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Conserved domains on  [gi|1243938503|ref|NP_001342425|]
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alpha-1,3/1,6-mannosyltransferase ALG2 isoform 2 [Mus musculus]

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 ...
67-334 2.70e-155

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 cd03805:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 392  Bit Score: 440.87  E-value: 2.70e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  67 PDLLLTQRNSALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHRNPDVLYPSLNIGSFDLAIPEKID-D 145
Cdd:cd03805   125 PDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPDPgD 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 146 LVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqEWDKVHLFMAGGYDDRIPENVEHYKELKKMVQE-SDLERHV 224
Cdd:cd03805   205 LIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLP--EFENVRLVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 225 TFLRSFSDRQKISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFI 304
Cdd:cd03805   283 LFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLA 362
                         250       260       270
                  ....*....|....*....|....*....|
gi 1243938503 305 HKPSLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03805   363 NDPDLADRMGAAGRKRVKEKFSREAFAERL 392
 
Name Accession Description Interval E-value
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
67-334 2.70e-155

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


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 440.87  E-value: 2.70e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  67 PDLLLTQRNSALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHRNPDVLYPSLNIGSFDLAIPEKID-D 145
Cdd:cd03805   125 PDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPDPgD 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 146 LVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqEWDKVHLFMAGGYDDRIPENVEHYKELKKMVQE-SDLERHV 224
Cdd:cd03805   205 LIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLP--EFENVRLVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 225 TFLRSFSDRQKISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFI 304
Cdd:cd03805   283 LFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLA 362
                         250       260       270
                  ....*....|....*....|....*....|
gi 1243938503 305 HKPSLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03805   363 NDPDLADRMGAAGRKRVKEKFSREAFAERL 392
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
151-320 8.62e-32

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: 116.60  E-value: 8.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 151 KQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLRSF 230
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNP-----NLKLVIAGDGEEE--------KRLKKLAEKLGLGDNVIFLGFV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 231 SDRQKISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSL 309
Cdd:pfam00534  68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEEL 147
                         170
                  ....*....|.
gi 1243938503 310 KATMGLAGKAR 320
Cdd:pfam00534 148 RERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
238-342 3.62e-23

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 92.75  E-value: 3.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 238 LLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLA 316
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*.
gi 1243938503 317 GKARVAEKFSADAFADQLYQYVTKLV 342
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
150-336 6.26e-15

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 74.76  E-value: 6.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 150 GKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLrs 229
Cdd:TIGR03088 192 DESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGA-ERLRLVIVGDGPAR--------GACEQMVRAAGLAHLVWLP-- 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 230 fSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKP 307
Cdd:TIGR03088 261 -GERDDVPALMQALDLFVLPSlAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPgDAVALARALQPYVSDP 339
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1243938503 308 SLKATMGLAGKARVAEKFSADAFADQ---LYQ 336
Cdd:TIGR03088 340 AARRAHGAAGRARAEQQFSINAMVAAyagLYD 371
PLN02949 PLN02949
transferase, transferring glycosyl groups
76-342 9.76e-13

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 68.61  E-value: 9.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  76 SALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHrnPDVLYPSLNIGSFDlAIPEKIDDLVPKgkqflF 155
Cdd:PLN02949  200 STCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPER--IKRVYPPCDTSGLQ-ALPLERSEDPPY-----I 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 156 LSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYddRIPENVEHYKELKKMVQESDLERHVTFLRSFSDRQK 235
Cdd:PLN02949  272 ISVAQFRPEKAHALQLEAFALALEKLDADV-PRPKLQFVGSC--RNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDL 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 236 ISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIV-----HKvTGFLCEPDPvHFSEAMEKFIHKPSlK 310
Cdd:PLN02949  349 VRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVldedgQQ-TGFLATTVE-EYADAILEVLRMRE-T 425
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1243938503 311 ATMGLAGKARV-AEKFSADAFADQLYQYVTKLV 342
Cdd:PLN02949  426 ERLEIAAAARKrANRFSEQRFNEDFKDAIRPIL 458
 
Name Accession Description Interval E-value
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
67-334 2.70e-155

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


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 440.87  E-value: 2.70e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  67 PDLLLTQRNSALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHRNPDVLYPSLNIGSFDLAIPEKID-D 145
Cdd:cd03805   125 PDQLLAQRKSLLKRLYRKPFDWLEEFTTGMADQIVVNSNFTAGVFKKTFPSLAKNPPEVLYPCVDTDSFDSTSEDPDPgD 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 146 LVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqEWDKVHLFMAGGYDDRIPENVEHYKELKKMVQE-SDLERHV 224
Cdd:cd03805   205 LIAKSNKKFFLSINRFERKKNIALAIEAFAKLKQKLP--EFENVRLVIAGGYDPRVAENVEYLEELQRLAEElLNVEDQV 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 225 TFLRSFSDRQKISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFI 304
Cdd:cd03805   283 LFLRSISDSQKEQLLSSALALLYTPSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEPTPEAFAEAMLKLA 362
                         250       260       270
                  ....*....|....*....|....*....|
gi 1243938503 305 HKPSLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03805   363 NDPDLADRMGAAGRKRVKEKFSREAFAERL 392
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
91-336 2.26e-33

