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Conserved domains on  [gi|380779697|gb|AFE63308|]
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waxy, partial [Hakea obliqua]

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 ...
 2-205 4.48e-92

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: 277.14  E-value: 4.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   2 SFDFMDGYEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRK--TGIAGIVNGMDVQEWNPSTDK 79
Cdd:cd03791  186 ELFHIDGLEFY---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRAraGKLSGILNGIDYDEWNPATDK 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  80 YIDVKYdSTTVLDAKPVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQI 159
Cdd:cd03791  262 LIPANY-SANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAF 340

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 380779697 160 QQLETKYPEKAIGITKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:cd03791  341 RELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQM 386
 
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 ...
 2-205 4.48e-92

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: 277.14  E-value: 4.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   2 SFDFMDGYEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRK--TGIAGIVNGMDVQEWNPSTDK 79
Cdd:cd03791  186 ELFHIDGLEFY---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRAraGKLSGILNGIDYDEWNPATDK 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  80 YIDVKYdSTTVLDAKPVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQI 159
Cdd:cd03791  262 LIPANY-SANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAF 340

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 380779697 160 QQLETKYPEKAIGITKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:cd03791  341 RELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQM 386
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 17-205 1.25e-83

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: 255.27  E-value: 1.25e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   17 KINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRKTG--IAGIVNGMDVQEWNPSTDKYIDVKYDSTTvLDAK 94
Cdd:TIGR02095 195 RVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-LAGK 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   95 PVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQIQQLETKYPEKAIGIT 174
Cdd:TIGR02095 273 AENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVII 352

                         170       180       190
                  ....*....|....*....|....*....|.
gi 380779697  175 KFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:TIGR02095 353 GYDEALAHLIYAGADFILMPSRFEPCGLTQL 383
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
2-205 9.09e-81

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 248.08  E-value: 9.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   2 SFDFMDGYEKPvkGrKINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRKTG--IAGIVNGMDVQEWNPSTDK 79
Cdd:COG0297  187 ELFTPDGLEFY--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDP 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  80 YIDVKYDSTTvLDAKPVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQI 159
Cdd:COG0297  263 YLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAF 341

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 380779697 160 QQLETKYPEKAIGITKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:COG0297  342 RELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQM 387
glgA PRK00654
glycogen synthase GlgA;
17-205 1.29e-70

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 221.92  E-value: 1.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  17 KINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRktGIA----GIVNGMDVQEWNPSTDKYIDVKYDSTTvLD 92
Cdd:PRK00654 187 QISFLKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLR--ARSgklsGILNGIDYDIWNPETDPLLAANYSADD-LE 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  93 AKPVLKEALQAEVGLPVDgNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQIQQLETKYPEK-AI 171
Cdd:PRK00654 263 GKAENKRALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKvGV 341

                        170       180       190
                 ....*....|....*....|....*....|....
gi 380779697 172 GITkFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:PRK00654 342 QIG-YDEALAHRIYAGADMFLMPSRFEPCGLTQL 374
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
6-58 7.03e-12

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 62.35  E-value: 7.03e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 380779697    6 MDGYEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRK 58
Cdd:pfam08323 191 LDGLEFY---GQINFLKAGIVYADAVTTVSPTYAEEIQTP-EFGGGLDGLLRE 239
 
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 ...
 2-205 4.48e-92

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: 277.14  E-value: 4.48e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   2 SFDFMDGYEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRK--TGIAGIVNGMDVQEWNPSTDK 79
Cdd:cd03791  186 ELFHIDGLEFY---GQINFLKAGIVYADRVTTVSPTYAKEILTP-EYGEGLDGVLRAraGKLSGILNGIDYDEWNPATDK 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  80 YIDVKYdSTTVLDAKPVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQI 159
Cdd:cd03791  262 LIPANY-SANDLEGKAENKAALQKELGLPVDPDAPLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAF 340

