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Conserved domains on  [gi|1170892743|emb|SLW51576|]
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mannosyltransferase B [Klebsiella variicola]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133545)

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_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 2-376 1.89e-124

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: 363.22  E-value: 1.89e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743   2 KIIFATEPIKYPLTGIGRYSLELVKRLAVAREIEELKLFHGASFIDQIPQVENKSDtkasNHGRLSAFLRRQPLLieayr 81
Cdd:cd03809     1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPEL----SLGVIKIKLWRELAL----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  82 llHPRRQAWALRDYKDYIYHGPNFYLPHRLE--RAVTTFHDISIFTCPEYHPKDRVRYMEKSLHESLDSAKLILTVSDFS 159
Cdd:cd03809    72 --LRWLQILLPKKDKPDLLHSPHNTAPLLLKgcPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEAT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 160 RSEIIRLFNYPADRIVTTKLACSSDYiprSPAECLPVLQKYQLAWQGYALYIGTMEPRKNIRGLLQAYQLLPMETRmRYP 239
Cdd:cd03809   150 RDDIIKFYGVPPEKIVVIPLGVDPSF---FPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGG-DLK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 240 LILSGYRGWEDDVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLP 319
Cdd:cd03809   226 LVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLP 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892743 320 EVVGDAGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQAKQFSWENCTTQTIN 376
Cdd:cd03809   306 EVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 2-376 1.89e-124

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: 363.22  E-value: 1.89e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743   2 KIIFATEPIKYPLTGIGRYSLELVKRLAVAREIEELKLFHGASFIDQIPQVENKSDtkasNHGRLSAFLRRQPLLieayr 81
Cdd:cd03809     1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPEL----SLGVIKIKLWRELAL----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  82 llHPRRQAWALRDYKDYIYHGPNFYLPHRLE--RAVTTFHDISIFTCPEYHPKDRVRYMEKSLHESLDSAKLILTVSDFS 159
Cdd:cd03809    72 --LRWLQILLPKKDKPDLLHSPHNTAPLLLKgcPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEAT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 160 RSEIIRLFNYPADRIVTTKLACSSDYiprSPAECLPVLQKYQLAWQGYALYIGTMEPRKNIRGLLQAYQLLPMETRmRYP 239
Cdd:cd03809   150 RDDIIKFYGVPPEKIVVIPLGVDPSF---FPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGG-DLK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 240 LILSGYRGWEDDVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLP 319
Cdd:cd03809   226 LVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLP 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892743 320 EVVGDAGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQAKQFSWENCTTQTIN 376
Cdd:cd03809   306 EVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 207-352 4.63e-36

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: 128.93  E-value: 4.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 207 YALYIGTMEPRKNIRGLLQAYQLLPmETRMRYPLILSGYRGWEDDVLWQLVERGTREGwIRYLGYVPDEDLPYLYAAART 286
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALLK-EKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDN-VIFLGFVSDEDLPELLKIADV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1170892743 287 FVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD--AGLVADPNDVDAISAHILQSLQDDSWRE 352
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDgeTGFLVKPNNAEALAEAIDKLLEDEELRE 149
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 107-368 9.66e-32

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


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 123.28  E-value: 9.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 107 LPHRLERAVTTFHDISIFTCPeyhpkdrvrYMEKSLHESLDSAKLILTVSDFSRSEIIRLFNYPADRI---VTTKlacss 183
Cdd:TIGR04047 106 AEGLIPGFVRTVHHLDDFDDP---------RLAACQERAIVEADAVLCVSAAWAAELRAEWGIDATVVpngVDAA----- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 184 DYIPRSPAECLPVLQKYQLAWQGYALYIGTMEPRKNIRGLLQAYQLLpmetRMRYP---LILSG------YRGWEDDVLW 254
Cdd:TIGR04047 172 RFSPAADAADAALRRRLGLRGGPYVLAVGGIEPRKNTIDLLEAFALL----RARRPqaqLVIAGgatlfdYDAYRREFRA 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 255 QLVERGTREGWIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD-AGLVADPND 333
Cdd:TIGR04047 248 RAAELGVDPGPVVITGPVPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRfDAAWADPSD 327

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1170892743 334 VDAISAHILQSLqDDSWREVATARGLAQAKQFSWE 368
Cdd:TIGR04047 328 PDSIADALALAL-DPARRPALRAAGPELAARYTWD 361
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 280-379 7.73e-28

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 105.84  E-value: 7.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 280 LYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWREVATAR 357
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIedGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|...
gi 1170892743 358 GLAQA-KQFSWENCTTQTINAYK 379
Cdd:COG0438    97 ARERAeERFSWEAIAERLLALYE 119
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 268-376 1.20e-13

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 72.05  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 268 YLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV-----GDAGLVADPNDVDAISAHIL 342
Cdd:PLN02871  316 FTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdqeGKTGFLYTPGDVDDCVEKLE 395

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1170892743 343 QSLQDDSWREVATARGLAQAKQFSWENCTTQTIN 376
Cdd:PLN02871  396 TLLADPELRERMGAAAREEVEKWDWRAATRKLRN 429
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 2-376 1.89e-124

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: 363.22  E-value: 1.89e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743   2 KIIFATEPIKYPLTGIGRYSLELVKRLAVAREIEELKLFHGASFIDQIPQVENKSDtkasNHGRLSAFLRRQPLLieayr 81
Cdd:cd03809     1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLLREYPEL----SLGVIKIKLWRELAL----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  82 llHPRRQAWALRDYKDYIYHGPNFYLPHRLE--RAVTTFHDISIFTCPEYHPKDRVRYMEKSLHESLDSAKLILTVSDFS 159
Cdd:cd03809    72 --LRWLQILLPKKDKPDLLHSPHNTAPLLLKgcPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLRRADAIITVSEAT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 160 RSEIIRLFNYPADRIVTTKLACSSDYiprSPAECLPVLQKYQLAWQGYALYIGTMEPRKNIRGLLQAYQLLPMETRmRYP 239
Cdd:cd03809   150 RDDIIKFYGVPPEKIVVIPLGVDPSF---FPPESAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGG-DLK 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 240 LILSGYRGWEDDVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLP 319
Cdd:cd03809   226 LVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLP 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892743 320 EVVGDAGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQAKQFSWENCTTQTIN 376
Cdd:cd03809   306 EVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-379 1.13e-48

