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Conserved domains on  [gi|489075231|ref|WP_002985181|]
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DUF1972 domain-containing protein [Streptococcus pyogenes]

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 ...
 3-381 0e+00

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 cd04955:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 379  Bit Score: 560.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231   3 DVFIIGSRGLPAKYGGFETFVEELISHQSSKNIRYHVACLSDTKHKVHFDYKGADCFYLNPPKLGPARVIAYDMMAITYA 82
Cdd:cd04955    1 HIFIIGSRGLPAKYGGFETFVEKLTERQQSDNIKYHVACLSENSKQQHFEYNGADCFYVKVPKIGPARAIAYDIAALNYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231  83 LSYSDQHQIQNPIFYVLGNTVGAFIAPFVKQIHNRGGRFFINPDGLEWKRSKWSKPVQAYLKFSEKQMTRQADLVISDNI 162
Cdd:cd04955   81 LKYIKEQNIKNPIFYILACRIGPFIAPYIKKIHKLGGKLFVNPDGLEWKRAKWSLPVRKYWKFSESLMVKHADLLICDSK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 163 GIDRYLKQVYPWSKTCFIAYGTQTQPSRLTTADSKVRAYFQTFDIREKDYYLILGRFVPENNYETAIKEFMASSTKRDLV 242
Cdd:cd04955  161 NIEKYIRKEYGKSNTTFIAYGTDTLKSSLSDEDEKVREWYKEKGVKPGKYYLIVGRFVPENNYETMIREFMKSSTKRDLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 243 IICNHEGNAYFKQLLAETECDKDPRIKFVGTLYDKELLAYIREQAYAYIHGHEVGGTNPGLLEALAHTNLNLVLGVDFNQ 322
Cdd:cd04955  241 IITNVEGNAYYELLLKKTAFDHDERIKFVGTVYDQELLKYIRENAFAYLHGHEVGGTNPSLLEALGSTDLNLLLDVGFNR 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489075231 323 SVAKSAALYWTKQKgqLAELINQVDAGFDSD--RLGKEAKAIIQEHYTWEKIVGEYEALFL 381
Cdd:cd04955  321 EVAEDAALYWKKEP--LASLIDEVDNLNPDEisDLGKKAKQRIEEAYTWEKIVDEYEELFL 379
 
Name Accession Description Interval E-value
GT4-like cd04955
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 3-381 0e+00

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


Pssm-ID: 340858 [Multi-domain]  Cd Length: 379  Bit Score: 560.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231   3 DVFIIGSRGLPAKYGGFETFVEELISHQSSKNIRYHVACLSDTKHKVHFDYKGADCFYLNPPKLGPARVIAYDMMAITYA 82
Cdd:cd04955    1 HIFIIGSRGLPAKYGGFETFVEKLTERQQSDNIKYHVACLSENSKQQHFEYNGADCFYVKVPKIGPARAIAYDIAALNYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231  83 LSYSDQHQIQNPIFYVLGNTVGAFIAPFVKQIHNRGGRFFINPDGLEWKRSKWSKPVQAYLKFSEKQMTRQADLVISDNI 162
Cdd:cd04955   81 LKYIKEQNIKNPIFYILACRIGPFIAPYIKKIHKLGGKLFVNPDGLEWKRAKWSLPVRKYWKFSESLMVKHADLLICDSK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 163 GIDRYLKQVYPWSKTCFIAYGTQTQPSRLTTADSKVRAYFQTFDIREKDYYLILGRFVPENNYETAIKEFMASSTKRDLV 242
Cdd:cd04955  161 NIEKYIRKEYGKSNTTFIAYGTDTLKSSLSDEDEKVREWYKEKGVKPGKYYLIVGRFVPENNYETMIREFMKSSTKRDLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 243 IICNHEGNAYFKQLLAETECDKDPRIKFVGTLYDKELLAYIREQAYAYIHGHEVGGTNPGLLEALAHTNLNLVLGVDFNQ 322
Cdd:cd04955  241 IITNVEGNAYYELLLKKTAFDHDERIKFVGTVYDQELLKYIRENAFAYLHGHEVGGTNPSLLEALGSTDLNLLLDVGFNR 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489075231 323 SVAKSAALYWTKQKgqLAELINQVDAGFDSD--RLGKEAKAIIQEHYTWEKIVGEYEALFL 381
Cdd:cd04955  321 EVAEDAALYWKKEP--LASLIDEVDNLNPDEisDLGKKAKQRIEEAYTWEKIVDEYEELFL 379
DUF1972 pfam09314
Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized ...
 1-185 6.24e-109

Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized domains are found in bacterial glycosyltransferases and rhamnosyltransferases.


