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Conserved domains on  [gi|1962964333|ref|WP_202069898|]
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glycosyltransferase family 4 protein [Rickettsia tillamookensis]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133614)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
15-368 3.54e-119

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: 349.35  E-value: 3.54e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPALVSGGVERGTIEVAKYLKILGHTPIIISAGGTLVKELDKEDIlhiEMNSSSKNPFVILNNAKLIAEIIKKYNV 94
Cdd:cd03819     1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGI---GLPGLKVPLLRALLGNVRLARLIRRERI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  95 DIVHTRSRAPAWSSYLATKWTNAKFLTTFHGVYNIPNSFKKYYNSIMLKGEKVIAVSNFVKQHLLENYKIDEDKIVVIER 174
Cdd:cd03819    78 DLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPERIRVIPN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 175 GVNCDYFDPANLTPEklkkcRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKH-RDFYCLMVGDISRHPNFTNRVk 253
Cdd:cd03819   158 GVDTDRFPPEAEAEE-----RAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDePDFRLLVAGDGPERDEIRRLV- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 254 eliAALKLQNKIQIFGNDSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNN 333
Cdd:cd03819   232 ---ERLGLRDRVTFTGFREDVPAALAASDVVVLPSLH-EEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGD 307
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1962964333 334 AEALAEKIDYCfsILGTDTAKKIQEAA---RHTVINNF 368
Cdd:cd03819   308 AEALADAIRAA--KLLPEAREKLQAAAaltEAVRELLL 343
 
Name Accession Description Interval E-value
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
15-368 3.54e-119

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: 349.35  E-value: 3.54e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPALVSGGVERGTIEVAKYLKILGHTPIIISAGGTLVKELDKEDIlhiEMNSSSKNPFVILNNAKLIAEIIKKYNV 94
Cdd:cd03819     1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGI---GLPGLKVPLLRALLGNVRLARLIRRERI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  95 DIVHTRSRAPAWSSYLATKWTNAKFLTTFHGVYNIPNSFKKYYNSIMLKGEKVIAVSNFVKQHLLENYKIDEDKIVVIER 174
Cdd:cd03819    78 DLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPERIRVIPN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 175 GVNCDYFDPANLTPEklkkcRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKH-RDFYCLMVGDISRHPNFTNRVk 253
Cdd:cd03819   158 GVDTDRFPPEAEAEE-----RAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDePDFRLLVAGDGPERDEIRRLV- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 254 eliAALKLQNKIQIFGNDSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNN 333
Cdd:cd03819   232 ---ERLGLRDRVTFTGFREDVPAALAASDVVVLPSLH-EEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGD 307
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1962964333 334 AEALAEKIDYCfsILGTDTAKKIQEAA---RHTVINNF 368
Cdd:cd03819   308 AEALADAIRAA--KLLPEAREKLQAAAaltEAVRELLL 343
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
205-362 2.89e-30

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: 113.91  E-value: 2.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 205 PIILMPSRMTSWKGHLVLVEALSKLK--HRDFYCLMVGDisrhPNFTNRVKELIAALKLQNKIQIFG--NDSDIINLYGI 280
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGD----GEEEKRLKKLAEKLGLGDNVIFLGfvSDEDLPELLKI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 281 SDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYCfsILGTDTAKKIQEAA 360
Cdd:pfam00534  79 ADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL--LEDEELRERLGENA 155

                  ..
gi 1962964333 361 RH 362
Cdd:pfam00534 156 RK 157
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
277-386 9.23e-22

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 89.66  E-value: 9.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 277 LYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYCFSIlgTDTAKKI 356
Cdd:COG0438    17 LLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED--PELRRRL 93
                          90       100       110
                  ....*....|....*....|....*....|
gi 1962964333 357 QEAARHTVINNFSLDLMLRKNLEVYKEILK 386
Cdd:COG0438    94 GEAARERAEERFSWEAIAERLLALYEELLA 123
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
78-371 7.67e-14

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 72.13  E-value: 7.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  78 ILNNAKLIAeiIKKYNVDIVHT--------RSRAPawssylatkwtNAKFLTTFHgvynipNSFKKyynSIMLKGEKVIA 149
Cdd:PRK15484   88 ILNIAHKFT--ITKDSVIVIHNsmklyrqiRERAP-----------QAKLVMHMH------NAFEP---ELLDKNAKIIV 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 150 VSNFVKQHLlENYKIDEDkIVVIERGvncdyFDPANLTPEKLKKCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKL 229
Cdd:PRK15484  146 PSQFLKKFY-EERLPNAD-ISIVPNG-----FCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 230 --KHRDFYCLMVGDI-----SRHPNFTNRVKELIAALKLQNkIQIFGNDSDII-NLYGISDIIVSASIEPEAFGRTIIEG 301
Cdd:PRK15484  219 atAHSNLKLVVVGDPtasskGEKAAYQKKVLEAAKRIGDRC-IMLGGQPPEKMhNYYPLADLVVVPSQVEEAFCMVAVEA 297
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1962964333 302 QAMEKLVIATNIGGAVETINNNITGFHV-EPNNAEALAEKIDycfSILGTDTAKKIQEAARHTVINNFSLD 371
Cdd:PRK15484  298 MAAGKPVLASTKGGITEFVLEGITGYHLaEPMTSDSIISDIN---RTLADPELTQIAEQAKDFVFSKYSWE 365
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
255-339 1.09e-03

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 41.30  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  255 LIAALKLQNKIQIFG--------NDSDIINLYGISD-----IIVSASIEPeaFGRTIIEGQAMEKLVIATNIGGAVETIN 321
Cdd:TIGR02468  534 LTSVLKLIDKYDLYGqvaypkhhKQSDVPDIYRLAAktkgvFINPAFIEP--FGLTLIEAAAHGLPMVATKNGGPVDIHR 611
                           90       100
                   ....*....|....*....|
gi 1962964333  322 --NNitGFHVEPNNAEALAE 339
Cdd:TIGR02468  612 vlDN--GLLVDPHDQQAIAD 629
 
Name Accession Description Interval E-value
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
15-368 3.54e-119

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: 349.35  E-value: 3.54e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPALVSGGVERGTIEVAKYLKILGHTPIIISAGGTLVKELDKEDIlhiEMNSSSKNPFVILNNAKLIAEIIKKYNV 94
Cdd:cd03819     1 ILMLTPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGI---GLPGLKVPLLRALLGNVRLARLIRRERI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  95 DIVHTRSRAPAWSSYLATKWTNAKFLTTFHGVYNIPNSFKKYYNSIMLKGEKVIAVSNFVKQHLLENYKIDEDKIVVIER 174
Cdd:cd03819    78 DLIHAHSRAPAWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRARGDRVIAVSELVRDHLIEALGVDPERIRVIPN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 175 GVNCDYFDPANLTPEklkkcRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKH-RDFYCLMVGDISRHPNFTNRVk 253
Cdd:cd03819   158 GVDTDRFPPEAEAEE-----RAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAAAELKDePDFRLLVAGDGPERDEIRRLV- 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 254 eliAALKLQNKIQIFGNDSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNN 333
Cdd:cd03819   232 ---ERLGLRDRVTFTGFREDVPAALAASDVVVLPSLH-EEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGD 307
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1962964333 334 AEALAEKIDYCfsILGTDTAKKIQEAA---RHTVINNF 368
Cdd:cd03819   308 AEALADAIRAA--KLLPEAREKLQAAAaltEAVRELLL 343
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
15-382 1.35e-59

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: 197.38  E-value: 1.35e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPAL--VSGGVERGTIEVAKYLKILGHTPIIISAGGTLVKELDKEDILHIEMNsssKNPFVILNNAKLIAEI---I 89
Cdd:cd03801     2 ILLLSPELppPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLL---PSLAALLRARRLLRELrplL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  90 KKYNVDIVHTRSRAPAWSSYLATKWTNAKFLTTFHG--------VYNIPNSFKKYYNSIMLKGEKVIAVSNFVKQHLLEN 161
Cdd:cd03801    79 RLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGaepgrlllLLAAERRLLARAEALLRRADAVIAVSEALRDELRAL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 162 YKIDEDKIVVIERGVNCDYFDPAnltpeklkkCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKHR--DFYCLMV 239
Cdd:cd03801   159 GGIPPEKIVVIPNGVDLERFSPP---------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRgpDVRLVIV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 240 GdisRHPNFTNRVKELiaALKLQNKIQIFG--NDSDIINLYGISDIIVSASIePEAFGRTIIEGQAMEKLVIATNIGGAV 317
Cdd:cd03801   230 G---GDGPLRAELEEL--ELGLGDRVRFLGfvPDEELPALYAAADVFVLPSR-YEGFGLVVLEAMAAGLPVVATDVGGLP 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1962964333 318 ETINNNITGFHVEPNNAEALAEKIdyCFSILGTDTAKKIQEAARHTVINNFSLDLMLRKNLEVYK 382
Cdd:cd03801   304 EVVEDGEGGLVVPPDDVEALADAL--LRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
14-382 3.35e-47

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: 164.80  E-value: 3.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  14 TILQVVPALVSGGVERGTIEVAKYLKILGHTPIIISAG--GTLVKELDKE--DILHIEMNSSsKNPFVILnnaKLIAeII 89
Cdd:cd03807     1 KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVVISLTgdGVLGEELLAAgvPVVCLGLSSG-KDPGVLL---RLAK-LI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  90 KKYNVDIVHTRSRAPAWSSYLATKW-TNAKFLTTFHGVyNIPNSFKKYYNSIMLKGEK----VIAVSNFVKQhLLENYKI 164
Cdd:cd03807    76 RKRNPDVVHTWMYHADLIGGLAAKLaGGVKVIWSVRSS-NIPQRLTRLVRKLCLLLSKfspaTVANSSAVAE-FHQEQGY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 165 DEDKIVVIERGVNCDYFDPanlTPEKLKKCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLK--HRDFYCLMVGDI 242
Cdd:cd03807   154 AKNKIVVIYNGIDLFKLSP---DDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVetHPDLRLLLVGRG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 243 SRHPNftnrVKELIAALKLQNKIQIFGNDSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINN 322
Cdd:cd03807   231 PERPN----LERLLLELGLEDRVHLLGERSDVPALLPAMDIFVLSSRT-EGFPNALLEAMACGLPVVATDVGGAAELVDD 305
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 323 NiTGFHVEPNNAEALAEKIDYCfsILGTDTAKKIQEAARHTVINNFSLDLMLRKNLEVYK 382
Cdd:cd03807   306 G-TGFLVPAGDPQALADAIRAL--LEDPEKRARLGRAARERIANEFSIDAMVRRYETLYY 362
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
21-376 9.48e-47

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: 163.54  E-value: 9.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  21 ALVSGGVERGTIEVAKYLKILGHTPIIISA-GGTLVKELDKEDILH--IEMNSSSKNPFVILNNAKLIAEIIKKYNVDIV 97
Cdd:cd03808     6 VNVDGGFQSFRLPLIKALVKKGYEVHVIAPdGDKLSDELKELGVKVidIPILRRGINPLKDLKALFKLYKLLKKEKPDIV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  98 HTRSRAPA-WSSYLATKWTNAKFLTTFHGV--YNIPNSFKKY-----YNSIMLKGEKVIAVSNFVKQHLLENYKIDEDKI 169
Cdd:cd03808    86 HCHTPKPGiLGRLAARLAGVPKVIYTVHGLgfVFTEGKLLRLlylllEKLALLFTDKVIFVNEDDRDLAIKKGIIKKKKT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 170 VVIE-RGVNCDYFdpanltpeklkkCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKHR--DFYCLMVGDISRHp 246
Cdd:cd03808   166 VLIPgSGVDLDRF------------QYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKgpNVRFLLVGDGELE- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 247 nftNRVKELIAALKLQNKIQIFGNDSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITG 326
Cdd:cd03808   233 ---NPSEILIEKLGLEGRIEFLGFRSDVPELLAESDVFVLPSYR-EGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNG 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1962964333 327 FHVEPNNAEALAEKIDYCfsILGTDTAKKIQEAARHTVINNFSLDLMLRK 376
Cdd:cd03808   309 FLVPPGDVEALADAIEKL--IEDPELRKEMGEAARKRVEEKFDEEKVVNK 356
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
15-370 2.68e-38

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: 140.57  E-value: 2.68e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPALVSGGVERGTIEVAKYLKILGH--TPIIISAGGTLVKELDKEDILHIEMNSSSKNPFVILNNAKL-IAEIIKK 91
Cdd:cd03811     2 ILFVIPSLSGGGAERVLLNLANALDKRGYdvTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILkLKRILKR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  92 YNVDIVHT-RSRAPAWSSYLATKwtNAKFLTTFHGVYNI---PNSFKKYYNSIMLKGEKVIAVSNFVKQHLLENYKIDED 167
Cdd:cd03811    82 AKPDVVISfLGFATYIVAKLAAA--RSKVIAWIHSSLSKlyyLKKKLLLKLKLYKKADKIVCVSKGIKEDLIRLGPSPPE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 168 KIVVIERGVNCDYFdpanltpEKLKKCRDKYDaPSNVPIILMPSRMTSWKGHLVLVEALSKL--KHRDFYCLMVGDISRH 245
Cdd:cd03811   160 KIEVIYNPIDIDRI-------RALAKEPILNE-PEDGPVILAVGRLDPQKGHDLLIEAFAKLrkKYPDVKLVILGDGPLR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 246 pnftNRVKELIAALKLQNKIQIFGNDSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNIT 325
Cdd:cd03811   232 ----EELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSSRY-EGFPNVLLEAMALGTPVVSTDCPGPREILDDGEN 306
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1962964333 326 GFHVEPNNAEALAEKIDYCFSILGTDTAKKIQEAARHTVINNFSL 370
Cdd:cd03811   307 GLLVPDGDAAALAGILAALLQKKLDAALRERLAKAQEAVFREYTI 351
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
205-362 2.89e-30