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: 168.49  E-value: 1.13e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743   2 KIIFATEPIKYPLTGIGRYSLELVKRLAvaREIEELKLFHGASFidqipqvenKSDTKASNHGRLSAFLRRQPLLIEAYR 81
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALA--ARGHDVTVLTPADP---------GEPPEELEDGVIVPLLPSLAALLRARR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  82 LLHPRRQAWALRDYkDYIY-HGPNFYLPHRL------ERAVTTFHDISIFTCPEYHPKDRvRYMEKSLhESLDSAKLILT 154
Cdd:cd03801    70 LLRELRPLLRLRKF-DVVHaHGLLAALLAALlalllgAPLVVTLHGAEPGRLLLLLAAER-RLLARAE-ALLRRADAVIA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 155 VSDFSRSEIIRLFNYPADRIVTTKLACSSDYIPRSPAECLPVLQKyqlawQGYALYIGTMEPRKNIRGLLQAYQLLPMET 234
Cdd:cd03801   147 VSEALRDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLGIPPD-----RPVLLFVGRLSPRKGVDLLLEALAKLLRRG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 235 RmRYPLILSGYRGWEDDVLWQLVERGtrEGWIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSN 314
Cdd:cd03801   222 P-DVRLVIVGGDGPLRAELEELELGL--GDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATD 298

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1170892743 315 VTSLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQ-AKQFSWENCTTQTINAYK 379
Cdd:cd03801   299 VGGLPEVVedGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 207-352 4.63e-36

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: 128.93  E-value: 4.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 207 YALYIGTMEPRKNIRGLLQAYQLLPmETRMRYPLILSGYRGWEDDVLWQLVERGTREGwIRYLGYVPDEDLPYLYAAART 286
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALLK-EKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDN-VIFLGFVSDEDLPELLKIADV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1170892743 287 FVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD--AGLVADPNDVDAISAHILQSLQDDSWRE 352
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDgeTGFLVKPNNAEALAEAIDKLLEDEELRE 149
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 107-368 9.66e-32

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


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 123.28  E-value: 9.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 107 LPHRLERAVTTFHDISIFTCPeyhpkdrvrYMEKSLHESLDSAKLILTVSDFSRSEIIRLFNYPADRI---VTTKlacss 183
Cdd:TIGR04047 106 AEGLIPGFVRTVHHLDDFDDP---------RLAACQERAIVEADAVLCVSAAWAAELRAEWGIDATVVpngVDAA----- 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 184 DYIPRSPAECLPVLQKYQLAWQGYALYIGTMEPRKNIRGLLQAYQLLpmetRMRYP---LILSG------YRGWEDDVLW 254
Cdd:TIGR04047 172 RFSPAADAADAALRRRLGLRGGPYVLAVGGIEPRKNTIDLLEAFALL----RARRPqaqLVIAGgatlfdYDAYRREFRA 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 255 QLVERGTREGWIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD-AGLVADPND 333
Cdd:TIGR04047 248 RAAELGVDPGPVVITGPVPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRfDAAWADPSD 327

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1170892743 334 VDAISAHILQSLqDDSWREVATARGLAQAKQFSWE 368
Cdd:TIGR04047 328 PDSIADALALAL-DPARRPALRAAGPELAARYTWD 361
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
209-347 3.66e-30

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 112.60  E-value: 3.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTM-EPRKNIRGLLQAYQLLpMETRMRYPLILSGyRGWEDDVlwQLVERGTREGwIRYLGYVpdEDLPYLYAAARTF 287
Cdd:pfam13692   5 LFVGRLhPNVKGVDYLLEAVPLL-RKRDNDVRLVIVG-DGPEEEL--EELAAGLEDR-VIFTGFV--EDLAELLAAADVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1170892743 288 VYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV-GDAGLVADPNDVDAISAHILQSLQD 347
Cdd:pfam13692  78 VLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVdGENGLLVPPGDPEALAEAILRLLED 138
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 209-374 6.68e-30

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: 118.50  E-value: 6.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLPMETRMRYPLILSGYRGWEDDVLWQLVERGTREGWI----RYLGYVPDEDLPYLYAAA 284
Cdd:cd03800   224 LALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDPLSMDREELAELAEELGLidrvRFPGRVSRDDLPELYRAA 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 285 RTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQA 362
Cdd:cd03800   304 DVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVrdGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERA 383

                         170
                  ....*....|...
gi 1170892743 363 KQ-FSWENCTTQT 374
Cdd:cd03800   384 RAhYTWESVADQL 396
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 280-379 7.73e-28

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 105.84  E-value: 7.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 280 LYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWREVATAR 357
Cdd:COG0438    17 LLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIedGETGLLVPPGDPEALAEAILRLLEDPELRRRLGEA 96

                          90       100
                  ....*....|....*....|...
gi 1170892743 358 GLAQA-KQFSWENCTTQTINAYK 379
Cdd:COG0438    97 ARERAeERFSWEAIAERLLALYE 119
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 207-369 8.64e-28

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: 112.47  E-value: 8.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 207 YALYIGTMEPRKNIRGLLQAYQLLPMEtRMRYPLILSGyRGWEDDVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAART 286
Cdd:cd03798   202 VILFVGRLIPRKGIDLLLEAFARLAKA-RPDVVLLIVG-DGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDV 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 287 FVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD--AGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQAKQ 364
Cdd:cd03798   280 FVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDpeTGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAER 359


                  ....*
gi 1170892743 365 FSWEN 369
Cdd:cd03798   360 FSWVK 364
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 113-381 2.08e-25