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 380779697 160 QQLETKYPEKAIGITKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:cd03791  341 RELAERYPGKVAVVIGFDEALAHRIYAGADFFLMPSRFEPCGLVQM 386
glgA TIGR02095
glycogen/starch synthase, ADP-glucose type; This family consists of glycogen (or starch) ...
 17-205 1.25e-83

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: 255.27  E-value: 1.25e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   17 KINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRKTG--IAGIVNGMDVQEWNPSTDKYIDVKYDSTTvLDAK 94
Cdd:TIGR02095 195 RVNFLKGGIVYADRVTTVSPTYAREILTP-EFGYGLDGVLKARSgkLRGILNGIDTEVWNPATDPYLKANYSADD-LAGK 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   95 PVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQIQQLETKYPEKAIGIT 174
Cdd:TIGR02095 273 AENKEALQEELGLPVDDDVPLFGVISRLTQQKGVDLLLAALPELLELGGQLVVLGTGDPELEEALRELAERYPGNVRVII 352

                         170       180       190
                  ....*....|....*....|....*....|.
gi 380779697  175 KFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:TIGR02095 353 GYDEALAHLIYAGADFILMPSRFEPCGLTQL 383
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
2-205 9.09e-81

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 248.08  E-value: 9.09e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   2 SFDFMDGYEKPvkGrKINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRKTG--IAGIVNGMDVQEWNPSTDK 79
Cdd:COG0297  187 ELFTPDGLEFY--G-QINFLKAGIVYADRVTTVSPTYAREIQTP-EFGEGLDGLLRARSgkLSGILNGIDYDVWNPATDP 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  80 YIDVKYDSTTvLDAKPVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQI 159
Cdd:COG0297  263 YLPANYSADD-LEGKAANKAALQEELGLPVDPDAPLIGMVSRLTEQKGLDLLLEALDELLEEDVQLVVLGSGDPEYEEAF 341

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 380779697 160 QQLETKYPEKAIGITKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:COG0297  342 RELAARYPGRVAVYIGYDEALAHRIYAGADFFLMPSRFEPCGLNQM 387
glgA PRK00654
glycogen synthase GlgA;
17-205 1.29e-70

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 221.92  E-value: 1.29e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  17 KINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRktGIA----GIVNGMDVQEWNPSTDKYIDVKYDSTTvLD 92
Cdd:PRK00654 187 QISFLKAGLYYADRVTTVSPTYAREITTP-EFGYGLEGLLR--ARSgklsGILNGIDYDIWNPETDPLLAANYSADD-LE 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  93 AKPVLKEALQAEVGLPVDgNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQIQQLETKYPEK-AI 171
Cdd:PRK00654 263 GKAENKRALQERFGLPDD-DAPLFAMVSRLTEQKGLDLVLEALPELLEQGGQLVLLGTGDPELEEAFRALAARYPGKvGV 341

                        170       180       190
                 ....*....|....*....|....*....|....
gi 380779697 172 GITkFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:PRK00654 342 QIG-YDEALAHRIYAGADMFLMPSRFEPCGLTQL 374
PRK14099 PRK14099
glycogen synthase GlgA;
18-205 1.07e-49

glycogen synthase GlgA;


Pssm-ID: 237610 [Multi-domain]  Cd Length: 485  Bit Score: 167.97  E-value: 1.07e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  18 INWMKAGILESDRVVTVSPYYAQElVSGVKKGVELDNIIRKTG--IAGIVNGMDVQEWNPSTDKYIDVKYDSTTvLDAKP 95
Cdd:PRK14099 200 IGYLKAGLQLADRITTVSPTYALE-IQGPEAGMGLDGLLRQRAdrLSGILNGIDTAVWNPATDELIAATYDVET-LAARA 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  96 VLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQIQQLETKYPEKAIGITK 175
Cdd:PRK14099 278 ANKAALQARFGLDPDPDALLLGVISRLSWQKGLDLLLEALPTLLGEGAQLALLGSGDAELEARFRAAAQAYPGQIGVVIG 357

