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Conserved domains on  [gi|503993252|ref|WP_014227246|]
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MULTISPECIES: glycosyltransferase family 4 protein [Klebsiella]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 5-371 2.28e-52

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: 178.12  E-value: 2.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   5 RLALVRQKYRPD-GGAERFVSRALEALDDSDLELNVITREWQGPVKPEW--NIHICNPRKWGRISRERGFADAARQLWQR 81
Cdd:cd03801    1 KILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELedGVIVPLLPSLAALLRARRLLRELRPLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  82 EAFDLVQSHERIPGCDLYRAGDGVHRRWLQQRSRILPGWKSRLLfadRYHRYVMQAERDMYQDAHlrGVICNAEMIKREI 161
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLL---AAERRLLARAEALLRRAD--AVIAVSEALRDEL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 162 IEDFGLPAEKIHVIYNAIDNQRFLPPTEEAFvalrakwNLPRQATCLIYVGSGFERKGLDAAIRAIAP-----TNRYLLV 236
Cdd:cd03801  156 RALGGIPPEKIVVIPNGVDLERFSPPLRRKL-------GIPPDRPVLLFVGRLSPRKGVDLLLEALAKllrrgPDVRLVI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 237 VGKD-KEQGRYQQLAktLNCEERVRFFGMQS--ETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFI 313
Cdd:cd03801  229 VGGDgPLRAELEELE--LGLGDRVRFLGFVPdeELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 314 VQGSNGYVCDALDIPALQESVIAL-PARALGSAQGERARERIM-TCTSERLSAQLLSLYQ 371
Cdd:cd03801  307 EDGEGGLVVPPDDVEALADALLRLlADPELRARLGRAARERVAeRFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 5-371 2.28e-52

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: 178.12  E-value: 2.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   5 RLALVRQKYRPD-GGAERFVSRALEALDDSDLELNVITREWQGPVKPEW--NIHICNPRKWGRISRERGFADAARQLWQR 81
Cdd:cd03801    1 KILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELedGVIVPLLPSLAALLRARRLLRELRPLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  82 EAFDLVQSHERIPGCDLYRAGDGVHRRWLQQRSRILPGWKSRLLfadRYHRYVMQAERDMYQDAHlrGVICNAEMIKREI 161
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLL---AAERRLLARAEALLRRAD--AVIAVSEALRDEL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 162 IEDFGLPAEKIHVIYNAIDNQRFLPPTEEAFvalrakwNLPRQATCLIYVGSGFERKGLDAAIRAIAP-----TNRYLLV 236
Cdd:cd03801  156 RALGGIPPEKIVVIPNGVDLERFSPPLRRKL-------GIPPDRPVLLFVGRLSPRKGVDLLLEALAKllrrgPDVRLVI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 237 VGKD-KEQGRYQQLAktLNCEERVRFFGMQS--ETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFI 313
Cdd:cd03801  229 VGGDgPLRAELEELE--LGLGDRVRFLGFVPdeELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 314 VQGSNGYVCDALDIPALQESVIAL-PARALGSAQGERARERIM-TCTSERLSAQLLSLYQ 371
Cdd:cd03801  307 EDGEGGLVVPPDDVEALADALLRLlADPELRARLGRAARERVAeRFSWERVAERLLDLYR 366
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
208-337 2.70e-27

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 104.90  E-value: 2.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  208 LIYVGS-GFERKGLDAAIRAIA-----PTNRYLLVVGKDKEQgRYQQLAKTLncEERVRFFGMQSETLPFYQMADGLLLP 281
Cdd:pfam13692   4 ILFVGRlHPNVKGVDYLLEAVPllrkrDNDVRLVIVGDGPEE-ELEELAAGL--EDRVIFTGFVEDLAELLAAADVFVLP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 503993252  282 TLYDPFPNVILEAMACGLPVITTTgCGGAEFIVQGSNGYVCDALDIPALQESVIAL 337
Cdd:pfam13692  81 SLYEGFGLKLLEAMAAGLPVVATD-VGGIPELVDGENGLLVPPGDPEALAEAILRL 135
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 271-375 2.25e-22

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 91.21  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 271 FYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIALPA-RALGSAQGER 349
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEdPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*..
gi 503993252 350 ARERIMT-CTSERLSAQLLSLYQDLVK 375
Cdd:COG0438   97 ARERAEErFSWEAIAERLLALYEELLA 123
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 161-374 4.05e-18

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: 84.78  E-value: 4.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  161 IIEDFGLPAEKIHVIYNAIDNQRFLPPTEEAFVALRAKWNLPRQATCLIyVGSGFERKGLDAAIRAIAPTNRY------- 233
Cdd:TIGR03088 151 LRGPVKVPPAKIHQIYNGVDTERFHPSRGDRSPILPPDFFADESVVVGT-VGRLQAVKDQPTLVRAFALLVRQlpegaer 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  234 --LLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAE 311
Cdd:TIGR03088 230 lrLVIVGDGPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPE 309

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503993252  312 FIVQGSNGYVCDALDIPALQESVIA-LPARALGSAQGERARERIMTCTS-ERLSAQLLSLYQDLV 374
Cdd:TIGR03088 310 LVQHGVTGALVPPGDAVALARALQPyVSDPAARRAHGAAGRARAEQQFSiNAMVAAYAGLYDQLL 374
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
142-335 7.17e-15

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 75.13  E-value: 7.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 142 YQDAHLrgVICNAemIKREIIeDFGLPAEKIHVIYNAIDNQRFL-PPTEEAFVALrakwnlprqatcLIYVGS-GFE-RK 218
Cdd:PRK09922 133 CADYHL--AISSG--IKEQMM-ARGISAQRISVIYNPVEIKTIIiPPPERDKPAV------------FLYVGRlKFEgQK 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 219 GLDAAIRAIAPT--NRYLLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQM----ADGLLLPTLYDPFPNVIL 292
Cdd:PRK09922 196 NVKELFDGLSQTtgEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVQQkiknVSALLLTSKFEGFPMTLL 275

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503993252 293 EAMACGLPVITTTG-CGGAEFIVQGSNGYVCDALDIPALQESVI 335
Cdd:PRK09922 276 EAMSYGIPCISSDCmSGPRDIIKPGLNGELYTPGNIDEFVGKLN 319
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 162-304 2.17e-06

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 49.54  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 162 IEDfGLPAEKIHVIYNAIDNQRFLPpteeafvaLRAKwnlpRQAT-----CLIyvGSGFERKGLDAAIRAIAPTNRYL-- 234
Cdd:NF038011 273 IAD-GAPPERTRVIPNGIDLPRLAP--------LRAQ----RPAGippvvGLI--GRVVPIKDIKTFIRAMRTVVRAMpe 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 235 ---LVVGKDKEQGRYQQ----LAKTLNCEERVRFFGMQ--SETLPfyQMadGLL-LPTLYDPFPNVILEAMACGLPVITT 304
Cdd:NF038011 338 aegWIVGPEEEDPAYAAecrsLVASLGLQDKVKFLGFQkiDDLLP--QV--GLMvLSSISEALPLVVLEAFAAGVPVVTT 413
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 5-371 2.28e-52