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: 126.50  E-value: 2.26e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  91 EYTTGMADRILVNSQYTASVFKETFKTLSHRnPDVLYPSLNIGSFDLAIPEKIDdlvPKGKQFLFLSINRYERKKNLPLA 170
Cdd:cd03801   135 EALLRRADAVIAVSEALRDELRALGGIPPEK-IVVIPNGVDLERFSPPLRRKLG---IPPDRPVLLFVGRLSPRKGVDLL 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 171 LRSLVQLRNRLPsqewdKVHLFMAGGYDdripenvEHYKELKKMvqESDLERHVTFLRSFSDRQKISLLHGCLCVLYTPS 250
Cdd:cd03801   211 LEALAKLLRRGP-----DVRLVIVGGDG-------PLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAADVFVLPSR 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 251 NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVH-FSEAMEKFIHKPSLKATMGLAGKARVAEKFSADA 329
Cdd:cd03801   277 YEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEaLADALLRLLADPELRARLGRAARERVAERFSWER 356

                  ....*..
gi 1243938503 330 FADQLYQ 336
Cdd:cd03801   357 VAERLLD 363
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
151-320 8.62e-32

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: 116.60  E-value: 8.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 151 KQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLRSF 230
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNP-----NLKLVIAGDGEEE--------KRLKKLAEKLGLGDNVIFLGFV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 231 SDRQKISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSL 309
Cdd:pfam00534  68 SDEDLPELLKIADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPnNAEALAEAIDKLLEDEEL 147
                         170
                  ....*....|.
gi 1243938503 310 KATMGLAGKAR 320
Cdd:pfam00534 148 RERLGENARKR 158
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
76-333 3.38e-28

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 113.47  E-value: 3.38e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  76 SALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKtlSHRNPDVLYPSLNIGSFdLAIPEKiddlvPKGKQFLF 155
Cdd:cd03806   169 SIAKLLYYRLFAFLYGLAGSFADVVMVNSTWTYNHIRQLWK--RNIKPSIVYPPCDTEEL-TKLPID-----EKTRENQI 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 156 LSINRYERKKNLPLALRSLVQLRNRLPSQEWDKVHLFMAGGY---DDRipENVEhykELKKMVQESDLERHVTFLRSFSD 232
Cdd:cd03806   241 LSIAQFRPEKNHPLQLRAFAELLKRLPESIRSNPKLVLIGSCrneEDK--ERVE---ALKLLAKELILEDSVEFVVDAPY 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 233 RQKISLLHGCLCVLYTPSNEHFGIVPLEamYMQCPVIAV--NNGGPLESIV----HKVTGFLCEpDPVHFSEAMEKFIHK 306
Cdd:cd03806   316 EELKELLSTASIGLHTMWNEHFGIGVVE--YMAAGLIPLahASAGPLLDIVvpwdGGPTGFLAS-TPEEYAEAIEKILTL 392
                         250       260
                  ....*....|....*....|....*..
gi 1243938503 307 PSLKATMGLAGKARVAEKFSADAFADQ 333
Cdd:cd03806   393 SEEERLQRREAARSSAERFSDEEFERD 419
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
75-334 1.92e-26

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: 107.68  E-value: 1.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  75 NSALKKFYRapidWIEEYTTGMADRILVNSQYTASVFKEtfKTLSHRNPDVLYPslNIGsFDLAIPEKIDDLVPKGKqFL 154
Cdd:cd03808   122 GKLLRLLYL----LLEKLALLFTDKVIFVNEDDRDLAIK--KGIIKKKKTVLIP--GSG-VDLDRFQYSPESLPSEK-VV 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 155 FLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRIPenvehykeLKKMVQESDLERHVTFLRSFSD-R 233
Cdd:cd03808   192 FLFVARLLKDKGIDELIEAAKILKKKGP-----NVRFLLVGDGELENP--------SEILIEKLGLEGRIEFLGFRSDvP 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 234 QKISLLHgcLCVLytPSN-EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKA 311
Cdd:cd03808   259 ELLAESD--VFVL--PSYrEGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPgDVEALADAIEKLIEDPELRK 334
                         250       260
                  ....*....|....*....|...
gi 1243938503 312 TMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03808   335 EMGEAARKRVEEKFDEEKVVNKL 357
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
238-342 3.62e-23

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 92.75  E-value: 3.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 238 LLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLA 316
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPgDPEALAEAILRLLEDPELRRRLGEA 96
                          90       100
                  ....*....|....*....|....*.
gi 1243938503 317 GKARVAEKFSADAFADQLYQYVTKLV 342
Cdd:COG0438    97 ARERAEERFSWEAIAERLLALYEELL 122
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
97-334 3.47e-22