                        170       180       190
                 ....*....|....*....|....*....|
gi 380779697 176 FNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:PRK14099 358 YDEALAHLIQAGADALLVPSRFEPCGLTQL 387
PRK14098 PRK14098
starch synthase;
13-205 1.25e-44

starch synthase;


Pssm-ID: 172588 [Multi-domain]  Cd Length: 489  Bit Score: 154.51  E-value: 1.25e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  13 VKGRKINWMKAGILESDRVVTVSPYYAQELVSGVKKGVELDNII--RKTGIAGIVNGMDVQEWNPSTDKYIDVKYdSTTV 90
Cdd:PRK14098 206 REGDEVNMLYTGVEHADLLTTTSPRYAEEIAGDGEEAFGLDKVLeeRKMRLHGILNGIDTRQWNPSTDKLIKKRY-SIER 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  91 LDAKPVLKEALQAEVGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQIQQLETKYPEKA 170
Cdd:PRK14098 285 LDGKLENKKALLEEVGLPFDEETPLVGVIINFDDFQGAELLAESLEKLVELDIQLVICGSGDKEYEKRFQDFAEEHPEQV 364

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380779697 171 IGITKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:PRK14098 365 SVQTEFTDAFFHLAIAGLDMLLMPGKIESCGMLQM 399
PLN02316 PLN02316
synthase/transferase
 28-205 8.62e-35

synthase/transferase


Pssm-ID: 215180 [Multi-domain]  Cd Length: 1036  Bit Score: 129.99  E-value: 8.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   28 SDRVVTVSPYYAQElVSGvkkgveldniirKTGIA-------GIVNGMDVQEWNPSTDKYIDVKYDSTTVLDAKPVLKEA 100
Cdd:PLN02316  762 ADKATTVSPTYSRE-VSG------------NSAIAphlykfhGILNGIDPDIWDPYNDNFIPVPYTSENVVEGKRAAKEA 828

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  101 LQAEVGLPvDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTgkkAMEKQIQ--------QLETKYPEKAIG 172
Cdd:PLN02316  829 LQQRLGLK-QADLPLVGIITRLTHQKGIHLIKHAIWRTLERNGQVVLLGS---APDPRIQndfvnlanQLHSSHHDRARL 904

                         170       180       190
                  ....*....|....*....|....*....|...
gi 380779697  173 ITKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:PLN02316  905 CLTYDEPLSHLIYAGADFILVPSIFEPCGLTQL 937
PLN02939 PLN02939
transferase, transferring glycosyl groups
 17-205 2.11e-29

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 114.61  E-value: 2.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  17 KINWMKAGILESDRVVTVSPYYAQELVSGVKKGVELDNIIRKTGIAGIVNGMDVQEWNPSTDKYIDVKYDSTTvLDAKPV 96
Cdd:PLN02939 683 RINVVKGAIVYSNIVTTVSPTYAQEVRSEGGRGLQDTLKFHSKKFVGILNGIDTDTWNPSTDRFLKVQYNAND-LQGKAA 761

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  97 LKEALQAEVGLP-VDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTG-----KKAMEKQIQQLETKYPEKA 170
Cdd:PLN02939 762 NKAALRKQLGLSsADASQPLVGCITRLVPQKGVHLIRHAIYKTAELGGQFVLLGSSpvphiQREFEGIADQFQSNNNIRL 841

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380779697 171 IgiTKFNVPLAHKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:PLN02939 842 I--LKYDEALSHSIYAASDMFIIPSMFEPCGLTQM 874
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 1-205 2.16e-14

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: 70.64  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697   1 SSFDFMDGYEKPVKGRKINWMKAGILESDRVVTVSPYYAQELVSgvKKGVELDNIIRktgiagIVNGMDVQEWNPSTDKy 80
Cdd:cd03801  114 GAEPGRLLLLLAAERRLLARAEALLRRADAVIAVSEALRDELRA--LGGIPPEKIVV------IPNGVDLERFSPPLRR- 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  81 idvkydsttvldakpvlkealqaevGLPVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGE--NVQIVILGtGKKAMEKQ 158
Cdd:cd03801  185 -------------------------KLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRgpDVRLVIVG-GDGPLRAE 238

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 380779697 159 IQQLEtKYPEKAIGITKFnVPLA--HKIIAGADFMLIPSRFEPCGLIQL 205
Cdd:cd03801  239 LEELE-LGLGDRVRFLGF-VPDEelPALYAAADVFVLPSRYEGFGLVVL 285
Glyco_transf_5 pfam08323
Starch synthase catalytic domain;
6-58 7.03e-12

Starch synthase catalytic domain;


Pssm-ID: 400563 [Multi-domain]  Cd Length: 239  Bit Score: 62.35  E-value: 7.03e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 380779697    6 MDGYEKPvkgRKINWMKAGILESDRVVTVSPYYAQELVSGvKKGVELDNIIRK 58
Cdd:pfam08323 191 LDGLEFY---GQINFLKAGIVYADAVTTVSPTYAEEIQTP-EFGGGLDGLLRE 239
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 16-199 1.95e-08

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: 53.13  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  16 RKINWMKAGILESDRVVTVSPyyaqelvsGVKKGVELDNIIRKTGIAGIVNGMDVQEwnpstdkyidvkydsttvldAKP 95
Cdd:cd03811  124 KKLLLKLKLYKKADKIVCVSK--------GIKEDLIRLGPSPPEKIEVIYNPIDIDR--------------------IRA 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  96 VLKEALQAEvglpvDGNIPVIGFIGRLEEQKGSDIL--AAAISQFVGENVQIVILGTG--KKAMEKQIQQLETKypEKAi 171
Cdd:cd03811  176 LAKEPILNE-----PEDGPVILAVGRLDPQKGHDLLieAFAKLRKKYPDVKLVILGDGplREELEKLAKELGLA--ERV- 247

                        170       180
                 ....*....|....*....|....*...
gi 380779697 172 gITKFNVPLAHKIIAGADFMLIPSRFEP 199
Cdd:cd03811  248 -IFLGFQSNPYPYLKKADLFVLSSRYEG 274
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 27-205 1.00e-07

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: 51.23  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  27 ESDRVVTVSPYYAQELVsgvKKGVELDNIIRktgiagIVNGmdvqewnpstdkyIDVKYDSttvldakpvlkeALQAEVG 106
Cdd:cd03798  150 RAARVIAVSKALAEELV---ALGVPRDRVDV------IPNG-------------VDPARFQ------------PEDRGLG 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697 107 LPVDGniPVIGFIGRLEEQKGSDILAAAIS--QFVGENVQIVILGTG--KKAMEKQIQQLetkypekaiGIT---KFNVP 179
Cdd:cd03798  196 LPLDA--FVILFVGRLIPRKGIDLLLEAFArlAKARPDVVLLIVGDGplREALRALAEDL---------GLGdrvTFTGR 264

                        170       180       190
                 ....*....|....*....|....*....|
gi 380779697 180 LAHKIIAG----ADFMLIPSRFEPCGLIQL 205
Cdd:cd03798  265 LPHEQVPAyyraCDVFVLPSRHEGFGLVLL 294
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 27-202 4.41e-07

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: 49.16  E-value: 4.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  27 ESDRVVTVSPYYAQELVSGVKKGVELDNIIRktgiagivNGMDVQEWNPSTDKyidvkydsttvldakpvlkEALQAEVG 106
Cdd:cd03800  163 AADRVIASTPQEADELISLYGADPSRINVVP--------PGVDLERFFPVDRA-------------------EARRARLL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697 107 LPVDGniPVIGFIGRLEEQKGSDIL--AAAISQFVGENVQIVILG---TGKKAMEK-QIQQLETKYpeKAIGITKFNVPL 180
Cdd:cd03800  216 LPPDK--PVVLALGRLDPRKGIDTLvrAFAQLPELRELANLVLVGgpsDDPLSMDReELAELAEEL--GLIDRVRFPGRV 291

                        170       180
                 ....*....|....*....|....*.
gi 380779697 181 AH----KIIAGADFMLIPSRFEPCGL 202
Cdd:cd03800  292 SRddlpELYRAADVFVVPSLYEPFGL 317
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 118-205 8.64e-07

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: 47.78  E-value: 8.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697 118 FIGRLEEQKGSDILAAAISQFV--GENVQIVILGTGKKAMEKQIQQLETKYPEKAIGITKF-NVPLAHKIIAGADFMLIP 194
Cdd:cd01635  115 SVGRLVPEKGIDLLLEALALLKarLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLvDDEVLELLLAAADVFVLP 194

                         90
                 ....*....|.
gi 380779697 195 SRFEPCGLIQL 205
Cdd:cd01635  195 SRSEGFGLVLL 205
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
114-202 1.33e-06

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 45.97  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  114 PVIGFIGRL-EEQKGSDILAAAISQFVGE--NVQIVILGTGKkamEKQIQQLETKYPEKAIgITKFnVPLAHKIIAGADF 190
Cdd:pfam13692   2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRdnDVRLVIVGDGP---EEELEELAAGLEDRVI-FTGF-VEDLAELLAAADV 76

                          90
                  ....*....|..
gi 380779697  191 MLIPSRFEPCGL 202
Cdd:pfam13692  77 FVLPSLYEGFGL 88
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 96-203 8.35e-05

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: 42.32  E-value: 8.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  96 VLKEALQAEVGLPV----DGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGtgkKAMEKQIQQLETKYPEKAI 171
Cdd:cd03823  170 VIPNAVEPDLAPPPrrrpGTERLRFGYIGRLTEEKGIDLLVEAFKRLPREDIELVIAG---HGPLSDERQIEGGRRIAFL 246

                         90       100       110
                 ....*....|....*....|....*....|...
gi 380779697 172 GITkFNVPLAHkIIAGADFMLIPSRF-EPCGLI 203
Cdd:cd03823  247 GRV-PTDDIKD-FYEKIDVLVVPSIWpEPFGLV 277
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 114-202 1.04e-04

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: 41.11  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  114 PVIGFIGRLEEQKGSD--ILAAAISQFVGENVQIVILGTG--KKAMEKQIQQLEtkyPEKAIGITKF----NVPLAHKIi 185
Cdd:pfam00534   3 KIILFVGRLEPEKGLDllIKAFALLKEKNPNLKLVIAGDGeeEKRLKKLAEKLG---LGDNVIFLGFvsdeDLPELLKI- 78

                          90
                  ....*....|....*..
gi 380779697  186 agADFMLIPSRFEPCGL 202
Cdd:pfam00534  79 --ADVFVLPSRYEGFGI 93
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 115-198 4.88e-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: 39.97  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697 115 VIGFIGRLEEQKGSDILAAAISQFV--GENVQIVILGTG--KKAMEKQIQQLETkypEKAIGITKFNVPLaHKIIAGADF 190
Cdd:cd03812  193 VLGHVGRFNEQKNHSFLIDIFEELKkkNPNVKLVLVGEGelKEKIKEKVKELGL---EDKVIFLGFRNDV-SEILSAMDV 268


                 ....*...
gi 380779697 191 MLIPSRFE 198
Cdd:cd03812  269 FLFPSLYE 276
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 16-198 6.26e-04