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: 178.12  E-value: 2.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   5 RLALVRQKYRPD-GGAERFVSRALEALDDSDLELNVITREWQGPVKPEW--NIHICNPRKWGRISRERGFADAARQLWQR 81
Cdd:cd03801    1 KILLLSPELPPPvGGAERHVRELARALAARGHDVTVLTPADPGEPPEELedGVIVPLLPSLAALLRARRLLRELRPLLRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  82 EAFDLVQSHERIPGCDLYRAGDGVHRRWLQQRSRILPGWKSRLLfadRYHRYVMQAERDMYQDAHlrGVICNAEMIKREI 161
Cdd:cd03801   81 RKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLL---AAERRLLARAEALLRRAD--AVIAVSEALRDEL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 162 IEDFGLPAEKIHVIYNAIDNQRFLPPTEEAFvalrakwNLPRQATCLIYVGSGFERKGLDAAIRAIAP-----TNRYLLV 236
Cdd:cd03801  156 RALGGIPPEKIVVIPNGVDLERFSPPLRRKL-------GIPPDRPVLLFVGRLSPRKGVDLLLEALAKllrrgPDVRLVI 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 237 VGKD-KEQGRYQQLAktLNCEERVRFFGMQS--ETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFI 313
Cdd:cd03801  229 VGGDgPLRAELEELE--LGLGDRVRFLGFVPdeELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVV 306

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 314 VQGSNGYVCDALDIPALQESVIAL-PARALGSAQGERARERIM-TCTSERLSAQLLSLYQ 371
Cdd:cd03801  307 EDGEGGLVVPPDDVEALADALLRLlADPELRARLGRAARERVAeRFSWERVAERLLDLYR 366
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 17-352 2.46e-47

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: 164.45  E-value: 2.46e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  17 GGAERFVSRALEALDDSDLELNVITREWQGPVKPEWNIHICNPRKWGRISRERGFADAARQLWQR-----EAFDLVQSHe 91
Cdd:cd03811   12 GGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKrilkrAKPDVVISF- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  92 RIPGCDLYRAGDGVHRRWLQQR----SRILPGWKSRLLFADRYHRYvmqaerdmyqdahlRGVICNAEMIKREIIEDFGL 167
Cdd:cd03811   91 LGFATYIVAKLAAARSKVIAWIhsslSKLYYLKKKLLLKLKLYKKA--------------DKIVCVSKGIKEDLIRLGPS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 168 PAEKIHVIYNAIDNQRFLPPTEEAFvalrakWNLPRQATCLIYVGSGFERKGLDAAIRAIA-----PTNRYLLVVGKDKE 242
Cdd:cd03811  157 PPEKIEVIYNPIDIDRIRALAKEPI------LNEPEDGPVILAVGRLDPQKGHDLLIEAFAklrkkYPDVKLVILGDGPL 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 243 QGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTgCGGA-EFIVQGSNGYV 321
Cdd:cd03811  231 REELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTD-CPGPrEILDDGENGLL 309

                        330       340       350
                 ....*....|....*....|....*....|.
gi 503993252 322 CDALDIPALQESVIALPARALGSAQGERARE 352
Cdd:cd03811  310 VPDGDAAALAGILAALLQKKLDAALRERLAK 340
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 15-370 2.89e-36

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: 135.14  E-value: 2.89e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  15 PDGGAERFVSRALEALDDSDLELNVITREWQGPVKPE---WNIHI-CNPRKWGRisRERGFADAARQLwQREAFDLVQSH 90
Cdd:cd03807   10 NVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEEllaAGVPVvCLGLSSGK--DPGVLLRLAKLI-RKRNPDVVHTW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  91 erIPGCDLYRA----GDGVHRRWLQQRSRILPGWKSRLLFADRYHRYVMQaerdmyqdahlRGVICNAEMIKREIIEDfG 166
Cdd:cd03807   87 --MYHADLIGGlaakLAGGVKVIWSVRSSNIPQRLTRLVRKLCLLLSKFS-----------PATVANSSAVAEFHQEQ-G 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 167 LPAEKIHVIYNAIDNQRFlPPTEEAFVALRAKWNLPRQATCLIYVGSGFERKGLDAAIRA---IAPT--NRYLLVVGKDK 241
Cdd:cd03807  153 YAKNKIVVIYNGIDLFKL-SPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAaalLVEThpDLRLLLVGRGP 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 242 EQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTgCGGAEFIVQGSNGYV 321
Cdd:cd03807  232 ERPNLERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATD-VGGAAELVDDGTGFL 310

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503993252 322 CDALDIPALQESVIALPARALGSAQ-GERARERIM-TCTSERLSAQLLSLY 370
Cdd:cd03807  311 VPAGDPQALADAIRALLEDPEKRARlGRAARERIAnEFSIDAMVRRYETLY 361
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 17-373 6.87e-31

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: 120.95  E-value: 6.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  17 GGAERFVSRALEALDDSDLELNVITRE----WQGPVKPEWNIHICNPR--------KWGRISRERGFADAARQLW---QR 81
Cdd:cd03798   14 PGRGIFVRRQVRALSRRGVDVEVLAPApwgpAAARLLRKLLGEAVPPRdgrrllplKPRLRLLAPLRAPSLAKLLkrrRR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  82 EAFDLVQSHeripgcDLYRAGDG--VHRRWLQQ-------RSRILPGWKSRLLFADryHRYVMQaerdmyqdaHLRGVIC 152
Cdd:cd03798   94 GPPDLIHAH------FAYPAGFAaaLLARLYGVpyvvtehGSDINVFPPRSLLRKL--LRWALR---------RAARVIA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 153 NAEMIKREIIEdFGLPAEKIHVIYNAIDNQRFLPPTEEAFVALRAKwnlprqatCLIYVGSGFERKGLDAAIRAIAPTNR 232
Cdd:cd03798  157 VSKALAEELVA-LGVPRDRVDVIPNGVDPARFQPEDRGLGLPLDAF--------VILFVGRLIPRKGIDLLLEAFARLAK 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 233 Y-----LLVVGKDKEQGRYQQLAKTLNCEERVRFFGmqseTLPFYQMA------DGLLLPTLYDPFPNVILEAMACGLPV 301
Cdd:cd03798  228 ArpdvvLLIVGDGPLREALRALAEDLGLGDRVTFTG----RLPHEQVPayyracDVFVLPSRHEGFGLVLLEAMACGLPV 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993252 302 ITTTgCGG-AEFIVQGSNGYVCDALDIPALQESVIALPARALGSAQGERARERIMTCTSERLSAQ-LLSLYQDL 373
Cdd:cd03798  304 VATD-VGGiPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAADrIAAAYRDV 376
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 120-373 8.54e-31

