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Conserved domains on  [gi|2526276233|ref|WP_287811682|]
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glycosyltransferase [Advenella sp.]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133549)

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_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 2-398 1.56e-77

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: 258.06  E-value: 1.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233   2 RIVIDMQGAqstGSRHRGIGRYTMALVQEIVRNRGDHEVILAVNgyfsdsiepirTAFDKLLPPENIQIWNTVTPTAKAe 81
Cdd:cd03809     1 KILIDGRSL---AQRLTGIGRYTRELLKALAKNDPDESVLAVPP-----------LPGELLRLLREYPELSLGVIKIKL- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  82 tdndWRRHAGELLREAFLASL-KPDVVLVSSLFEGLtdnavtsiaqFTRDFPTAVILYDLIPLIHHEIYLENpVVKAYYS 160
Cdd:cd03809    66 ----WRELALLRWLQILLPKKdKPDLLHSPHNTAPL----------LLKGCPQVVTIHDLIPLRYPEFFPKR-FRLYYRL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 161 EKIEFLRQADLWLAISESSRQEGISHLDLSKDWSANISTDADGHFRKvpvsAEAESELRKKYGLYHPFVMYTGGIDHRKN 240
Cdd:cd03809   131 LLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFP----PESAAVLIAKYLLPEPYFLYVGTLEPRKN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 241 IEGLIRSYAKLPQNLRAsHQLAIVCSIQAENRRNLEALarKCGLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFG 320
Cdd:cd03809   207 HERLLKAFALLKKQGGD-LKLVIVGGKGWEDEELLDLV--KKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFG 283

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526276233 321 LPALEAMRCGAPVIGANTSSLPEVIGLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMKFSWAESARRAI 398
Cdd:cd03809   284 LPVLEAMACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 422-809 2.08e-26

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: 112.25  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 422 KLAYISP-LPPERSGIADYSAELLPELARH-YDIEVVVVQDNVTDEWINANCPIRTVQYFRDNASSYDRVLYQFGnsafh 499
Cdd:cd03801     1 KILLLSPeLPPPVGGAERHVRELARALAARgHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 500 qhmFELLGTHPGVVVLHDFYLSGISHYMEAHAIEPAFWTkelYHAHGYAAFYDRYHSKDEVDVIWKYPCSLSVVqnslgV 579
Cdd:cd03801    76 ---PLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVT---LHGAEPGRLLLLLAAERRLLARAEALLRRADA-----V 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 580 IAHSQNSLRLAKRWYGDNGENWAVIPHMRDPhvNKDRVLARQALGLGVDDFVVCSFGMLGPTKLNHRLLEAwLNSRLGAD 659
Cdd:cd03801   145 IAVSEALRDELRALGGIPPEKIVVIPNGVDL--ERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEA-LAKLLRRG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 660 KNCHLVFVGENhpGTYGVELLEiiRNHRAEKNIRITGWADLDLFRNYLAAADMGVqlrTLSRGETSGTV-LDCMCHSLAT 738
Cdd:cd03801   222 PDVRLVIVGGD--GPLRAELEE--LELGLGDRVRFLGFVPDEELPALYAAADVFV---LPSRYEGFGLVvLEAMAAGLPV 294

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526276233 739 IVNANGSMADL--NEQAVWmLSDEFSDEELITALETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQDAIE 809
Cdd:cd03801   295 VATDVGGLPEVveDGEGGL-VVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 2-398 1.56e-77

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: 258.06  E-value: 1.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233   2 RIVIDMQGAqstGSRHRGIGRYTMALVQEIVRNRGDHEVILAVNgyfsdsiepirTAFDKLLPPENIQIWNTVTPTAKAe 81
Cdd:cd03809     1 KILIDGRSL---AQRLTGIGRYTRELLKALAKNDPDESVLAVPP-----------LPGELLRLLREYPELSLGVIKIKL- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  82 tdndWRRHAGELLREAFLASL-KPDVVLVSSLFEGLtdnavtsiaqFTRDFPTAVILYDLIPLIHHEIYLENpVVKAYYS 160
Cdd:cd03809    66 ----WRELALLRWLQILLPKKdKPDLLHSPHNTAPL----------LLKGCPQVVTIHDLIPLRYPEFFPKR-FRLYYRL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 161 EKIEFLRQADLWLAISESSRQEGISHLDLSKDWSANISTDADGHFRKvpvsAEAESELRKKYGLYHPFVMYTGGIDHRKN 240
Cdd:cd03809   131 LLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFP----PESAAVLIAKYLLPEPYFLYVGTLEPRKN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 241 IEGLIRSYAKLPQNLRAsHQLAIVCSIQAENRRNLEALarKCGLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFG 320
Cdd:cd03809   207 HERLLKAFALLKKQGGD-LKLVIVGGKGWEDEELLDLV--KKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFG 283

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526276233 321 LPALEAMRCGAPVIGANTSSLPEVIGLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMKFSWAESARRAI 398
Cdd:cd03809   284 LPVLEAMACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 227-384 1.03e-34

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: 130.09  E-value: 1.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 227 PFVMYTGGIDHRKNIEGLIRSYAKLPQNLrasHQLAIVCSIQAENRRNLEALARKCGLEeDELILTGFVSEEDLVRLYNL 306
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKN---PNLKLVIAGDGEEEKRLKKLAEKLGLG-DNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 307 CHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVI--GLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQ 384
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkdGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 422-809 2.08e-26