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: 95.89  E-value: 3.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  97 ADRILVNSQYTASVFKETFKtLSHRNPDVLYPSLNIgSFDLAIPEKIDDLVPKGKQFLFLSINRYERKKNLPLALRSLVQ 176
Cdd:cd03809   139 ADAIITVSEATRDDIIKFYG-VPPEKIVVIPLGVDP-SFFPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFAL 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 177 LRNRLPsqewdKVHLFMAGGYDDRipenvehYKELKKMVQESDLERHVTFLRSFSDRQKISLLHGCLCVLYtPS-NEHFG 255
Cdd:cd03809   217 LKKQGG-----DLKLVIVGGKGWE-------DEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVF-PSlYEGFG 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 256 IVPLEAMYMQCPVIAVNNGgplesiVHK-VTG---FLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARvAEKFSADAF 330
Cdd:cd03809   284 LPVLEAMACGTPVIASNIS------VLPeVAGdaaLYFDPlDPESIADAILRLLEDPSLREELIRKGLER-AKKFSWEKT 356

                  ....
gi 1243938503 331 ADQL 334
Cdd:cd03809   357 AEKT 360
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
74-331 1.88e-21

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: 93.49  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  74 RNSALKKFYRAPIDWieeyTTGMADRILVnsqyTASVFKETFKTL-SHRNPDVLYP-SLNIGSFDLAI--PEKIDDLVPK 149
Cdd:cd03795   119 KQKKLLKLYKPLMTR----FLRRADRIIA----TSPNYVETSPTLrEFKNKVRVIPlGIDKNVYNIPRvdFENIKREKKG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 150 GKQFLFLSINRYerKKNLPLALRSLVQLrnrlpsqewdKVHLFMAGgyddripENVEhYKELKKMVQESDLERhVTFLRS 229
Cdd:cd03795   191 KKIFLFIGRLVY--YKGLDYLIEAAQYL----------NYPIVIGG-------EGPL-KPDLEAQIELNLLDN-VKFLGR 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 230 FSDRQKISLLHGCLCVLYtPS---NEHFGIVPLEAMYMQCPVIAVNNGGPLESIV-HKVTGFLCEP-DPVHFSEAMEKFI 304
Cdd:cd03795   250 VDDEEKVIYLHLCDVFVF-PSvlrSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNnNGETGLVVPPkDPDALAEAIDKLL 328
                         250       260
                  ....*....|....*....|....*..
gi 1243938503 305 HKPSLKATMGLAGKARVAEKFSADAFA 331
Cdd:cd03795   329 SDEELRESYGENAKKRFEELFTAEKMK 355
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
148-334 3.19e-21

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: 93.46  E-value: 3.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 148 PKGKQFLFLSinRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRIPENVEhyKELKKMVQESDLERHVTFL 227
Cdd:cd03800   218 PDKPVVLALG--RLDPRKGIDTLVRAFAQLPELRE-----LANLVLVGGPSDDPLSMDR--EELAELAEELGLIDRVRFP 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 228 rSFSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIH 305
Cdd:cd03800   289 -GRVSRDDLPELYRAADVFVVPSlYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPhDPEALAAALRRLLD 367
                         170       180
                  ....*....|....*....|....*....
gi 1243938503 306 KPSLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03800   368 DPALWQRLSRAGLERARAHYTWESVADQL 396
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
139-338 3.84e-20

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: 90.03  E-value: 3.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 139 IPEKIDDLVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdkVHLFMAGGYDDRipenvehyKELKKMVQES 218
Cdd:cd03817   188 NTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEPN------IKLVIVGDGPER--------EELKELAREL 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 219 DLERHVTFLrSFSDRQKISLLHGCLCVLYTPSN-EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFS 297
Cdd:cd03817   254 GLADKVIFT-GFVPREELPEYYKAADLFVFASTtETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLA 332
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1243938503 298 EAMEKFIHKPSLKATMGLAGKARvAEKFSADAFADQLYQYV 338
Cdd:cd03817   333 EKLLHLRENLELLRKLSKNAEIS-AREFAFAKSVEKLYEEV 372
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
148-338 1.46e-19

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


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 87.73  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 148 PKGKQFLFLSinRYERKKNLPLALRSLVQLrnrlpsqewdKVHLFMAGGYDDRipenvEHYKELkkmvQESDLERHVTFL 227
Cdd:cd03802   167 DPEDYLAFLG--RIAPEKGLEDAIRVARRA----------GLPLKIAGKVRDE-----DYFYYL----QEPLPGPRIEFI 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 228 RSFSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPdpvhfSEAMEKFIHK 306
Cdd:cd03802   226 GEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLVDS-----VEEMAEAIAN 300
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1243938503 307 -PSLKatmGLAGKARVAEKFSADAFADQ---LYQYV 338
Cdd:cd03802   301 iDRID---RAACRRYAEDRFSAARMADRyeaLYRKV 333
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
68-336 3.26e-17