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: 120.46  E-value: 8.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 120 WKSRLLFADRYHRYVmqaeRDMYQdaHLRGVICNAEMIKREIIEdFGLpAEKIHVIYNAIDNQRFLPPTEEAFvalRAKW 199
Cdd:cd03817  127 PKGKLLVKAVVRKLV----RRFYN--HTDAVIAPSEKIKDTLRE-YGV-KGPIEVIPNGIDLDKFEKPLNTEE---RRKL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 200 NLPRQATCLIYVGS-GFErKGLDAAIRAIA----PTNRYLLVVGKDKEQGRYQQLAKTLNCEERVRFFGM--QSETLPFY 272
Cdd:cd03817  196 GLPPDEPILLYVGRlAKE-KNIDFLLRAFAelkkEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFvpREELPEYY 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 273 QMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIALPARALGSAQGERARE 352
Cdd:cd03817  275 KAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEI 354

                        250       260
                 ....*....|....*....|.
gi 503993252 353 RIMTCTSERlsaQLLSLYQDL 373
Cdd:cd03817  355 SAREFAFAK---SVEKLYEEV 372
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 17-367 3.49e-29

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: 115.53  E-value: 3.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  17 GGAERFVSRALEALDDSDLELNVITRewQGP-VKPEWNIHICNPRKWGRISRERGFADAARQLWQREAFDLVQSHERIPG 95
Cdd:cd03819   11 GGAETYILDLARALAERGHRVLVVTA--GGPlLPRLRQIGIGLPGLKVPLLRALLGNVRLARLIRRERIDLIHAHSRAPA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  96 cdlyRAGdgvhrrWLQQRSRILPgwksrllFADRYH--RYVMQAERDMYQDAHLRG--VICNAEMIKREIIEDFGLPAEK 171
Cdd:cd03819   89 ----WLG------WLASRLTGVP-------LVTTVHgsYLATYHPKDFALAVRARGdrVIAVSELVRDHLIEALGVDPER 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 172 IHVIYNAIDNQRFLPPTEEAFvalRAKWNLPRQATCLIYVGSGFERKGLDAAIRAIA----PTNRYLLVVGKDKEQGRYQ 247
Cdd:cd03819  152 IRVIPNGVDTDRFPPEAEAEE---RAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAelkdEPDFRLLVAGDGPERDEIR 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 248 QLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDI 327
Cdd:cd03819  229 RLVERLGLRDRVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDA 308

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 503993252 328 PALQESVIALPARAlgsaqgeRARERIMTCTSERLSAQLL 367
Cdd:cd03819  309 EALADAIRAAKLLP-------EAREKLQAAAALTEAVREL 341
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
208-337 2.70e-27

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 104.90  E-value: 2.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  208 LIYVGS-GFERKGLDAAIRAIA-----PTNRYLLVVGKDKEQgRYQQLAKTLncEERVRFFGMQSETLPFYQMADGLLLP 281
Cdd:pfam13692   4 ILFVGRlHPNVKGVDYLLEAVPllrkrDNDVRLVIVGDGPEE-ELEELAAGL--EDRVIFTGFVEDLAELLAAADVFVLP 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 503993252  282 TLYDPFPNVILEAMACGLPVITTTgCGGAEFIVQGSNGYVCDALDIPALQESVIAL 337
Cdd:pfam13692  81 SLYEGFGLKLLEAMAAGLPVVATD-VGGIPELVDGENGLLVPPGDPEALAEAILRL 135
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 149-373 1.37e-26

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: 108.98  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 149 GVICNAEMIKREIIEDFGlPAEKIHVIYNAIDNQRFLPPTEEAFValRAKWNLPRQATcLIYVgSGFER-KGLDAAIRAI 227
Cdd:cd04962  144 RVTAVSSSLRQETYELFD-VDKDIEVIHNFIDEDVFKRKPAGALK--RRLLAPPDEKV-VIHV-SNFRPvKRIDDVVRVF 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 228 A----PTNRYLLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVIT 303
Cdd:cd04962  219 ArvrrKIPAKLLLVGDGPERVPAEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVPVVS 298

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503993252 304 TTGCGGAEFIVQGSNGYVCDALDIPALQESVI------ALPARaLGSAQGERARERImtcTSERLSAQLLSLYQDL 373
Cdd:cd04962  299 SNAGGIPEVVKHGETGFLSDVGDVDAMAKSALsileddELYNR-MGRAARKRAAERF---DPERIVPQYEAYYRRL 370
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 115-337 2.71e-26

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: 107.83  E-value: 2.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 115 RILPGWKSRLLFADRYHRYVMQAERdmyqdAhlRGVICNAEMIKREIIEDFGLPAEKIHVIYNAIDNQRFLPPTEEAfva 194
Cdd:cd03809  114 LRYPEFFPKRFRLYYRLLLPISLRR-----A--DAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAAV--- 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 195 LRAKWNLPRQAtcLIYVGSGFERKGLDAAIRA--IAPTNRY---LLVVG-KDKEQGRYQQLAKTLNCEERVRFFGMQS-E 267
Cdd:cd03809  184 LIAKYLLPEPY--FLYVGTLEPRKNHERLLKAfaLLKKQGGdlkLVIVGgKGWEDEELLDLVKKLGLGGRVRFLGYVSdE 261

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503993252 268 TLP-FYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTgcGGAEFIVQGSNGYVCDALDIPALQESVIAL 337
Cdd:cd03809  262 DLPaLYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASN--ISVLPEVAGDAALYFDPLDPESIADAILRL 330
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 154-373 4.41e-26

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: 107.42  E-value: 4.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 154 AEMIKREiiedFGLPAEKIHVIYNAIDNQRFLP-PTEEAfvalRAKWNLPRQATCLIYVGSGFE--RKGLD---AAIRAI 227
Cdd:cd03825  149 ADMVRRS----PLLKGLPVVVIPNGIDTEIFAPvDKAKA----RKRLGIPQDKKVILFGAESVTkpRKGFDeliEALKLL 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 228 APTNRYLLVV-GKDKEQgryqqlakTLNCEERVRFFGM---QSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVIT 303
Cdd:cd03825  221 ATKDDLLLVVfGKNDPQ--------IVILPFDIISLGYiddDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVA 292

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993252 304 TTGCGGAEFIVQGSNGYVCDALDIPALQES---VIALPARALGSaqGERARERIMTCTSERLSAQ-LLSLYQDL 373
Cdd:cd03825  293 FDTGGSPEIVQHGVTGYLVPPGDVQALAEAiewLLANPKERESL--GERARALAENHFDQRVQAQrYLELYKDL 364
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 208-353 6.81e-26

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: 101.58  E-value: 6.81e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  208 LIYVGSGFERKGLDAAIRAIA-----PTNRYLLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQS-ETLP-FYQMADGLLL 280
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFAllkekNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSdEDLPeLLKIADVFVL 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993252  281 PTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVI-ALPARALGSAQGERARER 353
Cdd:pfam00534  85 PSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDkLLEDEELRERLGENARKR 158
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 150-354 7.64e-24