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: 112.25  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 422 KLAYISP-LPPERSGIADYSAELLPELARH-YDIEVVVVQDNVTDEWINANCPIRTVQYFRDNASSYDRVLYQFGnsafh 499
Cdd:cd03801     1 KILLLSPeLPPPVGGAERHVRELARALAARgHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 500 qhmFELLGTHPGVVVLHDFYLSGISHYMEAHAIEPAFWTkelYHAHGYAAFYDRYHSKDEVDVIWKYPCSLSVVqnslgV 579
Cdd:cd03801    76 ---PLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVT---LHGAEPGRLLLLLAAERRLLARAEALLRRADA-----V 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 580 IAHSQNSLRLAKRWYGDNGENWAVIPHMRDPhvNKDRVLARQALGLGVDDFVVCSFGMLGPTKLNHRLLEAwLNSRLGAD 659
Cdd:cd03801   145 IAVSEALRDELRALGGIPPEKIVVIPNGVDL--ERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEA-LAKLLRRG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 660 KNCHLVFVGENhpGTYGVELLEiiRNHRAEKNIRITGWADLDLFRNYLAAADMGVqlrTLSRGETSGTV-LDCMCHSLAT 738
Cdd:cd03801   222 PDVRLVIVGGD--GPLRAELEE--LELGLGDRVRFLGFVPDEELPALYAAADVFV---LPSRYEGFGLVvLEAMAAGLPV 294

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526276233 739 IVNANGSMADL--NEQAVWmLSDEFSDEELITALETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQDAIE 809
Cdd:cd03801   295 VATDVGGLPEVveDGEGGL-VVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 206-398 7.30e-26

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: 110.56  E-value: 7.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 206 RKVPVSAEAESELRKKYGLY-HPFVMYTGGIDHRKNIEGLIRSYAKLPQNLRashQLAIVCSIQA------ENRRNLEAL 278
Cdd:TIGR04047 172 RFSPAADAADAALRRRLGLRgGPYVLAVGGIEPRKNTIDLLEAFALLRARRP---QAQLVIAGGAtlfdydAYRREFRAR 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 279 ARKCGLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIganTSSLP----EVIGLPEALFDP 354
Cdd:TIGR04047 249 AAELGVDPGPVVITGPVPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVV---ASDIApfteYLGRFDAAWADP 325

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2526276233 355 HSDDDFARLMERALNDEDfRARLVKHGKHQAMKFSWAESARRAI 398
Cdd:TIGR04047 326 SDPDSIADALALALDPAR-RPALRAAGPELAARYTWDASARAHL 368
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 298-406 3.47e-23

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 95.83  E-value: 3.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 298 EDLVR-LYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEA--LFDPHSDDDFARLMERALNDEDFR 374
Cdd:COG0438    11 DLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETglLVPPGDPEALAEAILRLLEDPELR 90

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2526276233 375 ARLVKHGKHQAM-KFSWAESARRAIVQMERLVA 406
Cdd:COG0438    91 RRLGEAARERAEeRFSWEAIAERLLALYEELLA 123
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 99-395 2.08e-13

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 73.59  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  99 LASLKPDVVLVSS----LFEGLTDNAVTSIAqFTRDFPTAVILYdlIPLihheiYLENPVVKAYYSeKIEFL-RQADLWL 173
Cdd:PLN02871  140 VARFKPDLIHASSpgimVFGALFYAKLLCVP-LVMSYHTHVPVY--IPR-----YTFSWLVKPMWD-IIRFLhRAADLTL 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 174 ----AISESSRQEGISHLDLSKDWSANISTDA-DGHFRkvpvSAEAESELR--KKYGlyhPFVMYTGGIDHRKNIEGLIR 246
Cdd:PLN02871  211 vtspALGKELEAAGVTAANRIRVWNKGVDSESfHPRFR----SEEMRARLSggEPEK---PLIVYVGRLGAEKNLDFLKR 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 247 SYAKLPqNLRashqLAIVCsiQAENRRNLEALarkcgLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEA 326
Cdd:PLN02871  284 VMERLP-GAR----LAFVG--DGPYREELEKM-----FAGTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEA 351

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526276233 327 MRCGAPVIGANTSSLPEVIGLPEA-----LFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMKFSWAESAR 395
Cdd:PLN02871  352 MASGVPVVAARAGGIPDIIPPDQEgktgfLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDWRAATR 425
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 693-809 3.66e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 58.46  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 693 RITGWADLD-LFRNYLAAADMGVQlrTLSRGETSGTVLDCMCHSLATIVNANGSMADLNEQAVW-MLSDEFSDEELITAL 770
Cdd:COG0438     3 RLVPRKGLDlLLEALLAAADVFVL--PSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETgLLVPPGDPEALAEAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2526276233 771 ETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQDAIE 809
Cdd:COG0438    81 LRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYE 119
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 628-790 9.06e-09

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: 55.36  E-value: 9.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 628 DDFVVCSFGMLGPTKLNHRLLEAWlnSRLGADK-NCHLVFVGEnhpGTYGVELLEIIRNHRAEKNIRITGWADLDLFRNY 706
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAF--ALLKEKNpNLKLVIAGD---GEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 707 LAAADMGVQlrtLSRGETSGTV-LDCMCHSLATIVNANGSMADLNEQAVW-MLSDEFSDEELITALETLWQDGDKRQSLG 784
Cdd:pfam00534  76 LKIADVFVL---PSRYEGFGIVlLEAMACGLPVIASDVGGPPEVVKDGETgFLVKPNNAEALAEAIDKLLEDEELRERLG 152


