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Conserved domains on  [gi|15054992|gb|AAK82804|]
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granule-bound starch synthase, partial [Zea mays subsp. mays]

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 ...
 3-245 3.86e-98

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: 294.86  E-value: 3.86e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   3 MRLTGITGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAI 82
Cdd:cd03791 238 ARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDAL 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  83 PQLMEmvEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTP 162
Cdd:cd03791 317 PELLE--EGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 163 CACASTGGLVDTIIEG------KTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVGTP-AYEEMVRNCMIQDLSWKGP 235
Cdd:cd03791 395 PIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALALYRNPeLWRKLQKNAMKQDFSWDKS 464

                       250
                ....*....|
gi 15054992 236 AKNWENVLLS 245
Cdd:cd03791 465 AKEYLELYRS 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 ...
 3-245 3.86e-98

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: 294.86  E-value: 3.86e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   3 MRLTGITGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAI 82
Cdd:cd03791 238 ARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDAL 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  83 PQLMEmvEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTP 162
Cdd:cd03791 317 PELLE--EGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 163 CACASTGGLVDTIIEG------KTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVGTP-AYEEMVRNCMIQDLSWKGP 235
Cdd:cd03791 395 PIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALALYRNPeLWRKLQKNAMKQDFSWDKS 464

                       250
                ....*....|
gi 15054992 236 AKNWENVLLS 245
Cdd:cd03791 465 AKEYLELYRS 474
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 8-246 1.11e-91

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: 277.99  E-value: 1.11e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992     8 ITGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLME 87
Cdd:TIGR02095 240 LRGILNGIDTEVWNPATDPYLKANYSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLE 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    88 MveDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACAS 167
Cdd:TIGR02095 319 L--GGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVPIVRR 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   168 TGGLVDTIIEGK------TGFHMGRlsvdcnvVEPADvkkVATTLQRAIKvvgtpAY-------EEMVRNCMIQDLSWKG 234
Cdd:TIGR02095 397 TGGLADTVVDGDpeaesgTGFLFEE-------YDPGA---LLAALSRALR-----LYrqdpslwEALQKNAMSQDFSWDK 461

                         250
                  ....*....|..
gi 15054992   235 PAKNWENVLLSL 246
Cdd:TIGR02095 462 SAKQYVELYRSL 473
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
9-242 3.21e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 276.97  E-value: 3.21e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   9 TGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEM 88
Cdd:COG0297 245 SGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEE 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  89 veDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACAST 168
Cdd:COG0297 324 --DVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVPIVRRT 401

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 169 GGLVDTII------EGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVGTP-AYEEMVRNCMIQDLSWKGPAKNWEN 241
Cdd:COG0297 402 GGLADTVIdyneatGEGTGF----------VFDEYTAEALLAAIRRALALYRDPeAWRKLQRNAMKQDFSWEKSAKEYLE 471


                .
gi 15054992 242 V 242
Cdd:COG0297 472 L 472
glgA PRK00654
glycogen synthase GlgA;
9-237 1.47e-79

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 246.57  E-value: 1.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    9 TGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDrNIPLVAFIGRLEEQKGPDVMAAAIPQLMEm 88
Cdd:PRK00654 233 SGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLE- 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   89 vEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGT-PCAcAS 167
Cdd:PRK00654 310 -QGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTlPIV-RR 387

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15054992  168 TGGLVDTII------EGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVGTPA-YEEMVRNCMIQDLSWKGPAK 237
Cdd:PRK00654 388 TGGLADTVIdynpedGEATGF----------VFDDFNAEDLLRALRRALELYRQPPlWRALQRQAMAQDFSWDKSAE 454
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 61-211 6.61e-17

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: 75.39  E-value: 6.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    61 PLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRaVVKF--NAALaHHIMAGAD 138
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVI-FLGFvsDEDL-PELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15054992   139 VLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIK 211
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF----------LVKPNNAEALAEAIDKLLE 143
 
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 ...
 3-245 3.86e-98

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: 294.86  E-value: 3.86e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   3 MRLTGITGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAI 82
Cdd:cd03791 238 ARAGKLSGILNGIDYDEWNPATDKLIPANYSAND-LEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDAL 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  83 PQLMEmvEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTP 162
Cdd:cd03791 317 PELLE--EGGQLVVLGSGDPEYEQAFRELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQMYAMRYGTL 394