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: 105.51  E-value: 2.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 113 RAVTTFH--DISIFTcpeYHP--KDRVRYmekSLHESldsaKLILTVSDFSRSEIIRLFNYPADRIVTTKLACSSDYiPR 188
Cdd:cd04962   112 PIVTTLHgtDITLVG---YDPslQPAVRF---SINKS----DRVTAVSSSLRQETYELFDVDKDIEVIHNFIDEDVF-KR 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 189 SPAECLpVLQKYQLAWQGYALYIGTMEPRKNIRGLLQAYQLLPMETRMRypLILSGyRGWEDDVLWQLVERGTREGWIRY 268
Cdd:cd04962   181 KPAGAL-KRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPAK--LLLVG-DGPERVPAEELARELGVEDRVLF 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 269 LGYVPDEDlpYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQSLQ 346
Cdd:cd04962   257 LGKQDDVE--ELLSIADLFLLPSEKESFGLAALEAMACGVPVVSSNAGGIPEVVkhGETGFLSDVGDVDAMAKSALSILE 334

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1170892743 347 DDS-WREVATARGLAQAKQFSWENCTTQTINAYKLL 381
Cdd:cd04962   335 DDElYNRMGRAARKRAAERFDPERIVPQYEAYYRRL 370
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 209-368 1.15e-24

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: 103.60  E-value: 1.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLpMETRMRYPLILSGYRGWEDDVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAARTFV 288
Cdd:cd03821   208 LFLGRIHPKKGLDLLIRAARKL-AEQGRDWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFV 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 289 YPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV-GDAGLVADPNDvDAISAHILQSLQDDSWREVATARGLA---QAKQ 364
Cdd:cd03821   287 LPSYSENFGNVVAEALACGLPVVITDKCGLSELVeAGCGVVVDPNV-SSLAEALAEALRDPADRKRLGEMARRarqVEEN 365


                  ....
gi 1170892743 365 FSWE 368
Cdd:cd03821   366 FSWE 369
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 115-371 1.77e-24

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: 102.92  E-value: 1.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 115 VTTFHDISIFTCPEYHPKDRVRYMEKSLHESLDS--AKLILTVSDFSRSEIIRLfNYPADRIV-------TTKLAcssdy 185
Cdd:cd05844   108 VVTFHGFDITTSRAWLAASPGWPSQFQRHRRALQrpAALFVAVSGFIRDRLLAR-GLPAERIHvhyigidPAKFA----- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 186 iPRSPAECLPvlqkyqlawqgYALYIGTMEPRKNIRGLLQAYQLLpmetRMRYP---LILSGyRGWEDDVLWQLVERGTR 262
Cdd:cd05844   182 -PRDPAERAP-----------TILFVGRLVEKKGCDVLIEAFRRL----AARHPtarLVIAG-DGPLRPALQALAAALGR 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 263 egwIRYLGYVPDEDLPYLYAAARTFVYPSFY------EGFGLPILEAMSCGVPVVCSNVTSLPEVVGD--AGLVADPNDV 334
Cdd:cd05844   245 ---VRFLGALPHAEVQDWMRRAEIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDgeTGFLVPEGDV 321

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1170892743 335 DAISAHILQSLQDDSWREVATARGLAQA-KQFSWENCT 371
Cdd:cd05844   322 DALADALQALLADRALADRMGGAARAFVcEQFDIRVQT 359
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 65-381 1.17e-22

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: 97.77  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  65 RLSAFLRRqplliEAYRLLHprrqAWAlrdykdyiYHgPNFY--LPHRLERAVTTFHDISIFTCPEYHPKdRVRYMEKSL 142
Cdd:cd03807    70 RLAKLIRK-----RNPDVVH----TWM--------YH-ADLIggLAAKLAGGVKVIWSVRSSNIPQRLTR-LVRKLCLLL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 143 HeslDSAKLILTVSDFSRSEIIRLfNYPADRIVTTKLACSSDYIPRSPAECLPVLQKYQLAWQGYALYI-GTMEPRKNIR 221
Cdd:cd03807   131 S---KFSPATVANSSAVAEFHQEQ-GYAKNKIVVIYNGIDLFKLSPDDASRARARRRLGLAEDRRVIGIvGRLHPVKDHS 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 222 GLLQAYQLLPmETRMRYPLILSGyRGWEDDVLWQLVERGTREGWIRYLGYVPDedLPYLYAAARTFVYPSFYEGFGLPIL 301
Cdd:cd03807   207 DLLRAAALLV-ETHPDLRLLLVG-RGPERPNLERLLLELGLEDRVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALL 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 302 EAMSCGVPVVCSNVTSLPEVVGD-AGLVADPNDVDAISAHILQSLQD-DSWREVATARGLAQAKQFSWENCttqtINAYK 379
Cdd:cd03807   283 EAMACGLPVVATDVGGAAELVDDgTGFLVPAGDPQALADAIRALLEDpEKRARLGRAARERIANEFSIDAM----VRRYE 358


                  ..
gi 1170892743 380 LL 381
Cdd:cd03807   359 TL 360
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 3-362 2.63e-22

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: 96.66  E-value: 2.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743   3 IIFATEpiKYPLTGIGRYSLELvkrlavAREIEEL-----------KLFHGASFIDQIPQVENKSDTKASNHGRLSAFL- 70
Cdd:cd03819     1 ILMLTP--ALEIGGAETYILDL------ARALAERghrvlvvtaggPLLPRLRQIGIGLPGLKVPLLRALLGNVRLARLi 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  71 -RRQPLLIEAyrllHPRRQAWALrdykdyiyhgpnfYLPHRLERA--VTTFHDISIFTcpeYHPKDRVRYMEKSlhesld 147
Cdd:cd03819    73 rRERIDLIHA----HSRAPAWLG-------------WLASRLTGVplVTTVHGSYLAT---YHPKDFALAVRAR------ 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 148 sAKLILTVSDFSRSEIIRLFNYPADRIVTtklacssdyIPRS--PAECLPVLQKYQLAWQGYA------LYIGTMEPRKN 219
Cdd:cd03819   127 -GDRVIAVSELVRDHLIEALGVDPERIRV---------IPNGvdTDRFPPEAEAEERAQLGLPegkpvvGYVGRLSPEKG 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 220 IRGLLQAYQLLPMETRMRypLILSGyRGWEDDVLWQLVERGTREGWIRYLGYvpDEDLPYLYAAARTFVYPSFYEGFGLP 299
Cdd:cd03819   197 WLLLVDAAAELKDEPDFR--LLVAG-DGPERDEIRRLVERLGLRDRVTFTGF--REDVPAALAASDVVVLPSLHEEFGRV 271