                  ....*.
gi 2526276233 785 KRAREV 790
Cdd:pfam00534 153 ENARKR 158
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 2-398 1.56e-77

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: 258.06  E-value: 1.56e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233   2 RIVIDMQGAqstGSRHRGIGRYTMALVQEIVRNRGDHEVILAVNgyfsdsiepirTAFDKLLPPENIQIWNTVTPTAKAe 81
Cdd:cd03809     1 KILIDGRSL---AQRLTGIGRYTRELLKALAKNDPDESVLAVPP-----------LPGELLRLLREYPELSLGVIKIKL- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  82 tdndWRRHAGELLREAFLASL-KPDVVLVSSLFEGLtdnavtsiaqFTRDFPTAVILYDLIPLIHHEIYLENpVVKAYYS 160
Cdd:cd03809    66 ----WRELALLRWLQILLPKKdKPDLLHSPHNTAPL----------LLKGCPQVVTIHDLIPLRYPEFFPKR-FRLYYRL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 161 EKIEFLRQADLWLAISESSRQEGISHLDLSKDWSANISTDADGHFRKvpvsAEAESELRKKYGLYHPFVMYTGGIDHRKN 240
Cdd:cd03809   131 LLPISLRRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSFFP----PESAAVLIAKYLLPEPYFLYVGTLEPRKN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 241 IEGLIRSYAKLPQNLRAsHQLAIVCSIQAENRRNLEALarKCGLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFG 320
Cdd:cd03809   207 HERLLKAFALLKKQGGD-LKLVIVGGKGWEDEELLDLV--KKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFG 283

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2526276233 321 LPALEAMRCGAPVIGANTSSLPEVIGLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMKFSWAESARRAI 398
Cdd:cd03809   284 LPVLEAMACGTPVIASNISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTL 361
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 227-384 1.03e-34

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: 130.09  E-value: 1.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 227 PFVMYTGGIDHRKNIEGLIRSYAKLPQNLrasHQLAIVCSIQAENRRNLEALARKCGLEeDELILTGFVSEEDLVRLYNL 306
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKN---PNLKLVIAGDGEEEKRLKKLAEKLGLG-DNVIFLGFVSDEDLPELLKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 307 CHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVI--GLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQ 384
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVkdGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 19-396 1.57e-34

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: 136.13  E-value: 1.57e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  19 GIGRYTMALVQEIVRNRGDHEVIlavngyfsdsiepirTAFDKLLPPENIQIWNTVTPTAKAETDNDWRRHAGELlrEAF 98
Cdd:cd03801    15 GAERHVRELARALAARGHDVTVL---------------TPADPGEPPEELEDGVIVPLLPSLAALLRARRLLREL--RPL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  99 LASLKPDVVLVSSLFegltdnAVTSIAQFTRDFPTAVILYdliplIHHEIYLENPVVKAYYSEKIE----FLRQADLWLA 174
Cdd:cd03801    78 LRLRKFDVVHAHGLL------AALLAALLALLLGAPLVVT-----LHGAEPGRLLLLLAAERRLLAraeaLLRRADAVIA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 175 ISESSRQEGISHLDLSKDwsanistdadgHFRKVP---VSAEAESELRKKYGLY--HPFVMYTGGIDHRKNIEGLIRSYA 249
Cdd:cd03801   147 VSEALRDELRALGGIPPE-----------KIVVIPngvDLERFSPPLRRKLGIPpdRPVLLFVGRLSPRKGVDLLLEALA 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 250 KLPQNLRASHqlAIVCSIQAENRRNLEALARKCGleeDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRC 329
Cdd:cd03801   216 KLLRRGPDVR--LVIVGGDGPLRAELEELELGLG---DRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAA 290

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 330 GAPVIGANTSSLPEVIGLPEA--LFDPHSDDDFARLMERALNDEDFRARLVKHG-KHQAMKFSWAESARR 396
Cdd:cd03801   291 GLPVVATDVGGLPEVVEDGEGglVVPPDDVEALADALLRLLADPELRARLGRAArERVAERFSWERVAER 360
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 227-396 1.02e-27

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: 116.57  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 227 PFVMYTGGIDHRKNIEGLIRSYAKLPQnLRASHQLAIVC----SIQAENRRNLEALARKCGLEeDELILTGFVSEEDLVR 302
Cdd:cd03800   221 PVVLALGRLDPRKGIDTLVRAFAQLPE-LRELANLVLVGgpsdDPLSMDREELAELAEELGLI-DRVRFPGRVSRDDLPE 298

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 303 LYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVI-----GLpeaLFDPHSDDDFARLMERALNDEDFRARL 377
Cdd:cd03800   299 LYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVrdgrtGL---LVDPHDPEALAAALRRLLDDPALWQRL 375

                         170       180
                  ....*....|....*....|
gi 2526276233 378 VKHG-KHQAMKFSWAESARR 396
Cdd:cd03800   376 SRAGlERARAHYTWESVADQ 395
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 422-809 2.08e-26