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 163 CACASTGGLVDTIIEG------KTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVGTP-AYEEMVRNCMIQDLSWKGP 235
Cdd:cd03791 395 PIVRRTGGLADTVFDYdpetgeGTGF----------VFEDYDAEALLAALRRALALYRNPeLWRKLQKNAMKQDFSWDKS 464

                       250
                ....*....|
gi 15054992 236 AKNWENVLLS 245
Cdd:cd03791 465 AKEYLELYRS 474
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 8-246 1.11e-91

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: 277.99  E-value: 1.11e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992     8 ITGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLME 87
Cdd:TIGR02095 240 LRGILNGIDTEVWNPATDPYLKANYSADD-LAGKAENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLE 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    88 MveDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACAS 167
Cdd:TIGR02095 319 L--GGQLVVLGTGDPELEEALRELAERYPGNVRVIIGYDEALAHLIYAGADFILMPSRFEPCGLTQLYAMRYGTVPIVRR 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   168 TGGLVDTIIEGK------TGFHMGRlsvdcnvVEPADvkkVATTLQRAIKvvgtpAY-------EEMVRNCMIQDLSWKG 234
Cdd:TIGR02095 397 TGGLADTVVDGDpeaesgTGFLFEE-------YDPGA---LLAALSRALR-----LYrqdpslwEALQKNAMSQDFSWDK 461

                         250
                  ....*....|..
gi 15054992   235 PAKNWENVLLSL 246
Cdd:TIGR02095 462 SAKQYVELYRSL 473
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
9-242 3.21e-91

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 276.97  E-value: 3.21e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   9 TGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEM 88
Cdd:COG0297 245 SGILNGIDYDVWNPATDPYLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEE 323

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  89 veDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACAST 168
Cdd:COG0297 324 --DVQLVVLGSGDPEYEEAFRELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQMYALRYGTVPIVRRT 401

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 169 GGLVDTII------EGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVGTP-AYEEMVRNCMIQDLSWKGPAKNWEN 241
Cdd:COG0297 402 GGLADTVIdyneatGEGTGF----------VFDEYTAEALLAAIRRALALYRDPeAWRKLQRNAMKQDFSWEKSAKEYLE 471


                .
gi 15054992 242 V 242
Cdd:COG0297 472 L 472
glgA PRK00654
glycogen synthase GlgA;
9-237 1.47e-79

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 246.57  E-value: 1.47e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    9 TGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDrNIPLVAFIGRLEEQKGPDVMAAAIPQLMEm 88
Cdd:PRK00654 233 SGILNGIDYDIWNPETDPLLAANYSADD-LEGKAENKRALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLE- 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   89 vEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGT-PCAcAS 167
Cdd:PRK00654 310 -QGGQLVLLGTGDPELEEAFRALAARYPGKVGVQIGYDEALAHRIYAGADMFLMPSRFEPCGLTQLYALRYGTlPIV-RR 387

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15054992  168 TGGLVDTII------EGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVGTPA-YEEMVRNCMIQDLSWKGPAK 237
Cdd:PRK00654 388 TGGLADTVIdynpedGEATGF----------VFDDFNAEDLLRALRRALELYRQPPlWRALQRQAMAQDFSWDKSAE 454
PRK14099 PRK14099
glycogen synthase GlgA;
4-239 5.40e-56

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 186.08  E-value: 5.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    4 RLTGITGIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIP 83
Cdd:PRK14099 240 RADRLSGILNGIDTAVWNPATDELIAATYDVET-LAARAANKAALQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALP 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   84 QLMEmvEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPC 163
Cdd:PRK14099 319 TLLG--EGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIGYDEALAHLIQAGADALLVPSRFEPCGLTQLCALRYGAVP 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  164 ACASTGGLVDTIIEGK---------TGFHMGRLSVDCnvvepadvkkVATTLQRAIKVVGTPA-YEEMVRNCMIQDLSWK 233
Cdd:PRK14099 397 VVARVGGLADTVVDANemaiatgvaTGVQFSPVTADA----------LAAALRKTAALFADPVaWRRLQRNGMTTDVSWR 466