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1170892743 300 ILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQ-SLQDDSWREVATARGLAQA 362
Cdd:cd03819   272 ALEAMACGTPVVATDVGGAREIVvhGRTGLLVPPGDAEALADAIRAaKLLPEAREKLQAAAALTEA 337
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 145-352 7.81e-22

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: 95.12  E-value: 7.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 145 SLDSAKLILTVSDFSRSEIIRLFNYPADRIVTtklacssDYIPRSPAECLPVLQKYQLAWQGYALYI---GTMEPRKNIR 221
Cdd:cd03811   132 LYKKADKIVCVSKGIKEDLIRLGPSPPEKIEV-------IYNPIDIDRIRALAKEPILNEPEDGPVIlavGRLDPQKGHD 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 222 GLLQAYQLLPmETRMRYPLILSGYrGWEDDVLWQLVERGTREGWIRYLGYVPDedlPY-LYAAARTFVYPSFYEGFGLPI 300
Cdd:cd03811   205 LLIEAFAKLR-KKYPDVKLVILGD-GPLREELEKLAKELGLAERVIFLGFQSN---PYpYLKKADLFVLSSRYEGFPNVL 279

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892743 301 LEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDA---ISAHILQSLQDDSWRE 352
Cdd:cd03811   280 LEAMALGTPVVSTDCPGPREILddGENGLLVPDGDAAAlagILAALLQKKLDAALRE 336
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 208-378 2.82e-21

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: 93.90  E-value: 2.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 208 ALYIGTMEPRKNIRGLLQAYQLLPMETRMRYPLILSG-YRGWEDDVLWQLVergtregwirYLGYVPDEDLPYLYAAART 286
Cdd:cd03814   201 LLYVGRLAPEKNLEALLDADLPLAASPPVRLVVVGDGpARAELEARGPDVI----------FTGFLTGEELARAYASADV 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 287 FVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD--AGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQAKQ 364
Cdd:cd03814   271 FVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPggTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAER 350

                         170
                  ....*....|....
gi 1170892743 365 FSWENCTTQTINAY 378
Cdd:cd03814   351 YSWEAFLDNLLDYY 364
thiol_BshA TIGR03999
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, ...
 113-381 4.32e-20

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA; Members of this protein family are BshA, a glycosyltransferase required for bacillithiol biosynthesis. This enzyme combines UDP-GlcNAc and L-malate to form N-acetyl-alpha-D-glucosaminyl L-malate synthase. Bacillithiol is a low-molecular-weight thiol, an analog of glutathione and mycothiol, and is found largely in the Firmicutes. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 274914 [Multi-domain]  Cd Length: 374  Bit Score: 90.74  E-value: 4.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 113 RAVTTFH--DISIFTcpeYHP--KDRVRYmekslheSLDSAKLILTVSDFSRSEIIRLFNYPADRIVTTKLACSSDYIPR 188
Cdd:TIGR03999 115 PIVTTLHgtDITLVG---ADPsfKPAVRF-------SIEKSDGVTAVSESLKEETYELFDIDKPIEVIPNFVDTDRYRRK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 189 SPAEClpvlqKYQLAW---QGYALYIGTMEPRKNIRGLLQAYQLLPMETRMRypLILSGyRGWEDDVLWQLVERGTREGW 265
Cdd:TIGR03999 185 NDPAL-----KRKLGApedEKVLIHISNFRPVKRVEDVIEVFARVQQEVPAK--LLLVG-DGPERSPAEQLVRELGLTDR 256

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 266 IRYLGYVPDedLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQ 343
Cdd:TIGR03999 257 VLFLGKQDD--VAELLSISDLFLLPSEKESFGLAALEAMACGVPVIASNAGGIPEVVehGVTGFLCDVGDVETMAEYAIS 334

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1170892743 344 SLQDDSWREVATARGLAQAK-QFSWENCTTQTINAYKLL 381
Cdd:TIGR03999 335 LLEDEELLQRFSAAARERAKeRFDSEKIVPQYEALYRRL 373
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 209-352 5.93e-20

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: 90.03  E-value: 5.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLpmetrmRYPLILSGyRGWEDDVLWQLVERGTREGwIRYLGYVPDEDLPYLYAAARTFV 288
Cdd:cd03795   195 LFIGRLVYYKGLDYLIEAAQYL------NYPIVIGG-EGPLKPDLEAQIELNLLDN-VKFLGRVDDEEKVIYLHLCDVFV 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1170892743 289 YPSFY--EGFGLPILEAMSCGVPVVCSNV-TSLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWRE 352
Cdd:cd03795   267 FPSVLrsEAFGIVLLEAMMCGKPVISTNIgTGVPYVNnnGETGLVVPPKDPDALAEAIDKLLSDEELRE 335
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 149-352 2.06e-19

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: 88.42  E-value: 2.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 149 AKLILTVSDFSRSEIIRLFNYPADRIVTTKL-ACSSDYIPRSPaECLPvLQKYQLawqgyaLYIGTMEPRKNIRGLLQAY 227
Cdd:cd03808   140 TDKVIFVNEDDRDLAIKKGIIKKKKTVLIPGsGVDLDRFQYSP-ESLP-SEKVVF------LFVARLLKDKGIDELIEAA 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 228 QLLpmetRMRYP---LILSGYrGWEDDVLWQLVERGTREGWIRYLGYVpdEDLPYLYAAARTFVYPSFYEGFGLPILEAM 304
Cdd:cd03808   212 KIL----KKKGPnvrFLLVGD-GELENPSEILIEKLGLEGRIEFLGFR--SDVPELLAESDVFVLPSYREGLPRSLLEAM 284

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1170892743 305 SCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWRE 352
Cdd:cd03808   285 AAGRPVITTDVPGCRELVidGVNGFLVPPGDVEALADAIEKLIEDPELRK 334
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 208-322 2.11e-19

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


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 86.30  E-value: 2.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 208 ALYIGTMEPRKNIRGLLQAYQLLPMETRmRYPLILSGYRGWEDDVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAARTF 287
Cdd:cd01635   113 KVSVGRLVPEKGIDLLLEALALLKARLP-DLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVF 191

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1170892743 288 VYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV 322
Cdd:cd01635   192 VLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 209-366 2.62e-18

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: 85.41  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLPMETRMRypLILSGyRGWEDDVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAARTFV 288
Cdd:cd03817   205 LYVGRLAKEKNIDFLLRAFAELKKEPNIK--LVIVG-DGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFV 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 289 YPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVdAISAHILQSLQDDSWREVATARGLAQAKQFS 366
Cdd:cd03817   282 FASTTETQGLVYLEAMAAGLPVVAAKDPAASELVedGENGFLFEPNDE-TLAEKLLHLRENLELLRKLSKNAEISAREFA 360
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 209-347 5.63e-17

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: 81.22  E-value: 5.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLPmetRMRYPLILSGYRGWEDDVLWQLVERgtregwIRYLGYVPDEDLPYLYAAARTFV 288
Cdd:cd03823   195 GYIGRLTEEKGIDLLVEAFKRLP---REDIELVIAGHGPLSDERQIEGGRR------IAFLGRVPTDDIKDFYEKIDVLV 265

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1170892743 289 YPS-FYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGDA--GLVADPNDVDAISAHILQSLQD 347
Cdd:cd03823   266 VPSiWPEPFGLVVREAIAAGLPVIASDLGGIAELIQPGvnGLLFAPGDAEDLAAAMRRLLTD 327
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 211-379 3.10e-16

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: 79.30  E-value: 3.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 211 IGTMEPRKNIRGLLQAYQLLPMETRMRypLILSGYRGweddvlwqlVERGTREGWIRYLGYV-PDEDLPYLYAAARTFVY 289
Cdd:cd03825   201 ESVTKPRKGFDELIEALKLLATKDDLL--LVVFGKND---------PQIVILPFDIISLGYIdDDEQLVDIYSAADLFVH 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 290 PSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWREV--ATARGLAQaKQF 365
Cdd:cd03825   270 PSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVqhGVTGYLVPPGDVQALAEAIEWLLANPKERESlgERARALAE-NHF 348

                         170
                  ....*....|....
gi 1170892743 366 SWENCTTQTINAYK 379
Cdd:cd03825   349 DQRVQAQRYLELYK 362
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 125-369 2.20e-14

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: 73.43  E-value: 2.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 125 TCPEYHPKDRVRYMEKSLheSLDSAKLILTVSdfsRSEIIRLFNYPADRIVTTKLACSsdYIPRSPAECLPvlQKYQLAw 204
Cdd:cd03820   117 NNYEAYNKGLRRLLLRRL--LYKRADKIVVLT---EADKLKKYKQPNSNVVVIPNPLS--FPSEEPSTNLK--SKRILA- 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 205 qgyalyIGTMEPRKNIRGLLQAYQLLPMetrmRYP---LILSGyRGWEDDVLWQLVERGTREGWIRYLGyvPDEDLPYLY 281
Cdd:cd03820   187 ------VGRLTYQKGFDLLIEAWALIAK----KHPdwkLRIYG-DGPEREELEKLIDKLGLEDRVKLLG--PTKNIAEEY 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 282 AAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLP-EVV--GDAGLVADPNDVDAISAHILQSLQDDSWREVATARG 358
Cdd:cd03820   254 ANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPsEIIedGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNA 333

                         250
                  ....*....|.
gi 1170892743 359 LAQAKQFSWEN 369
Cdd:cd03820   334 RKNAERFSIEK 344
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 135-371 3.66e-14

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


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 73.15  E-value: 3.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 135 VRYMEKSLhesLDSAKLILTVSDfSRSEIIRLFNYPADRIVTTKLACSSDYIPRSPAECLPVLqkyqLAWQG--YALYIG 212
Cdd:cd03794   153 LKKLERKL---YRLADAIIVLSP-GLKEYLLRKGVPKEKIIVIPNWADLEEFKPPPKDELRKK----LGLDDkfVVVYAG 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 213 TMEPRKNIRGLLQAYQLLPMETRMRYPLIlsgyrGWEDDVLWqLVERGTREGW--IRYLGYVPDEDLPYLYAAARTFVYP 290
Cdd:cd03794   225 NIGKAQGLETLLEAAERLKRRPDIRFLFV-----GDGDEKER-LKELAKARGLdnVTFLGRVPKEEVPELLSAADVGLVP 298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 291 ---SFYEGFGLP--ILEAMSCGVPVVCSNV--TSLPEVVGDAGLVADPNDVDAISAHILQSLQDDSWREV--ATARGLAQ 361
Cdd:cd03794   299 lkdNPANRGSSPskLFEYMAAGKPILASDDggSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAmgENGRELAE 378

                         250
                  ....*....|
gi 1170892743 362 aKQFSWENCT 371
Cdd:cd03794   379 -EKFSREKLA 387
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 268-376 1.20e-13

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 72.05  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 268 YLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV-----GDAGLVADPNDVDAISAHIL 342
Cdd:PLN02871  316 FTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdqeGKTGFLYTPGDVDDCVEKLE 395

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1170892743 343 QSLQDDSWREVATARGLAQAKQFSWENCTTQTIN 376
Cdd:PLN02871  396 TLLADPELRERMGAAAREEVEKWDWRAATRKLRN 429
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 209-366 6.63e-11

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


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 63.23  E-value: 6.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLPmETRMRYPLILSGYRGWEDDVLWQLVERGTREGwIRYLGYVpdEDLPYLYAAARTFV 288
Cdd:cd04951   192 LNVGRLTEAKDYPNLLLAISELI-LSKNDFKLLIAGDGPLRNELERLICNLNLVDR-VILLGQI--SNISEYYNAADLFV 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 289 YPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGDAglvadpNDVDAISAHILQSLQ-------DDSWREVATARGLAQ 361
Cdd:cd04951   268 LSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDH------NYVVPVSDPQLLAEKikeifdmSDEERDILGNKNEYI 341


                  ....*
gi 1170892743 362 AKQFS 366
Cdd:cd04951   342 AKNFS 346
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 205-357 9.13e-11

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: 62.31  E-value: 9.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 205 QGYALYIGTMEPRKNIRGLLQAYQllpmetRMRYPLILSGYRGWED--DVLWQLVERGTregwIRYLGYVPDEDLPYLYA 282
Cdd:cd03802   169 EDYLAFLGRIAPEKGLEDAIRVAR------RAGLPLKIAGKVRDEDyfYYLQEPLPGPR----IEFIGEVGHDEKQELLG 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 283 AARTFVYPS-FYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGDA--GLVADPndVDAISAHILQSLQDDSW--REVATAR 357
Cdd:cd03802   239 GARALLFPInWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGetGFLVDS--VEEMAEAIANIDRIDRAacRRYAEDR 316
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
 215-372 3.96e-10

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: 61.72  E-value: 3.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  215 EPRKNIRGLLQAY-QLLPMETRMRYPLILsGYRGWEDD-----------VLwQLVERGTREGWIRYLGYVPDEDLPYLYA 282
Cdd:TIGR02468  489 DPKKNITTLVKAFgECRPLRELANLTLIM-GNRDDIDEmssgsssvltsVL-KLIDKYDLYGQVAYPKHHKQSDVPDIYR 566

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  283 -AART---FVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEV--VGDAGLVADPNDVDAISAHILQSLQDDS-WREvAT 355
Cdd:TIGR02468  567 lAAKTkgvFINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIhrVLDNGLLVDPHDQQAIADALLKLVADKQlWAE-CR 645

                          170
                   ....*....|....*...
gi 1170892743  356 ARGLAQAKQFSW-ENCTT 372
Cdd:TIGR02468  646 QNGLKNIHLFSWpEHCKT 663
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 211-379 7.78e-10

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: 60.04  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 211 IGTMEPRKNIRGLLQAYQLLpmetRMRYPlilsGYRGW-----EDDVLW-----QLVERGTREGWIRYLGYVPDEDLpyl 280
Cdd:cd03813   299 VGRVVPIKDVKTFIRAFKLV----RRAMP----DAEGWligpeDEDPEYaqeckRLVASLGLENKVKFLGFQNIKEY--- 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 281 YAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD-------AGLVADPNDVDAISAHILQSLQDDSWREV 353
Cdd:cd03813   368 YPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGaddalgqAGLVVPPADPEALAEALIKLLRDPELRQA 447

                         170       180
                  ....*....|....*....|....*..
gi 1170892743 354 ATARGLAQAKQ-FSWENCTTQTINAYK 379
Cdd:cd03813   448 FGEAGRKRVEKyYTLEGMIDSYRKLYL 474
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 205-369 4.06e-09

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: 57.68  E-value: 4.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 205 QGYALYIGTMEPRKNIRGLLQAYqllpmeTRMRYPLILSGyrgwEDDVLWQLVERGTREgwIRYLGYVPDEDLPYLYAAA 284
Cdd:cd03804   199 EDYYLTASRLVPYKRIDLAVEAF------NELPKRLVVIG----DGPDLDRLRAMASPN--VEFLGYQPDEVLKELLSKA 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 285 RTFVYPSfYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISA--HILQSLQDDSWREVATARgla 360
Cdd:cd03804   267 RAFVFAA-EEDFGIVPVEAQACGTPVIAFGKGGALETVrpGPTGILFGEQTVESLKAavEEFEQNFDRFKPQAIRAN--- 342


                  ....*....
gi 1170892743 361 qAKQFSWEN 369
Cdd:cd03804   343 -AERFSRAR 350
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 115-356 7.53e-09

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


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 56.69  E-value: 7.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 115 VTTFH--DISIFTcPEYHPKDRVRYMEKSlhesldsaKLILTVSDFSRSEIIRLfNYPADRIVTTKLACSSDYIPRSPAE 192
Cdd:cd03799    99 VTSFRgyDISMYV-ILEGNKVYPQLFAQG--------DLFLPNCELFKHRLIAL-GCDEKKIIVHRSGIDCNKFRFKPRY 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 193 cLPVLQKYQLawqgyaLYIGTMEPRKNIRGLLQAY-QLLPMETRMRYPLIlsGYRGWEDDvLWQLVERGTREGWIRYLGY 271
Cdd:cd03799   169 -LPLDGKIRI------LTVGRLTEKKGLEYAIEAVaKLAQKYPNIEYQII--GDGDLKEQ-LQQLIQELNIGDCVKLLGW 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 272 VPDEDLPYLYAAARTFVYPSF------YEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD--AGLVADPNDVDAIsAHILQ 343
Cdd:cd03799   239 KPQEEIIEILDEADIFIAPSVtaadgdQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDgvSGFLVPERDAEAI-AEKLT 317

                         250
                  ....*....|....*
gi 1170892743 344 SL--QDDSWREVATA 356
Cdd:cd03799   318 YLieHPAIWPEMGKA 332
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 209-379 1.19e-08