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: 112.25  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 422 KLAYISP-LPPERSGIADYSAELLPELARH-YDIEVVVVQDNVTDEWINANCPIRTVQYFRDNASSYDRVLYQFGnsafh 499
Cdd:cd03801     1 KILLLSPeLPPPVGGAERHVRELARALAARgHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELR----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 500 qhmFELLGTHPGVVVLHDFYLSGISHYMEAHAIEPAFWTkelYHAHGYAAFYDRYHSKDEVDVIWKYPCSLSVVqnslgV 579
Cdd:cd03801    76 ---PLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVT---LHGAEPGRLLLLLAAERRLLARAEALLRRADA-----V 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 580 IAHSQNSLRLAKRWYGDNGENWAVIPHMRDPhvNKDRVLARQALGLGVDDFVVCSFGMLGPTKLNHRLLEAwLNSRLGAD 659
Cdd:cd03801   145 IAVSEALRDELRALGGIPPEKIVVIPNGVDL--ERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEA-LAKLLRRG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 660 KNCHLVFVGENhpGTYGVELLEiiRNHRAEKNIRITGWADLDLFRNYLAAADMGVqlrTLSRGETSGTV-LDCMCHSLAT 738
Cdd:cd03801   222 PDVRLVIVGGD--GPLRAELEE--LELGLGDRVRFLGFVPDEELPALYAAADVFV---LPSRYEGFGLVvLEAMAAGLPV 294

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526276233 739 IVNANGSMADL--NEQAVWmLSDEFSDEELITALETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQDAIE 809
Cdd:cd03801   295 VATDVGGLPEVveDGEGGL-VVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLYR 366
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
 206-398 7.30e-26

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: 110.56  E-value: 7.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 206 RKVPVSAEAESELRKKYGLY-HPFVMYTGGIDHRKNIEGLIRSYAKLPQNLRashQLAIVCSIQA------ENRRNLEAL 278
Cdd:TIGR04047 172 RFSPAADAADAALRRRLGLRgGPYVLAVGGIEPRKNTIDLLEAFALLRARRP---QAQLVIAGGAtlfdydAYRREFRAR 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 279 ARKCGLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIganTSSLP----EVIGLPEALFDP 354
Cdd:TIGR04047 249 AAELGVDPGPVVITGPVPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVV---ASDIApfteYLGRFDAAWADP 325

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2526276233 355 HSDDDFARLMERALNDEDfRARLVKHGKHQAMKFSWAESARRAI 398
Cdd:TIGR04047 326 SDPDSIADALALALDPAR-RPALRAAGPELAARYTWDASARAHL 368
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 141-396 2.70e-24

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: 105.82  E-value: 2.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 141 IPLIH----------HEIYLENPVVKAY-YSEKIEFLRQADLWLAISESSRQEGISHlDLSKDWSAnISTDAD-GHFRKV 208
Cdd:cd03817   109 IPIVHtyhtmyedylHYIPKGKLLVKAVvRKLVRRFYNHTDAVIAPSEKIKDTLREY-GVKGPIEV-IPNGIDlDKFEKP 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 209 PvsaeaESELRKKYGLYH--PFVMYTGGIDHRKNIEGLIRSYAKLPQNLRAshQLAIVCSIQAenRRNLEALARKCGLEE 286
Cdd:cd03817   187 L-----NTEERRKLGLPPdePILLYVGRLAKEKNIDFLLRAFAELKKEPNI--KLVIVGDGPE--REELKELARELGLAD 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 287 DeLILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEA--LFDPhSDDDFARLM 364
Cdd:cd03817   258 K-VIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENgfLFEP-NDETLAEKL 335

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2526276233 365 ERALNDEDFRARLVKHGKHQAMKFSWAESARR 396
Cdd:cd03817   336 LHLRENLELLRKLSKNAEISAREFAFAKSVEK 367
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 298-406 3.47e-23

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 95.83  E-value: 3.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 298 EDLVR-LYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEA--LFDPHSDDDFARLMERALNDEDFR 374
Cdd:COG0438    11 DLLLEaLLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETglLVPPGDPEALAEAILRLLEDPELR 90

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2526276233 375 ARLVKHGKHQAM-KFSWAESARRAIVQMERLVA 406
Cdd:COG0438    91 RRLGEAARERAEeRFSWEAIAERLLALYEELLA 123
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
227-370 6.96e-23

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 95.27  E-value: 6.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 227 PFVMYTGGIDHR-KNIEGLIRSYAKL-PQNLRAshQLAIVCSiqaENRRNLEALARKCgleEDELILTGFVseEDLVRLY 304
Cdd:pfam13692   2 PVILFVGRLHPNvKGVDYLLEAVPLLrKRDNDV--RLVIVGD---GPEEELEELAAGL---EDRVIFTGFV--EDLAELL 71

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526276233 305 NLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVI-GLPEALFDPHSDDDFARLMERALND 370
Cdd:pfam13692  72 AAADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVdGENGLLVPPGDPEALAEAILRLLED 138
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 226-398 3.12e-21

