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Conserved domains on  [gi|12278435|gb|AAG48958|]
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granule-bound starch synthase, partial [Elymus riparius]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 1-248 4.82e-97

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.


The actual alignment was detected with superfamily member cd03791:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 474  Bit Score: 292.16  E-value: 4.82e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   1 CELDNI--MRLTGITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:cd03791 230 EGLDGVlrARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKG 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:cd03791 309 VDLILDALPELL-EEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMY 387

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 159 GMRYGTPCACASTGGLVDTIVEG------KTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVGTP-AYQEMVKNCMIQ 231
Cdd:cd03791 388 AMRYGTLPIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALALYRNPeLWRKLQKNAMKQ 457

                       250
                ....*....|....*..
gi 12278435 232 DLSWKGPAKNWEDVLLE 248
Cdd:cd03791 458 DFSWDKSAKEYLELYRS 474
 
Name Accession Description Interval E-value
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 1-248 4.82e-97

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 292.16  E-value: 4.82e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   1 CELDNI--MRLTGITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:cd03791 230 EGLDGVlrARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKG 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:cd03791 309 VDLILDALPELL-EEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMY 387

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 159 GMRYGTPCACASTGGLVDTIVEG------KTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVGTP-AYQEMVKNCMIQ 231
Cdd:cd03791 388 AMRYGTLPIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALALYRNPeLWRKLQKNAMKQ 457

                       250
                ....*....|....*..
gi 12278435 232 DLSWKGPAKNWEDVLLE 248
Cdd:cd03791 458 DFSWDKSAKEYLELYRS 474
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 1-249 1.01e-92

glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273969 [Multi-domain]  Cd Length: 473  Bit Score: 281.08  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435     1 CELDNIMRLTG--ITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:TIGR02095 227 YGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKG 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:TIGR02095 306 VDLLLAALPELL-ELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLY 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   159 GMRYGTPCACASTGGLVDTIVEGK------TGFHMGRlsvdcnvVEPADvkkVATTLKRAVKvvgtpAY-------QEMV 225
Cdd:TIGR02095 385 AMRYGTVPIVRRTGGLADTVVDGDpeaesgTGFLFEE-------YDPGA---LLAALSRALR-----LYrqdpslwEALQ 449

                         250       260
                  ....*....|....*....|....
gi 12278435   226 KNCMIQDLSWKGPAKNWEDVLLEL 249
Cdd:TIGR02095 450 KNAMSQDFSWDKSAKQYVELYRSL 473
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
1-245 2.15e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 277.74  E-value: 2.15e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   1 CELDNIMRLTG--ITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:COG0297 231 EGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKG 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:COG0297 310 LDLLLEALDELL-EEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMY 388

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 159 GMRYGTPCACASTGGLVDTIV------EGKTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVGTP-AYQEMVKNCMIQ 231
Cdd:COG0297 389 ALRYGTVPIVRRTGGLADTVIdyneatGEGTGF----------VFDEYTAEALLAAIRRALALYRDPeAWRKLQRNAMKQ 458

                       250
                ....*....|....
gi 12278435 232 DLSWKGPAKNWEDV 245
Cdd:COG0297 459 DFSWEKSAKEYLEL 472
glgA PRK00654
glycogen synthase GlgA;
13-245 1.24e-80

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 249.65  E-value: 1.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   13 TGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDrKVPLVAFIGRLEEQKGPDVMIAAIPEIVkE 92
Cdd:PRK00654 233 SGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELL-E 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   93 EDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQGMRYGT-PCAcAST 171
Cdd:PRK00654 310 QGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTlPIV-RRT 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  172 GGLVDTIV------EGKTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVGTPA-YQEMVKNCMIQDLSWKGPAKNWED 244
Cdd:PRK00654 389 GGLADTVIdynpedGEATGF----------VFDDFNAEDLLRALRRALELYRQPPlWRALQRQAMAQDFSWDKSAEEYLE 458


                 .
gi 12278435  245 V 245
Cdd:PRK00654 459 L 459
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
65-211 1.35e-18