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: 56.24  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLPMET-RMRYpLILSG-------YRGwEDDVLWQLVERGTREGWIRYLGYVPDEDLPYL 280
Cdd:cd03822   191 LTFGFIGPGKGLEILLEALPELKAEFpDVRL-VIAGElhpslarYEG-ERYRKAAIEELGLQDHVDFHNNFLPEEEVPRY 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 281 YAAARTFVYPsFYEGF----GLPILeAMSCGVPVVCSNVTSLPE-VVGDAGLVADPNDVDAISAHILQSLQDDSWREVAT 355
Cdd:cd03822   269 ISAADVVVLP-YLNTEqsssGTLSY-AIACGKPVISTPLRHAEElLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIA 346

                         170       180
                  ....*....|....*....|....
gi 1170892743 356 ARGLAQAKQFSWENCTTQTINAYK 379
Cdd:cd03822   347 ERAYAYARAMTWESIADRYLRLFN 370
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 209-373 2.60e-08

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


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 55.00  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLpmetRMRYP---LILSGYrGWEDDVLWQLVERGTREGWIRYLGYVPDEDLpyLYAAAR 285
Cdd:cd04949   164 ITISRLAPEKQLDHLIEAVAKA----VKKVPeitLDIYGY-GEEREKLKKLIEELHLEDNVFLKGYHSNLDQ--EYQDAY 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 286 TFVYPSFYEGFGLPILEAMSCGVPVVCSNVT-SLPEVV--GDAGLVADPNDVDAISAHILQSLQDDSWREVATARGLAQA 362
Cdd:cd04949   237 LSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIedGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIA 316

                         170
                  ....*....|.
gi 1170892743 363 KQFSWENCTTQ 373
Cdd:cd04949   317 EKYSTENVMEK 327
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 210-324 4.84e-08

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: 54.22  E-value: 4.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 210 YIGTMEPRKNIRGLLQAYQLLPmETRMRYPLILSGyRGWEDDVLWQLVERGTREGWIRYLGYVpdEDLPYLYAAARTFVY 289
Cdd:cd03812   196 HVGRFNEQKNHSFLIDIFEELK-KKNPNVKLVLVG-EGELKEKIKEKVKELGLEDKVIFLGFR--NDVSEILSAMDVFLF 271

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1170892743 290 PSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGD 324
Cdd:cd03812   272 PSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN 306
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 189-358 3.31e-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: 51.55  E-value: 3.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 189 SPAECLPVLQKYQLAW--QGYALYIGTMEPRKNIRGLLQAYQLLpmetRMRYP---LILSGYrGWEDDvlwqlvergtRE 263
Cdd:cd03792   179 SPADIRYYLEKPFVIDpeRPYILQVARFDPSKDPLGVIDAYKLF----KRRAEepqLVICGH-GAVDD----------PE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 264 GWIRY-----------LGYV-----PDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDA 325
Cdd:cd03792   244 GSVVYeevmeyagddhDIHVlrlppSDQEINALQRAATVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVidGET 323

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1170892743 326 GLVADPNDVDAIsaHILQSLQDDSWREVATARG 358
Cdd:cd03792   324 GFLVNSVEGAAV--RILRLLTDPELRRKMGLAA 354
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 238-347 1.74e-06

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 49.67  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 238 YPLILSGYRGWEDDVLWQLveRGTREGwIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTS 317
Cdd:cd03818   258 YGSPPPDGGSWKQKMLAEL--GVDLER-VHFVGKVPYDQYVRLLQLSDAHVYLTYPFVLSWSLLEAMACGCPVIGSDTAP 334

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1170892743 318 LPEVV--GDAGLVADPNDVDAISAHILQSLQD 347
Cdd:cd03818   335 VREVIrdGRNGLLVDFFDPDALAAAVLELLED 366
PLN00142 PLN00142
sucrose synthase
 287-381 1.82e-06

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 49.98  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 287 FVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADPNDVDAISAHI---LQSLQDDS--WREVATArGL 359
Cdd:PLN00142  670 FVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIvdGVSGFHIDPYHGDEAANKIadfFEKCKEDPsyWNKISDA-GL 748

                          90       100
                  ....*....|....*....|..
gi 1170892743 360 AQAkqfswENCTTQTINAYKLL 381
Cdd:PLN00142  749 QRI-----YECYTWKIYAERLL 765
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 251-378 4.86e-06

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


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 48.00  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 251 DVLWQLVERGTREGWIRYLGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVV-GDAGLVA 329
Cdd:cd03796   237 IELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEVLpPDMILLA 316

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1170892743 330 DPnDVDAIS------AHILQSLQDDSW---REVatarglaqAKQFSWENCTTQTINAY 378
Cdd:cd03796   317 EP-DPEDIVrkleeaISILRTGKHDPWsfhNRV--------KKMYSWEDVARRTEKVY 365
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 268-354 1.01e-05

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


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 47.07  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 268 YLGYVPDEDLPYLYA--AARTFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPEVVGDA--GLVAD----PND-VDAIS 338
Cdd:cd04946   287 FTGEVSNKEVKQLYKenDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENEtnGLLLDkdptPNEiVSSIM 366

                          90
                  ....*....|....*.
gi 1170892743 339 AHILQSLQDDSWREVA 354
Cdd:cd04946   367 KFYLDGGDYKTMKISA 382
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
209-371 2.35e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 45.94  E-value: 2.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTMEPRKNIRGLLQAYQLLpMETRMRYPLILSG-----YRG----WEDDVLWQLVERGTRegwIRYLGYVPDEDLPY 279
Cdd:PRK15484  197 LYAGRISPDKGILLLMQAFEKL-ATAHSNLKLVVVGdptasSKGekaaYQKKVLEAAKRIGDR---CIMLGGQPPEKMHN 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 280 LYAAARTFVYPS-FYEGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGL-VADPNDVDAISAHILQSLQDDSWREVA- 354
Cdd:PRK15484  273 YYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEFVleGITGYhLAEPMTSDSIISDINRTLADPELTQIAe 352