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: 97.07  E-value: 3.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 226 HPFVMYTGGIDHRKNIEGLIRSYAKLPQNLRASHqLAIVCSiqAENRRNLEALARKCGLEEDeLILTGFVSEEDLVRLYN 305
Cdd:cd03798   200 AFVILFVGRLIPRKGIDLLLEAFARLAKARPDVV-LLIVGD--GPLREALRALAEDLGLGDR-VTFTGRLPHEQVPAYYR 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 306 LCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEA--LFDPHSDDDFARLMERALND-------EDFRAR 376
Cdd:cd03798   276 ACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETglLVPPGDADALAAALRRALAEpylrelgEAARAR 355

                         170       180
                  ....*....|....*....|..
gi 2526276233 377 LVKhgkhqamKFSWAESARRAI 398
Cdd:cd03798   356 VAE-------RFSWVKAADRIA 370
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 97-380 4.41e-20

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: 92.81  E-value: 4.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  97 AFLASLKPDVVLVsslFEGLTDNAVTSIAQFTrdfptavilydlIPLI--HHEIYLENPVVKAYYSEKIEFLRQADLWLA 174
Cdd:cd03811    77 RILKRAKPDVVIS---FLGFATYIVAKLAAAR------------SKVIawIHSSLSKLYYLKKKLLLKLKLYKKADKIVC 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 175 ISESSRQEGISHLDLSKDwsaNISTDADG-HFRKVPVSAEAESELRKKYGlyhPFVMYTGGIDHRKNIEGLIRSYAKLPQ 253
Cdd:cd03811   142 VSKGIKEDLIRLGPSPPE---KIEVIYNPiDIDRIRALAKEPILNEPEDG---PVILAVGRLDPQKGHDLLIEAFAKLRK 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 254 NLRASHqLAIVCSIqaENRRNLEALARKCGLEeDELILTGFVSeeDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPV 333
Cdd:cd03811   216 KYPDVK-LVILGDG--PLREELEKLAKELGLA-ERVIFLGFQS--NPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPV 289

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2526276233 334 IGANTSSLPEVI-----GLPEALFDPHSDDDFARLMERALNDEDFRARLVKH 380
Cdd:cd03811   290 VSTDCPGPREILddgenGLLVPDGDAAALAGILAALLQKKLDAALRERLAKA 341
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 230-345 1.19e-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: 89.00  E-value: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 230 MYTGGIDHRKNIEGLIRSYAKLPQNLRASHQLAIVCsiqAENRRNLEALARKCGLEEDELILTGFVSEEDLVRLYNLCHL 309
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGG---GGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADV 190

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2526276233 310 FVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVI 345
Cdd:cd01635   191 FVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 174-387 1.81e-18

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: 88.56  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 174 AISESSRQEGISHLDLSKDW--------SANISTDADGHFRKVPVSAEAESelrkkyglyhpFVMYTGGIDHRKNIEGLI 245
Cdd:cd04962   147 AVSSSLRQETYELFDVDKDIevihnfidEDVFKRKPAGALKRRLLAPPDEK-----------VVIHVSNFRPVKRIDDVV 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 246 RSYAKLPQNLRAshQLAIVCSiqAENRRNLEALARKCGLEEDELILTgfvSEEDLVRLYNLCHLFVFPSWHEGFGLPALE 325
Cdd:cd04962   216 RVFARVRRKIPA--KLLLVGD--GPERVPAEELARELGVEDRVLFLG---KQDDVEELLSIADLFLLPSEKESFGLAALE 288

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526276233 326 AMRCGAPVIGANTSSLPEVI--GLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMK 387
Cdd:cd04962   289 AMACGVPVVSSNAGGIPEVVkhGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAE 352
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 19-397 3.30e-18

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


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 87.41  E-value: 3.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  19 GIGRYTMALVQEIVRNrgDHEVILAVNGyfsDSIEPIRTAFDKLLPpeniqiwntVTPTAKAETDNDWRRHAGELLREaf 98
Cdd:cd03819    12 GAETYILDLARALAER--GHRVLVVTAG---GPLLPRLRQIGIGLP---------GLKVPLLRALLGNVRLARLIRRE-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  99 laslKPDVVLVSSLfeglTDNAVTSIAQFTRDFPtavilydlIPLIHHEIYLENPVVKAYYSEKIEFLRQAdlwLAISES 178
Cdd:cd03819    76 ----RIDLIHAHSR----APAWLGWLASRLTGVP--------LVTTVHGSYLATYHPKDFALAVRARGDRV---IAVSEL 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 179 SRQEGISHLDLSKDWSANI--STDADghfrkvPVSAEAESELRKKYGLYH--PFVMYTGGIDHRKNIEGLIRSYAKLPqn 254
Cdd:cd03819   137 VRDHLIEALGVDPERIRVIpnGVDTD------RFPPEAEAEERAQLGLPEgkPVVGYVGRLSPEKGWLLLVDAAAELK-- 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 255 lrasHQLAIVCSIQ--AENRRNLEALARKCGLEeDELILTGFVseEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAP 332
Cdd:cd03819   209 ----DEPDFRLLVAgdGPERDEIRRLVERLGLR-DRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTP 281

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2526276233 333 VIGANTSSLPEVI--GLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMkfsWAESARRA 397
Cdd:cd03819   282 VVATDVGGAREIVvhGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAAALTEA---VRELLLRV 345
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 19-402 4.91e-18

