLVVF-HESVRDRL 125
Cdd:cd03822   71 LNFKKPDVVHIQHefgifGGKYGLYALGLLLHLRIPVITTLH--TVLDLSDPGKQALKVLFRIATLSERVVvMAPISRFL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 126 LNHLSQLEANTV-VIPQGVELPEEPCRRAREFPFSSDSFSFLLPAGL-RPVKNVLFPLGPLAALHDQYPRIRLILAGPVl 203
Cdd:cd03822  149 LVRIKLIPAVNIeVIPHGVPEVPQDPTTALKRLLLPEGKKVILTFGFiGPGKGLEILLEALPELKAEFPDVRLVIAGEL- 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 204 dpaYAAQVMDSLEGYPFAH------------YLGGIGHDEMGCLYNKAEVVLNTSIFEGGMANSILE-ALAYGKAVLAAD 270
Cdd:cd03822  228 ---HPSLARYEGERYRKAAieelglqdhvdfHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGTLSyAIACGKPVISTP 304

                        250
                 ....*....|.
gi 501814207 271 IEGNRSLIADG 281
Cdd:cd03822  305 LRHAEELLADG 315
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
18-145 2.67e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 40.98  E-value: 2.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   18 AVTVRRIEKNLANAGVEVAVYSLDAMTAEEIGSE-----------------------------VDAARPELIHAFHGHSG 68
Cdd:pfam13439   4 ERYVLELARALARRGHEVTVVTPGGPGPLAEEVVrvvrvprvplplpprllrslaflrrlrrlLRRERPDVVHAHSPFPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   69 GRVAYRLKEQYGIPYVITL-------TGTDIYEAIIDHRREETFRALNGAAGLVVFH-ESVRDRLLNHLSQLEANTVVIP 140
Cdd:pfam13439  84 GLAALAARLRLGIPLVVTYhglfpdyKRLGARLSPLRRLLRRLERRLLRRADRVIAVsEAVADELRRLYGVPPEKIRVIP 163


                  ....*
gi 501814207  141 QGVEL 145
Cdd:pfam13439 164 NGVDL 168
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 257-325 3.06e-04

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 42.19  E-value: 3.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 257 LEALAYGKAVLAADIEGNRSLIADGKTGFLYQ-NERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPE 325
Cdd:cd03805  317 LEAMYAGKPVIACNSGGPLETVVEGVTGFLCEpTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSRE 386
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 255-332 8.12e-04

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 40.81  E-value: 8.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207 255 SILEALAYGKAVLAADIEGNRSLIADGKTGFL--YQNERQFLQKAEQLVCRPDMRAAFGAAGRTLARERFAPEKEIAGYL 332
Cdd:cd03818  316 SLLEAMACGCPVIGSDTAPVREVIRDGRNGLLvdFFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCLARYL 395
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
52-140 1.84e-03

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 38.54  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501814207   52 VDAARPELIHAfHGHSGGRVAYRLKEQYGIPYVITLTGTDIYEAIIDHRREETF---RALNGAAGLVVFHESVRDRLLNH 128
Cdd:pfam13579  67 LRAERPDVVHA-HSPTAGLAARLARRRRGVPLVVTVHGLALDYGSGWKRRLARAlerRLLRRADAVVVVSEAEAELLRAL 145

                          90
                  ....*....|..
gi 501814207  129 LSQlEANTVVIP 140
Cdd:pfam13579 146 GVP-AARVVVVP 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH