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Conserved domains on  [gi|2544592186|ref|WP_300374842.1|]
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glycosyltransferase family 4 protein

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 ...
 2-348 3.81e-30

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: 118.02  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIVTTLAPFIKGGAEYLAANLAQACSAAGHQVDIFKLPFLDSSADSIQKSMDLCL---------------QEDFSLWG 66
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLlpslaallrarrllrELRPLLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  67 QQADLVICLKFPAYYV------QHPCKIMWVLHQHRSAYDLWDHAAAQGhtystediALREQImaldkRVFNSALQNFTI 140
Cdd:cd03801    81 RKFDVVHAHGLLAALLaallalLLGAPLVVTLHGAEPGRLLLLLAAERR--------LLARAE-----ALLRRADAVIAV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 141 SKTVSNRLKHYNHIESSPL-YHPPALANAFAMDDTQAETGDF-----IFAPSRFEPLKRQHLLLEALRLTKHP---VKAV 211
Cdd:cd03801   148 SEALRDELRALGGIPPEKIvVIPNGVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRKGVDLLLEALAKLLRRgpdVRLV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 212 LCGS-GSYEHHLRNFvvHYGLQDRVTLHTHLSVAEMISHYKNSlAVFFAP-YDEDYGYVTLEAMLAEKAVITcNDSGGTN 289
Cdd:cd03801   228 IVGGdGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAA-DVFVLPsRYEGFGLVVLEAMAAGLPVVA-TDVGGLP 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 290 EFVVHDHTGYI-EPPEAEQIAARLDALFMDRNLAVSIGQNALHHYQSLsLSWDNVLNQLL 348
Cdd:cd03801   304 EVVEDGEGGLVvPPDDVEALADALLRLLADPELRARLGRAARERVAER-FSWERVAERLL 362
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-348 3.81e-30

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: 118.02  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIVTTLAPFIKGGAEYLAANLAQACSAAGHQVDIFKLPFLDSSADSIQKSMDLCL---------------QEDFSLWG 66
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLlpslaallrarrllrELRPLLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  67 QQADLVICLKFPAYYV------QHPCKIMWVLHQHRSAYDLWDHAAAQGhtystediALREQImaldkRVFNSALQNFTI 140
Cdd:cd03801    81 RKFDVVHAHGLLAALLaallalLLGAPLVVTLHGAEPGRLLLLLAAERR--------LLARAE-----ALLRRADAVIAV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 141 SKTVSNRLKHYNHIESSPL-YHPPALANAFAMDDTQAETGDF-----IFAPSRFEPLKRQHLLLEALRLTKHP---VKAV 211
Cdd:cd03801   148 SEALRDELRALGGIPPEKIvVIPNGVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRKGVDLLLEALAKLLRRgpdVRLV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 212 LCGS-GSYEHHLRNFvvHYGLQDRVTLHTHLSVAEMISHYKNSlAVFFAP-YDEDYGYVTLEAMLAEKAVITcNDSGGTN 289
Cdd:cd03801   228 IVGGdGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAA-DVFVLPsRYEGFGLVVLEAMAAGLPVVA-TDVGGLP 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 290 EFVVHDHTGYI-EPPEAEQIAARLDALFMDRNLAVSIGQNALHHYQSLsLSWDNVLNQLL 348
Cdd:cd03801   304 EVVEDGEGGLVvPPDDVEALADALLRLLADPELRARLGRAARERVAER-FSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 181-329 3.16e-27

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: 105.05  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 181 FIFAPSRFEPLKRQHLLLEALRL---TKHPVKAVLCGSGSYEHHLRNFVVHYGLQDRVTLHTHLSVAEMISHYKNSLAVF 257
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALlkeKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2544592186 258 FAPYDEDYGYVTLEAMLAEKAVITcNDSGGTNEFVVHDHTGY-IEPPEAEQIAARLDALFMDRNLAVSIGQNA 329
Cdd:pfam00534  84 LPSRYEGFGIVLLEAMACGLPVIA-SDVGGPPEVVKDGETGFlVKPNNAEALAEAIDKLLEDEELRERLGENA 155
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 249-348 3.28e-14

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 68.48  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 249 HYKNSLAVFFAPYDEDYGYVTLEAMLAEKAVITCnDSGGTNEFVVHDHTGY-IEPPEAEQIAARLDALFMDRNLAVSIGQ 327
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAT-DVGGLPEVIEDGETGLlVPPGDPEALAEAILRLLEDPELRRRLGE 95