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: 113.91  E-value: 2.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 205 PIILMPSRMTSWKGHLVLVEALSKLK--HRDFYCLMVGDisrhPNFTNRVKELIAALKLQNKIQIFG--NDSDIINLYGI 280
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKekNPNLKLVIAGD----GEEEKRLKKLAEKLGLGDNVIFLGfvSDEDLPELLKI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 281 SDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYCfsILGTDTAKKIQEAA 360
Cdd:pfam00534  79 ADVFVLPSRY-EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL--LEDEELRERLGENA 155

                  ..
gi 1962964333 361 RH 362
Cdd:pfam00534 156 RK 157
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
25-179 3.87e-27

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 105.69  E-value: 3.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  25 GGVERGTIEVAKYLKILGHTPIIIS--AGGTLVKELDKEDILHIEMNSSSKNPFVILNNAKLIAEIIKKYNVDIVHTRSR 102
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTpgGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 103 APAWSSYLATK-WTNAKFLTTFHGVYN-----------IPNSFKKYYNSIMLKGEKVIAVSNFVKQHLLENYKIDEDKIV 170
Cdd:pfam13439  81 FPLGLAALAARlRLGIPLVVTYHGLFPdykrlgarlspLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKIR 160

                  ....*....
gi 1962964333 171 VIERGVNCD 179
Cdd:pfam13439 161 VIPNGVDLE 169
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
15-341 5.18e-27

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: 110.11  E-value: 5.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVV---PALVSGGVERGTIEVAKYLKILGHTPIIISAG---------GTLVKEL---DKEDILH-----IEMNSSSKN 74
Cdd:cd03823     2 ILLVNslyPPQRVGGAEISVHDLAEALVAEGHEVAVLTAGvgppgqatvARSVVRYrraPDETLPLalkrrGYELFETYN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  75 PFVilnnAKLIAEIIKKYNVDIVHTRS----RAPAWssYLATKwTNAKFLTTFHGVYNI-PNSFkkyynsiMLK--GEKV 147
Cdd:cd03823    82 PGL----RRLLARLLEDFRPDVVHTHNlsglGASLL--DAARD-LGIPVVHTLHDYWLLcPRQF-------LFKkgGDAV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 148 IAVSNFVKQHLLENYkIDEDKIVVIERGVNcdyFDPAnltpekLKKCRDKYDAPSNVPIIlmpSRMTSWKGHLVLVEALS 227
Cdd:cd03823   148 LAPSRFTANLHEANG-LFSARISVIPNAVE---PDLA------PPPRRRPGTERLRFGYI---GRLTEEKGIDLLVEAFK 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 228 KLKHRDFYCLMVGDISRHPnftnrvkelIAALKLQNKIQIFGN--DSDIINLYGISDIIVSASIEPEAFGRTIIEGQAME 305
Cdd:cd03823   215 RLPREDIELVIAGHGPLSD---------ERQIEGGRRIAFLGRvpTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAG 285
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1962964333 306 KLVIATNIGGAVETINNNITGFHVEPNNAEALAEKI 341
Cdd:cd03823   286 LPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAM 321
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
75-384 6.09e-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: 107.44  E-value: 6.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  75 PFVILNNAKLIAEIIKKYNVDIVHTRSRAP-AWSSYLATKWTNAKF--LTTFHG-----VYNIPnSFKKYYNSIMLKGEK 146
Cdd:cd04962    66 PPYTLALASKIVEVAKEHKLDVLHAHYAIPhASCAYLAREILGEKIpiVTTLHGtditlVGYDP-SLQPAVRFSINKSDR 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 147 VIAVSNFVKQHLLENYKIDEDkIVVIERGVNCDYFDPANLTPeklkkCRDKYDAPSNVPIILMPSRMTSWKG-------- 218
Cdd:cd04962   145 VTAVSSSLRQETYELFDVDKD-IEVIHNFIDEDVFKRKPAGA-----LKRRLLAPPDEKVVIHVSNFRPVKRiddvvrvf 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 219 HLVLVEALSKLkhrdfycLMVGDisrHPNFTNrVKELIAALKLQNKIQIFGNDSDIINLYGISDIIVSASiEPEAFGRTI 298
Cdd:cd04962   219 ARVRRKIPAKL-------LLVGD---GPERVP-AEELARELGVEDRVLFLGKQDDVEELLSIADLFLLPS-EKESFGLAA 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 299 IEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEkidYCFSILGTD-TAKKIQEAARHTVINNFSLDLMLRKN 377
Cdd:cd04962   287 LEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAK---SALSILEDDeLYNRMGRAARKRAAERFDPERIVPQY 363

                  ....*..
gi 1962964333 378 LEVYKEI 384
Cdd:cd04962   364 EAYYRRL 370
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
89-346 1.33e-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: 101.16  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  89 IKKYNV--DIVHTRSRAPAWSSYLATKWTNAKFLTTFH--GVYNIPNSFKKYYNSIM--LKGEK-VIAVSNFV------- 154
Cdd:cd03800    95 IAREGGryDLIHSHYWDSGLVGALLARRLGVPLVHTFHslGRVKYRHLGAQDTYHPSlrITAEEqILEAADRViastpqe 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 155 KQHLLENYKIDEDKIVVIERGVNCDYFDP-----ANLTPEKLkkcrdkydaPSNVPIILMPSRMTSWKGHLVLVEALSKL 229
Cdd:cd03800   175 ADELISLYGADPSRINVVPPGVDLERFFPvdraeARRARLLL---------PPDKPVVLALGRLDPRKGIDTLVRAFAQL 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 230 KHRDFYCLMV---GDI-SRHPNFTNRVKELIAALKLQNKIQIFG--NDSDIINLYGISDIIVSASIEpEAFGRTIIEGQA 303
Cdd:cd03800   246 PELRELANLVlvgGPSdDPLSMDREELAELAEELGLIDRVRFPGrvSRDDLPELYRAADVFVVPSLY-EPFGLTAIEAMA 324
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1962964333 304 MEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYCFS 346
Cdd:cd03800   325 CGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD 367
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
82-384 1.69e-23

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: 100.53  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  82 AKLIAEIIKKYnVDIVHtrsRAPAWSS-YLATK---WTNAKFLTTFHG--VYNIPN--SFKKYYNSIMLKGEKVIAVSNF 153
Cdd:cd03798    85 AKLLKRRRRGP-PDLIH---AHFAYPAgFAAALlarLYGVPYVVTEHGsdINVFPPrsLLRKLLRWALRRAARVIAVSKA 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 154 VKQhLLENYKIDEDKIVVIERGVNCDYFDPANLTPeklkkcrdkyDAPSNVPIILMPSRMTSWKGHLVLVEALSKL--KH 231
Cdd:cd03798   161 LAE-ELVALGVPRDRVDVIPNGVDPARFQPEDRGL----------GLPLDAFVILFVGRLIPRKGIDLLLEAFARLakAR 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 232 RDFYCLMVGDISRHPnftnRVKELIAALKLQNKIQIFGN--DSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVI 309
Cdd:cd03798   230 PDVVLLIVGDGPLRE----ALRALAEDLGLGDRVTFTGRlpHEQVPAYYRACDVFVLPSRH-EGFGLVLLEAMACGLPVV 304
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1962964333 310 ATNIGGAVETINNNITGFHVEPNNAEALAEKIDYcfsILGTDTAKKIQEAARHTVINNFSLDLMLRKNLEVYKEI 384
Cdd:cd03798   305 ATDVGGIPEVVGDPETGLLVPPGDADALAAALRR---ALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
25-373 5.05e-23

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: 98.89  E-value: 5.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  25 GGVERGTIEVAKYLKILGHTPIIISAGGTLVKELDKEDILHIEMNSSSKNPFVILNNAKLIAEIIKKY-NVDIVHTRSRA 103
Cdd:cd03795    14 GGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVASTPFSPSYIKRFKKLAkEYDIIHYHFPN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 104 P------AWSSYlatkwtNAKFLTTFHGVYNIPNSFKKYYN---SIMLKGEKVIAVS--NFVKQ-HLLENYKideDKIVV 171
Cdd:cd03795    94 PladlllFFSGA------KKPVVVHWHSDIVKQKKLLKLYKplmTRFLRRADRIIATspNYVETsPTLREFK---NKVRV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 172 IERGVNCDYFDPANLTPEKLKKCRDKYdapsnvPIILMPSRMTSWKGHLVLVEALSKLkhrDFYCLMVGDisrhPNFTNR 251
Cdd:cd03795   165 IPLGIDKNVYNIPRVDFENIKREKKGK------KIFLFIGRLVYYKGLDYLIEAAQYL---NYPIVIGGE----GPLKPD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 252 VKELIAALKLQNkIQIFG--NDSDIINLYGISDIIVSASIE-PEAFGRTIIEGQAMEKLVIATNIGGAVETINNN-ITGF 327
Cdd:cd03795   232 LEAQIELNLLDN-VKFLGrvDDEEKVIYLHLCDVFVFPSVLrSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNgETGL 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1962964333 328 HVEPNNAEALAEKIDycFSILGTDTAKKIQEAARHTVINNFSLDLM 373
Cdd:cd03795   311 VVPPKDPDALAEAID--KLLSDEELRESYGENAKKRFEELFTAEKM 354
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
205-341 2.79e-22

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 91.42  E-value: 2.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 205 PIILMPSRMTSW-KGHLVLVEALSKLKHRDFYC--LMVGDisrhpnftNRVKELIA-ALKLQNKIQIFGNDSDIINLYGI 280
Cdd:pfam13692   2 PVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVrlVIVGD--------GPEEELEElAAGLEDRVIFTGFVEDLAELLAA 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1962964333 281 SDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETInNNITGFHVEPNNAEALAEKI 341
Cdd:pfam13692  74 ADVFVLPSLY-EGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAI 132
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
21-341 7.07e-22

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 95.89  E-value: 7.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  21 ALVSGGVERGTIEVAKYLKILGHTPIIIsaggtLVKELDKEDILHIEMNSSSKNPFV-------ILNNAKLIAEIIKKYN 93
Cdd:cd03809    10 AQRLTGIGRYTRELLKALAKNDPDESVL-----AVPPLPGELLRLLREYPELSLGVIkiklwreLALLRWLQILLPKKDK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  94 VDIVH-TRSRAPAWSSylatkwtNAKFLTTFHGV------YNIPNSFKKYYNSIML----KGEKVIAVSNFVKQHLLENY 162
Cdd:cd03809    85 PDLLHsPHNTAPLLLK-------GCPQVVTIHDLiplrypEFFPKRFRLYYRLLLPislrRADAIITVSEATRDDIIKFY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 163 KIDEDKIVVIERGVNCDYFdpanlTPEKLKKCRDKYDAPSnvPIILMPSRMTSWKGHLVLVEALSKLK--HRDFYCLMVG 240
Cdd:cd03809   158 GVPPEKIVVIPLGVDPSFF-----PPESAAVLIAKYLLPE--PYFLYVGTLEPRKNHERLLKAFALLKkqGGDLKLVIVG 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 241 diSRHPNFTNRVKeLIAALKLQNKIQIFGN--DSDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIgGAVE 318
Cdd:cd03809   231 --GKGWEDEELLD-LVKKLGLGGRVRFLGYvsDEDLPALYRGARAFVFPSLY-EGFGLPVLEAMACGTPVIASNI-SVLP 305
                         330       340
                  ....*....|....*....|...
gi 1962964333 319 TINNNiTGFHVEPNNAEALAEKI 341
Cdd:cd03809   306 EVAGD-AALYFDPLDPESIADAI 327
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
147-384 7.18e-22

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: 95.86  E-value: 7.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 147 VIAVSNFVKQHLLENYKIDEDKIVVIERGVNCDYFDPANLtpeklKKCRDKYDAPSNVPIILMPSRMT--SWKGHLVLVE 224
Cdd:cd03825   141 IVAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAPVDK-----AKARKRLGIPQDKKVILFGAESVtkPRKGFDELIE 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 225 ALSKL-KHRDFYCLMVGDISrhpnftnrvkELIAALKLQnkIQIFG---NDSDIINLYGISDIIVSASIEpEAFGRTIIE 300
Cdd:cd03825   216 ALKLLaTKDDLLLVVFGKND----------PQIVILPFD--IISLGyidDDEQLVDIYSAADLFVHPSLA-DNLPNTLLE 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 301 GQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYCfsILGTDTAKKIQEAARHTVINNFSLDLMLRKNLEV 380
Cdd:cd03825   283 AMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWL--LANPKERESLGERARALAENHFDQRVQAQRYLEL 360

                  ....
gi 1962964333 381 YKEI 384
Cdd:cd03825   361 YKDL 364
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
24-342 8.78e-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: 8.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  24 SGGVERGTIEVAKYLKILGHTPIIIS---AGGTLVKELDkEDILHIEMNSSSKNPF-VILNNAKLIA---EIIKKYNVDI 96
Cdd:cd03820    12 AGGAERVAINLANHLAKKGYDVTIISldsAEKPPFYELD-DNIKIKNLGDRKYSHFkLLLKYFKKVRrlrKYLKNNKPDV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  97 V---HTRSRapawsSYLATKWTNAKFLTTFHGVYNIPNSFKKYYNSIML---KGEKVIAVSNFVKqhlLENYKIDEDKIV 170
Cdd:cd03820    91 VisfRTSLL-----TFLALIGLKSKLIVWEHNNYEAYNKGLRRLLLRRLlykRADKIVVLTEADK---LKKYKQPNSNVV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 171 VIErgvN-CDYFDPANLTPEKLKkcrdkydapsnvpIILMPSRMTSWKGHLVLVEALSKL--KHRDFYCLMVGDISRHPN 247
Cdd:cd03820   163 VIP---NpLSFPSEEPSTNLKSK-------------RILAVGRLTYQKGFDLLIEAWALIakKHPDWKLRIYGDGPEREE 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 248 FtnrvKELIAALKLQNKIQIFGNDSDIINLYGISDIIVSASiEPEAFGRTIIEGQAMEKLVIATNI-GGAVETINNNITG 326
Cdd:cd03820   227 L----EKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSS-RYEGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENG 301
                         330
                  ....*....|....*.
gi 1962964333 327 FHVEPNNAEALAEKID 342
Cdd:cd03820   302 LLVPNGDVDALAEALL 317
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
277-386 9.23e-22

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 89.66  E-value: 9.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 277 LYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYCFSIlgTDTAKKI 356
Cdd:COG0438    17 LLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRLLED--PELRRRL 93
                          90       100       110
                  ....*....|....*....|....*....|
gi 1962964333 357 QEAARHTVINNFSLDLMLRKNLEVYKEILK 386
Cdd:COG0438    94 GEAARERAEERFSWEAIAERLLALYEELLA 123
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
15-381 1.62e-21

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: 94.82  E-value: 1.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPALVSGGVERGTIEVAKYLKILGH-TPIIISAGGTLVKELDKEDILH-IEMnssSKNPFVILNNAKLIAEIIKKY 92
Cdd:cd04951     2 ILYVITGLGLGGAEKQTVLLADQMFIRGHdVNIVYLTGEVEVKPLNNNIIIYnLGM---DKNPRSLLKALLKLKKIISAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  93 NVDIVHTRS-RAPAWSSYLATKWTNAKFLTTFHGVYNIPNSFKKYYNSIMLKGEKVIAVSNFVKQHLLENYKIDEDKIVV 171
Cdd:cd04951    79 KPDVVHSHMfHANIFARFLRMLYPIPLLICTAHNKNEGGRIRMFIYRLTDFLCDITTNVSREALDEFIAKKAFSKNKSVP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 172 IERGVNCDYFDpanLTPEKLKKCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKL--KHRDFYCLMVGDisrhPNFT 249
Cdd:cd04951   159 VYNGIDLNKFK---KDINVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELilSKNDFKLLIAGD----GPLR 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 250 NRVKELIAALKLQNKIQIFGNDSDIINLYGISDIIVSASiEPEAFGRTIIEGQAMEKLVIATNIGGAVETINNniTGFHV 329
Cdd:cd04951   232 NELERLICNLNLVDRVILLGQISNISEYYNAADLFVLSS-EWEGFGLVVAEAMACERPVVATDAGGVAEVVGD--HNYVV 308
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1962964333 330 EPNNAEALAEKIDYCFSIlgTDTAKKIQEAARHTVINNFSLDLMLRKNLEVY 381
Cdd:cd04951   309 PVSDPQLLAEKIKEIFDM--SDEERDILGNKNEYIAKNFSINTIVNEWERLY 358
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
35-342 7.17e-21

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: 93.11  E-value: 7.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  35 AKYLKILGHTPIIIsagGTLVKELDKEDILHIEMNSS-----SKNPFVILNNAKLIAEIIKKYNVDIVHTRSR--APAWS 107
Cdd:cd03817    24 ARALEKRGHEVYVI---TPSDPGAEDEEEVVRYRSFSipirkYHRQHIPFPFKKAVIDRIKELGPDIIHTHTPfsLGKLG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 108 SYLATKWtNAKFLTTFHGVY-----NIPNSF-----------KKYYNsimlKGEKVIAVSNFVKQhLLENYKIDeDKIVV 171
Cdd:cd03817   101 LRIARKL-KIPIVHTYHTMYedylhYIPKGKllvkavvrklvRRFYN----HTDAVIAPSEKIKD-TLREYGVK-GPIEV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 172 IERGVNCDYFDPanltpEKLKKCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKHR-DFYCLMVGDISRHPNFtn 250
Cdd:cd03817   174 IPNGIDLDKFEK-----PLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEpNIKLVIVGDGPEREEL-- 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 251 rvKELIAALKLQNKIQIFG--NDSDIINLYGISDIIVSASiEPEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFH 328
Cdd:cd03817   247 --KELARELGLADKVIFTGfvPREELPEYYKAADLFVFAS-TTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFL 323
                         330
                  ....*....|....
gi 1962964333 329 VEPNNaEALAEKID 342
Cdd:cd03817   324 FEPND-ETLAEKLL 336
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
61-343 1.91e-19

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: 88.66  E-value: 1.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  61 EDILH---IEMNSSSKNPFVILNNAkliaeiIKKYNVDIVHTR---SRAPAwSSYLATKWTNAKFLTTFHGvYNIPNSFK 134
Cdd:cd03799    41 LVKRHpdvEKYNVPSLNLLYAIVGL------NKKGAYDIIHCQfgpLGALG-ALLRRLKVLKGKLVTSFRG-YDISMYVI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 135 KY----YNSIMLKGEKVIAVSNFVKQHLLeNYKIDEDKIVVIERGVNCDYFdpaNLTPEKLkkcrdkydaPSNVPI-ILM 209
Cdd:cd03799   113 LEgnkvYPQLFAQGDLFLPNCELFKHRLI-ALGCDEKKIIVHRSGIDCNKF---RFKPRYL---------PLDGKIrILT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 210 PSRMTSWKGHLVLVEALSKL--KHRDFYCLMVGDISRHpnftNRVKELIAALKLQNKIQIFG--NDSDIINLYGISDIIV 285
Cdd:cd03799   180 VGRLTEKKGLEYAIEAVAKLaqKYPNIEYQIIGDGDLK----EQLQQLIQELNIGDCVKLLGwkPQEEIIEILDEADIFI 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1962964333 286 SASI-----EPEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDY 343
Cdd:cd03799   256 APSVtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTY 318
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
168-329 4.08e-16

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: 77.06  E-value: 4.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 168 KIVVIERGVNC-DYFDPANLTPEKLKKCRDKYDApsnvpiiLMPSRMTSWKGHLVLVEALSKLKHR--DFYCLMVGDISR 244
Cdd:cd01635    80 PIVVTVHGPDSlESTRSELLALARLLVSLPLADK-------VSVGRLVPEKGIDLLLEALALLKARlpDLVLVLVGGGGE 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 245 HPnftnRVKELIAALKLQNKIQIFGN---DSDIINLYGISDIIVSASIePEAFGRTIIEGQAMEKLVIATNIGGAVETIN 321
Cdd:cd01635   153 RE----EEEALAAALGLLERVVIIGGlvdDEVLELLLAAADVFVLPSR-SEGFGLVLLEAMAAGKPVIATDVGGIPEFVV 227

                  ....*...
gi 1962964333 322 NNITGFHV 329
Cdd:cd01635   228 DGENGLLV 235
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
78-371 7.67e-14

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 72.13  E-value: 7.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  78 ILNNAKLIAeiIKKYNVDIVHT--------RSRAPawssylatkwtNAKFLTTFHgvynipNSFKKyynSIMLKGEKVIA 149
Cdd:PRK15484   88 ILNIAHKFT--ITKDSVIVIHNsmklyrqiRERAP-----------QAKLVMHMH------NAFEP---ELLDKNAKIIV 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 150 VSNFVKQHLlENYKIDEDkIVVIERGvncdyFDPANLTPEKLKKCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKL 229
Cdd:PRK15484  146 PSQFLKKFY-EERLPNAD-ISIVPNG-----FCLETYQSNPQPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 230 --KHRDFYCLMVGDI-----SRHPNFTNRVKELIAALKLQNkIQIFGNDSDII-NLYGISDIIVSASIEPEAFGRTIIEG 301
Cdd:PRK15484  219 atAHSNLKLVVVGDPtasskGEKAAYQKKVLEAAKRIGDRC-IMLGGQPPEKMhNYYPLADLVVVPSQVEEAFCMVAVEA 297
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1962964333 302 QAMEKLVIATNIGGAVETINNNITGFHV-EPNNAEALAEKIDycfSILGTDTAKKIQEAARHTVINNFSLD 371
Cdd:PRK15484  298 MAAGKPVLASTKGGITEFVLEGITGYHLaEPMTSDSIISDIN---RTLADPELTQIAEQAKDFVFSKYSWE 365
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
24-376 5.62e-13

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: 69.68  E-value: 5.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  24 SGGVERGTIEVAKYLKILGHTPIIISAG---------GTLVKELDKEDILHIEMNSSSKNPFVILNN---------AKLI 85
Cdd:cd03794    13 KGAAAARVYELAKELVRRGHEVTVLTPSpnyplgrifAGATETKDGIRVIRVKLGPIKKNGLIRRLLnylsfalaaLLKL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  86 AEIIKKYNVDIVHTRSRAPAWSSYLATKWTNAKFLTTFHGVYniPNSF-------KKYYNSIMLKGEK--------VIAV 150
Cdd:cd03794    93 LVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLW--PESLialgvlkKGSLLKLLKKLERklyrladaIIVL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 151 SNFVKQHLLENYkIDEDKIVVIERGVNCDYFDPANLTPEKLKKCRDKydapsnvPIILMPSR-MTSWKGHLVLVEALSKL 229
Cdd:cd03794   171 SPGLKEYLLRKG-VPKEKIIVIPNWADLEEFKPPPKDELRKKLGLDD-------KFVVVYAGnIGKAQGLETLLEAAERL 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 230 KHRDFYCLM-VGDISRHPnftnRVKELIAALKLQNkIQIFG--NDSDIINLYGISDIIVsASIEPEAFGRTIIEGQ---- 302
Cdd:cd03794   243 KRRPDIRFLfVGDGDEKE----RLKELAKARGLDN-VTFLGrvPKEEVPELLSAADVGL-VPLKDNPANRGSSPSKlfey 316
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1962964333 303 -AMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYCfsILGTDTAKKIQEAARHTVINNFSLDLMLRK 376
Cdd:cd03794   317 mAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILEL--LDDPELRRAMGENGRELAEEKFSREKLADR 389
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
94-382 1.88e-12

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: 68.52  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  94 VDIVHTRSRAPA-WSSYLATKWTNAKFLTTFHGVY------NIPNSF--KKYYNSIMLK------------GEKVIAVSN 152
Cdd:cd03813   174 ADLYHSVSTGYAgLLGALARHRRGIPFLLTEHGIYtrerkiEILQSTwiMGYIKKLWIRfferlgklayqqADKIISLYE 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 153 FVKQHLLEnYKIDEDKIVVIERGVNCDYFDPANLTPEKlkkcrdkydapSNVPIILMPSRMTSWKGHLVLVEALSKLKHR 232
Cdd:cd03813   254 GNRRRQIR-LGADPDKTRVIPNGIDIQRFAPAREERPE-----------KEPPVVGLVGRVVPIKDVKTFIRAFKLVRRA 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 233 --DFYCLMVGDISRHPNFTNRVKELIAALKLQNKIQIFGNDsDIINLYGISDIIVSASIEpEAFGRTIIEGQAMEKLVIA 310
Cdd:cd03813   322 mpDAEGWLIGPEDEDPEYAQECKRLVASLGLENKVKFLGFQ-NIKEYYPKLGLLVLTSIS-EGQPLVILEAMASGVPVVA 399
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1962964333 311 TNIGGAVETI-----NNNITGFHVEPNNAEALAEKIDYcfsiLGTDTAK--KIQEAARHTVINNFSLDLMLRKNLEVYK 382
Cdd:cd03813   400 TDVGSCRELIygaddALGQAGLVVPPADPEALAEALIK----LLRDPELrqAFGEAGRKRVEKYYTLEGMIDSYRKLYL 474
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
148-373 2.91e-11

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: 64.53  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 148 IAV-SNFVKQHLLENYKIDEDKIV-VIERGVNCDYFDPAnltpEKLKKCRDKyDAPSNVPIILMPSRMTSWKGHLVLVEA 225
Cdd:cd03805   158 IVVnSNFTAGVFKKTFPSLAKNPPeVLYPCVDTDSFDST----SEDPDPGDL-IAKSNKKFFLSINRFERKKNIALAIEA 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 226 LSKLK--HRDFYCLMV----GdisrhpnFTNRVKELIAALK-LQNKIQIFGNDSD-IINLYGISD----IIVSASI---- 289
Cdd:cd03805   233 FAKLKqkLPEFENVRLviagG-------YDPRVAENVEYLEeLQRLAEELLNVEDqVLFLRSISDsqkeQLLSSALally 305
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 290 --EPEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPnNAEALAEKIDYCFSilGTDTAKKIQEAARHTVINN 367
Cdd:cd03805   306 tpSNEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCEP-TPEAFAEAMLKLAN--DPDLADRMGAAGRKRVKEK 382

                  ....*.
gi 1962964333 368 FSLDLM 373
Cdd:cd03805   383 FSREAF 388
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
120-372 5.42e-11