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 79.48  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    65 PLVAFIGRL-EEQKGPDVMIAAIPEIVKEE-DVQIVLLGTGK-KKFERLLKSVEEK--FPGKVRAVVRFnaplahqmMAG 139
Cdd:pfam13692   2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRDnDVRLVIVGDGPeEELEELAAGLEDRviFTGFVEDLAEL--------LAA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12278435   140 ADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDtIVEGKTGFhmgrlsvdcnVVEPADVKKVATTLKR 211
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGL----------LVPPGDPEALAEAILR 134
 
Name Accession Description Interval E-value
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 1-248 4.82e-97

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 292.16  E-value: 4.82e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   1 CELDNI--MRLTGITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:cd03791 230 EGLDGVlrARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKG 308

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:cd03791 309 VDLILDALPELL-EEGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMY 387

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 159 GMRYGTPCACASTGGLVDTIVEG------KTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVGTP-AYQEMVKNCMIQ 231
Cdd:cd03791 388 AMRYGTLPIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALALYRNPeLWRKLQKNAMKQ 457

                       250
                ....*....|....*..
gi 12278435 232 DLSWKGPAKNWEDVLLE 248
Cdd:cd03791 458 DFSWDKSAKEYLELYRS 474
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 1-249 1.01e-92

glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) synthases that use ADP-glucose (EC 2.4.1.21), rather than UDP-glucose (EC 2.4.1.11) as in animals, as the glucose donor. This enzyme is found in bacteria and plants. Whether the name given is glycogen synthase or starch synthase depends on context, and therefore on substrate. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273969 [Multi-domain]  Cd Length: 473  Bit Score: 281.08  E-value: 1.01e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435     1 CELDNIMRLTG--ITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:TIGR02095 227 YGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKG 305

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:TIGR02095 306 VDLLLAALPELL-ELGGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLY 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   159 GMRYGTPCACASTGGLVDTIVEGK------TGFHMGRlsvdcnvVEPADvkkVATTLKRAVKvvgtpAY-------QEMV 225
Cdd:TIGR02095 385 AMRYGTVPIVRRTGGLADTVVDGDpeaesgTGFLFEE-------YDPGA---LLAALSRALR-----LYrqdpslwEALQ 449

                         250       260
                  ....*....|....*....|....
gi 12278435   226 KNCMIQDLSWKGPAKNWEDVLLEL 249
Cdd:TIGR02095 450 KNAMSQDFSWDKSAKQYVELYRSL 473
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
1-245 2.15e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 277.74  E-value: 2.15e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   1 CELDNIMRLTG--ITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:COG0297 231 EGLDGLLRARSgkLSGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKG 309

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:COG0297 310 LDLLLEALDELL-EEDVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMY 388

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 159 GMRYGTPCACASTGGLVDTIV------EGKTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVGTP-AYQEMVKNCMIQ 231
Cdd:COG0297 389 ALRYGTVPIVRRTGGLADTVIdyneatGEGTGF----------VFDEYTAEALLAAIRRALALYRDPeAWRKLQRNAMKQ 458

                       250
                ....*....|....
gi 12278435 232 DLSWKGPAKNWEDV 245
Cdd:COG0297 459 DFSWEKSAKEYLEL 472
glgA PRK00654
glycogen synthase GlgA;
13-245 1.24e-80

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 249.65  E-value: 1.24e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   13 TGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDrKVPLVAFIGRLEEQKGPDVMIAAIPEIVkE 92
Cdd:PRK00654 233 SGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELL-E 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   93 EDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQGMRYGT-PCAcAST 171
Cdd:PRK00654 310 QGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTlPIV-RRT 388

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  172 GGLVDTIV------EGKTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVGTPA-YQEMVKNCMIQDLSWKGPAKNWED 244
Cdd:PRK00654 389 GGLADTVIdynpedGEATGF----------VFDDFNAEDLLRALRRALELYRQPPlWRALQRQAMAQDFSWDKSAEEYLE 458


                 .
gi 12278435  245 V 245
Cdd:PRK00654 459 L 459
PRK14099 PRK14099
glycogen synthase GlgA;
3-242 1.27e-55