                 ....*.
gi 15054992  234 GPAKNW 239
Cdd:PRK14099 467 NPAQHY 472
PRK14098 PRK14098
starch synthase;
10-239 6.34e-46

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 159.90  E-value: 6.34e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   10 GIVNGMDVSEWDPSRDKYIAVKYDVSTaVEAKALNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEMv 89
Cdd:PRK14098 258 GILNGIDTRQWNPSTDKLIKKRYSIER-LDGKLENKKALLEEVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVEL- 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   90 eDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGT-PCACAsT 168
Cdd:PRK14098 336 -DIQLVICGSGDKEYEKRFQDFAEEHPEQVSVQTEFTDAFFHLAIAGLDMLLMPGKIESCGMLQMFAMSYGTiPVAYA-G 413

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15054992  169 GGLVDTIIE----GKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIKVVG-TPAYEEMVRNCMIQDLSWKGPAKNW 239
Cdd:PRK14098 414 GGIVETIEEvsedKGSGF----------IFHDYTPEALVAKLGEALALYHdEERWEELVLEAMERDFSWKNSAEEY 479
PLN02316 PLN02316
synthase/transferase
 10-236 2.54e-36

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 136.15  E-value: 2.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    10 GIVNGMDVSEWDPSRDKYIAVKYDVSTAVEAKALNKEALQAEVGLPvDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEmv 89
Cdd:PLN02316  791 GILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEALQQRLGLK-QADLPLVGIITRLTHQKGIHLIKHAIWRTLE-- 867

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    90 EDVQIVLLGTG-----KKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCA 164
Cdd:PLN02316  868 RNGQVVLLGSApdpriQNDFVNLANQLHSSHHDRARLCLTYDEPLSHLIYAGADFILVPSIFEPCGLTQLTAMRYGSIPV 947

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   165 CASTGGLVDTIIEgktgfhmgrlsVD-------CNVVEP-------ADVKKVATTLQRAIKVV--GTPAYEEMVRNCMIQ 228
Cdd:PLN02316  948 VRKTGGLFDTVFD-----------VDhdkeraqAQGLEPngfsfdgADAAGVDYALNRAISAWydGRDWFNSLCKRVMEQ 1016


                  ....*...
gi 15054992   229 DLSWKGPA 236
Cdd:PLN02316 1017 DWSWNRPA 1024
PLN02939 PLN02939
transferase, transferring glycosyl groups
 10-245 4.83e-33

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 126.94  E-value: 4.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   10 GIVNGMDVSEWDPSRDKYIAVKYDVsTAVEAKALNKEALQAEVGLP-VDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEM 88
Cdd:PLN02939 729 GILNGIDTDTWNPSTDRFLKVQYNA-NDLQGKAANKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAEL 807

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   89 veDVQIVLLGTG-----KKKFERMlmsaEEKFPGK--VRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGT 161
Cdd:PLN02939 808 --GGQFVLLGSSpvphiQREFEGI----ADQFQSNnnIRLILKYDEALSHSIYAASDMFIIPSMFEPCGLTQMIAMRYGS 881

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  162 PCACASTGGLVDTI---------IEGKTGFHMGRlsvdcnvvepADVKKVATTLQRAIKVV--GTPAYEEMVRNCMIQDL 230
Cdd:PLN02939 882 VPIVRKTGGLNDSVfdfddetipVELRNGFTFLT----------PDEQGLNSALERAFNYYkrKPEVWKQLVQKDMNIDF 951

                        250
                 ....*....|....*
gi 15054992  231 SWKGPAKNWENVLLS 245
Cdd:PLN02939 952 SWDSSASQYEELYQR 966
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 43-243 1.29e-20

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: 89.52  E-value: 1.29e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  43 LNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKKKFERmLMSAEEKFPGKVRAV 122
Cdd:cd03801 175 LERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAE-LEELELGLGDRVRFL 253

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 123 VKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKV 202
Cdd:cd03801 254 GFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGL----------VVPPDDVEAL 323