                          90       100
                  ....*....|....*....|.
gi 2544592186 328 NALHHYQSlSLSWDNVLNQLL 348
Cdd:COG0438    96 AARERAEE-RFSWEAIAERLL 115
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
182-346 1.94e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 45.94  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 182 IFAPSRFEPLKRQHLLLEA---LRLTKHPVKAVLCG---------SGSYEHHLRNfvvhygLQDRVTLHTHL----SVAE 245
Cdd:PRK15484  196 LLYAGRISPDKGILLLMQAfekLATAHSNLKLVVVGdptasskgeKAAYQKKVLE------AAKRIGDRCIMlggqPPEK 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 246 MISHYK-NSLAVFFAPYDEDYGYVTLEAMLAEKAVITcNDSGGTNEFVVHDHTGY--IEPPEAEQIAARLDALFMDRNLA 322
Cdd:PRK15484  270 MHNYYPlADLVVVPSQVEEAFCMVAVEAMAAGKPVLA-STKGGITEFVLEGITGYhlAEPMTSDSIISDINRTLADPELT 348

                         170       180
                  ....*....|....*....|....*...
gi 2544592186 323 vSIGQNA----LHHYqslslSWDNVLNQ 346
Cdd:PRK15484  349 -QIAEQAkdfvFSKY-----SWEGVTQR 370
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-348 3.81e-30

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: 118.02  E-value: 3.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIVTTLAPFIKGGAEYLAANLAQACSAAGHQVDIFKLPFLDSSADSIQKSMDLCL---------------QEDFSLWG 66
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLlpslaallrarrllrELRPLLRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  67 QQADLVICLKFPAYYV------QHPCKIMWVLHQHRSAYDLWDHAAAQGhtystediALREQImaldkRVFNSALQNFTI 140
Cdd:cd03801    81 RKFDVVHAHGLLAALLaallalLLGAPLVVTLHGAEPGRLLLLLAAERR--------LLARAE-----ALLRRADAVIAV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 141 SKTVSNRLKHYNHIESSPL-YHPPALANAFAMDDTQAETGDF-----IFAPSRFEPLKRQHLLLEALRLTKHP---VKAV 211
Cdd:cd03801   148 SEALRDELRALGGIPPEKIvVIPNGVDLERFSPPLRRKLGIPpdrpvLLFVGRLSPRKGVDLLLEALAKLLRRgpdVRLV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 212 LCGS-GSYEHHLRNFvvHYGLQDRVTLHTHLSVAEMISHYKNSlAVFFAP-YDEDYGYVTLEAMLAEKAVITcNDSGGTN 289
Cdd:cd03801   228 IVGGdGPLRAELEEL--ELGLGDRVRFLGFVPDEELPALYAAA-DVFVLPsRYEGFGLVVLEAMAAGLPVVA-TDVGGLP 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 290 EFVVHDHTGYI-EPPEAEQIAARLDALFMDRNLAVSIGQNALHHYQSLsLSWDNVLNQLL 348
Cdd:cd03801   304 EVVEDGEGGLVvPPDDVEALADALLRLLADPELRARLGRAARERVAER-FSWERVAERLL 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 181-329 3.16e-27

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: 105.05  E-value: 3.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 181 FIFAPSRFEPLKRQHLLLEALRL---TKHPVKAVLCGSGSYEHHLRNFVVHYGLQDRVTLHTHLSVAEMISHYKNSLAVF 257
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALlkeKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2544592186 258 FAPYDEDYGYVTLEAMLAEKAVITcNDSGGTNEFVVHDHTGY-IEPPEAEQIAARLDALFMDRNLAVSIGQNA 329
Cdd:pfam00534  84 LPSRYEGFGIVLLEAMACGLPVIA-SDVGGPPEVVKDGETGFlVKPNNAEALAEAIDKLLEDEELRERLGENA 155
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 158-329 2.04e-19

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: 87.80  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 158 PLYHPPALANAFAmdDTQAETGDFIFA-PSRFEPLKRQHLLLEALRLTKH--PVKAVLCGSGSYEHHLRNFVVHYGLQDR 234
Cdd:cd03819   162 DRFPPEAEAEERA--QLGLPEGKPVVGyVGRLSPEKGWLLLVDAAAELKDepDFRLLVAGDGPERDEIRRLVERLGLRDR 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 235 VTLHTHLSvaEMISHYKNSLAVFFAPYDEDYGYVTLEAMLAEKAVITcNDSGGTNEFVVHDHTGYIEPP-EAEQIAARLD 313
Cdd:cd03819   240 VTFTGFRE--DVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVA-TDVGGAREIVVHGRTGLLVPPgDAEALADAIR 316

                         170
                  ....*....|....*.
gi 2544592186 314 ALFMDRNLAVSIGQNA 329
Cdd:cd03819   317 AAKLLPEAREKLQAAA 332
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 2-337 7.27e-18

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: 83.56  E-value: 7.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIVTTlaPFIKGGAEYLAANLAQACSAAGHQVDIF------KLPFLDSSADSIQKSmDLCLQEDFSLWGQQA------ 69
Cdd:cd03811     1 KILFVIP--SLSGGGAERVLLNLANALDKRGYDVTLVllrdegDLDKQLNGDVKLIRL-LIRVLKLIKLGLLKAilklkr 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  70 -------DLVIC-LKFPAYYVQHPCKIMWVLHQHRsaydlwdHAAAQGHTYSTEDIALREQIMAL-DKRVFNS------A 134
Cdd:cd03811    78 ilkrakpDVVISfLGFATYIVAKLAAARSKVIAWI-------HSSLSKLYYLKKKLLLKLKLYKKaDKIVCVSkgikedL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 135 LQNFTISKtvsNRLKH-YNHIESsplyhPPALANAFAMDDTQAETGDFIFAPSRFEPLKRQHLLLEAL-RLTKH--PVKA 210
Cdd:cd03811   151 IRLGPSPP---EKIEViYNPIDI-----DRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFaKLRKKypDVKL 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 211 VLCGSGSYEHHLRNFVVHYGLQDRVTLHTHLS-VAemiSHYKNSLAVFFAPYDEDYGYVTLEAMLAEKAVITcNDSGGTN 289
Cdd:cd03811   223 VILGDGPLREELEKLAKELGLAERVIFLGFQSnPY---PYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVS-TDCPGPR 298

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2544592186 290 EFVVHDHTGYIEPPEAEQIAARLDALFMDRNLAVSIGQNALHHYQSLS 337
Cdd:cd03811   299 EILDDGENGLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVF 346
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 169-329 2.32e-16

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: 79.18  E-value: 2.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 169 FAMDDTQAETGDFIFA-PSRFEPLKRQHLLLEALRLTKH---PVKAVLCGSGSYEHHLRNFVVHYGLQDRVTLHTHLS-V 243
Cdd:cd03808   178 FQYSPESLPSEKVVFLfVARLLKDKGIDELIEAAKILKKkgpNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSdV 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 244 AEMISHYKnslaVFFAP-YDEDYGYVTLEAMLAEKAVITcNDSGGTNEFVVHDHTGYIEPP-EAEQIAARLDALFMDRNL 321
Cdd:cd03808   258 PELLAESD----VFVLPsYREGLPRSLLEAMAAGRPVIT-TDVPGCRELVIDGVNGFLVPPgDVEALADAIEKLIEDPEL 332


                  ....*...
gi 2544592186 322 AVSIGQNA 329
Cdd:cd03808   333 RKEMGEAA 340
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 186-330 2.58e-16

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: 79.25  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 186 SRFEPLKRQHLLLEALR--LTKHPVKAVLCGSGSYEHHLRNFVVHYGLQDRVTLHTHLSVAEMISHYKNSLAVFFAPYDE 263
Cdd:cd03817   208 GRLAKEKNIDFLLRAFAelKKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTE 287

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544592186 264 DYGYVTLEAMLAEKAVItCNDSGGTNEFVVHDHTGYIEPPEAEQIAARLDALFMDRNLAVSIGQNAL 330
Cdd:cd03817   288 TQGLVYLEAMAAGLPVV-AAKDPAASELVEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAE 353
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 127-329 3.85e-16

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: 78.78  E-value: 3.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 127 DKRVFNSalqNFTiSKTVSNRLKHYNHIESSPLYhPPALANAFAMDDTQAETGDFIFAPS--------RFEPLKRQHLLL 198
Cdd:cd03805   156 DQIVVNS---NFT-AGVFKKTFPSLAKNPPEVLY-PCVDTDSFDSTSEDPDPGDLIAKSNkkfflsinRFERKKNIALAI 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 199 EALRLTK------HPVKAVLCGSgsYEHHLRNFVVHY-----------GLQDRVTLHTHLSVAEMISHYKNSLAVFFAPY 261
Cdd:cd03805   231 EAFAKLKqklpefENVRLVIAGG--YDPRVAENVEYLeelqrlaeellNVEDQVLFLRSISDSQKEQLLSSALALLYTPS 308

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2544592186 262 DEDYGYVTLEAMLAEKAVITCNdSGGTNEFVVHDHTGYIEPPEAEQIAARLDALFMDRNLAVSIGQNA 329
Cdd:cd03805   309 NEHFGIVPLEAMYAGKPVIACN-SGGPLETVVEGVTGFLCEPTPEAFAEAMLKLANDPDLADRMGAAG 375
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 187-312 5.34e-16

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: 78.19  E-value: 5.34e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 187 RFEPLKRQHLLLEAL-RLTK-HP-VKAVLCGSGSYEHHLRNFVVHYGLQDRVTLHTHLSVAEMISHYkNSLAVFFAP-YD 262
Cdd:cd03798   208 RLIPRKGIDLLLEAFaRLAKaRPdVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYY-RACDVFVLPsRH 286

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2544592186 263 EDYGYVTLEAMLAEKAVItCNDSGGTNEFVVHDHTGYIEPPE-AEQIAARL 312
Cdd:cd03798   287 EGFGLVLLEAMACGLPVV-ATDVGGIPEVVGDPETGLLVPPGdADALAAAL 336
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 2-346 4.57e-15

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: 75.35  E-value: 4.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIV-TTLAPfiKGGAEYLAANLAQACSAAGHQVDIF------KLPF--LDSS------ADSIQKSMDLCLQEDFSLWG 66
Cdd:cd03820     1 KIAIViPSISN--AGGAERVAINLANHLAKKGYDVTIIsldsaeKPPFyeLDDNikiknlGDRKYSHFKLLLKYFKKVRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  67 -------QQADLVI-----CLKFPAYYvQHPCK-IMWVlHQHRSAYdlwdhaaaqgHTYSTEDIALREQIMALDKRVfns 133
Cdd:cd03820    79 lrkylknNKPDVVIsfrtsLLTFLALI-GLKSKlIVWE-HNNYEAY----------NKGLRRLLLRRLLYKRADKIV--- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 134 ALQNFTISKTVSNRLKH----YNhiessPLyHPPALANAFAMDDTQaetgdfIFAPSRFEPLKRQHLLLEALRL--TKHP 207
Cdd:cd03820   144 VLTEADKLKKYKQPNSNvvviPN-----PL-SFPSEEPSTNLKSKR------ILAVGRLTYQKGFDLLIEAWALiaKKHP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 208 -VKAVLCGSGSYEHHLRNFVVHYGLQDRVTLHThlSVAEMISHYKNSlAVF-FAPYDEDYGYVTLEAMLAEKAVITCNDS 285
Cdd:cd03820   212 dWKLRIYGDGPEREELEKLIDKLGLEDRVKLLG--PTKNIAEEYANS-SIFvLSSRYEGFPMVLLEAMAYGLPIISFDCP 288

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2544592186 286 GGTNEFVVHDHTGYIEPPE-AEQIAARLDALFMDRNLAVSIGQNALH---HYqslslSWDNVLNQ 346
Cdd:cd03820   289 TGPSEIIEDGENGLLVPNGdVDALAEALLRLMEDEELRKKMGKNARKnaeRF-----SIEKIIKQ 348
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 249-348 3.28e-14

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 68.48  E-value: 3.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 249 HYKNSLAVFFAPYDEDYGYVTLEAMLAEKAVITCnDSGGTNEFVVHDHTGY-IEPPEAEQIAARLDALFMDRNLAVSIGQ 327
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAT-DVGGLPEVIEDGETGLlVPPGDPEALAEAILRLLEDPELRRRLGE 95

                          90       100
                  ....*....|....*....|.
gi 2544592186 328 NALHHYQSlSLSWDNVLNQLL 348
Cdd:COG0438    96 AARERAEE-RFSWEAIAERLL 115
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
182-318 1.84e-13

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 66.77  E-value: 1.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 182 IFAPSRF-EPLKRQHLLLEA---LRLTKHPVKAVLCGSGSYEHhLRNFVVhyGLQDRVTLHTHlsVAEMISHYKNSlAVF 257
Cdd:pfam13692   4 ILFVGRLhPNVKGVDYLLEAvplLRKRDNDVRLVIVGDGPEEE-LEELAA--GLEDRVIFTGF--VEDLAELLAAA-DVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2544592186 258 FAPYD-EDYGYVTLEAMLAEKAVITcNDSGGTNEfVVHDHTGY-IEPPEAEQIAARLDALFMD 318
Cdd:pfam13692  78 VLPSLyEGFGLKLLEAMAAGLPVVA-TDVGGIPE-LVDGENGLlVPPGDPEALAEAILRLLED 138
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 175-333 1.54e-12

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: 67.68  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 175 QAETGDFIFAPSRFEPLKRQHLLLEALRLTKHPVkaVLCGSGSYEHHLRNFVvHYGLQDRVTLHTHLSVAEMISHYKNSL 254
Cdd:cd03795   187 EKKGKKIFLFIGRLVYYKGLDYLIEAAQYLNYPI--VIGGEGPLKPDLEAQI-ELNLLDNVKFLGRVDDEEKVIYLHLCD 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 255 AVFFAPY--DEDYGYVTLEAMLAEKAVITCNDSGGTNEFVVHDHTGYIEPPE-AEQIAARLDALFMDRNLAVSIGQNALH 331
Cdd:cd03795   264 VFVFPSVlrSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPKdPDALAEAIDKLLSDEELRESYGENAKK 343


                  ..
gi 2544592186 332 HY 333
Cdd:cd03795   344 RF 345
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 182-348 7.44e-12

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: 65.72  E-value: 7.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 182 IFAPSRFEPLKRQHLLLEA---LRLTKHPVKAVLCGSGSYE------HHLRNFVVHYGLQDRVTLHTHLSVAEMiSHYKN 252
Cdd:cd03800   223 VLALGRLDPRKGIDTLVRAfaqLPELRELANLVLVGGPSDDplsmdrEELAELAEELGLIDRVRFPGRVSRDDL-PELYR 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 253 SLAVFFAP-YDEDYGYVTLEAMLAEKAVI-TCNdsGGTNEFVVHDHTGY-IEPPEAEQIAARLDALFMDRNLAVSIGQNA 329
Cdd:cd03800   302 AADVFVVPsLYEPFGLTAIEAMACGTPVVaTAV--GGLQDIVRDGRTGLlVDPHDPEALAAALRRLLDDPALWQRLSRAG 379

                         170
                  ....*....|....*....
gi 2544592186 330 LHHYQSLsLSWDNVLNQLL 348
Cdd:cd03800   380 LERARAH-YTWESVADQLL 397
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 151-332 8.31e-12

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: 65.42  E-value: 8.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 151 YNHIESSPLYHPPALANAFAMDDTQAETGDFIFAPSRFEPLKRQHLLLEALRL--TKHP-VKAVLCGSGSYEHHLRNFVV 227
Cdd:cd03807   162 YNGIDLFKLSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALlvETHPdLRLLLVGRGPERPNLERLLL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 228 HYGLQDRVTLhthLSVAEMISHYKNSLAVFFAPYD-EDYGYVTLEAMLAEKAVITcNDSGGtNEFVVHDHTGYIEPPEAE 306
Cdd:cd03807   242 ELGLEDRVHL---LGERSDVPALLPAMDIFVLSSRtEGFPNALLEAMACGLPVVA-TDVGG-AAELVDDGTGFLVPAGDP 316

                         170       180
                  ....*....|....*....|....*..
gi 2544592186 307 Q-IAARLDALFMDRNLAVSIGQNALHH 332
Cdd:cd03807   317 QaLADAIRALLEDPEKRARLGRAARER 343
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 185-300 1.71e-10

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: 60.50  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 185 PSRFEPLKRQHLLLEALRL---TKHPVKAVLCGSGSYEHHLRNFVVHYGLQDRVTLHTHLSVAEMISHYKNSLAVFFAP- 260
Cdd:cd01635   116 VGRLVPEKGIDLLLEALALlkaRLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPs 195

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2544592186 261 YDEDYGYVTLEAMLAEKAVItCNDSGGTNEFVVHDHTGYI 300
Cdd:cd01635   196 RSEGFGLVLLEAMAAGKPVI-ATDVGGIPEFVVDGENGLL 234
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 90-298 2.81e-10

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: 60.76  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  90 WVLHQHRsaydLWDHAAAQGhtystedialreqimaLDKRVFNSALqnftisktVSNRLKHYNHIESSPLYhPPALANAF 169
Cdd:cd03804   142 LFLHYLR----LWDVRTAQR----------------VDLFIANSQF--------VARRIKKFYGRESTVIY-PPVDTDAF 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 170 AMddtQAETGDFIFAPSRFEPLKRQHLLLEALRltKHPVKAVLCGSGSYEHHLRNFvvhygLQDRVTLHTHLSVAEMISH 249
Cdd:cd03804   193 AP---AADKEDYYLTASRLVPYKRIDLAVEAFN--ELPKRLVVIGDGPDLDRLRAM-----ASPNVEFLGYQPDEVLKEL 262

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2544592186 250 YKNSLAvFFAPYDEDYGYVTLEAMLAEKAVItCNDSGGTNEFVVHDHTG 298
Cdd:cd03804   263 LSKARA-FVFAAEEDFGIVPVEAQACGTPVI-AFGKGGALETVRPGPTG 309
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 169-348 5.50e-10

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: 60.00  E-value: 5.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 169 FAMDDTQAETGDFIF-APSRFEPLKRQHLLLEA-LRLTKH-PVKAVLCGSGSYEHHL--RNFVVHY-GLQDRVTLHTHLS 242
Cdd:cd03814   187 AALRRRLGPPGRPLLlYVGRLAPEKNLEALLDAdLPLAASpPVRLVVVGDGPARAELeaRGPDVIFtGFLTGEELARAYA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 243 VAEmishyknslaVFFAPYD-EDYGYVTLEAMLAEKAVItCNDSGGTNEFVVHDHTGYIEPP-EAEQIAARLDALFMDRN 320
Cdd:cd03814   267 SAD----------VFVFPSRtETFGLVVLEAMASGLPVV-AADAGGPRDIVRPGGTGALVEPgDAAAFAAALRALLEDPE 335

                         170       180
                  ....*....|....*....|....*...
gi 2544592186 321 LAVSIGQNALHHyqSLSLSWDNVLNQLL 348
Cdd:cd03814   336 LRRRMAARARAE--AERYSWEAFLDNLL 361
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 70-348 1.06e-08

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: 56.22  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  70 DLVICLKFPAYYVQHPCK-IMWVlhqhrsaYDLW--DHAaaqgHTYSTEDIALREQIMaldKRVFNSALQNFTISKTVSN 146
Cdd:cd03809    86 DLLHSPHNTAPLLLKGCPqVVTI-------HDLIplRYP----EFFPKRFRLYYRLLL---PISLRRADAIITVSEATRD 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 147 RLKHY-----NHI-----ESSPLYHPPALANAFAmdDTQAETGDFIFAPSRFEPLKRQHLLLEA---LRLTKHPVKAVL- 212
Cdd:cd03809   152 DIIKFygvppEKIvviplGVDPSFFPPESAAVLI--AKYLLPEPYFLYVGTLEPRKNHERLLKAfalLKKQGGDLKLVIv 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 213 CGSGSYEHHLRNFVVHYGLQDRVTLHTHLSVAEMISHYKNSLAVFFAPYDEDYGYVTLEAMLAEKAVITCNdsGGTNEFV 292
Cdd:cd03809   230 GGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASN--ISVLPEV 307

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2544592186 293 VHDHTGYIEPPEAEQIAARLDALFMD---RNLAVSIGQNALHHYqslslSWDNVLNQLL 348
Cdd:cd03809   308 AGDAALYFDPLDPESIADAILRLLEDpslREELIRKGLERAKKF-----SWEKTAEKTL 361
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 186-330 1.83e-08

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: 55.44  E-value: 1.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 186 SRFEPLKRQHLLLEALRL--TKHPVKAVLCGSGSYEHHLRNFVVHYGLQDRVTLhthLSVAEMISHYKNSLAVFFAP-YD 262
Cdd:cd04962   203 SNFRPVKRIDDVVRVFARvrRKIPAKLLLVGDGPERVPAEELARELGVEDRVLF---LGKQDDVEELLSIADLFLLPsEK 279

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544592186 263 EDYGYVTLEAMLAEKAVITCNdSGGTNEFVVHDHTGYIEPP-EAEQIAARLDALFMDRNLAVSIGQNAL 330
Cdd:cd04962   280 ESFGLAALEAMACGVPVVSSN-AGGIPEVVKHGETGFLSDVgDVDAMAKSALSILEDDELYNRMGRAAR 347
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 2-330 5.19e-08

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 53.87  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIVTTL-APFIKGGAEYLAANLAQACSAAGHQV---------------DIFKLPFLDSSADSIQKSMDLCLQEDFSLW 65
Cdd:cd03823     1 KILLVNSLyPPQRVGGAEISVHDLAEALVAEGHEVavltagvgppgqatvARSVVRYRRAPDETLPLALKRRGYELFETY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  66 gQQADLVICLKFPAYYVQHpckimwVLHQHRS---AYDLWDHAAAQG----HTystediaLRE-------QIMAL---DK 128
Cdd:cd03823    81 -NPGLRRLLARLLEDFRPD------VVHTHNLsglGASLLDAARDLGipvvHT-------LHDywllcprQFLFKkggDA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 129 RVFNSA------LQNFTISKTVSnrlKHYNHIESsPLYHPPALANAfamddtqAETGDFIFApSRFEPLKRQHLLLEA-L 201
Cdd:cd03823   147 VLAPSRftanlhEANGLFSARIS---VIPNAVEP-DLAPPPRRRPG-------TERLRFGYI-GRLTEEKGIDLLVEAfK 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 202 RLTKHPVKAVLCGSGSyEHHLRnfvvHYGLQDRVTLHTHLSVAEMISHYKNsLAVFFAP--YDEDYGYVTLEAMLAEKAV 279
Cdd:cd03823   215 RLPREDIELVIAGHGP-LSDER----QIEGGRRIAFLGRVPTDDIKDFYEK-IDVLVVPsiWPEPFGLVVREAIAAGLPV 288

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2544592186 280 ItCNDSGGTNEFVVHDHTGYIEPPE-AEQIAARLDALFMDRNLAVSIGQNAL 330
Cdd:cd03823   289 I-ASDLGGIAELIQPGVNGLLFAPGdAEDLAAAMRRLLTDPALLERLRAGAE 339
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 130-328 8.93e-07

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


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 50.14  E-value: 8.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 130 VFNSALQNFtISKTVSNRLKH---YNHIESSPLYHPP----ALANAFAMDDTQAetgdFIFAPSRFEPLKRQHLLLEALR 202
Cdd:cd04951   137 VSREALDEF-IAKKAFSKNKSvpvYNGIDLNKFKKDInvrlKIRNKLNLKNDEF----VILNVGRLTEAKDYPNLLLAIS 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 203 ---LTKHPVKAVLCGSGSYEHHLRNFVVHYGLQDRVTLhthLSVAEMISHYKNSLAVFFAPYD-EDYGYVTLEAMLAEKA 278
Cdd:cd04951   212 eliLSKNDFKLLIAGDGPLRNELERLICNLNLVDRVIL---LGQISNISEYYNAADLFVLSSEwEGFGLVVAEAMACERP 288

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2544592186 279 VITcNDSGGTNEfVVHDHTGYIEPPEAEQIAARLDALF-MDRNLAVSIGQN 328
Cdd:cd04951   289 VVA-TDAGGVAE-VVGDHNYVVPVSDPQLLAEKIKEIFdMSDEERDILGNK 337
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 2-319 9.21e-07

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: 49.98  E-value: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIVTTLAPFIK----GGAEYLAANLAQACSAAGHQVDIFklpfldSSADSI-QKSMDLCLQEDFSLWGQQADLVICLK 76
Cdd:cd03802     1 RIAQVSPPRGPVPpgkyGGTELVVSALTEGLVRRGHEVTLF------APGDSHtSAPLVAVIPRALRLDPIPQESKLAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  77 FPAYYVQHPCKIMWVLHQHrsaYDLWDHAAAQG-HTYSTEDIALREQIMALDKRVFNSalQNFTISKTVSNRLKHYNHIE 155
Cdd:cd03802    75 LEALEVQLRASDFDVIHNH---SYDWLPPFAPLiGTPFVTTLHGPSIPPSLAIYAAEP--PVNYVSISDAQRAATPPIDY 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 156 SSPLYHPPALAnafamddtqaetgDFIFAP---------SRFEPLKRQHLLLEALRLTKHPVKavLCGSGSYEHHLRnFV 226
Cdd:cd03802   150 LTVVHNGLDPA-------------DYRFQPdpedylaflGRIAPEKGLEDAIRVARRAGLPLK--IAGKVRDEDYFY-YL 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 227 VHYGLQDRVTLHTHLSVAEMISHYKNSLAVFFAP-YDEDYGYVTLEAMLAEKAVITCNdSGGTNEFVVHDHTGYIEPPEA 305
Cdd:cd03802   214 QEPLPGPRIEFIGEVGHDEKQELLGGARALLFPInWDEPFGLVMIEAMACGTPVIAYR-RGGLPEVIQHGETGFLVDSVE 292

                         330
                  ....*....|....*.
gi 2544592186 306 EQIAA--RLDALfmDR 319
Cdd:cd03802   293 EMAEAiaNIDRI--DR 306
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 2-348 5.69e-06

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 47.75  E-value: 5.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186   2 RIAIVTTLAPFIKGGAEYLAANLAQACSAAGHQVDIFklpFLDSSADSIQKSMDLCLQEDFSLWGQ-------------- 67
Cdd:cd03821     1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIV---STGDGYESLVVEENGRYIPPQDGFASipllrqgagrtdfs 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186  68 ------------QADLVIC---LKFPAYYVQHPC---KIMWVLHQHrSAYDLWDHAAAQGHtysteDIALREQIMalDKR 129
Cdd:cd03821    78 pglpnwlrrnlrEYDVVHIhgvWTYTSLAACKLArrrGIPYVVSPH-GMLDPWALQQKHWK-----KRIALHLIE--RRN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 130 VFNSALQNFTISKTVSN--RLKHYNHIE------SSPLYHPpalANAFAMDDTQAETGDFIFAPSRFEPLKRQHLLLEAL 201
Cdd:cd03821   150 LNNAALVHFTSEQEADElrRFGLEPPIAvipngvDIPEFDP---GLRDRRKHNGLEDRRIILFLGRIHPKKGLDLLIRAA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 202 RLTKHP---VKAVLCGSGSYEH-HLRNFVVHYGLQDRVTLHTHLSVAEMISHYKNSLAVFFAPYDEDYGYVTLEAMLAEK 277
Cdd:cd03821   227 RKLAEQgrdWHLVIAGPDDGAYpAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGL 306