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: 39.89  E-value: 6.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  16 RKINWMKAGILE------SDRVVTVSPYYAQELVSgvKKGVELDNIIRKTGiagivNGMDVQEWNPSTDKYIDvkydstt 89
Cdd:cd03808  122 GKLLRLLYLLLEklallfTDKVIFVNEDDRDLAIK--KGIIKKKKTVLIPG-----SGVDLDRFQYSPESLPS------- 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  90 vldakpvlkealqaevglpvdgNIPVIGFIGRLEEQKGSDILAAAISQ--FVGENVQIVILGTG--KKAMEKQIQQLETk 165
Cdd:cd03808  188 ----------------------EKVVFLFVARLLKDKGIDELIEAAKIlkKKGPNVRFLLVGDGelENPSEILIEKLGL- 244

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 380779697 166 ypEKAIGITKF--NVPlahKIIAGADFMLIPSRFE 198
Cdd:cd03808  245 --EGRIEFLGFrsDVP---ELLAESDVFVLPSYRE 274
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 114-205 8.77e-04

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: 39.20  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697 114 PVIGFIGRLEEQKGSDILAAAISQFVGEN-VQIVILGTGKkamekQIQQLETKYPEKAIGITKFNVPLAhKIIAGADFML 192
Cdd:cd03814  199 PLLLYVGRLAPEKNLEALLDADLPLAASPpVRLVVVGDGP-----ARAELEARGPDVIFTGFLTGEELA-RAYASADVFV 272

                         90
                 ....*....|...
gi 380779697 193 IPSRFEPCGLIQL 205
Cdd:cd03814  273 FPSRTETFGLVVL 285
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 16-162 1.31e-03

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: 38.84  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  16 RKINWMKAGILESDRV-VTVSPyyaqelvsGVKKgVELDNIIRKTGIAGIVNGMDVQEWNPSTDKyidvkydsttvldak 94
Cdd:cd03807  121 RLVRKLCLLLSKFSPAtVANSS--------AVAE-FHQEQGYAKNKIVVIYNGIDLFKLSPDDAS--------------- 176

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 380779697  95 pvlKEALQAEVGLPVDGniPVIGFIGRLEEQKGSDILAAAISQFVGENVQIVILGTGKKAMEKQIQQL 162
Cdd:cd03807  177 ---RARARRRLGLAEDR--RVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERL 239
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 81-202 1.67e-03

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: 38.49  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697  81 IDVKYDSTTVLDAKPVLKEALQAEVGLPvdGNIPVIGFIGRLEEQKGSDILAAAISQFVGE-NVQIVILGTG--KKAMEK 157
Cdd:cd03819  152 IRVIPNGVDTDRFPPEAEAEERAQLGLP--EGKPVVGYVGRLSPEKGWLLLVDAAAELKDEpDFRLLVAGDGpeRDEIRR 229

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 380779697 158 QIQQLETkypEKAIGITKFNVPLAHkIIAGADFMLIPSRFEPCGL 202
Cdd:cd03819  230 LVERLGL---RDRVTFTGFREDVPA-ALAASDVVVLPSLHEEFGR 270
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 111-202 3.84e-03

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: 37.35  E-value: 3.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697 111 GNIPVIGFIGRLEEQKGSDIL--AAAISQFVGENVQIVILGTGKKAMEKQIQQLETKYPEKAIGITKFNVPLAHKII-AG 187
Cdd:cd03821  202 EDRRIILFLGRIHPKKGLDLLirAARKLAEQGRDWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALyAS 281

                         90
                 ....*....|....*
gi 380779697 188 ADFMLIPSRFEPCGL 202
Cdd:cd03821  282 ADLFVLPSYSENFGN 296
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 108-201 4.23e-03

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: 37.43  E-value: 4.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 380779697 108 PVDGNIPVIGFIGRLEEQKGSDILAAAISQFVGENVQ--IVILGTGkkAMEKQIQQLetkypEKAIGITKFNVPLAHKII 185
Cdd:cd05844  184 DPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTarLVIAGDG--PLRPALQAL-----AAALGRVRFLGALPHAEV 256

                         90       100
                 ....*....|....*....|
gi 380779697 186 A----GADFMLIPSRFEPCG 201
Cdd:cd05844  257 QdwmrRAEIFCLPSVTAASG 276
 
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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