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: 81.66  E-value: 3.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  68 DLLLTQRNSALKKFYRapidwieeYTTGMADRILVNSQYTASVFKETFktLSHRNPDVLYpslNigSFDLAIPEKIDD-L 146
Cdd:cd03798   130 DINVFPPRSLLRKLLR--------WALRRAARVIAVSKALAEELVALG--VPRDRVDVIP---N--GVDPARFQPEDRgL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 147 VPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSqewdkVHLFMAGGYDDRIPenvehykeLKKMVQESDLERHVTF 226
Cdd:cd03798   195 GLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPD-----VVLLIVGDGPLREA--------LRALAEDLGLGDRVTF 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 227 LRSFSdRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFI 304
Cdd:cd03798   262 TGRLP-HEQVPAYYRACDVFVLPSrHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPgDADALAAALRRAL 340
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1243938503 305 HKPsLKATMGLAGKARVAEKFSADAFADQLYQ 336
Cdd:cd03798   341 AEP-YLRELGEAARARVAERFSWVKAADRIAA 371
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
97-333 1.86e-16

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: 79.20  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  97 ADRILVNSQYTasvfKETFKTLSHRNPDVLYpslNIGSFDLaiPEKIDDLvpkgKQFLFLSINRYERKKNLPLALRSLVQ 176
Cdd:cd03820   139 ADKIVVLTEAD----KLKKYKQPNSNVVVIP---NPLSFPS--EEPSTNL----KSKRILAVGRLTYQKGFDLLIEAWAL 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 177 LRNRLPsqEWDkvhLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLRSFSDRQKISLLHGCLCVlyTPSNEHFGI 256
Cdd:cd03820   206 IAKKHP--DWK---LRIYGDGPER--------EELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVL--SSRYEGFPM 270
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243938503 257 VPLEAMYMQCPVIAVN-NGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARvAEKFSADAFADQ 333
Cdd:cd03820   271 VLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNgDVDALAEALLRLMEDEELRKKMGKNARKN-AERFSIEKIIKQ 348
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
158-342 2.08e-15

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: 76.24  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 158 INRYERKKNLPLALRSLVQLRNRLPSQewdkvhLFMAGGYDDRIPenvehykeLKKMVQESDLERHVTFLRSFSDRQKIs 237
Cdd:cd04962   202 VSNFRPVKRIDDVVRVFARVRRKIPAK------LLLVGDGPERVP--------AEELARELGVEDRVLFLGKQDDVEEL- 266
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 238 lLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVH-FSEAMEKFIHKPSLKATMGLA 316
Cdd:cd04962   267 -LSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDaMAKSALSILEDDELYNRMGRA 345
                         170       180
                  ....*....|....*....|....*.
gi 1243938503 317 GKARVAEKFSADAFADQlYQYVTKLV 342
Cdd:cd04962   346 ARKRAAERFDPERIVPQ-YEAYYRRL 370
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
150-336 6.26e-15

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 74.76  E-value: 6.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 150 GKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLrs 229
Cdd:TIGR03088 192 DESVVVGTVGRLQAVKDQPTLVRAFALLVRQLPEGA-ERLRLVIVGDGPAR--------GACEQMVRAAGLAHLVWLP-- 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 230 fSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKP 307
Cdd:TIGR03088 261 -GERDDVPALMQALDLFVLPSlAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPgDAVALARALQPYVSDP 339
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1243938503 308 SLKATMGLAGKARVAEKFSADAFADQ---LYQ 336
Cdd:TIGR03088 340 AARRAHGAAGRARAEQQFSINAMVAAyagLYD 371
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
98-330 9.02e-15

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: 74.24  E-value: 9.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  98 DRILVNSQYTASVFKETFktlsHRNPDVLYPSLNIGSFDLAiPEKIDDlvpkgkqflFLSINRYERKKNLPLALRSLvql 177
Cdd:cd03804   159 DLFIANSQFVARRIKKFY----GRESTVIYPPVDTDAFAPA-ADKEDY---------YLTASRLVPYKRIDLAVEAF--- 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 178 rNRLPSQewdkvhLFMAGGYDDRipenvehyKELKKMVQesdleRHVTFLRSFSDRQKISLLHGCLCVLYtPSNEHFGIV 257
Cdd:cd03804   222 -NELPKR------LVVIGDGPDL--------DRLRAMAS-----PNVEFLGYQPDEVLKELLSKARAFVF-AAEEDFGIV 280
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938503 258 PLEAMYMQCPVIAVNNGGPLESIVHKVTGFL-CEPDPVHFSEAMEKFIHKPSL---KATMglagkaRVAEKFSADAF 330
Cdd:cd03804   281 PVEAQACGTPVIAFGKGGALETVRPGPTGILfGEQTVESLKAAVEEFEQNFDRfkpQAIR------ANAERFSRARF 351
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
150-305 1.77e-14