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 185.31  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    3 LDNIMRLTG--ITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKGPD 80
Cdd:PRK14099 233 LDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLD 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   81 VMIAAIPEIVKEeDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQGM 160
Cdd:PRK14099 312 LLLEALPTLLGE-GAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCAL 390

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  161 RYGTPCACASTGGLVDTIVEGK---------TGFHMGRLSVDCnvvepadvkkVATTLKRAVKVVGTPA-YQEMVKNCMI 230
Cdd:PRK14099 391 RYGAVPVVARVGGLADTVVDANemaiatgvaTGVQFSPVTADA----------LAAALRKTAALFADPVaWRRLQRNGMT 460

                        250
                 ....*....|..
gi 12278435  231 QDLSWKGPAKNW 242
Cdd:PRK14099 461 TDVSWRNPAQHY 472
PRK14098 PRK14098
starch synthase;
1-249 3.81e-44

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 155.28  E-value: 3.81e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    1 CELDNIM--RLTGITGIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLPVDRKVPLVAFIGRLEEQKG 78
Cdd:PRK14098 243 FGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLEEVGLPFDEETPLVGVIINFDDFQG 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   79 PDVMIAAIPEIVkEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQ 158
Cdd:PRK14098 322 AELLAESLEKLV-ELDIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIESCGMLQMF 400

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  159 GMRYGT-PCACAsTGGLVDTIVE----GKTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKVVG-TPAYQEMVKNCMIQD 232
Cdd:PRK14098 401 AMSYGTiPVAYA-GGGIVETIEEvsedKGSGF----------IFHDYTPEALVAKLGEALALYHdEERWEELVLEAMERD 469

                        250
                 ....*....|....*..
gi 12278435  233 LSWKGPAKNWEDVLLEL 249
Cdd:PRK14098 470 FSWKNSAEEYAQLYREL 486
PLN02316 PLN02316
synthase/transferase
 14-239 2.25e-36

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 136.54  E-value: 2.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    14 GIVNGMDVSEWDPTKDKFLAVNYDITTALEAKALNKEALQAEVGL-PVDrkVPLVAFIGRLEEQKGPDVMIAAIPEIVkE 92
Cdd:PLN02316  791 GILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLkQAD--LPLVGIITRLTHQKGIHLIKHAIWRTL-E 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    93 EDVQIVLLGTG-----KKKFERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCA 167
Cdd:PLN02316  868 RNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPV 947

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   168 CASTGGLVDTIVEgktgfhmgrlsVD-------CNVVEP-------ADVKKVATTLKRAVKVV--GTPAYQEMVKNCMIQ 231
Cdd:PLN02316  948 VRKTGGLFDTVFD-----------VDhdkeraqAQGLEPngfsfdgADAAGVDYALNRAISAWydGRDWFNSLCKRVMEQ 1016


                  ....*...
gi 12278435   232 DLSWKGPA 239
Cdd:PLN02316 1017 DWSWNRPA 1024
PLN02939 PLN02939
transferase, transferring glycosyl groups
 14-245 7.38e-33

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 126.56  E-value: 7.38e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   14 GIVNGMDVSEWDPTKDKFLAVNYDITTaLEAKALNKEALQAEVGLP-VDRKVPLVAFIGRLEEQKGPDVMIAAIPEIVkE 92
Cdd:PLN02939 729 GILNGIDTDTWNPSTDRFLKVQYNAND-LQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTA-E 806

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   93 EDVQIVLLGTGK-KKFERLLKSVEEKFPGK--VRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACA 169
Cdd:PLN02939 807 LGGQFVLLGSSPvPHIQREFEGIADQFQSNnnIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGSVPIVR 886

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  170 STGGLVDTI---------VEGKTGFHMGRlsvdcnvvepADVKKVATTLKRAVKVV--GTPAYQEMVKNCMIQDLSWKGP 238
Cdd:PLN02939 887 KTGGLNDSVfdfddetipVELRNGFTFLT----------PDEQGLNSALERAFNYYkrKPEVWKQLVQKDMNIDFSWDSS 956


                 ....*..
gi 12278435  239 AKNWEDV 245
Cdd:PLN02939 957 ASQYEEL 963
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 47-246 9.61e-22