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: 63.63  E-value: 5.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 120 LTTFHGvYNI-------------PNSFKKYYNSIMLKGEKVIAVSNFVKQHLLENyKIDEDKIVVIERGVNCDYFDPAnl 186
Cdd:cd05844   108 VVTFHG-FDIttsrawlaaspgwPSQFQRHRRALQRPAALFVAVSGFIRDRLLAR-GLPAERIHVHYIGIDPAKFAPR-- 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 187 tpeklkkcrdkyDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKHR--DFYCLMVGDISrhpnFTNRVKELIAALklqNK 264
Cdd:cd05844   184 ------------DPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARhpTARLVIAGDGP----LRPALQALAAAL---GR 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 265 IQIFGNDS--DIINLYGISDI-----IVSASIEPEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEAL 337
Cdd:cd05844   245 VRFLGALPhaEVQDWMRRAEIfclpsVTAASGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDAL 324
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1962964333 338 AEKIDycfSILGTDT-AKKIQEAARHTVINNFSLDL 372
Cdd:cd05844   325 ADALQ---ALLADRAlADRMGGAARAFVCEQFDIRV 357
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
165-364 1.65e-08

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: 55.84  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 165 DEDKIVVIERGVNCDYFDPANLTPEKLKKCRDKydapsnvPIILMPSRMTSWKGHLVLVEALSKL--KHRDFYCLMVG-D 241
Cdd:cd03821   172 LEPPIAVIPNGVDIPEFDPGLRDRRKHNGLEDR-------RIILFLGRIHPKKGLDLLIRAARKLaeQGRDWHLVIAGpD 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 242 ISRHPNFtnrvKELIAALKLQNKIQIFG--NDSDIINLYGISDIIVSASiEPEAFGRTIIEGQAME-KLVIATNIGGAVE 318
Cdd:cd03821   245 DGAYPAF----LQLQSSLGLGDRVTFTGplYGEAKWALYASADLFVLPS-YSENFGNVVAEALACGlPVVITDKCGLSEL 319
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1962964333 319 TINNNitGFHVEPNN---AEALAEKIDYcfsilgTDTAKKIQEAARHTV 364
Cdd:cd03821   320 VEAGC--GVVVDPNVsslAEALAEALRD------PADRKRLGEMARRAR 360
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
133-345 6.63e-08

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


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 53.84  E-value: 6.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 133 FKKYYNSIM--LKGEKVIAVSNFVKQHLLENYKIDEDKIVVIERGvncdyFDPANLTPEKLKKcRDKYdapsnvpIILMP 210
Cdd:cd04949   100 IKNFYKYVFenLNKYDAIIVSTEQQKQDLSERFNKYPPIFTIPVG-----YVDQLDTAESNHE-RKSN-------KIITI 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 211 SRMTSWKGHLVLVEALSKLKHR------DFYCLmvGDISRHPnftnrvKELIAALKLQNKIQIFGNDSDIINLYGISDII 284
Cdd:cd04949   167 SRLAPEKQLDHLIEAVAKAVKKvpeitlDIYGY--GEEREKL------KKLIEELHLEDNVFLKGYHSNLDQEYQDAYLS 238
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1962964333 285 VSASiEPEAFGRTIIEGQAMEKLVIATNIG-GAVETINNNITGFHVEPNNAEALAEKIDYCF 345
Cdd:cd04949   239 LLTS-QMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELL 299
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
118-342 2.81e-07

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 52.00  E-value: 2.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 118 KFLTTFHGVYNIPNSFKKYYNSIMLKGEKVIAVsnFVKQHLLEN-----YKIDEDKIVVIERGVNCDYFDPanltpeklK 192
Cdd:cd03822   106 PVITTLHTVLDLSDPGKQALKVLFRIATLSERV--VVMAPISRFllvriKLIPAVNIEVIPHGVPEVPQDP--------T 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 193 KCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLK--HRDFYCLMVG----DISRHPNFTNRVKElIAALKLQNKIQ 266
Cdd:cd03822   176 TALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKaeFPDVRLVIAGelhpSLARYEGERYRKAA-IEELGLQDHVD 254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 267 I---FGNDSDIINLYGISDIIVSA--SIEPEAFGrTIIEGQAMEKLVIATNIGGAVEtINNNITGFHVEPNNAEALAEKI 341
Cdd:cd03822   255 FhnnFLPEEEVPRYISAADVVVLPylNTEQSSSG-TLSYAIACGKPVISTPLRHAEE-LLADGRGVLVPFDDPSAIAEAI 332

                  .
gi 1962964333 342 D 342
Cdd:cd03822   333 L 333
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
15-346 4.95e-07

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: 51.14  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPALVSGGVERGTIEVAKYLKILGHTPIIISAggTLVKELDKEDI--LHIEMNSSSKNPFVILNNAKLIAEIIKKY 92
Cdd:cd03812     2 ILHIVGGMNVGGIETFLMNLYRKLDKSKIEFDFLAT--SDDKGEYDEELeeLGGKIFYIPPKKKNIIKYFIKLLKLIKKE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  93 NVDIVHTRS----RAPAWSSYLA-----------TKWTNAKFLTTFHGVYNIPnsFKKYYNsimlkgeKVIAVSNFVKQH 157
Cdd:cd03812    80 KYDIVHVHGsssnGIILLLAAKAgvpvriahshnTKDSSIKLRKIRKNVLKKL--IERLST-------KYLACSEDAGEW 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 158 LLEnyKIDEDKIVVIERGVNCDYFDPanltPEKLKKCRDKYDAPSNVPIILMPSRMTSWKGHLVLVEALSKLKHR--DFY 235
Cdd:cd03812   151 LFG--EVENGKFKVIPNGIDIEKYKF----NKEKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKnpNVK 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 236 CLMVGDISrhpnFTNRVKELIAALKLQNKIQIFGNDSDIINLYGISDIIVSASiEPEAFGRTIIEGQAMEKLVIATNIGG 315
Cdd:cd03812   225 LVLVGEGE----LKEKIKEKVKELGLEDKVIFLGFRNDVSEILSAMDVFLFPS-LYEGLPLVAVEAQASGLPCLLSDTIT 299
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1962964333 316 AVETINNNITGFHVEpNNAEALAEKIDYCFS 346
Cdd:cd03812   300 KECDITNNVEFLPLN-ETPSTWAEKILKLIK 329
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
205-368 5.60e-07

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: 51.17  E-value: 5.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 205 PIILMPSRMTSWKGHLVLVEALSKLKHRDFYCLMVgdISRHPNftnrVKELIAALKLQNKIQIFGNDSDI---------- 274
Cdd:cd03792   198 PYILQVARFDPSKDPLGVIDAYKLFKRRAEEPQLV--ICGHGA----VDDPEGSVVYEEVMEYAGDDHDIhvlrlppsdq 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 275 -IN-LYGISDIIVSASIePEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALaekidyCFSILGTDT 352
Cdd:cd03792   272 eINaLQRAATVVLQLST-REGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAV------RILRLLTDP 344
                         170
                  ....*....|....*...
gi 1962964333 353 A--KKIQEAARHTVINNF 368
Cdd:cd03792   345 ElrRKMGLAAREHVRDNF 362
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
130-382 2.36e-06