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: 101.13  E-value: 7.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 150 VICNAEMIKREIIEDFGLPAEKIHVIYNAIDNQRFLPPTEEafvalrakwNLPRQATCLIYVGSGFERKGLDAAIRAIA- 228
Cdd:cd03808  143 VIFVNEDDRDLAIKKGIIKKKKTVLIPGSGVDLDRFQYSPE---------SLPSEKVVFLFVARLLKDKGIDELIEAAKi 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 229 PTNRY----LLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITT 304
Cdd:cd03808  214 LKKKGpnvrFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITT 293

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503993252 305 --TGCggAEFIVQGSNGYVCDALDIPALQESVIAL---PARALgsAQGERARERI 354
Cdd:cd03808  294 dvPGC--RELVIDGVNGFLVPPGDVEALADAIEKLiedPELRK--EMGEAARKRV 344
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 150-368 1.68e-23

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: 100.39  E-value: 1.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 150 VICNAEMIKREIIEDFGLPAEKIHVIYNAIDNQRFLPPTEEAfvALRAKWNLPRQATCLIYVGSGFERKGLDAAIRAIA- 228
Cdd:cd03800  167 VIASTPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAE--ARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAq 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 229 ------PTNryLLVVG------KDKEQGRYQQLAKTLNCEERVRFFGM--QSETLPFYQMADGLLLPTLYDPFPNVILEA 294
Cdd:cd03800  245 lpelreLAN--LVLVGgpsddpLSMDREELAELAEELGLIDRVRFPGRvsRDDLPELYRAADVFVVPSLYEPFGLTAIEA 322

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503993252 295 MACGLPVITTTgCGGAEFIVQ-GSNGYVCDALDIPALQESVIALPA-RALGSAQGERARERIM-TCTSERLSAQLLS 368
Cdd:cd03800  323 MACGTPVVATA-VGGLQDIVRdGRTGLLVDPHDPEALAAALRRLLDdPALWQRLSRAGLERARaHYTWESVADQLLT 398
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 55-352 1.34e-22

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: 97.52  E-value: 1.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  55 HICNPRKWGRISRERGFADAARQLWQRE--AFDLVQSH------------ER--IPGCDLYRAGDG-VHRRWLQQRsril 117
Cdd:cd05844   51 GGSGPLRWLRQMAQRLLGWSAPRLGGAAglAPALVHAHfgrdgvyalplaRAlgVPLVVTFHGFDItTSRAWLAAS---- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 118 PGWKSRLlfadRYHRYVMQAerdmyqdaHLRGVICNAEMIKREIIEdFGLPAEKIHVIYNAIDNQRFLPPTEeafvalra 197
Cdd:cd05844  127 PGWPSQF----QRHRRALQR--------PAALFVAVSGFIRDRLLA-RGLPAERIHVHYIGIDPAKFAPRDP-------- 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 198 kwnlPRQATCLIYVGSGFERKGLDAAIRAIA------PTNRyLLVVGKDKEQGRYQQLAKTLNceeRVRFFGMQS--ETL 269
Cdd:cd05844  186 ----AERAPTILFVGRLVEKKGCDVLIEAFRrlaarhPTAR-LVIAGDGPLRPALQALAAALG---RVRFLGALPhaEVQ 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 270 PFYQMADGLLLPTLYDP------FPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIALPA-RAL 342
Cdd:cd05844  258 DWMRRAEIFCLPSVTAAsgdsegLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLAdRAL 337

                        330
                 ....*....|
gi 503993252 343 GSAQGERARE 352
Cdd:cd05844  338 ADRMGGAARA 347
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 114-368 1.53e-22

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: 97.44  E-value: 1.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 114 SRILPGWKSRLLFADRYHRYVMQAerdmyqdahlRGVICNAEMIKREIiEDFGLPaEKIHVIYNAIDNQRFlPPTeeafV 193
Cdd:cd03821  130 ALQQKHWKKRIALHLIERRNLNNA----------ALVHFTSEQEADEL-RRFGLE-PPIAVIPNGVDIPEF-DPG----L 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 194 ALRAKWNLPRQATCLIYVGSGFERKGLDAAIRAIAP----TNRY-LLVVGKDKEQGRY-QQLAKTLNCEERVRFFGM--Q 265
Cdd:cd03821  193 RDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKlaeqGRDWhLVIAGPDDGAYPAfLQLQSSLGLGDRVTFTGPlyG 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 266 SETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGsNGYVCDaLDIPALQESVIAL-----PAR 340
Cdd:cd03821  273 EAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVD-PNVSSLAEALAEAlrdpaDRK 350

                        250       260
                 ....*....|....*....|....*...
gi 503993252 341 ALGsAQGERARERIMTCTSERLSAQLLS 368
Cdd:cd03821  351 RLG-EMARRARQVEENFSWEAVAGQLGE 377
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 271-375 2.25e-22

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 91.21  E-value: 2.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 271 FYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIALPA-RALGSAQGER 349
Cdd:COG0438   17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLEdPELRRRLGEA 96

                         90       100
                 ....*....|....*....|....*..
gi 503993252 350 ARERIMT-CTSERLSAQLLSLYQDLVK 375
Cdd:COG0438   97 ARERAEErFSWEAIAERLLALYEELLA 123
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 158-337 6.16e-22

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: 95.38  E-value: 6.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 158 KREIIEDFGLPAEKIHVIYNAIDnqrfLPPTEEAFvalrakwnlPRQATCLIYVGSGFERKGLDAAIRAIAP-TNRY--- 233
Cdd:cd03820  147 EADKLKKYKQPNSNVVVIPNPLS----FPSEEPST---------NLKSKRILAVGRLTYQKGFDLLIEAWALiAKKHpdw 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 234 -LLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGG-AE 311
Cdd:cd03820  214 kLRIYGDGPEREELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGpSE 293

                        170       180
                 ....*....|....*....|....*.
gi 503993252 312 FIVQGSNGYVCDALDIPALQESVIAL 337
Cdd:cd03820  294 IIEDGENGLLVPNGDVDALAEALLRL 319
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 117-367 9.95e-22

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: 95.49  E-value: 9.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 117 LPGWKSRLLFadRYHRYVmqaERDMYQDAHlrGVICNAEMIKREIIeDFGLPAEKIHVIYNAIDNQRFLPPTEEAfvaLR 196
Cdd:cd03794  141 LGVLKKGSLL--KLLKKL---ERKLYRLAD--AIIVLSPGLKEYLL-RKGVPKEKIIVIPNWADLEEFKPPPKDE---LR 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 197 AKWNLPRQATcLIYVGS-GFERkGLDAAIRAIAPTNRY----LLVVGKDKEQGRYQQLAKTLNCEeRVRFFGMQS--ETL 269
Cdd:cd03794  210 KKLGLDDKFV-VVYAGNiGKAQ-GLETLLEAAERLKRRpdirFLFVGDGDEKERLKELAKARGLD-NVTFLGRVPkeEVP 286