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: 92.60  E-value: 9.61e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  47 LNKEALQAEVGLPVDRKVPLVAFIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGTGKKKFERLlksveEKFPGKVRAV 125
Cdd:cd03801 175 LERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRgPDVRLVIVGGDGPLRAEL-----EELELGLGDR 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 126 VRF----NAPLAHQMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPAD 201
Cdd:cd03801 250 VRFlgfvPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGL----------VVPPDD 319

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 12278435 202 VKKVATTLKRAVKvvGTPAYQEMVKN---CMIQDLSWKGPAKNWEDVL 246
Cdd:cd03801 320 VEALADALLRLLA--DPELRARLGRAareRVAERFSWERVAERLLDLY 365
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
65-211 1.35e-18

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 79.48  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    65 PLVAFIGRL-EEQKGPDVMIAAIPEIVKEE-DVQIVLLGTGK-KKFERLLKSVEEK--FPGKVRAVVRFnaplahqmMAG 139
Cdd:pfam13692   2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRDnDVRLVIVGDGPeEELEELAAGLEDRviFTGFVEDLAEL--------LAA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 12278435   140 ADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDtIVEGKTGFhmgrlsvdcnVVEPADVKKVATTLKR 211
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGL----------LVPPGDPEALAEAILR 134
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 49-214 1.67e-17

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: 80.75  E-value: 1.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  49 KEALQAEVGLPVDRKVplVAFIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLG----TGKKKFERLLKSVEEKFpgKVR 123
Cdd:cd03800 207 AEARRARLLLPPDKPV--VLALGRLDPRKGIDTLVRAFAQLPELrELANLVLVGgpsdDPLSMDREELAELAEEL--GLI 282

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 124 AVVRFNAPLAHQMMA----GADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFHmgrlsvdcnvVEP 199
Cdd:cd03800 283 DRVRFPGRVSRDDLPelyrAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLL----------VDP 352

                       170
                ....*....|....*
gi 12278435 200 ADVKKVATTLKRAVK 214
Cdd:cd03800 353 HDPEALAAALRRLLD 367
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 63-214 2.03e-16

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: 74.23  E-value: 2.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435    63 KVPLVAFIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGTGKKKfERLLKSVEEKfpgKVRAVVRF----NAPLAHQMM 137
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKnPNLKLVIAGDGEEE-KRLKKLAEKL---GLGDNVIFlgfvSDEDLPELL 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 12278435   138 AGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPADVKKVATTLKRAVK 214
Cdd:pfam00534  77 KIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF----------LVKPNNAEALAEAIDKLLE 143
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 69-185 1.09e-14

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: 71.28  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  69 FIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGTGkkkFERLLKSVEEKFPGKVRAVVRFNAPLAHQ----MMAGADLL 143
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARlPDLVLVLVGGG---GEREEEEALAAALGLLERVVIIGGLVDDEvlelLLAAADVF 191

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 12278435 144 AVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGF 185
Cdd:cd01635 192 VLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 50-213 1.33e-13

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: 69.72  E-value: 1.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  50 EALQAEVGLPVDRKVplVAFIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGTG--KKKFERLLKSveEKFPGKVRAVV 126
Cdd:cd03798 188 QPEDRGLGLPLDAFV--ILFVGRLIPRKGIDLLLEAFARLAKArPDVVLLIVGDGplREALRALAED--LGLGDRVTFTG 263

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 127 RFnapLAHQM---MAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPADVK 203
Cdd:cd03798 264 RL---PHEQVpayYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGL----------LVPPGDAD 330

                       170
                ....*....|
gi 12278435 204 KVATTLKRAV 213
Cdd:cd03798 331 ALAAALRRAL 340
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 60-226 3.18e-13

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: 68.15  E-value: 3.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  60 VDRKVPLVAFIGRLEEQKGPDVMIAAIPEIVKEEDVQIVLLGTG------KKKFERLLKSVEEKFPGKVRAVVRFnapla 133
Cdd:cd03819 178 LPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDEPDFRLLVAGDGperdeiRRLVERLGLRDRVTFTGFREDVPAA----- 252