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 49.65  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 130 PNSFKKYYNSI---MLKGEKVIAVSNFVK--QHLLENYKIDEDKIVVIERGVncdyfdpANLTPEKLKKCRDKY------ 198
Cdd:PRK15179  440 PDRYRVEYDIIyseLLKMRGVALSSNSQFaaHRYADWLGVDERRIPVVYNGL-------APLKSVQDDACTAMMaqfdar 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 199 --DAPSNVPIILmpsRMTSWKGHLVLVEALSKL--KHRDFYCLMVGDISRHPNftnrVKELIAALKLQNKIQIFGNDSDI 274
Cdd:PRK15179  513 tsDARFTVGTVM---RVDDNKRPFLWVEAAQRFaaSHPKVRFIMVGGGPLLES----VREFAQRLGMGERILFTGLSRRV 585
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 275 INLYGISDIIVSASiEPEAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHV------EPNNAEALAEKIDYCfsil 348
Cdd:PRK15179  586 GYWLTQFNAFLLLS-RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLpadtvtAPDVAEALARIHDMC---- 660
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1962964333 349 GTDTAkkIQEAARHTVINNFSLDLMLRKNLEVYK 382
Cdd:PRK15179  661 AADPG--IARKAADWASARFSLNQMIASTVRCYQ 692
PLN00142 PLN00142
sucrose synthase
292-341 3.70e-06

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 49.21  E-value: 3.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1962964333 292 EAFGRTIIEGQAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKI 341
Cdd:PLN00142  677 EAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGFHIDPYHGDEAANKI 726
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
15-384 8.45e-06

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: 47.28  E-value: 8.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  15 ILQVVPALVS------GGVERGTIEVAKYLKILGHTPIIISAGG--------TLVKELDKEDILHIEmnSSSKNPFVILn 80
Cdd:cd03802     2 IAQVSPPRGPvppgkyGGTELVVSALTEGLVRRGHEVTLFAPGDshtsaplvAVIPRALRLDPIPQE--SKLAELLEAL- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  81 nakliAEIIKKYNVDIVHTRS--RAPAWSSYLATKwtnakFLTTFHGVYNIPNSFKKYYNSIMLkgekVIAVSNFVKQHL 158
Cdd:cd03802    79 -----EVQLRASDFDVIHNHSydWLPPFAPLIGTP-----FVTTLHGPSIPPSLAIYAAEPPVN----YVSISDAQRAAT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 159 LenykiDEDKIVVIERGVNCDYFDPANLTPEKLkkcrdkydapsnvpiiLMPSRMTSWKGHLVLVEALSKLKHRdfyCLM 238
Cdd:cd03802   145 P-----PIDYLTVVHNGLDPADYRFQPDPEDYL----------------AFLGRIAPEKGLEDAIRVARRAGLP---LKI 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 239 VGDISRHPNFtnrvkELIAALKLQNKIQIFG--NDSDIINLYGISDIIVSASIEPEAFGRTIIEGQAMEKLVIATNIGGA 316
Cdd:cd03802   201 AGKVRDEDYF-----YYLQEPLPGPRIEFIGevGHDEKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGL 275
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1962964333 317 VETINNNITGFHVEPnnAEALAEkidycfSILGTDTAKKiqEAARHTVINNFSLDLMLRKNLEVYKEI 384
Cdd:cd03802   276 PEVIQHGETGFLVDS--VEEMAE------AIANIDRIDR--AACRRYAEDRFSAARMADRYEALYRKV 333
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
146-344 1.41e-04

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: 43.43  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 146 KVIAVSNFVKQHLLENYKIDEdkiVVIERGVNCDYFDPANltpeklkkCRDKYdapsnvpiILMPSRMTSWKGHLVLVEA 225
Cdd:cd03804   160 LFIANSQFVARRIKKFYGRES---TVIYPPVDTDAFAPAA--------DKEDY--------YLTASRLVPYKRIDLAVEA 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 226 LSKLKHRdfyCLMVGDisrHPNFtNRVKEliaalKLQNKIQIFGNDSDIInlygISDIIVSAS--IEP--EAFGRTIIEG 301
Cdd:cd03804   221 FNELPKR---LVVIGD---GPDL-DRLRA-----MASPNVEFLGYQPDEV----LKELLSKARafVFAaeEDFGIVPVEA 284
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1962964333 302 QAMEKLVIATNIGGAVETINNNITGFHVEPNNAEALAEKIDYC 344
Cdd:cd03804   285 QACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEF 327
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
255-339 1.09e-03

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 41.30  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  255 LIAALKLQNKIQIFG--------NDSDIINLYGISD-----IIVSASIEPeaFGRTIIEGQAMEKLVIATNIGGAVETIN 321
Cdd:TIGR02468  534 LTSVLKLIDKYDLYGqvaypkhhKQSDVPDIYRLAAktkgvFINPAFIEP--FGLTLIEAAAHGLPMVATKNGGPVDIHR 611
                           90       100
                   ....*....|....*....|
gi 1962964333  322 --NNitGFHVEPNNAEALAE 339
Cdd:TIGR02468  612 vlDN--GLLVDPHDQQAIAD 629
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
31-152 2.27e-03

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 38.07  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333  31 TIEVAKYLKILGHTPIIISAGGTLVKELDKEDILHIEMNSSSKNPFVILnNAKLIAEIIKKYNVDIVHTRSRAPAW--SS 108
Cdd:pfam13477  13 TLRWADALADRGYDVHVISSKGPAKDELIAEGIHVHRLKVPRKGPLGYL-KAFRLKKLIKKIKPDVVHVHYAKPYGllAG 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1962964333 109 YLATKWTNAKFLTTFHG--VYNIPN--SFKKYYNSIMLKGEKVIAVSN 152
Cdd:pfam13477  92 LAARLSGFPPVVLSAWGldVYKFPNksRLKKLLLKLNLKKATLIISTS 139
PRK05749 PRK05749
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed
220-367 2.41e-03

3-deoxy-D-manno-octulosonic-acid transferase; Reviewed


Pssm-ID: 235589 [Multi-domain]  Cd Length: 425  Bit Score: 39.82  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 220 LVLvEALSKLK--HRDFYCLMVgdiSRHPNftnRVKELIAALKLQN-------KIQIFGNDSDII---------NLYGIS 281
Cdd:PRK05749  248 LVL-DAHRALLkqFPNLLLILV---PRHPE---RFKEVEELLKKAGlsyvrrsQGEPPSADTDVLlgdtmgelgLLYAIA 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1962964333 282 DI-IVSAS---------IEPEAFGRTIIEG-------QAMEKLViatNIGGAVETinnnitgfhvepNNAEALAEKIDYC 344
Cdd:PRK05749  321 DIaFVGGSlvkrgghnpLEPAAFGVPVISGphtfnfkEIFERLL---QAGAAIQV------------EDAEDLAKAVTYL 385
                         170       180
                  ....*....|....*....|...
gi 1962964333 345 FSilGTDTAKKIQEAARHTVINN 367
Cdd:PRK05749  386 LT--DPDARQAYGEAGVAFLKQN 406
 
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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