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 270 PFYQMADGLLLP----TLYDP-FPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIALPA-RALG 343
Cdd:cd03794  287 ELLSAADVGLVPlkdnPANRGsSPSKLFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDdPELR 366

                        250       260
                 ....*....|....*....|....*
gi 503993252 344 SAQGERARERIMT-CTSERLSAQLL 367
Cdd:cd03794  367 RAMGENGRELAEEkFSREKLADRLL 391
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 209-322 2.12e-19

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: 86.30  E-value: 2.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 209 IYVGSGFERKGLDAAIRAIA-----PTNRYLLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLP---FYQMADGLLL 280
Cdd:cd01635  114 VSVGRLVPEKGIDLLLEALAllkarLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVlelLLAAADVFVL 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 503993252 281 PTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVC 322
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 5-372 2.45e-19

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: 88.15  E-value: 2.45e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   5 RLALVRQKYRPD--GGAERFVSRALEALDDSDLELNVIT---REWQGPVKPEWNIHICNPRKWGRISRERGFAD-AARQL 78
Cdd:cd03823    1 KILLVNSLYPPQrvGGAEISVHDLAEALVAEGHEVAVLTagvGPPGQATVARSVVRYRRAPDETLPLALKRRGYeLFETY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  79 WQREAFDLVQSHERI-PgcdlyragDGVHRRWLQqrsrilpGWKSRLLFA--DRYHRYVMQAeRD---------MYQDAH 146
Cdd:cd03823   81 NPGLRRLLARLLEDFrP--------DVVHTHNLS-------GLGASLLDAarDLGIPVVHTL-HDywllcprqfLFKKGG 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 147 LRgVICNAEMIKReIIEDFGLPAEKIHVIYNAIDNQRFLPPTeeafvalraKWNLPRQATCLiYVGSGFERKGLD---AA 223
Cdd:cd03823  145 DA-VLAPSRFTAN-LHEANGLFSARISVIPNAVEPDLAPPPR---------RRPGTERLRFG-YIGRLTEEKGIDllvEA 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 224 IRAIAPTNRYLLVVGKDKEQGRYQQLAktlncEERVRFFG-MQSETLP-FYQMADGLLLPTL-YDPFPNVILEAMACGLP 300
Cdd:cd03823  213 FKRLPREDIELVIAGHGPLSDERQIEG-----GRRIAFLGrVPTDDIKdFYEKIDVLVVPSIwPEPFGLVVREAIAAGLP 287

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503993252 301 VITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIAL---PARALGSAQGERARErimtcTSERLSAQLLSLYQD 372
Cdd:cd03823  288 VIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLltdPALLERLRAGAEPPR-----STESQAEEYLKLYRD 357
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 161-374 4.05e-18

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: 84.78  E-value: 4.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  161 IIEDFGLPAEKIHVIYNAIDNQRFLPPTEEAFVALRAKWNLPRQATCLIyVGSGFERKGLDAAIRAIAPTNRY------- 233
Cdd:TIGR03088 151 LRGPVKVPPAKIHQIYNGVDTERFHPSRGDRSPILPPDFFADESVVVGT-VGRLQAVKDQPTLVRAFALLVRQlpegaer 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  234 --LLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAE 311
Cdd:TIGR03088 230 lrLVIVGDGPARGACEQMVRAAGLAHLVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPE 309

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503993252  312 FIVQGSNGYVCDALDIPALQESVIA-LPARALGSAQGERARERIMTCTS-ERLSAQLLSLYQDLV 374
Cdd:TIGR03088 310 LVQHGVTGALVPPGDAVALARALQPyVSDPAARRAHGAAGRARAEQQFSiNAMVAAYAGLYDQLL 374
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
17-180 5.63e-18

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 80.65  E-value: 5.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   17 GGAERFVSRALEALDDSDLELNVITREWQGPVKPEW----NIHICNPRKWGRISRERGFADAARQLWQREAFDLVQSHER 92
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVvrvvRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   93 IPgcdlyrAGDGVHRRWLQQRSRI-------LPGWKSRLLFADRYHRYVMQAERDMYQDAHLrgVICNAEMIKREIIEDF 165
Cdd:pfam13439  81 FP------LGLAALAARLRLGIPLvvtyhglFPDYKRLGARLSPLRRLLRRLERRLLRRADR--VIAVSEAVADELRRLY 152

                         170
                  ....*....|....*
gi 503993252  166 GLPAEKIHVIYNAID 180
Cdd:pfam13439 153 GVPPEKIRVIPNGVD 167
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 5-370 1.03e-16

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: 80.42  E-value: 1.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   5 RLALVRQKYRPD-GGAERFVSRALEALDDSDLELNVIT-----------------REWQGPVKPEWNIHICNPRKwgris 66
Cdd:cd03814    1 RIALVTDTYHPQvNGVVRTLERLVDHLRRRGHEVRVVApgpfdeaesaegrvvsvPSFPLPFYPEYRLALPLPRR----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  67 rergfadaARQLWQREAFDLVQ--SHERIPGCDLYRAGD-------GVHRRWLQQRSRILPGWKSRLLFA--DRYHRyvm 135
Cdd:cd03814   76 --------VRRLIKEFQPDIIHiaTPGPLGLAALRAARRlglpvvtSYHTDFPEYLSYYTLGPLSWLAWAylRWFHN--- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 136 qaerdmyqdaHLRGVICNAEMIKREIIedfGLPAEKIHVIYNAIDNQRFLPptEEAFVALRAKWnLPRQATCLIYVGSGF 215
Cdd:cd03814  145 ----------PFDTTLVPSPSIARELE---GHGFERVRLWPRGVDTELFHP--SRRDAALRRRL-GPPGRPLLLYVGRLA 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 216 ERKGLDAAIRAIAPTNRY----LLVVGkDKEQgRYQQLAKTLNceerVRFFGMQ-SETLP-FYQMADGLLLPTLYDPFPN 289
Cdd:cd03814  209 PEKNLEALLDADLPLAASppvrLVVVG-DGPA-RAELEARGPD----VIFTGFLtGEELArAYASADVFVFPSRTETFGL 282

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 290 VILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIALPA-RALGSAQGERARERIMTCTSERLSAQLLS 368
Cdd:cd03814  283 VVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEdPELRRRMAARARAEAERYSWEAFLDNLLD 362


                 ..
gi 503993252 369 LY 370
Cdd:cd03814  363 YY 364
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 159-356 9.43e-16