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 134 hqmMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrLSVDCNVVEPADVKK-VATTLKRA 212
Cdd:cd03819 253 ---LAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGL----LVPPGDAEALADAIRaAKLLPEAR 325

                       170
                ....*....|....
gi 12278435 213 VKVVGTPAYQEMVK 226
Cdd:cd03819 326 EKLQAAAALTEAVR 339
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 43-185 1.10e-12

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: 66.61  E-value: 1.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  43 EAKALNKEALQAEvglpvDRKVPLVAFIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGTGKKKfERLLKSVEE----- 116
Cdd:cd03811 172 RIRALAKEPILNE-----PEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKyPDVKLVILGDGPLR-EELEKLAKElglae 245

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12278435 117 --KFPGKVRAVVRFnaplahqmMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGF 185
Cdd:cd03811 246 rvIFLGFQSNPYPY--------LKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL 308
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 45-186 2.31e-11

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: 63.07  E-value: 2.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  45 KALNKEALQAevgLPVDRKVPLVAFIGRLEEQKGPDVMIAAIPEIVKEEDVQIVLLGTGKKKfERLLKSVEEKfpgKVRA 124
Cdd:cd03817 185 KPLNTEERRK---LGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPNIKLVIVGDGPER-EELKELAREL---GLAD 257

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 12278435 125 VVRFNAPLAHQMM----AGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFH 186
Cdd:cd03817 258 KVIFTGFVPREELpeyyKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFL 323
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 137-249 2.99e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 56.54  E-value: 2.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 137 MAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPADVKKVATTLKRAVKvv 216
Cdd:COG0438  18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGL----------LVPPGDPEALAEAILRLLE-- 85

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 12278435 217 GTPAYQEMVKNC---MIQDLSWKGPAKNWEDVLLEL 249
Cdd:COG0438  86 DPELRRRLGEAArerAEERFSWEAIAERLLALYEEL 121
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 63-203 3.16e-10

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: 59.53  E-value: 3.16e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  63 KVPLVAFIGRLEEQKGPDVMIAAIpEIVKE--EDVQIVLLG---TGKKKFERLLKSVEEK---FPGKVRAVvrfnaplaH 134
Cdd:cd03808 188 EKVVFLFVARLLKDKGIDELIEAA-KILKKkgPNVRFLLVGdgeLENPSEILIEKLGLEGrieFLGFRSDV--------P 258

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 12278435 135 QMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPADVK 203
Cdd:cd03808 259 ELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGF----------LVPPGDVE 317
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 67-211 3.69e-10

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: 59.17  E-value: 3.69e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  67 VAFIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGTG--KKKFERLLKS--VEE--KFPGKVRAVvrfnaplaHQMMAG 139
Cdd:cd03820 184 ILAVGRLTYQKGFDLLIEAWALIAKKhPDWKLRIYGDGpeREELEKLIDKlgLEDrvKLLGPTKNI--------AEEYAN 255

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12278435 140 ADLLAVTSRFEPCGLIQLQGMRYGTPCAC-ASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPADVKKVATTLKR 211
Cdd:cd03820 256 SSIFVLSSRYEGFPMVLLEAMAYGLPIISfDCPTGPSEIIEDGENGL----------LVPNGDVDALAEALLR 318
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
48-246 4.11e-09

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 56.34  E-value: 4.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   48 NKEALQAEVGLPVDRKVPLVAfiGRLEEQKGPDVMIAAIPEIVKEED-VQIVLLG--TGKKKFERllksveEKFPGKVRA 124
Cdd:PRK15484 179 PQPNLRQQLNISPDETVLLYA--GRISPDKGILLLMQAFEKLATAHSnLKLVVVGdpTASSKGEK------AAYQKKVLE 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  125 VVRfnAPLAHQMMAG-------------ADLLAVTSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFHMGrl 190
Cdd:PRK15484 251 AAK--RIGDRCIMLGgqppekmhnyyplADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLA-- 326