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 69.46  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 150 GKQFLFLSiNRYERKKNLPLALRSLVQLRNRLpsqewDKVHLFMAGGYDDRipenvehykELKKMVQesDLERHVTFLRS 229
Cdd:pfam13692   1 RPVILFVG-RLHPNVKGVDYLLEAVPLLRKRD-----NDVRLVIVGDGPEE---------ELEELAA--GLEDRVIFTGF 63
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1243938503 230 FSDrqKISLLHGC-LCVLytPSN-EHFGIVPLEAMYMQCPVIAVNNGGPLEsIVHKVTGFLCEP-DPVHFSEAMEKFIH 305
Cdd:pfam13692  64 VED--LAELLAAAdVFVL--PSLyEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPgDPEALAEAILRLLE 137
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
155-289 2.92e-14

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


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 71.28  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 155 FLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLRSFSDRQ 234
Cdd:cd01635   113 KVSVGRLVPEKGIDLLLEALALLKARLP-----DLVLVLVGGGGER--------EEEEALAAALGLLERVVIIGGLVDDE 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1243938503 235 KISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLC 289
Cdd:cd01635   180 VLELLLAAADVFVLPSrSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
122-335 4.23e-14

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: 72.35  E-value: 4.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 122 NPDVLYPSLN-IGSFDLAIPEKIDD-----LVPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAG 195
Cdd:cd03807   154 AKNKIVVIYNgIDLFKLSPDDASRArarrrLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHP-----DLRLLLVG 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 196 GYDDRipenvehyKELKKMVQESDLERHVTFLrsfSDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNG 274
Cdd:cd03807   229 RGPER--------PNLERLLLELGLEDRVHLL---GERSDVPALLPAMDIFVLSSrTEGFPNALLEAMACGLPVVATDVG 297
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938503 275 GPLEsIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFA---DQLY 335
Cdd:cd03807   298 GAAE-LVDDGTGFLVPAgDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVrryETLY 361
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
154-337 5.62e-14

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: 71.94  E-value: 5.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 154 LFLSINRYERKKNLPlALRSLVQlrnRLPSQewDKVHLFMAGGYDDRipenvehykelkkmvqeSDLER---HVTFLRsF 230
Cdd:cd03814   200 LLLYVGRLAPEKNLE-ALLDADL---PLAAS--PPVRLVVVGDGPAR-----------------AELEArgpDVIFTG-F 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 231 SDRQKISLLHGCLCVLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPS 308
Cdd:cd03814   256 LTGEELARAYASADVFVFPSrTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPgDAAAFAAALRALLEDPE 335
                         170       180
                  ....*....|....*....|....*....
gi 1243938503 309 LKATMGLAGKARvAEKFSADAFADQLYQY 337
Cdd:cd03814   336 LRRRMAARARAE-AERYSWEAFLDNLLDY 363
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
67-334 5.84e-14

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


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 71.99  E-value: 5.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  67 PDLLLTQRNSALKKFYRApIDWIEEYTTGMADRILVNSQYTASVFKEtfKTLSHRNPDVLYPSLNIGSFDLAIPEKIDDL 146
Cdd:cd03794   135 PESLIALGVLKKGSLLKL-LKKLERKLYRLADAIIVLSPGLKEYLLR--KGVPKEKIIVIPNWADLEEFKPPPKDELRKK 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 147 VPKGKQFLFLSINryerkkNLPLA--LRSLVQLRNRLPSQewDKVHLFMAGGYDDRipenvehyKELKKMVQESDLERhV 224
Cdd:cd03794   212 LGLDDKFVVVYAG------NIGKAqgLETLLEAAERLKRR--PDIRFLFVGDGDEK--------ERLKELAKARGLDN-V 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 225 TFLRSFSDRQKISLLHGC--LCVLYTPSNEHFGIVP---LEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSE 298
Cdd:cd03794   275 TFLGRVPKEEVPELLSAAdvGLVPLKDNPANRGSSPsklFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPgDPEALAD 354
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1243938503 299 AMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03794   355 AILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
96-317 3.32e-13

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


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 69.69  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  96 MADRILVNSQYTASVFKETFKTLSHRnPDVLYPSLNIGSFDLAI-PEKIDDLVPKGKQFLFLSINRYERKKNLPLALRSL 174
Cdd:cd03819   126 RGDRVIAVSELVRDHLIEALGVDPER-IRVIPNGVDTDRFPPEAeAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAA 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 175 VQLRNRLPsqewdkVHLFMAGgyDDRIPENVEHYKElkkmvqESDLERHVTFLrSFSDRQKiSLLHGCLCVLYTPSNEHF 254
Cdd:cd03819   205 AELKDEPD------FRLLVAG--DGPERDEIRRLVE------RLGLRDRVTFT-GFREDVP-AALAASDVVVLPSLHEEF 268
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243938503 255 GIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAG 317
Cdd:cd03819   269 GRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPgDAEALADAIRAAKLLPEAREKLQAAA 332
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
72-312 9.51e-13