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: 86.96  E-value: 4.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  19 GIGRYTMALVQEIVRNrgDHEVILavngyfsdsIEPirTAFDKLLPPENIQIWntvTPTAKAETDNDWR---RHAGELLR 95
Cdd:cd03814    15 GVVRTLERLVDHLRRR--GHEVRV---------VAP--GPFDEAESAEGRVVS---VPSFPLPFYPEYRlalPLPRRVRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  96 EafLASLKPDVVLVSSlfEGLT---------DNAVTSIAQFTRDFPTAVILYDLIPLihheiylenpvVKAYYSEKIEFL 166
Cdd:cd03814    79 L--IKEFQPDIIHIAT--PGPLglaalraarRLGLPVVTSYHTDFPEYLSYYTLGPL-----------SWLAWAYLRWFH 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 167 RQADLWLAISESSRQE----GISHLDLskdWSANISTDAdghFRKVPVSAEaeseLRKKYG-LYHPFVMYTGGIDHRKNI 241
Cdd:cd03814   144 NPFDTTLVPSPSIAREleghGFERVRL---WPRGVDTEL---FHPSRRDAA----LRRRLGpPGRPLLLYVGRLAPEKNL 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 242 EGLIRSYAKLPQnlRASHQLAIVCSiqAENRRNLEAlarkcglEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGL 321
Cdd:cd03814   214 EALLDADLPLAA--SPPVRLVVVGD--GPARAELEA-------RGPDVIFTGFLTGEELARAYASADVFVFPSRTETFGL 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 322 PALEAMRCGAPVIGANTSSLPEVIGLPE--ALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMKFSWAESARRAIV 399
Cdd:cd03814   283 VVLEAMASGLPVVAADAGGPRDIVRPGGtgALVEPGDAAAFAAALRALLEDPELRRRMAARARAEAERYSWEAFLDNLLD 362


                  ...
gi 2526276233 400 QME 402
Cdd:cd03814   363 YYA 365
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 238-396 5.94e-17

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: 83.91  E-value: 5.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 238 RKNIEGLIRSYAKLPQnlrASHQLAIVCSIQAENRRNLEALARKCGLEEDeLILTGFVSeeDLVRLYNLCHLFVFPSWHE 317
Cdd:cd03807   202 VKDHSDLLRAAALLVE---THPDLRLLLVGRGPERPNLERLLLELGLEDR-VHLLGERS--DVPALLPAMDIFVLSSRTE 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 318 GFGLPALEAMRCGAPVIGANTSSLPEVIG-LPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMK-FSWAESAR 395
Cdd:cd03807   276 GFPNALLEAMACGLPVVATDVGGAAELVDdGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANeFSIDAMVR 355


                  .
gi 2526276233 396 R 396
Cdd:cd03807   356 R 356
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 19-380 3.81e-14

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: 75.06  E-value: 3.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  19 GIGRYTMALVQEIVRnrGDHEVilAVngYFSDSIEPIRTAFDKLLPPENIQIWNTVTPTAKAETDNDWRRHAGELLR--E 96
Cdd:cd03823    16 GAEISVHDLAEALVA--EGHEV--AV--LTAGVGPPGQATVARSVVRYRRAPDETLPLALKRRGYELFETYNPGLRRllA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  97 AFLASLKPDVVLVSSLfEGLTDNAVTSIAQftRDFPTAVILYDLIPL-IHHEIYLENPvvkayysekieflrqaDLWLAI 175
Cdd:cd03823    90 RLLEDFRPDVVHTHNL-SGLGASLLDAARD--LGIPVVHTLHDYWLLcPRQFLFKKGG----------------DAVLAP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 176 S----ESSRQEGISHLDLSKDWSANISTDAdghfrkVPVSAEAESElRKKYGlyhpfvmYTGGIDHRKNIEGLIRSYAKL 251
Cdd:cd03823   151 SrftaNLHEANGLFSARISVIPNAVEPDLA------PPPRRRPGTE-RLRFG-------YIGRLTEEKGIDLLVEAFKRL 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 252 PQNlrashqlAIVCSIQAENRrnLEALARKCGLEEDELIltGFVSEEDLVRLYNLCHLFVFPS-WHEGFGLPALEAMRCG 330
Cdd:cd03823   217 PRE-------DIELVIAGHGP--LSDERQIEGGRRIAFL--GRVPTDDIKDFYEKIDVLVVPSiWPEPFGLVVREAIAAG 285

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2526276233 331 APVIGANTSSLPEVI--GLPEALFDPHSDDDFARLMERALNDEDFRARLVKH 380
Cdd:cd03823   286 LPVIASDLGGIAELIqpGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAG 337
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 213-390 3.94e-14

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: 75.48  E-value: 3.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 213 EAESELRKKYGLYH--PFVMYTGGIDHRKNIEGLIRSYAKLPQNLRASHqLAIVCSIQAENRRNLEALARKcGLEeDELI 290
Cdd:cd03821   189 DPGLRDRRKHNGLEdrRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWH-LVIAGPDDGAYPAFLQLQSSL-GLG-DRVT 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 291 LTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEALFDPHSDDDFARLMERALND 370
Cdd:cd03821   266 FTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRD 345

                         170       180
                  ....*....|....*....|...
gi 2526276233 371 EDFRARL---VKHGKHQAMKFSW 390
Cdd:cd03821   346 PADRKRLgemARRARQVEENFSW 368
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 216-387 1.18e-13