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15054992 203 ATTLQRAIKvvGTPAYEEMVRN---CMIQDLSWKGPAKNWENVL 243
Cdd:cd03801 324 ADALLRLLA--DPELRARLGRAareRVAERFSWERVAERLLDLY 365
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 45-211 1.04e-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: 81.52  E-value: 1.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  45 KEALQAEVGLPVDRniPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTG------KKKFERMLMSAEEKFPGK 118
Cdd:cd03800 207 AEARRARLLLPPDK--PVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPsddplsMDREELAELAEELGLIDR 284

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 119 VRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFHmgrlsvdcnvVEPAD 198
Cdd:cd03800 285 VRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLL----------VDPHD 354

                       170
                ....*....|...
gi 15054992 199 VKKVATTLQRAIK 211
Cdd:cd03800 355 PEALAAALRRLLD 367
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 61-211 6.61e-17

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: 75.39  E-value: 6.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    61 PLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRaVVKF--NAALaHHIMAGAD 138
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVI-FLGFvsDEDL-PELLKIAD 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15054992   139 VLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIK 211
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGF----------LVKPNNAEALAEAIDKLLE 143
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
61-211 1.37e-16

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 74.08  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992    61 PLVAFIGRL-EEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGK-KKFERMLMSAEEK--FPGKVRAVVKFnaalahhiMAG 136
Cdd:pfam13692   2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPeEELEELAAGLEDRviFTGFVEDLAEL--------LAA 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15054992   137 ADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDtIIEGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIK 211
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGL----------LVPPGDPEALAEAILRLLE 137
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 65-182 2.41e-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: 70.13  E-value: 2.41e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  65 FIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNA-ALAHHIMAGADVLAVT 143
Cdd:cd01635 115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDdEVLELLLAAADVFVLP 194

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15054992 144 SRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGF 182
Cdd:cd01635 195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGL 233
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 46-210 3.92e-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: 68.18  E-value: 3.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  46 EALQAEVGLPVDRniPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTG--KKKFERMLMSAeekfpgKVRAVV 123
Cdd:cd03798 188 QPEDRGLGLPLDA--FVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGplREALRALAEDL------GLGDRV 259

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 124 KFNAALAHH----IMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADV 199
Cdd:cd03798 260 TFTGRLPHEqvpaYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGL----------LVPPGDA 329

                       170
                ....*....|.
gi 15054992 200 KKVATTLQRAI 210
Cdd:cd03798 330 DALAAALRRAL 340
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 128-246 6.50e-11

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 58.08  E-value: 6.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 128 ALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVATTLQ 207
Cdd:COG0438  12 LLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGL----------LVPPGDPEALAEAIL 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15054992 208 RAIKvvGTPAYEEMVRNC---MIQDLSWKGPAKNWENVLLSL 246
Cdd:COG0438  82 RLLE--DPELRRRLGEAArerAEERFSWEAIAERLLALYEEL 121
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 39-182 1.26e-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: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  39 EAKALNKEALQAEvglpvDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKKKFErmLMS-AEE---- 113
Cdd:cd03811 172 RIRALAKEPILNE-----PEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREE--LEKlAKElgla 244

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15054992 114 ---KFPGKVRAVVKFnaalahhiMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGF 182
Cdd:cd03811 245 ervIFLGFQSNPYPY--------LKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL 308
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 56-223 1.45e-10

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: 60.45  E-value: 1.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  56 VDRNIPLVAFIGRLEEQKGPDVMAAAIPqlmEMVEDVQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAALAHHIMA 135
Cdd:cd03819 178 LPEGKPVVGYVGRLSPEKGWLLLVDAAA---ELKDEPDFRLLVAGDGPERDEIRRLVERLGLRDRVTFTGFREDVPAALA 254

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 136 GADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFhmgrLSVDCNVVEPADVKK-VATTLQRAIKVVG 214
Cdd:cd03819 255 ASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGL----LVPPGDAEALADAIRaAKLLPEAREKLQA 330