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: 68.15  E-value: 9.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  72 TQRNSALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHRNpDVLYpslNIGSFDLAIPE-KIDDLVPKG 150
Cdd:cd03811   111 WIHSSLSKLYYLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPEKI-EVIY---NPIDIDRIRALaKEPILNEPE 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 151 KQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLrsf 230
Cdd:cd03811   187 DGPVILAVGRLDPQKGHDLLIEAFAKLRKKYP-----DVKLVILGDGPLR--------EELEKLAKELGLAERVIFL--- 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 231 sDRQK--ISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFIHKPS 308
Cdd:cd03811   251 -GFQSnpYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGILAALLQKK 329

                  ....
gi 1243938503 309 LKAT 312
Cdd:cd03811   330 LDAA 333
PLN02949 PLN02949
transferase, transferring glycosyl groups
76-342 9.76e-13

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 68.61  E-value: 9.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  76 SALKKFYRAPIDWIEEYTTGMADRILVNSQYTASVFKETFKTLSHrnPDVLYPSLNIGSFDlAIPEKIDDLVPKgkqflF 155
Cdd:PLN02949  200 STCKILYYRAFAWMYGLVGRCAHLAMVNSSWTKSHIEALWRIPER--IKRVYPPCDTSGLQ-ALPLERSEDPPY-----I 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 156 LSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYddRIPENVEHYKELKKMVQESDLERHVTFLRSFSDRQK 235
Cdd:PLN02949  272 ISVAQFRPEKAHALQLEAFALALEKLDADV-PRPKLQFVGSC--RNKEDEERLQKLKDRAKELGLDGDVEFHKNVSYRDL 348
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 236 ISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIV-----HKvTGFLCEPDPvHFSEAMEKFIHKPSlK 310
Cdd:PLN02949  349 VRLLGGAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKMDIVldedgQQ-TGFLATTVE-EYADAILEVLRMRE-T 425
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1243938503 311 ATMGLAGKARV-AEKFSADAFADQLYQYVTKLV 342
Cdd:PLN02949  426 ERLEIAAAARKrANRFSEQRFNEDFKDAIRPIL 458
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
137-325 9.49e-12

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


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 65.42  E-value: 9.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 137 LAIPEKIDDLVPKGKQF--------------------LFLSINRYERKKNLPLALRSLVQLRNRLPSqewdkVHLFMAGG 196
Cdd:cd03792   162 FYIPPSIDPLSGKNKDLspadiryylekpfvidperpYILQVARFDPSKDPLGVIDAYKLFKRRAEE-----PQLVICGH 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 197 YDDRIPENVEHYKELKKMvqeSDLERHVTFLR-SFSDRQKISLLHGCLCVLYTPSNEHFGIVPLEAMYMQCPVIAVNNGG 275
Cdd:cd03792   237 GAVDDPEGSVVYEEVMEY---AGDDHDIHVLRlPPSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGG 313
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1243938503 276 PLESIVHKVTGFLC---EPDPVHFseamEKFIHKPSLKATMGLAGKARVAEKF 325
Cdd:cd03792   314 IPLQVIDGETGFLVnsvEGAAVRI----LRLLTDPELRRKMGLAAREHVRDNF 362
PLN00142 PLN00142
sucrose synthase
141-341 1.62e-11

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 65.39  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 141 EKIDDLVPKGKQFLFlSINRYERKKNLPlalrSLVQL--RN-RLPsqewDKVHLFMAGGYDDRIPEN-VEHYKELKKM-- 214
Cdd:PLN00142  563 EHIGYLKDRKKPIIF-SMARLDRVKNLT----GLVEWygKNkRLR----ELVNLVVVGGFIDPSKSKdREEIAEIKKMhs 633
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 215 -VQESDLERHVTFLRSFSDRQKISLLHGCLC---------VLYtpsnEHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKV 284
Cdd:PLN00142  634 lIEKYNLKGQFRWIAAQTNRVRNGELYRYIAdtkgafvqpALY----EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGV 709
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1243938503 285 TGFLCepDPVHFSEAMEK---FIHK----PSLKATMGLAGKARVAEKFSADAFADQL---------YQYVTKL 341
Cdd:PLN00142  710 SGFHI--DPYHGDEAANKiadFFEKckedPSYWNKISDAGLQRIYECYTWKIYAERLltlggvygfWKYVSKL 780
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
125-333 5.58e-11