Pssm-ID: 430520  Cd Length: 186  Bit Score: 317.12  E-value: 6.24e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231    1 MQDVFIIGSRGLPAKYGGFETFVEELISHQSSKNIRYHVACLSDTKHKV-HFDYKGADCFYLNPPKLGPARVIAYDMMAI 79
Cdd:pfam09314   1 MQHVFIIGSRGLPAKYGGFETFVEKLTEYQKNKSIKYHVACLSENSAKSeHFEYNGADCFTIKVPKIGPARVIAYDIMAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231   80 TYALSYSDQHQIQNPIFYVLGNTVGAFIAPFVKQIHNRGGRFFINPDGLEWKRSKWSKPVQAYLKFSEKQMTRQADLVIS 159
Cdd:pfam09314  81 NYALKYIKDHNIKEPIFYILGNTIGPFIAHFARKIHKLGGKLYVNPDGLEWKRAKWSAPVRQYLKFSEKLMTKYADLLIS 160

                         170       180
                  ....*....|....*....|....*.
gi 489075231  160 DNIGIDRYLKQVYPWSKTCFIAYGTQ 185
Cdd:pfam09314 161 DNKGIEKYIHDEYGNPKTTYIAYGTE 186
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 281-380 2.78e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 40.36  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 281 AYIReQAYAYIHGHEVGGTNPGLLEALAHTNLNLVLGVDFNQSV---AKSAALYWTKQKGQLAELINQVDAGFDS-DRLG 356
Cdd:COG0438   16 ALLA-AADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEViedGETGLLVPPGDPEALAEAILRLLEDPELrRRLG 94

                         90       100
                 ....*....|....*....|....
gi 489075231 357 KEAKAIIQEHYTWEKIVGEYEALF 380
Cdd:COG0438   95 EAARERAEERFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
GT4-like cd04955
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 3-381 0e+00

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


Pssm-ID: 340858 [Multi-domain]  Cd Length: 379  Bit Score: 560.97  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231   3 DVFIIGSRGLPAKYGGFETFVEELISHQSSKNIRYHVACLSDTKHKVHFDYKGADCFYLNPPKLGPARVIAYDMMAITYA 82
Cdd:cd04955    1 HIFIIGSRGLPAKYGGFETFVEKLTERQQSDNIKYHVACLSENSKQQHFEYNGADCFYVKVPKIGPARAIAYDIAALNYA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231  83 LSYSDQHQIQNPIFYVLGNTVGAFIAPFVKQIHNRGGRFFINPDGLEWKRSKWSKPVQAYLKFSEKQMTRQADLVISDNI 162
Cdd:cd04955   81 LKYIKEQNIKNPIFYILACRIGPFIAPYIKKIHKLGGKLFVNPDGLEWKRAKWSLPVRKYWKFSESLMVKHADLLICDSK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 163 GIDRYLKQVYPWSKTCFIAYGTQTQPSRLTTADSKVRAYFQTFDIREKDYYLILGRFVPENNYETAIKEFMASSTKRDLV 242
Cdd:cd04955  161 NIEKYIRKEYGKSNTTFIAYGTDTLKSSLSDEDEKVREWYKEKGVKPGKYYLIVGRFVPENNYETMIREFMKSSTKRDLV 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 243 IICNHEGNAYFKQLLAETECDKDPRIKFVGTLYDKELLAYIREQAYAYIHGHEVGGTNPGLLEALAHTNLNLVLGVDFNQ 322
Cdd:cd04955  241 IITNVEGNAYYELLLKKTAFDHDERIKFVGTVYDQELLKYIRENAFAYLHGHEVGGTNPSLLEALGSTDLNLLLDVGFNR 320

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489075231 323 SVAKSAALYWTKQKgqLAELINQVDAGFDSD--RLGKEAKAIIQEHYTWEKIVGEYEALFL 381
Cdd:cd04955  321 EVAEDAALYWKKEP--LASLIDEVDNLNPDEisDLGKKAKQRIEEAYTWEKIVDEYEELFL 379
DUF1972 pfam09314
Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized ...
 1-185 6.24e-109

Domain of unknown function (DUF1972); Members of this family of functionally uncharacterized domains are found in bacterial glycosyltransferases and rhamnosyltransferases.


Pssm-ID: 430520  Cd Length: 186  Bit Score: 317.12  E-value: 6.24e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231    1 MQDVFIIGSRGLPAKYGGFETFVEELISHQSSKNIRYHVACLSDTKHKV-HFDYKGADCFYLNPPKLGPARVIAYDMMAI 79
Cdd:pfam09314   1 MQHVFIIGSRGLPAKYGGFETFVEKLTEYQKNKSIKYHVACLSENSAKSeHFEYNGADCFTIKVPKIGPARVIAYDIMAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231   80 TYALSYSDQHQIQNPIFYVLGNTVGAFIAPFVKQIHNRGGRFFINPDGLEWKRSKWSKPVQAYLKFSEKQMTRQADLVIS 159
Cdd:pfam09314  81 NYALKYIKDHNIKEPIFYILGNTIGPFIAHFARKIHKLGGKLYVNPDGLEWKRAKWSAPVRQYLKFSEKLMTKYADLLIS 160