                ....*....
gi 15054992 215 TPAYEEMVR 223
Cdd:cd03819 331 AAALTEAVR 339
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 25-211 3.67e-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: 59.15  E-value: 3.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  25 DKYIAV-KYDVSTAVEAKALNKEalQAEV----GLPVDR----------NIPLVAFIGRLEEQKGPDVMAAAIPQLMEMV 89
Cdd:cd03808 141 DKVIFVnEDDRDLAIKKGIIKKK--KTVLipgsGVDLDRfqyspeslpsEKVVFLFVARLLKDKGIDELIEAAKILKKKG 218

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  90 EDVQIVLLGTGKKKfERMLMSAEE-------KFPGKVRAVvkfnaalaHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTP 162
Cdd:cd03808 219 PNVRFLLVGDGELE-NPSEILIEKlglegriEFLGFRSDV--------PELLAESDVFVLPSYREGLPRSLLEAMAAGRP 289

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15054992 163 CACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIK 211
Cdd:cd03808 290 VITTDVPGCRELVIDGVNGF----------LVPPGDVEALADAIEKLIE 328
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 61-208 1.00e-09

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: 57.85  E-value: 1.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  61 PLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKkkfERMLMSAEEKFPGKVRavvkFNAALAH----HIMAG 136
Cdd:cd05844 190 PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGP---LRPALQALAAALGRVR----FLGALPHaevqDWMRR 262

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15054992 137 ADVLAVTSRF------EPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVATTLQR 208
Cdd:cd05844 263 AEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGF----------LVPEGDVDALADALQA 330
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
44-243 2.59e-09

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 56.72  E-value: 2.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   44 NKEALQAEVGLPVDRNIPLVAfiGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLG--TGKKKFERmlmsaeEKFPGKVRA 121
Cdd:PRK15484 179 PQPNLRQQLNISPDETVLLYA--GRISPDKGILLLMQAFEKLATAHSNLKLVVVGdpTASSKGEK------AAYQKKVLE 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  122 VVKfnAALAHHIMAG-------------ADVLAVTSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFHMGrl 187
Cdd:PRK15484 251 AAK--RIGDRCIMLGgqppekmhnyyplADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITGYHLA-- 326

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15054992  188 svdcnvvEPADVKKVATTLQRAIKVVGTPAYEEMVRNCMIQDLSWKGPAKNWENVL 243
Cdd:PRK15484 327 -------EPMTSDSIISDINRTLADPELTQIAEQAKDFVFSKYSWEGVTQRFEEQI 375
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 63-211 5.26e-09

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: 55.71  E-value: 5.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  63 VAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTG--KKKFERML----MSAEEKFPGKVRAVvkfnaalaHHIMAG 136
Cdd:cd03820 184 ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGpeREELEKLIdklgLEDRVKLLGPTKNI--------AEEYAN 255

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15054992 137 ADVLAVTSRFEPCGLIQLQGMRYGTPCAC-ASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVATTLQRAIK 211
Cdd:cd03820 256 SSIFVLSSRYEGFPMVLLEAMAYGLPIISfDCPTGPSEIIEDGENGL----------LVPNGDVDALAEALLRLME 321
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 61-207 5.79e-08

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 52.79  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992   61 PLVAFIGRLEEQKGPDvmaaAIPQLMEMVEDVQIVLLGTG--KKKFERMLMSAEEKFPGKVRAVvKFNAALAhhimaGAD 138
Cdd:PLN02871 264 PLIVYVGRLGAEKNLD----FLKRVMERLPGARLAFVGDGpyREELEKMFAGTPTVFTGMLQGD-ELSQAYA-----SGD 333

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15054992  139 VLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTI---IEGKTGFhmgrlsvdcnVVEPADVKKVATTLQ 207
Cdd:PLN02871 334 VFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGF----------LYTPGDVDDCVEKLE 395
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 63-210 7.96e-08

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: 52.33  E-value: 7.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  63 VAFIGRLEEQKGPDVMAAAIPQLMEmvEDVQIVLLGTGKKKFERMLMSAEE-KFPGKVRavvkfNAALAHHiMAGADVLA 141
Cdd:cd03823 194 FGYIGRLTEEKGIDLLVEAFKRLPR--EDIELVIAGHGPLSDERQIEGGRRiAFLGRVP-----TDDIKDF-YEKIDVLV 265