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: 78.15  E-value: 9.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 159 REIIEDFGLPAEKIHVIYNAIDNQRFLPPTEEafvalRAKWNLPRqatcLIYVGSGFERKGLDAAIRAIA------PTNR 232
Cdd:cd03813  256 RRRQIRLGADPDKTRVIPNGIDIQRFAPAREE-----RPEKEPPV----VGLVGRVVPIKDVKTFIRAFKlvrramPDAE 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 233 YLLVVGKDKEQGRYQ---QLAKTLNCEERVRFFGMQS--ETLPFYQMadgLLLPTLYDPFPNVILEAMACGLPVITTT-- 305
Cdd:cd03813  327 GWLIGPEDEDPEYAQeckRLVASLGLENKVKFLGFQNikEYYPKLGL---LVLTSISEGQPLVILEAMASGVPVVATDvg 403

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503993252 306 GC-----GGAEFIvqGSNGYVCDALDIPALQESVIAL---PARAlgSAQGERARERIMT 356
Cdd:cd03813  404 SCreliyGADDAL--GQAGLVVPPADPEALAEALIKLlrdPELR--QAFGEAGRKRVEK 458
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 13-354 1.24e-15

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: 77.31  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  13 YRPD-GGAERFVSRALEALDDSDLELNVIT--REWQGPVKPEWNIHICNPRKWGRISRERGFADAARQLWQREA-FDLVQ 88
Cdd:cd03795    9 YYPDiGGIEQVIYDLAEGLKKKGIEVDVLCfsKEKETPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKKLAKeYDIIH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  89 SHERIPGCDLYRAGDGVHRRW-LQQRSRILPGWKSRLLFADRYHRYVMQAERdmyqdahlrgVICNAEMIKR--EIIEDF 165
Cdd:cd03795   89 YHFPNPLADLLLFFSGAKKPVvVHWHSDIVKQKKLLKLYKPLMTRFLRRADR----------IIATSPNYVEtsPTLREF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 166 glpAEKIHVIYNAIDNQRFLPPTEEAFvalrAKWNLPRQATCLIYVGSGFERKGLDAAIRAIAPTNRYLLVVGKDKEQGR 245
Cdd:cd03795  159 ---KNKVRVIPLGIDKNVYNIPRVDFE----NIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPIVIGGEGPLKPD 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 246 YQQLAKtLNCEERVRFFGMQS--ETLPFYQMADGLLLP--TLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQ-GSNGY 320
Cdd:cd03795  232 LEAQIE-LNLLDNVKFLGRVDdeEKVIYLHLCDVFVFPsvLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNnGETGL 310

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 503993252 321 VCDALDIPALQESVIAL---PARAlgSAQGERARERI 354
Cdd:cd03795  311 VVPPKDPDALAEAIDKLlsdEELR--ESYGENAKKRF 345
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 166-373 2.34e-15

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: 76.17  E-value: 2.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 166 GLPAEKIHVIYNAIDNQRFLPPTE-EAFvalrakwnlprqatcLIYVGSGFERKGLDAAIRAIAPTNRYLLVVGKDKEQG 244
Cdd:cd03802  144 TPPIDYLTVVHNGLDPADYRFQPDpEDY---------------LAFLGRIAPEKGLEDAIRVARRAGLPLKIAGKVRDED 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 245 RYQQLAKtLNCEERVRFFGM--QSETLPFYQMADGLLLPTLYD-PFPNVILEAMACGLPVItTTGCGG-AEFIVQGSNGY 320
Cdd:cd03802  209 YFYYLQE-PLPGPRIEFIGEvgHDEKQELLGGARALLFPINWDePFGLVMIEAMACGTPVI-AYRRGGlPEVIQHGETGF 286

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503993252 321 VCdaldiPALQESVIALpaRALGSAQGERARERIMTCTS-ERLSAQLLSLYQDL 373
Cdd:cd03802  287 LV-----DSVEEMAEAI--ANIDRIDRAACRRYAEDRFSaARMADRYEALYRKV 333
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 132-356 2.54e-15

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: 76.34  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 132 RYVMQAERDMYQDAHLRG--VICNAEMIKREIIEdFGLPAEKIHVIYNAIDNQRFlppteeafvALRAKWNLPRQATCLI 209
Cdd:cd03799  109 MYVILEGNKVYPQLFAQGdlFLPNCELFKHRLIA-LGCDEKKIIVHRSGIDCNKF---------RFKPRYLPLDGKIRIL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 210 YVGSGFERKGLDAAIRAIA------PTNRYLlVVGKDKEQGRYQQLAKTLNCEERVRFFGM--QSETLPFYQMADGLLLP 281
Cdd:cd03799  179 TVGRLTEKKGLEYAIEAVAklaqkyPNIEYQ-IIGDGDLKEQLQQLIQELNIGDCVKLLGWkpQEEIIEILDEADIFIAP 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 282 TL------YDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIAL-PARALGSAQGERARERI 354
Cdd:cd03799  258 SVtaadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLiEHPAIWPEMGKAGRARV 337


                 ..
gi 503993252 355 MT 356
Cdd:cd03799  338 EE 339
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
142-335 7.17e-15

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 75.13  E-value: 7.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 142 YQDAHLrgVICNAemIKREIIeDFGLPAEKIHVIYNAIDNQRFL-PPTEEAFVALrakwnlprqatcLIYVGS-GFE-RK 218
Cdd:PRK09922 133 CADYHL--AISSG--IKEQMM-ARGISAQRISVIYNPVEIKTIIiPPPERDKPAV------------FLYVGRlKFEgQK 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 219 GLDAAIRAIAPT--NRYLLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQM----ADGLLLPTLYDPFPNVIL 292
Cdd:PRK09922 196 NVKELFDGLSQTtgEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQPWEVVQQkiknVSALLLTSKFEGFPMTLL 275

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 503993252 293 EAMACGLPVITTTG-CGGAEFIVQGSNGYVCDALDIPALQESVI 335
Cdd:PRK09922 276 EAMSYGIPCISSDCmSGPRDIIKPGLNGELYTPGNIDEFVGKLN 319
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 170-303 1.67e-13

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: 70.78  E-value: 1.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 170 EKIHVIYNAIDNQRFLPPTEEAFValRAKWNLPRQATCLIYVGSGFERKGLDAAIRAIA-----PTNRYLLVVGKDKEQG 244
Cdd:cd03812  158 GKFKVIPNGIDIEKYKFNKEKRRK--RRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEelkkkNPNVKLVLVGEGELKE 235

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503993252 245 RYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVIT 303
Cdd:cd03812  236 KIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLL 294
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 157-311 1.19e-11

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: 65.16  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 157 IKREIIEDF----GLPAEKIHVIYNAIDNQRFlPPTEEAFVALRAKWNLPRQATCLIYVGSGFERKGLDAAIRAIAPT-- 230
Cdd:cd04951  137 VSREALDEFiakkAFSKNKSVPVYNGIDLNKF-KKDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELil 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 231 --NRY-LLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGC 307
Cdd:cd04951  216 skNDFkLLIAGDGPLRNELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAG 295


                 ....
gi 503993252 308 GGAE 311
Cdd:cd04951  296 GVAE 299
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
151-323 2.11e-11