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


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 63.51  E-value: 5.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 125 VLYPSLNIGSFDLAIPEKiddlvPKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGGYDdripEN 204
Cdd:cd03813   271 VIPNGIDIQRFAPAREER-----PEKEPPVVGLVGRVVPIKDVKTFIRAFKLVRRAMP-----DAEGWLIGPED----ED 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 205 VEHYKELKKMVQESDLERHVTFLrsfsDRQKIS--LLHGCLCVLyTPSNEHFGIVPLEAMYMQCPVIAVNNGGPLESIVH 282
Cdd:cd03813   337 PEYAQECKRLVASLGLENKVKFL----GFQNIKeyYPKLGLLVL-TSISEGQPLVILEAMASGVPVVATDVGSCRELIYG 411
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938503 283 KV-----TGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQ 333
Cdd:cd03813   412 ADdalgqAGLVVPPaDPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMIDS 468
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
155-334 1.90e-10

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: 61.31  E-value: 1.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 155 FLSINRYERKKNLPLALRSLVQLRNRLPSqewdkVHLFMAGGYDDRipenvehyKELKKMVqeSDLERhVTFLRSFSDRQ 234
Cdd:cd05844   192 ILFVGRLVEKKGCDVLIEAFRRLAARHPT-----ARLVIAGDGPLR--------PALQALA--AALGR-VRFLGALPHAE 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 235 KISLLHG----CLCVLYTPSN--EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLC-EPDPVHFSEAMEKFIHKP 307
Cdd:cd05844   256 VQDWMRRaeifCLPSVTAASGdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVpEGDVDALADALQALLADR 335
                         170       180
                  ....*....|....*....|....*..
gi 1243938503 308 SLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd05844   336 ALADRMGGAARAFVCEQFDIRVQTAKL 362
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
106-334 4.08e-10

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: 60.46  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 106 YTASVFKETFKTLSHRNPDVLYP-SLNIGSFD--LAIPEKIDDLvPKGKQFLFLSinRYERKKNLPLALRSLVQLRNRLP 182
Cdd:cd03821   158 FTSEQEADELRRFGLEPPIAVIPnGVDIPEFDpgLRDRRKHNGL-EDRRIILFLG--RIHPKKGLDLLIRAARKLAEQGR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 183 sqewdKVHLFMAGgYDDRipenvEHYKELKKMvQESDLERHVTFLRSFSDRQKISLLHGCLC-VLytPS-NEHFGIVPLE 260
Cdd:cd03821   235 -----DWHLVIAG-PDDG-----AYPAFLQLQ-SSLGLGDRVTFTGPLYGEAKWALYASADLfVL--PSySENFGNVVAE 300
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1243938503 261 AMYMQCPVIaVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFIHKPSLKATMGLAGKARVA--EKFSADAFADQL 334
Cdd:cd03821   301 ALACGLPVV-ITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQveENFSWEAVAGQL 375
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
98-334 5.00e-10

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: 60.04  E-value: 5.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503  98 DRILVNSQYTASVFKETFKTLSHRNpdVLYPSLnigSFDLAIPEKIddlVPKGKQFLFLSINRYERKKNLPLALRSLvql 177
Cdd:cd03823   145 DAVLAPSRFTANLHEANGLFSARIS--VIPNAV---EPDLAPPPRR---RPGTERLRFGYIGRLTEEKGIDLLVEAF--- 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 178 rNRLPSQEWdkvHLFMAGGYDDRIPEnvehykelkkmvqESDLERHVTFLrSFSDRQKISLLHGCLCVLYTPS--NEHFG 255
Cdd:cd03823   214 -KRLPREDI---ELVIAGHGPLSDER-------------QIEGGRRIAFL-GRVPTDDIKDFYEKIDVLVVPSiwPEPFG 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 256 IVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03823   276 LVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPgDAEDLAAAMRRLLTDPALLERLRAGAEPPRSTESQAEEYLKLY 355
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
148-334 1.67e-09

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 58.23  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 148 PKGKQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQEWDKVhlfmagGYDDRipenvehYKELKKMVQESDLERHVTFL 227
Cdd:cd03799   170 PLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQII------GDGDL-------KEQLQQLIQELNIGDCVKLL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 228 RSFSDRQKISLLHGCLcVLYTPS------NEHFGIVPL-EAMYMQCPVIAVNNGGPLESIVHKVTGFLC-EPDPVHFSEA 299
Cdd:cd03799   237 GWKPQEEIIEILDEAD-IFIAPSvtaadgDQDGPPNTLkEAMAMGLPVISTEHGGIPELVEDGVSGFLVpERDAEAIAEK 315
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1243938503 300 MEKFIHKPSLKATMGLAGKARVAEKFSADAFADQL 334
Cdd:cd03799   316 LTYLIEHPAIWPEMGKAGRARVEEEYDINKLNDEL 350
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
151-326 1.27e-08