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 142 VTSRF-EPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFHmgrlsvdcnvVEPADVKKVATTLQRAI 210
Cdd:cd03823 266 VPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLL----------FAPGDAEDLAAAMRRLL 325
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 61-182 4.93e-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: 49.99  E-value: 4.93e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  61 PLVAFIGRLEEQKGPDVMAAAIPQLMEMvEDVQIVLLGTG--KKKFERMLMSAeeKFPGkvravVKFNAALAHHiMAGAD 138
Cdd:cd03814 199 PLLLYVGRLAPEKNLEALLDADLPLAAS-PPVRLVVVGDGpaRAELEARGPDV--IFTG-----FLTGEELARA-YASAD 269

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15054992 139 VLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGF 182
Cdd:cd03814 270 VFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGA 313
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 41-183 2.37e-06

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: 47.66  E-value: 2.37e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  41 KALNKEALQAevgLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEMVeDVQIVLLGTG--KKKFERMlmsAEEKfpgK 118
Cdd:cd03817 185 KPLNTEERRK---LGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEP-NIKLVIVGDGpeREELKEL---AREL---G 254

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 119 VRAVVKF-----NAALAHhIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFH 183
Cdd:cd03817 255 LADKVIFtgfvpREELPE-YYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFL 323
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 61-225 5.41e-06

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: 46.88  E-value: 5.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  61 PLVAFIGRLEEQKGPDVMAAAIPQLmemveDVQIVLLGTGKKKfERMLMSAEEKFPGKVRAVVKFNAALAHHIMAGADVL 140
Cdd:cd03795 192 KIFLFIGRLVYYKGLDYLIEAAQYL-----NYPIVIGGEGPLK-PDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVF 265

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 141 AVTS--RFEPCGLIQLQGMRYGTP-CACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVAttlqRAIKVV--GT 215
Cdd:cd03795 266 VFPSvlRSEAFGIVLLEAMMCGKPvISTNIGTGVPYVNNNGETGL----------VVPPKDPDALA----EAIDKLlsDE 331

                       170
                ....*....|
gi 15054992 216 PAYEEMVRNC 225
Cdd:cd03795 332 ELRESYGENA 341
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 59-241 7.04e-06

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: 46.59  E-value: 7.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  59 NIPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTGKKKFERMLMSAEEK-------FPGKVRAVVKfnAALah 131
Cdd:cd03821 203 DRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDDGAYPAFLQLQSSLglgdrvtFTGPLYGEAK--WAL-- 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 132 hiMAGADVLAVTSRFEPCGLIQLQGMRYGTPcacastgglvdTIIEGKTGFHMGRlSVDCNVVEPADVKKVATTLQRAIK 211
Cdd:cd03821 279 --YASADLFVLPSYSENFGNVVAEALACGLP-----------VVITDKCGLSELV-EAGCGVVVDPNVSSLAEALAEALR 344

                       170       180       190
                ....*....|....*....|....*....|...
gi 15054992 212 VVGTP-AYEEMVRNC--MIQDLSWKGPAKNWEN 241
Cdd:cd03821 345 DPADRkRLGEMARRArqVEENFSWEAVAGQLGE 377
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 20-182 1.52e-05

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: 45.39  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  20 WDPSRDKYIAVKYDVST-AVEAKALNKEALQaevgLPVDRNIPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLG 98
Cdd:cd03807 153 YAKNKIVVIYNGIDLFKlSPDDASRARARRR----LGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVG 228

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  99 TGKKKFERMLMSAEEKFPGKV-----RAVVkfnAALAHHimagADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGLVD 173
Cdd:cd03807 229 RGPERPNLERLLLELGLEDRVhllgeRSDV---PALLPA----MDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAE 301


                ....*....
gi 15054992 174 TIIEGkTGF 182
Cdd:cd03807 302 LVDDG-TGF 309
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 11-211 6.89e-05

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: 43.47  E-value: 6.89e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  11 IVNGMDVSEWDPsrdkyiavkydvstaveakaLNKEALQAEVGLPVDRNIPLVAFIGRLEEQKGPDVMAAAIpQLMEMVE 90
Cdd:cd03825 166 IPNGIDTEIFAP--------------------VDKAKARKRLGIPQDKKVILFGAESVTKPRKGFDELIEAL-KLLATKD 224