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 65.11  E-value: 2.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 151 ICNAEMIKREIIEDFGLPAEKIHVIYNAIdnqrfLPPTEEAFVALRAK-WNLPRQAT---------CLIYVGSGFERKGL 220
Cdd:PRK15490 343 MSNNHCVTRHYADWLKLEAKHFQVVYNGV-----LPPSTEPSSEVPHKiWQQFTQKTqdadttiggVFRFVGDKNPFAWI 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 221 DAAIRAIA--PTNRYLLVvGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACG 298
Cdd:PRK15490 418 DFAARYLQhhPATRFVLV-GDGDLRAEAQKRAEQLGILERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVG 496

                        170       180
                 ....*....|....*....|....*
gi 503993252 299 LPVITTTGCGGAEFIVQGSNGYVCD 323
Cdd:PRK15490 497 VPVISTPAGGSAECFIEGVSGFILD 521
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 128-371 3.16e-11

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 64.67  E-value: 3.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 128 DRYHRYVMQAErDMYQD-AHLRGV--ICNAEMIKREIIEDFGLPAEKIHVIYNAidnqrfLPPTE-EAFVALRAKWNLPR 203
Cdd:PRK15179 438 DRPDRYRVEYD-IIYSElLKMRGValSSNSQFAAHRYADWLGVDERRIPVVYNG------LAPLKsVQDDACTAMMAQFD 510

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 204 QAT--CLIYVGSGF-----ERKGL--DAAIRAIA--PTNRYLLVvGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFY 272
Cdd:PRK15179 511 ARTsdARFTVGTVMrvddnKRPFLwvEAAQRFAAshPKVRFIMV-GGGPLLESVREFAQRLGMGERILFTGLSRRVGYWL 589

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 273 QMADGLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDALDI--PALQESVIALPAR-ALGSAQGER 349
Cdd:PRK15179 590 TQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVtaPDVAEALARIHDMcAADPGIARK 669

                        250       260
                 ....*....|....*....|...
gi 503993252 350 ARERIMTCTS-ERLSAQLLSLYQ 371
Cdd:PRK15179 670 AADWASARFSlNQMIASTVRCYQ 692
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 146-337 2.78e-10

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: 60.78  E-value: 2.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 146 HLRGVICNAEMIKREIIEDFGlPAEKIHVIYNAIDNQrflppteeafvALRAKWNLPRQATCLIYVGSGFERKGLDAAIR 225
Cdd:cd04949  113 KYDAIIVSTEQQKQDLSERFN-KYPPIFTIPVGYVDQ-----------LDTAESNHERKSNKIITISRLAPEKQLDHLIE 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 226 AIAPTNRY-----LLVVGKDKEQGRYQQLAKTLNCEERVRFFGMQSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLP 300
Cdd:cd04949  181 AVAKAVKKvpeitLDIYGYGEEREKLKKLIEELHLEDNVFLKGYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLP 260

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 503993252 301 VIT-TTGCGGAEFIVQGSNGYVCDALDIPALQESVIAL 337
Cdd:cd04949  261 VVSyDVKYGPSELIEDGENGYLIEKNNIDALADKIIEL 298
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
153-342 5.46e-10

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 60.19  E-value: 5.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 153 NAEMI-KREIIEDF---GLPAEKIHVIYNAIDNQRFLPPTEEAfvaLRAKWNLPRQATCLIYVGSGFERKGLDAAIRAI- 227
Cdd:PRK15484 140 NAKIIvPSQFLKKFyeeRLPNADISIVPNGFCLETYQSNPQPN---LRQQLNISPDETVLLYAGRISPDKGILLLMQAFe 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 228 ----APTNRYLLVVG-----KDKEQGRYQQ----LAKTLNceERVRFFGMQS--ETLPFYQMADGLLLPTLY-DPFPNVI 291
Cdd:PRK15484 217 klatAHSNLKLVVVGdptasSKGEKAAYQKkvleAAKRIG--DRCIMLGGQPpeKMHNYYPLADLVVVPSQVeEAFCMVA 294

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503993252 292 LEAMACGLPVITTTGCGGAEFIVQGSNGYvcdALDIPALQESVIALPARAL 342
Cdd:PRK15484 295 VEAMAAGKPVLASTKGGITEFVLEGITGY---HLAEPMTSDSIISDINRTL 342
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 133-372 8.73e-10

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 59.72  E-value: 8.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  133 YVMQAERDMYQDAhlRGVICNAEMIKREIIEDFGLPAEkihVIYNAIDNQRFLPPTEEAFVALRAKWNLpRQATCLIYVG 212
Cdd:TIGR04047 127 RLAACQERAIVEA--DAVLCVSAAWAAELRAEWGIDAT---VVPNGVDAARFSPAADAADAALRRRLGL-RGGPYVLAVG 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  213 SGFERKG----LDA--AIRAIAPTNRylLVVG-------KDKEQGRYQQLAKTLNCE-ERVRFFGM--QSETLPFYQMAD 276
Cdd:TIGR04047 201 GIEPRKNtidlLEAfaLLRARRPQAQ--LVIAggatlfdYDAYRREFRARAAELGVDpGPVVITGPvpDADLPALYRCAD 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252  277 GLLLPTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSnGYVCDALDIPALQESVIALPARALGSAQGERARERIMT 356
Cdd:TIGR04047 279 AFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRFD-AAWADPSDPDSIADALALALDPARRPALRAAGPELAAR 357

                         250
                  ....*....|....*.
gi 503993252  357 CTSERLSAQLLSLYQD 372
Cdd:TIGR04047 358 YTWDASARAHLEFYRR 373
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 150-334 2.10e-06

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: 49.21  E-value: 2.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 150 VICNAEMIKREIIEDFGLPAEkihVIYNAIDNQRFLP--PTEEAFVALrakwnlprqatcliyvGSGFERKGLDAAIRAI 227
Cdd:cd03804  161 FIANSQFVARRIKKFYGREST---VIYPPVDTDAFAPaaDKEDYYLTA----------------SRLVPYKRIDLAVEAF 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 228 APTNRYLLVVGKDKEQGRYQQLAKtlnceERVRFFGMQS--ETLPFYQMADGLLLPTLYDpFPNVILEAMACGLPVItTT 305
Cdd:cd03804  222 NELPKRLVVIGDGPDLDRLRAMAS-----PNVEFLGYQPdeVLKELLSKARAFVFAAEED-FGIVPVEAQACGTPVI-AF 294

                        170       180       190
                 ....*....|....*....|....*....|
gi 503993252 306 GCGGA-EFIVQGSNGYVCDALDIPALQESV 334
Cdd:cd03804  295 GKGGAlETVRPGPTGILFGEQTVESLKAAV 324
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
 162-304 2.17e-06