                         170
                  ....*....|....*..
gi 1170892743 355 TARGLAQAKqFSWENCT 371
Cdd:PRK15484  353 QAKDFVFSK-YSWEGVT 368
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
151-360 8.01e-05

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 44.15  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 151 LILTvsdFSRSEIIRLFNYPADRIVTTKLACSSD-YIPRSPAEclpvlqkyqlAWQGYALYIGTMEP--RKNIRGLLQAY 227
Cdd:COG4641    95 LVFT---FDGDCVEEYRALGARRVFYLPFAADPElHRPVPPEA----------RFRYDVAFVGNYYPdrRARLEELLLAP 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 228 qllpmetrMRYPLILSGyRGWEDDvlwqlvergTREGWIRYLGYVPDEDLPYLYAAAR-TFVYPSFYEGFGLP---ILEA 303
Cdd:COG4641   162 --------AGLRLKIYG-PGWPKL---------ALPANVRRGGHLPGEEHPAAYASSKiTLNVNRMAASPDSPtrrTFEA 223

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1170892743 304 MSCGVPVVCSNVTSLPE--VVGDAGLVADpnDVDAISAHILQSLQDDSWREVATARGLA 360
Cdd:COG4641   224 AACGAFLLSDPWEGLEElfEPGEEVLVFR--DGEELAEKLRYLLADPEERRAIAEAGRR 280
PHA01633 PHA01633
putative glycosyl transferase group 1
 269-311 1.15e-04

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 43.81  E-value: 1.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1170892743 269 LGYVPDEDLPYLYAAARTFVYPSFYEGFGLPILEAMSCGVPVV 311
Cdd:PHA01633  209 FGHNSREYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMGTPVI 251
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
209-343 6.53e-04

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 41.24  E-value: 6.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 209 LYIGTM--EPRKNIRGLLQAYQLLPMETRMRypLILSGyrgwEDDVLWQ-------LVERGTREGWIRYLGYVPDEDLPY 279
Cdd:PRK09922  184 LYVGRLkfEGQKNVKELFDGLSQTTGEWQLH--IIGDG----SDFEKCKaysrelgIEQRIIWHGWQSQPWEVVQQKIKN 257

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1170892743 280 LYAaartFVYPSFYEGFGLPILEAMSCGVPVVCSNVTSLPE--VVGDA-GLVADPNDVDAISAHILQ 343
Cdd:PRK09922  258 VSA----LLLTSKFEGFPMTLLEAMSYGIPCISSDCMSGPRdiIKPGLnGELYTPGNIDEFVGKLNK 320
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
16-176 7.46e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 39.82  E-value: 7.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  16 GIGRYSLELVKRLA--------VAREIEElKLFHGASFIDQIPQVENKSDTKASNHGRLSAFLRRqplLIEAYR--LLHp 85
Cdd:pfam13439   2 GVERYVLELARALArrghevtvVTPGGPG-PLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRR---LLRRERpdVVH- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743  86 rrqawaLRDYKDYIYHGPNFYLPHRLeRAVTTFHDISIFTCPEYHPKDRVRYMEKSLHE-SLDSAKLILTVSDFSRSEII 164
Cdd:pfam13439  77 ------AHSPFPLGLAALAARLRLGI-PLVVTYHGLFPDYKRLGARLSPLRRLLRRLERrLLRRADRVIAVSEAVADELR 149

                         170
                  ....*....|..
gi 1170892743 165 RLFNYPADRIVT 176
Cdd:pfam13439 150 RLYGVPPEKIRV 161
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 149-314 7.58e-04

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: 41.42  E-value: 7.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 149 AKLILTVSDFSRSEIIRLFNYPADRIVTTKL-ACSSDYIPRSPAECLPVLQkyqLAWQGYALY--IGTMEPRKNIRGLLQ 225
Cdd:cd03805   155 ADQIVVNSNFTAGVFKKTFPSLAKNPPEVLYpCVDTDSFDSTSEDPDPGDL---IAKSNKKFFlsINRFERKKNIALAIE 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 226 AYQLLPMETRMRYP--LILSGyrGWEDDV---------LWQLVERGT-REGWIRYLGYVPDEDLPYLYAAARTFVY-PSf 292
Cdd:cd03805   232 AFAKLKQKLPEFENvrLVIAG--GYDPRVaenveyleeLQRLAEELLnVEDQVLFLRSISDSQKEQLLSSALALLYtPS- 308

                         170       180
                  ....*....|....*....|..
gi 1170892743 293 YEGFGLPILEAMSCGVPVVCSN 314
Cdd:cd03805   309 NEHFGIVPLEAMYAGKPVIACN 330
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
 266-377 1.43e-03

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 40.43  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 266 IRYLGYVPDEDLP-YLY------------AAARtFVYPsfyegfgLPILEAMSCGVPVVCSNVTSLPEVVGDAGLVADPN 332
Cdd:cd04950   255 IHWLGPKPYKELPaYLAgfdvallpfalnEYTR-FISP-------LKLFEYLAAGKPVVATSIPSVVRFYGEAVLCGDDP 326

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1170892743 333 D--VDAISAHILQSLQDDSWREVAtarglAQAKQFSWeNCTTQTINA 377
Cdd:cd04950   327 DefSAAIEKALALKGDARDKRLAR-----ALARQESW-DERARAMEE 367
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
294-373 5.08e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 36.04  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1170892743 294 EGFGLPILEAMSCGVPVVCSNVTSLPEVV--GDAGLVADpnDVDAISAHILQSLQDDSWREVATARGLAQA-KQFSWENC 370
Cdd:pfam13524  10 DSPNMRVFEAAACGAPLLTDRTPGLEELFepGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAGRERVlAEHTYAHR 87


                  ...
gi 1170892743 371 TTQ 373
Cdd:pfam13524  88 AEQ 90
 
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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