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 12278435  191 svdcnvvEPADVKKVATTLKRAVKVVGTPAYQEMVKNCMIQDLSWKGPAKNWEDVL 246
Cdd:PRK15484 327 -------EPMTSDSIISDINRTLADPELTQIAEQAKDFVFSKYSWEGVTQRFEEQI 375
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 25-193 4.26e-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: 4.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  25 DPTKDKFLAVNYDITTALEA-------KALNKEALQAEVGLPVDRKV---PL-VAFIGRLEEQKGPDVMIAAIPEIvKEE 93
Cdd:cd03823 141 KKGGDAVLAPSRFTANLHEAnglfsarISVIPNAVEPDLAPPPRRRPgteRLrFGYIGRLTEEKGIDLLVEAFKRL-PRE 219

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  94 DVQIVLLGTGKKKFERLLKSVEE-KFPGKVRavvrfNAPLAHQmMAGADLLAVTSRF-EPCGLIQLQGMRYGTPCACAST 171
Cdd:cd03823 220 DIELVIAGHGPLSDERQIEGGRRiAFLGRVP-----TDDIKDF-YEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDL 293

                       170       180
                ....*....|....*....|..
gi 12278435 172 GGLVDTIVEGKTGFHMGRLSVD 193
Cdd:cd03823 294 GGIAELIQPGVNGLLFAPGDAE 315
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 65-185 4.40e-08

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: 53.23  E-value: 4.40e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  65 PLVAFIGRLEEQKGPDVMIAAIPEIV-KEEDVQIVLLGTGKkkferLLKSVEEKFPGKVRavVRFNAPLAH----QMMAG 139
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAaRHPTARLVIAGDGP-----LRPALQALAAALGR--VRFLGALPHaevqDWMRR 262

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 12278435 140 ADLLAVTSRF------EPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGF 185
Cdd:cd05844 263 AEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGF 314
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 65-228 6.67e-08

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar 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 and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 52.66  E-value: 6.67e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  65 PLVAFIGRLEEQKGPDVMIAAipeiVKEEDVQIVLLGTGKKKfERLLKSVEEKFPGKVRAVVRFNAPLAHQMMAGADLLA 144
Cdd:cd03795 192 KIFLFIGRLVYYKGLDYLIEA----AQYLNYPIVIGGEGPLK-PDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFV 266

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 145 VTS--RFEPCGLIQLQGMRYGTP-CACASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPADVKKVATTLKravKVVGTP-A 220
Cdd:cd03795 267 FPSvlRSEAFGIVLLEAMMCGKPvISTNIGTGVPYVNNNGETGL----------VVPPKDPDALAEAID---KLLSDEeL 333


                ....*...
gi 12278435 221 YQEMVKNC 228
Cdd:cd03795 334 RESYGENA 341
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 65-185 2.98e-07

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: 50.76  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  65 PLVAFIGRLEEQKGPDVMIAAIPEIVKEEDVQIVLLGTGkkkfeRLLKSVEEKFPGKVRAVVRFNAPLAhQMMAGADLLA 144
Cdd:cd03814 199 PLLLYVGRLAPEKNLEALLDADLPLAASPPVRLVVVGDG-----PARAELEARGPDVIFTGFLTGEELA-RAYASADVFV 272

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 12278435 145 VTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGF 185
Cdd:cd03814 273 FPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGA 313
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 34-211 1.41e-06

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: 48.48  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  34 VNYDITTALEAKAlNKEALQAEVGLPVDRKVPLVAFIGRLEEQKGPDVMIAAIPEIVKEEDVQIVLLGTGKKKFERLlks 113
Cdd:cd03825 166 IPNGIDTEIFAPV-DKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEALKLLATKDDLLLVVFGKNDPQIVIL--- 241

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 114 veekfPGKVRAVVRFNAplAHQMM---AGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrl 190
Cdd:cd03825 242 -----PFDIISLGYIDD--DEQLVdiySAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGY----- 309

                       170       180
                ....*....|....*....|.
gi 12278435 191 svdcnVVEPADVKKVATTLKR 211
Cdd:cd03825 310 -----LVPPGDVQALAEAIEW 325
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 65-210 1.81e-06