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


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 55.77  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 151 KQFLFLSINRYERKKNLPLALRSLVQLRNRLPSQewdKVHLFmagGYDDripenvEHYKeLKKMVQESDLERHVT---FL 227
Cdd:cd04949   159 KSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEI---TLDIY---GYGE------EREK-LKKLIEELHLEDNVFlkgYH 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 228 RSFSDRQKISLLhgclcVLYTPSNEHFGIVPLEAMYMQCPVIAVN-NGGPLESIVHKVTGFLCEPDPVH-FSEAMEKFIH 305
Cdd:cd04949   226 SNLDQEYQDAYL-----SLLTSQMEGFGLTLMEAIGHGLPVVSYDvKYGPSELIEDGENGYLIEKNNIDaLADKIIELLN 300
                         170       180
                  ....*....|....*....|.
gi 1243938503 306 KPSLKATMGlAGKARVAEKFS 326
Cdd:cd04949   301 DPEKLQQFS-EESYKIAEKYS 320
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
152-336 5.78e-07

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


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 50.52  E-value: 5.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 152 QFLFLSINRYERKK---NLPLALRSLVQLRNRlpsqewdkVHLFMAGGYDDRipenvehyKELKKMVQESDLERHVTFLR 228
Cdd:cd04951   188 EFVILNVGRLTEAKdypNLLLAISELILSKND--------FKLLIAGDGPLR--------NELERLICNLNLVDRVILLG 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 229 SFSDrqkISLLHgCLCVLYTPSN--EHFGIVPLEAMYMQCPVIAVNNGGPLEsIVHKVTGFLCEPDPVHFSEAM-EKFIH 305
Cdd:cd04951   252 QISN---ISEYY-NAADLFVLSSewEGFGLVVAEAMACERPVVATDAGGVAE-VVGDHNYVVPVSDPQLLAEKIkEIFDM 326
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1243938503 306 KPSLKATMGLAGKARvAEKFSADAFADQLYQ 336
Cdd:cd04951   327 SDEERDILGNKNEYI-AKNFSINTIVNEWER 356
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
252-336 6.76e-06

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


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 47.33  E-value: 6.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 252 EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAF 330
Cdd:cd03825   274 DNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQ 353

                  ....*....
gi 1243938503 331 ADQ---LYQ 336
Cdd:cd03825   354 AQRyleLYK 362
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
245-326 2.70e-05

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 45.86  E-value: 2.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 245 VLYTPS-NEHFGIVPLEAMYMQCPVIAVNNGGpLESIVHK----VTGFLCEP-DPVHFSEAMEKFIHKPSLKATMGLAGK 318
Cdd:PLN02871  334 VFVMPSeSETLGFVVLEAMASGVPVVAARAGG-IPDIIPPdqegKTGFLYTPgDVDDCVEKLETLLADPELRERMGAAAR 412

                  ....*...
gi 1243938503 319 ARVaEKFS 326
Cdd:PLN02871  413 EEV-EKWD 419
PHA01633 PHA01633
putative glycosyl transferase group 1
136-269 4.77e-04

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 41.50  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 136 DLAIPEKIDDLVPKGKQFL---------FLSINRYERKKNLPLALRSLVQLRNRLPSQEwDKVHLFMAGGYD---DRIPE 203
Cdd:PHA01633  123 NFKIVENAEKLVPQLKQKLdkdfpdtikFGIVSGLTKRKNMDLMLQVFNELNTKYPDIA-KKIHFFVISHKQftqLEVPA 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1243938503 204 NVEHYKELkkmvqesdlerhvtflrSFSDRQKISLLHGCLCVLYTPSN-EHFGIVPLEAMYMQCPVI 269
Cdd:PHA01633  202 NVHFVAEF-----------------GHNSREYIFAFYGAMDFTIVPSGtEGFGMPVLESMAMGTPVI 251
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
153-306 8.48e-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: 40.74  E-value: 8.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1243938503 153 FLFLSINRYERKKNLPLALRSLVQLRNRLPsqewdKVHLFMAGgyddripeNVEHYKELKKMVQESDLERHVTFLRSFSD 232
Cdd:cd03812   192 LVLGHVGRFNEQKNHSFLIDIFEELKKKNP-----NVKLVLVG--------EGELKEKIKEKVKELGLEDKVIFLGFRND 258
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1243938503 233 RQKIsLLHgcLCVLYTPSN-EHFGIVPLEAMYMQCPVIAVNNGGPLESIVHKVTGFLCEPDPVHFSEAMEKFIHK 306
Cdd:cd03812   259 VSEI-LSA--MDVFLFPSLyEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFLPLNETPSTWAEKILKLIKR 330
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
259-331 1.77e-03

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 40.04  E-value: 1.77e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1243938503 259 LEAMYMQCPVIAVNNGGPLESIVHKVTGFLCE-PDPVHFSEAMEKFIHKPSLKATMGLAGKARVAEKFSADAFA 331
Cdd:cd03818   318 LEAMACGCPVIGSDTAPVREVIRDGRNGLLVDfFDPDALAAAVLELLEDPDRAAALRRAARRTVERSDSLDVCL 391
 
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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