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2544592186 278 AVITCNDSGGTNEFVVHDhtGYIEPPEAEQIAARLDALFMDRNLAVSIGQNALHHYQSLSL-SWDNVLNQLL 348
Cdd:cd03821   307 PVVITDKCGLSELVEAGC--GVVVDPNVSSLAEALAEALRDPADRKRLGEMARRARQVEENfSWEAVAGQLG 376
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
182-346 1.94e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 45.94  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 182 IFAPSRFEPLKRQHLLLEA---LRLTKHPVKAVLCG---------SGSYEHHLRNfvvhygLQDRVTLHTHL----SVAE 245
Cdd:PRK15484  196 LLYAGRISPDKGILLLMQAfekLATAHSNLKLVVVGdptasskgeKAAYQKKVLE------AAKRIGDRCIMlggqPPEK 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 246 MISHYK-NSLAVFFAPYDEDYGYVTLEAMLAEKAVITcNDSGGTNEFVVHDHTGY--IEPPEAEQIAARLDALFMDRNLA 322
Cdd:PRK15484  270 MHNYYPlADLVVVPSQVEEAFCMVAVEAMAAGKPVLA-STKGGITEFVLEGITGYhlAEPMTSDSIISDINRTLADPELT 348

                         170       180
                  ....*....|....*....|....*...
gi 2544592186 323 vSIGQNA----LHHYqslslSWDNVLNQ 346
Cdd:PRK15484  349 -QIAEQAkdfvFSKY-----SWEGVTQR 370
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 256-329 8.73e-05

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


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 43.86  E-value: 8.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2544592186 256 VFFAP-YDEDYGYVTLEAMLAEKAVItCNDSGGTNEFVVHDHTGYIEPP-EAEQIAARLDALFMDRNLAVSIGQNA 329
Cdd:cd03825   266 LFVHPsLADNLPNTLLEAMACGTPVV-AFDTGGSPEIVQHGVTGYLVPPgDVQALAEAIEWLLANPKERESLGERA 340
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 197-348 3.89e-04

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: 41.94  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 197 LLEALRLTKH--PVKAVLCGSGSYEHHLRNF--------VVHYGLQDRVTLHTHLSVAEmishyknslaVFFAPYDED-- 264
Cdd:cd03794   235 LLEAAERLKRrpDIRFLFVGDGDEKERLKELakargldnVTFLGRVPKEEVPELLSAAD----------VGLVPLKDNpa 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 265 YGYV----TLEAMLAEKAVItCNDSGGTNEFVVHDHTGYI-EPPEAEQIAARLDALFMDRNLAVSIGQNAlHHYQSLSLS 339
Cdd:cd03794   305 NRGSspskLFEYMAAGKPIL-ASDDGGSDLAVEINGCGLVvEPGDPEALADAILELLDDPELRRAMGENG-RELAEEKFS 382


                  ....*....
gi 2544592186 340 WDNVLNQLL 348
Cdd:cd03794   383 REKLADRLL 391
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 186-332 4.70e-04

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


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 41.54  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 186 SRFEPLKRQHLLLEALRL----TKHPvKAVLCGSGS---------YEHHLRN-------FVVHYGLQDRVtLHTHLSVAE 245
Cdd:cd03792   204 ARFDPSKDPLGVIDAYKLfkrrAEEP-QLVICGHGAvddpegsvvYEEVMEYagddhdiHVLRLPPSDQE-INALQRAAT 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 246 MISHykNSLAvffapydEDYGYVTLEAMLAEKAVITCNdSGGTNEFVVHDHTGYIEPPEAEQiAARLDALFMDRNLAVSI 325
Cdd:cd03792   282 VVLQ--LSTR-------EGFGLTVSEALWKGKPVIATP-AGGIPLQVIDGETGFLVNSVEGA-AVRILRLLTDPELRRKM 350


                  ....*..
gi 2544592186 326 GQNALHH 332
Cdd:cd03792   351 GLAAREH 357
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 186-337 9.55e-04

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: 40.75  E-value: 9.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544592186 186 SRFEPLKRQHLLLEALRLTKHPVKAV---LCGSGSYEHHLRNFVVHYGLQDRVTLHT-HLSVAEMISHYKNSLAvffAPY 261
Cdd:cd04949   167 SRLAPEKQLDHLIEAVAKAVKKVPEItldIYGYGEEREKLKKLIEELHLEDNVFLKGyHSNLDQEYQDAYLSLL---TSQ 243

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2544592186 262 DEDYGYVTLEAMLAEKAVITCNDSGGTNEFVVHDHTGY-IEPPEAEQIAARLDALFMDRNLAVSIGQNALHHYQSLS 337
Cdd:cd04949   244 MEGFGLTLMEAIGHGLPVVSYDVKYGPSELIEDGENGYlIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKYS 320
 
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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