                         170       180
                  ....*....|....*....|....*.
gi 489075231  160 DNIGIDRYLKQVYPWSKTCFIAYGTQ 185
Cdd:pfam09314 161 DNKGIEKYIHDEYGNPKTTYIAYGTE 186
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 9-380 1.25e-12

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: 68.33  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231   9 SRGLPAKYGGFETFVEELISHQSSKNIRYHVACLSDTKHKVHFDYKGADCFYLNPPKLGPA--RVIAYdmMAITYALSYS 86
Cdd:cd03801    6 SPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRarRLLRE--LRPLLRLRKF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231  87 DQHQIQNPIFYVLGNTVGAFI-APFVKQIHnrgGRFFINPDGLEWKRSKWskpVQAYLkfsekQMTRQADLVI--SDNIG 163
Cdd:cd03801   84 DVVHAHGLLAALLAALLALLLgAPLVVTLH---GAEPGRLLLLLAAERRL---LARAE-----ALLRRADAVIavSEALR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 164 idRYLKQVY--PWSKTCFIAYGTQTQPSRlttadskvRAYFQTFDIREKDYYLI-LGRFVPENNYETAIkEFMASSTKRD 240
Cdd:cd03801  153 --DELRALGgiPPEKIVVIPNGVDLERFS--------PPLRRKLGIPPDRPVLLfVGRLSPRKGVDLLL-EALAKLLRRG 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 241 ---LVIICNHEGnAYFKQLlAETECDKDPRIKFVGTLYDKELLAYIReQAYAYIHG--HE----------------VGGT 299
Cdd:cd03801  222 pdvRLVIVGGDG-PLRAEL-EELELGLGDRVRFLGFVPDEELPALYA-AADVFVLPsrYEgfglvvleamaaglpvVATD 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 300 NPGLLEALAHTNLNLVLGVDFNQSVAKsaalywtkqkgQLAELINQVDAgfdSDRLGKEAKAIIQEHYTWEKIVGEYEAL 379
Cdd:cd03801  299 VGGLPEVVEDGEGGLVVPPDDVEALAD-----------ALLRLLADPEL---RARLGRAARERVAERFSWERVAERLLDL 364


                 .
gi 489075231 380 F 380
Cdd:cd03801  365 Y 365
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 188-309 2.30e-04

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: 42.39  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 188 PSRLTTADSKVRAYFQTFDIREKDYYLILGRFVPENNYETAIKEFMASSTKRD---LVIICNHEGNAYFKQLLAETecDK 264
Cdd:cd01635   88 PDSLESTRSELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEALALLKARLPdlvLVLVGGGGEREEEEALAAAL--GL 165

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489075231 265 DPRIKFVGTLYDKELLAYIREQAYAYIHGHEVGGTNPGLLEALAH 309
Cdd:cd01635  166 LERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAA 210
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 281-380 2.78e-04

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 40.36  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 281 AYIReQAYAYIHGHEVGGTNPGLLEALAHTNLNLVLGVDFNQSV---AKSAALYWTKQKGQLAELINQVDAGFDS-DRLG 356
Cdd:COG0438   16 ALLA-AADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEViedGETGLLVPPGDPEALAEAILRLLEDPELrRRLG 94

                         90       100
                 ....*....|....*....|....
gi 489075231 357 KEAKAIIQEHYTWEKIVGEYEALF 380
Cdd:COG0438   95 EAARERAEERFSWEAIAERLLALY 118
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 209-308 3.14e-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: 40.72  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231  209 EKDYYLILGRFVPENNYETAIKEFmASSTKRD----LVIICNHEGNAYFKqLLAEtECDKDPRIKFVGTLYDKELLAYIR 284
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAF-ALLKEKNpnlkLVIAGDGEEEKRLK-KLAE-KLGLGDNVIFLGFVSDEDLPELLK 77

                          90       100
                  ....*....|....*....|....*.
gi 489075231  285 eQAYAYIHG--HEVGGTNpgLLEALA 308
Cdd:pfam00534  78 -IADVFVLPsrYEGFGIV--LLEAMA 100
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 211-308 8.52e-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: 38.03  E-value: 8.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489075231 211 DYYLILGRFVPENNYETAIKEFmaSSTKRDLVIICNHEGNAYFKQLLAetecdkdPRIKFVGTLYDKELLAYIREqAYAY 290
Cdd:cd03804  200 DYYLTASRLVPYKRIDLAVEAF--NELPKRLVVIGDGPDLDRLRAMAS-------PNVEFLGYQPDEVLKELLSK-ARAF 269

                         90
                 ....*....|....*....
gi 489075231 291 IH-GHEVGGTNPglLEALA 308
Cdd:cd03804  270 VFaAEEDFGIVP--VEAQA 286
 
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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