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: 73.52  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 216 SELRKKYGLYHPFVMY----TGGIDHRKNIEGLIRSYAKLPQNLRashqLAIVC-SIQAENRRNLEALARKCGLEEDEli 290
Cdd:cd03825   181 AKARKRLGIPQDKKVIlfgaESVTKPRKGFDELIEALKLLATKDD----LLLVVfGKNDPQIVILPFDIISLGYIDDD-- 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 291 ltgfvseEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEA-----LFDPHsddDFARLME 365
Cdd:cd03825   255 -------EQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTgylvpPGDVQ---ALAEAIE 324

                         170       180
                  ....*....|....*....|..
gi 2526276233 366 RALNDEDFRARLVKHGKHQAMK 387
Cdd:cd03825   325 WLLANPKERESLGERARALAEN 346
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 422-728 1.26e-13

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: 73.57  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 422 KLAYISPLPPERSGIADYSaELLPELARHYDIEVVVVQDNVTDEWINANCPIRTVQYFRDNASSYDRVLYQFGNSAFH-- 499
Cdd:cd03822     1 KIAVLGTLPPRKCGIATYT-DDLVEGLRKGGPVVIVVIVSPQDEILKDDDFEVPNEIKSWNSNEYFRLLDHLNFKKPDvv 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 500 --QHMFELLGTHPGVVVLHDFYLSGISHYMEAHAIEPAF--WTKELYHAHGYAAFYDRyhskdevdviwkypcslsvvqn 575
Cdd:cd03822    80 hiQHEFGIFGGKYGLYALGLLLHLRIPVITTLHTVLDLSdpGKQALKVLFRIATLSER---------------------- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 576 slgVIAHSQNSLRLAKRWYGDNGENWAVIPHmRDPHVNKDRVLARQALGLGVDDFVVCSFGMLGPTKLNHRLLEAwLNSR 655
Cdd:cd03822   138 ---VVVMAPISRFLLVRIKLIPAVNIEVIPH-GVPEVPQDPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEA-LPEL 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 656 LGADKNCHLVFVGENHPGT----YGVELLEIIRNHRAEKNIRItGWADL---DLFRnYLAAADMGVqLRTLSRGET-SGT 727
Cdd:cd03822   213 KAEFPDVRLVIAGELHPSLaryeGERYRKAAIEELGLQDHVDF-HNNFLpeeEVPR-YISAADVVV-LPYLNTEQSsSGT 289


                  .
gi 2526276233 728 V 728
Cdd:cd03822   290 L 290
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 426-789 1.66e-13

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: 73.17  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 426 ISPLPPERSGIADYSAELLPELARHYDIEVVVV-------------QDNVTDEWINANCPIRTVQYFRdnasSYDRVLYQ 492
Cdd:cd03809     6 GRSLAQRLTGIGRYTRELLKALAKNDPDESVLAvpplpgellrllrEYPELSLGVIKIKLWRELALLR----WLQILLPK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 493 FGNSAFHQHMFELLGTH----PGVVVLHDFYlsgishymeahaiepafwtkELYHAHGYAAFYDRYHSkdevdviWKYPC 568
Cdd:cd03809    82 KDKPDLLHSPHNTAPLLlkgcPQVVTIHDLI--------------------PLRYPEFFPKRFRLYYR-------LLLPI 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 569 SLsvvQNSLGVIAHSQNSLRLAKRWYGDNGENWAVIPHMRDPH-VNKDRVLARQALGLGVDDFVVCsFGMLGPTKlNH-R 646
Cdd:cd03809   135 SL---RRADAIITVSEATRDDIIKFYGVPPEKIVVIPLGVDPSfFPPESAAVLIAKYLLPEPYFLY-VGTLEPRK-NHeR 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 647 LLEAWLNSRlGADKNCHLVFVGENHPGTYgvELLEIIRNHRAEKNIRITGWADLDLFRNYLAAADMGVQlrtLSRGETSG 726
Cdd:cd03809   210 LLKAFALLK-KQGGDLKLVIVGGKGWEDE--ELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVF---PSLYEGFG 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526276233 727 T-VLDCMCHSLATIVNANGSMADLNEQAVWMLsDEFSDEELITALETLWQDGDKRQSLGKRARE 789
Cdd:cd03809   284 LpVLEAMACGTPVIASNISVLPEVAGDAALYF-DPLDPESIADAILRLLEDPSLREELIRKGLE 346
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 17-396 1.77e-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: 73.53  E-value: 1.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  17 HRGIGRYTMALVQEIVRNrgDHEV-ILAVNGYFSDSIEPIRTAFDKllppENIQIWNTVTP----TAKAETDNDWRRHAG 91
Cdd:cd03794    13 KGAAAARVYELAKELVRR--GHEVtVLTPSPNYPLGRIFAGATETK----DGIRVIRVKLGpikkNGLIRRLLNYLSFAL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  92 ELLREAFLASLKPDVVLVSS--LFEGLtdnAVTSIAQFTRdFPTAVILYDLIPlihhEIYLENPVVKA----YYSEKIE- 164
Cdd:cd03794    87 AALLKLLVREERPDVIIAYSppITLGL---AALLLKKLRG-APFILDVRDLWP----ESLIALGVLKKgsllKLLKKLEr 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 165 -FLRQADLWLAISESsRQEGISHLDLSKDwsaNISTdadghfrkVP-------VSAEAESELRKKYGLYHPF-VMYTGGI 235
Cdd:cd03794   159 kLYRLADAIIVLSPG-LKEYLLRKGVPKE---KIIV--------IPnwadleeFKPPPKDELRKKLGLDDKFvVVYAGNI 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 236 DHRKNIEGLIRSYAKLPQnlRASHQLAIVcsIQAENRRNLEALARKCGLeeDELILTGFVSEEDLVRLYNLCHLFVFP-- 313
Cdd:cd03794   227 GKAQGLETLLEAAERLKR--RPDIRFLFV--GDGDEKERLKELAKARGL--DNVTFLGRVPKEEVPELLSAADVGLVPlk 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 314 SWHE-GFGLPA--LEAMRCGAPVIGAN--TSSLPEVIGLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAM-K 387
Cdd:cd03794   301 DNPAnRGSSPSklFEYMAAGKPILASDdgGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEeK 380