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  91 DVQIVLLGTGkkkfermlmsAEEKFPGKVRaVVKF----NAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACA 166
Cdd:cd03825 225 DLLLVVFGKN----------DPQIVILPFD-IISLgyidDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAF 293

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15054992 167 STGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVkkvaTTLQRAIK 211
Cdd:cd03825 294 DTGGSPEIVQHGVTGY----------LVPPGDV----QALAEAIE 324
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 16-169 3.94e-04

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: 41.19  E-value: 3.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  16 DVSEWDPSRDKYIAVKYDVSTAVEAKALNKEALQAEVGLPVdrniPLVAFIGRLEEQKGPDVMAAAIPQLMEMVEDVQIV 95
Cdd:cd03809 152 DIIKFYGVPPEKIVVIPLGVDPSFFPPESAAVLIAKYLLPE----PYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLV 227

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15054992  96 LLGTGKKKFERMLMSAEE-KFPGKVRAVVKFNAALAHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTG 169
Cdd:cd03809 228 IVGGKGWEDEELLDLVKKlGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNIS 302
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 92-223 1.21e-03

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: 39.64  E-value: 1.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  92 VQIVLLGTGKKKFERMLMSAEEKFPGKVRAVVKFNAAlaHHIMAGADVLAVTSRFEPCGLIQLQGMRYGTPCACASTGGL 171
Cdd:cd04962 227 AKLLLVGDGPERVPAEELARELGVEDRVLFLGKQDDV--EELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGI 304

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15054992 172 VDTIIEGKTGF------------HMGRLSVD---CNVVEPADVKKVATTLQRAIKVvgtPAYEEMVR 223
Cdd:cd04962 305 PEVVKHGETGFlsdvgdvdamakSALSILEDdelYNRMGRAARKRAAERFDPERIV---PQYEAYYR 368
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 66-163 1.64e-03

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: 39.19  E-value: 1.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  66 IGRLEEQKGPDVMAAAIPQLMEMVEDVQIVLLGTG----KKKFERMLMSAEEK--FPGKVRAVvkfnaalaHHIMAGADV 139
Cdd:cd03812 197 VGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGelkeKIKEKVKELGLEDKviFLGFRNDV--------SEILSAMDV 268

                        90       100
                ....*....|....*....|....
gi 15054992 140 LAVTSRFEPCGLIQLQGMRYGTPC 163
Cdd:cd03812 269 FLFPSLYEGLPLVAVEAQASGLPC 292
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 63-203 2.09e-03

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: 38.86  E-value: 2.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  63 VAFIGRLEEQKGPDVMAAAIpQLMEMVEDVQIVLLGTGKKKFERMLMSAEEKFPGkvravVKF----NAALAHHIMAGAD 138
Cdd:cd03794 220 VVYAGNIGKAQGLETLLEAA-ERLKRRPDIRFLFVGDGDEKERLKELAKARGLDN-----VTFlgrvPKEEVPELLSAAD 293

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992 139 VLAVTSRFEPCGL----IQLQG-MRYGTPCACASTGGLVDTIIEGKTGFhmgrlsvdcnVVEPADVKKVA 203
Cdd:cd03794 294 VGLVPLKDNPANRgsspSKLFEyMAAGKPILASDDGGSDLAVEINGCGL----------VVEPGDPEALA 353
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 67-191 7.68e-03

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: 37.26  E-value: 7.68e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15054992  67 GRLEEQKGPDVMAAAIPQLmemveDVQIVLLGTGK--KKFERMLmSAEEKFPGKVRAVVkfnaaLAHHIM-AGADVLAVT 143
Cdd:cd03804 206 SRLVPYKRIDLAVEAFNEL-----PKRLVVIGDGPdlDRLRAMA-SPNVEFLGYQPDEV-----LKELLSkARAFVFAAE 274

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15054992 144 SRFepcGLIQLQGMRYGTPCACASTGGLVDTIIEGKTGFHMGRLSVDC 191
Cdd:cd03804 275 EDF---GIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVES 319
 
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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