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 48.55  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435   65 PLVAFIGRLEEQKGPDV---MIAAIPEivkeedVQIVLLGTG--KKKFERLLKSVEEKFPGKVRAvvrfnAPLAhQMMAG 139
Cdd:PLN02871 264 PLIVYVGRLGAEKNLDFlkrVMERLPG------ARLAFVGDGpyREELEKMFAGTPTVFTGMLQG-----DELS-QAYAS 331

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 12278435  140 ADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTI---VEGKTGFhmgrlsvdcnVVEPADVKKVATTLK 210
Cdd:PLN02871 332 GDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGF----------LYTPGDVDDCVEKLE 395
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 59-185 2.12e-06

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: 48.05  E-value: 2.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  59 PVDRKVPLVAFIGRLEEQKGPDVMIaaipEIVKEEDVQIVLLGTGKKK--FERLlksvEEKFPGkvrAVVRFNAPLAHQ- 135
Cdd:cd03802 164 FQPDPEDYLAFLGRIAPEKGLEDAI----RVARRAGLPLKIAGKVRDEdyFYYL----QEPLPG---PRIEFIGEVGHDe 232

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 12278435 136 ---MMAGADLLAVTSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGF 185
Cdd:cd03802 233 kqeLLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGF 286
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 21-172 2.47e-06

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: 47.74  E-value: 2.47e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  21 VSEWdpTKD---KFLAVNYD--ITTALEAKALNKEALQAEVGLP-VDRKVPLVAFIGRLEEQKGPDVMIAAIpEIVKEE- 93
Cdd:cd03809 145 VSEA--TRDdiiKFYGVPPEkiVVIPLGVDPSFFPPESAAVLIAkYLLPEPYFLYVGTLEPRKNHERLLKAF-ALLKKQg 221

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  94 -DVQIVLLGTGKKKFERLLKSVEE-KFPGKVRAVVRFNAPLAHQMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACAST 171
Cdd:cd03809 222 gDLKLVIVGGKGWEDEELLDLVKKlGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNI 301


                .
gi 12278435 172 G 172
Cdd:cd03809 302 S 302
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 15-202 3.06e-06

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: 47.70  E-value: 3.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  15 IVNGMDVSEWDPTKDKflavnydittaleakalnKEALQAEVGLPVDRKVplVAFIGRLEEQKGPDVMIAAIPEIVKE-E 93
Cdd:cd03807 161 IYNGIDLFKLSPDDAS------------------RARARRRLGLAEDRRV--IGIVGRLHPVKDHSDLLRAAALLVEThP 220

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  94 DVQIVLLGTG--KKKFERLLK--SVEEKfpgkvravVRFNAPLAH--QMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCA 167
Cdd:cd03807 221 DLRLLLVGRGpeRPNLERLLLelGLEDR--------VHLLGERSDvpALLPAMDIFVLSSRTEGFPNALLEAMACGLPVV 292

                       170       180       190
                ....*....|....*....|....*....|....*
gi 12278435 168 CASTGGLVDtIVEGKTGFhmgrlsvdcnVVEPADV 202
Cdd:cd03807 293 ATDVGGAAE-LVDDGTGF----------LVPAGDP 316
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 45-227 1.73e-05

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: 45.42  E-value: 1.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  45 KALNKEALQAEVGLPVDRKVplVAFIGRLEEQKGPDVMIAAIPEIVKEEDVQIVLLGTGKKKFERLLKSVEEKFPGKVRA 124
Cdd:cd04962 179 KRKPAGALKRRLLAPPDEKV--VIHVSNFRPVKRIDDVVRVFARVRRKIPAKLLLVGDGPERVPAEELARELGVEDRVLF 256

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 125 VVRFNaPLAHqMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFhmgrlsvdcnVVEPADVKK 204
Cdd:cd04962 257 LGKQD-DVEE-LLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGF----------LSDVGDVDA 324

                       170       180
                ....*....|....*....|....
gi 12278435 205 VAttlKRAVKVVGTPA-YQEMVKN 227
Cdd:cd04962 325 MA---KSALSILEDDElYNRMGRA 345
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 15-236 4.60e-05