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 49.54  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 162 IEDfGLPAEKIHVIYNAIDNQRFLPpteeafvaLRAKwnlpRQAT-----CLIyvGSGFERKGLDAAIRAIAPTNRYL-- 234
Cdd:NF038011 273 IAD-GAPPERTRVIPNGIDLPRLAP--------LRAQ----RPAGippvvGLI--GRVVPIKDIKTFIRAMRTVVRAMpe 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 235 ---LVVGKDKEQGRYQQ----LAKTLNCEERVRFFGMQ--SETLPfyQMadGLL-LPTLYDPFPNVILEAMACGLPVITT 304
Cdd:NF038011 338 aegWIVGPEEEDPAYAAecrsLVASLGLQDKVKFLGFQkiDDLLP--QV--GLMvLSSISEALPLVVLEAFAAGVPVVTT 413
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 168-341 2.40e-06

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: 48.90  E-value: 2.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 168 PAE---KIHVIYNAIDNQRFLPPTEEAFVALRAKwNLPRQATCLIYVGSGFER-KGLDAAIRAIA------PTNRyLLVV 237
Cdd:cd03818  174 PAAyrdRISVIHDGVDTDRLAPDPAARLRLLNGT-ELKAGDPVITYVARNLEPyRGFHVFMRALPriqarrPDAR-VVVV 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 238 GKDK----------EQGRYQQLAKTLNCEERVRFFGM--QSETLPFYQMADGLLLPTlydpFPNV----ILEAMACGLPV 301
Cdd:cd03818  252 GGDGvsygspppdgGSWKQKMLAELGVDLERVHFVGKvpYDQYVRLLQLSDAHVYLT----YPFVlswsLLEAMACGCPV 327

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 503993252 302 ITTTGCGGAEFIVQGSNGYVCDALDIPALQESVIAL---PARA 341
Cdd:cd03818  328 IGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELledPDRA 370
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 166-304 3.20e-06

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 48.77  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 166 GLPAEKIHVIYNAIDNQRFLPPTEEAfvalrakwnlPRQATCLIYVGSGFERKGLDAAIRAIAP-----TNRYLLVVGKD 240
Cdd:cd03796  164 SLDPRIVSVIPNAVDSSDFTPDPSKP----------DPNKITIVVISRLVYRKGIDLLVGIIPRickkhPNVRFIIGGDG 233

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503993252 241 KEQGRYQQLAKTLNCEERVRFFGM--QSETLPFYQMADGLLLPTLYDPFPNVILEAMACGLPVITT 304
Cdd:cd03796  234 PKRIELEEMREKYQLQDRVELLGAvpHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVST 299
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
166-353 5.50e-06

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 48.05  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 166 GLPAEKIHVIYNAIDNQRFLPPTEEAFVALRAKWNLPRQATCLIYVGSGFERKGL----DAAIRAIAPTNRYLLVVGKDK 241
Cdd:PRK10307 190 GVAAEKVIFFPNWSEVARFQPVADADVDALRAQLGLPDGKKIVLYSGNIGEKQGLelviDAARRLRDRPDLIFVICGQGG 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 242 EQGRyqqLAKTLNCE--ERVRFFGMQS-ETLP-FYQMADGLLLPTLYDP----FPNVILEAMACGLPVITTTGCGGAEFI 313
Cdd:PRK10307 270 GKAR---LEKMAQCRglPNVHFLPLQPyDRLPaLLKMADCHLLPQKAGAadlvLPSKLTNMLASGRNVVATAEPGTELGQ 346

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 503993252 314 VQGSNGYVCDALDIPALQESVIALPARALG-SAQGERARER 353
Cdd:PRK10307 347 LVEGIGVCVEPESVEALVAAIAALARQALLrPKLGTVAREY 387
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 215-324 2.62e-05

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: 45.66  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 215 FER-KGLDAAIRAIA-------PTNRYLLVV--GKDK---EQGRY----QQLAKTL-NCEERVRFFGMQSETLPFYQMAD 276
Cdd:cd03805  220 FERkKNIALAIEAFAklkqklpEFENVRLVIagGYDPrvaENVEYleelQRLAEELlNVEDQVLFLRSISDSQKEQLLSS 299

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503993252 277 GLLLptLYDP----FPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCDA 324
Cdd:cd03805  300 ALAL--LYTPsnehFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP 349
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
17-178 5.56e-05

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 43.16  E-value: 5.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   17 GGAERFVSRALEALDDSDLELNVITREWQGPVKPEW----NIHICN-PRKWGRISRERgFADAARQLWQREAFDLVQSHE 91
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVgdgvRVHRLPvPPRPSPLADLA-ALRRLRRLLRAERPDVVHAHS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252   92 RIPGCDLYRAGDGVHRRWLQQRSRILPGWKSRLLfadryHRYVMQAERDMYQDAHlrGVICNAEMIKREIIEdFGLPAEK 171
Cdd:pfam13579  80 PTAGLAARLARRRRGVPLVVTVHGLALDYGSGWK-----RRLARALERRLLRRAD--AVVVVSEAEAELLRA-LGVPAAR 151


                  ....*..
gi 503993252  172 IHVIYNA 178
Cdd:pfam13579 152 VVVVPNG 158
PLN00142 PLN00142
sucrose synthase
 281-323 1.96e-04

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 43.43  E-value: 1.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 503993252 281 PTLYDPFPNVILEAMACGLPVITTTGCGGAEFIVQGSNGYVCD 323
Cdd:PLN00142 673 PALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHID 715
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 245-365 3.89e-04

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 42.06  E-value: 3.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 245 RYQQLAKTLNCEERVRFFGM--QSETLPFYQMADglllptlYDPFPNV---------ILEAMACGLPVITTTGCGGAEFI 313
Cdd:cd04946  271 RLEKLAENKLENVKVNFTGEvsNKEVKQLYKEND-------VDVFVNVsesegipvsIMEAISFGIPVIATNVGGTREIV 343

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503993252 314 VQGSNGYVCDalDIPALQESVIALPARALGSAQGERARERIMTCTSERLSAQ 365
Cdd:cd04946  344 ENETNGLLLD--KDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAE 393
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 157-357 4.95e-03

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 38.92  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 157 IKREIIEDFGLPAEKIHVIYNAIDNQRFLPPTEEAfvALRAKWNLPRQATCLI-YVGS-GFErKGLDAAIRAIA--PTNR 232
Cdd:PLN02871 216 LGKELEAAGVTAANRIRVWNKGVDSESFHPRFRSE--EMRARLSGGEPEKPLIvYVGRlGAE-KNLDFLKRVMErlPGAR 292

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993252 233 yLLVVGKDKEQGRYQQLAKTLNceerVRFFGM-QSETLP-FYQMADGLLLPTLYDPFPNVILEAMACGLPVITTTGcGGA 310
Cdd:PLN02871 293 -LAFVGDGPYREELEKMFAGTP----TVFTGMlQGDELSqAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARA-GGI 366

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503993252 311 EFIV----QGSNGYVCDALDIPALQESVIALPA-RALGSAQGERARERIMTC 357
Cdd:PLN02871 367 PDIIppdqEGKTGFLYTPGDVDDCVEKLETLLAdPELRERMGAAAREEVEKW 418
 
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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