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: 43.90  E-value: 4.60e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  15 IVNGMDVSEWDPTkdkflavnydittaleakalnkEALQAEVGLPVDRKVPLvaFIGRLEEQKGPDVMIAAIPEIVKEE- 93
Cdd:cd03821 179 IPNGVDIPEFDPG----------------------LRDRRKHNGLEDRRIIL--FLGRIHPKKGLDLLIRAARKLAEQGr 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  94 DVQIVLLGTGKKKFERLLKSVEEK-------FPGKVRAVVRFNAplahqmMAGADLLAVTSRFEPCGLIQLQGMRYGTPc 166
Cdd:cd03821 235 DWHLVIAGPDDGAYPAFLQLQSSLglgdrvtFTGPLYGEAKWAL------YASADLFVLPSYSENFGNVVAEALACGLP- 307

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 12278435 167 acastgglvdTIVEGKTGFHMGRlSVDCNVVEPADVKKVATTLKRAVKVVGTP-AYQEMVKNC--MIQDLSWK 236
Cdd:cd03821 308 ----------VVITDKCGLSELV-EAGCGVVVDPNVSSLAEALAEALRDPADRkRLGEMARRArqVEENFSWE 369
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 70-166 3.96e-04

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 41.12  E-value: 3.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  70 IGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGTG----KKKFERLLKSVEEK--FPGKVRAVVRFnaplahqMMAgADL 142
Cdd:cd03812 197 VGRFNEQKNHSFLIDIFEELKKKnPNVKLVLVGEGelkeKIKEKVKELGLEDKviFLGFRNDVSEI-------LSA-MDV 268

                        90       100
                ....*....|....*....|....
gi 12278435 143 LAVTSRFEPCGLIQLQGMRYGTPC 166
Cdd:cd03812 269 FLFPSLYEGLPLVAVEAQASGLPC 292
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 45-214 4.11e-04

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: 41.17  E-value: 4.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  45 KALNKEALQAEVGLPvDRKVplVAFIGRLEEQKGPDVMIAAIPEIVKEEDVQIVLLGTGKKKfERLLKSVEEkfpgKVRA 124
Cdd:cd03794 201 KPPPKDELRKKLGLD-DKFV--VVYAGNIGKAQGLETLLEAAERLKRRPDIRFLFVGDGDEK-ERLKELAKA----RGLD 272

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435 125 VVRFNAPLAHQMM----AGADLLAVTSRFEPCGL----IQLQG-MRYGTPCACASTGGLVDTIVEGKTGFhmgrlsvdcn 195
Cdd:cd03794 273 NVTFLGRVPKEEVpellSAADVGLVPLKDNPANRgsspSKLFEyMAAGKPILASDDGGSDLAVEINGCGL---------- 342

                       170
                ....*....|....*....
gi 12278435 196 VVEPADVKKVATTLKRAVK 214
Cdd:cd03794 343 VVEPGDPEALADAILELLD 361
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 59-194 6.41e-04

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 40.35  E-value: 6.41e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 12278435  59 PVDRKVPLVA--------FIGRLEEQKGPDVMIAAIPEIVKeedvQIVLLGTGKKkfERLLKSVEE---KFPGKVRAVVr 127
Cdd:cd03804 186 PVDTDAFAPAadkedyylTASRLVPYKRIDLAVEAFNELPK----RLVVIGDGPD--LDRLRAMASpnvEFLGYQPDEV- 258

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 12278435 128 fnapLAHQMM-AGADLLAVTSRFepcGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGFHMGRLSVDC 194
Cdd:cd03804 259 ----LKELLSkARAFVFAAEEDF---GIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVES 319
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 135-185 2.95e-03

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: 38.34  E-value: 2.95e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 12278435 135 QMMAGADLLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIVEGKTGF 185
Cdd:cd03805 295 QLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGF 345
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 43-102 7.52e-03

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: 37.36  E-value: 7.52e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 12278435  43 EAKALNKEALQAEvGLPVDRKVplVAFIGRLEEQKGPDVMIAAIPEIVKE-EDVQIVLLGT 102
Cdd:cd03822 169 EVPQDPTTALKRL-LLPEGKKV--ILTFGFIGPGKGLEILLEALPELKAEfPDVRLVIAGE 226
 
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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