                  ....*....
gi 2526276233 388 FSWAESARR 396
Cdd:cd03794   381 FSREKLADR 389
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 99-395 2.08e-13

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 73.59  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  99 LASLKPDVVLVSS----LFEGLTDNAVTSIAqFTRDFPTAVILYdlIPLihheiYLENPVVKAYYSeKIEFL-RQADLWL 173
Cdd:PLN02871  140 VARFKPDLIHASSpgimVFGALFYAKLLCVP-LVMSYHTHVPVY--IPR-----YTFSWLVKPMWD-IIRFLhRAADLTL 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 174 ----AISESSRQEGISHLDLSKDWSANISTDA-DGHFRkvpvSAEAESELR--KKYGlyhPFVMYTGGIDHRKNIEGLIR 246
Cdd:PLN02871  211 vtspALGKELEAAGVTAANRIRVWNKGVDSESfHPRFR----SEEMRARLSggEPEK---PLIVYVGRLGAEKNLDFLKR 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 247 SYAKLPqNLRashqLAIVCsiQAENRRNLEALarkcgLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEA 326
Cdd:PLN02871  284 VMERLP-GAR----LAFVG--DGPYREELEKM-----FAGTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGFVVLEA 351

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526276233 327 MRCGAPVIGANTSSLPEVIGLPEA-----LFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMKFSWAESAR 395
Cdd:PLN02871  352 MASGVPVVAARAGGIPDIIPPDQEgktgfLYTPGDVDDCVEKLETLLADPELRERMGAAAREEVEKWDWRAATR 425
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 275-382 1.65e-12

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 70.00  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 275 LEALARKCGLEEDELIltGFVSEEDLVRLYNLCHLFVFPSwH---EGFGLPALEAMRCGAPVIGAN--TSSLPEVIGLPE 349
Cdd:cd03795   232 LEAQIELNLLDNVKFL--GRVDDEEKVIYLHLCDVFVFPS-VlrsEAFGIVLLEAMMCGKPVISTNigTGVPYVNNNGET 308

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2526276233 350 ALFDPHSD-DDFARLMERALNDEDFRARLVKHGK 382
Cdd:cd03795   309 GLVVPPKDpDALAEAIDKLLSDEELRESYGENAK 342
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 98-381 1.66e-12

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: 69.93  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  98 FLASLKPDVVLVSSLFEGLtdnaVTSIAQF-TRDFPTavilydlIPLIH--HEIYLENPVVKAYYS--EKIEFLRQADLW 172
Cdd:cd03808    76 LLKKEKPDIVHCHTPKPGI----LGRLAARlAGVPKV-------IYTVHglGFVFTEGKLLRLLYLllEKLALLFTDKVI 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 173 LaISESSRQEGISHLDLSKDWSA---NISTDADgHFRKVPVSAEAEselrkkyglyHPFVMYTGGIDHRKNIEGLIRSYA 249
Cdd:cd03808   145 F-VNEDDRDLAIKKGIIKKKKTVlipGSGVDLD-RFQYSPESLPSE----------KVVFLFVARLLKDKGIDELIEAAK 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 250 KLPQ---NLRashqLAIVCSIQAENRRnlEALARKCGLEEDeLILTGFVSeeDLVRLYNLCHLFVFPSWHEGFGLPALEA 326
Cdd:cd03808   213 ILKKkgpNVR----FLLVGDGELENPS--EILIEKLGLEGR-IEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEA 283

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 327 MRCGAPVIGANTSSLPEVI-----GLpeaLFDPHSDDDFARLMERALNDEDFRARLVKHG 381
Cdd:cd03808   284 MAAGRPVITTDVPGCRELVidgvnGF---LVPPGDVEALADAIEKLIEDPELRKEMGEAA 340
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 229-390 9.83e-12

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: 67.65  E-value: 9.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 229 VMYTGGIDHRKNIEGLIRSYAKLPQNlRASHQLAIVCSiqAENRRNLEALARKCGLEeDELILTGFVSEEDLvrLYNLCH 308
Cdd:cd03820   184 ILAVGRLTYQKGFDLLIEAWALIAKK-HPDWKLRIYGD--GPEREELEKLIDKLGLE-DRVKLLGPTKNIAE--EYANSS 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 309 LFVFPSWHEGFGLPALEAMRCGAPVIG-ANTSSLPEVI-----GLpeaLFDPHSDDDFARLMERALNDEDFRARLVKHGK 382
Cdd:cd03820   258 IFVLSSRYEGFPMVLLEAMAYGLPIISfDCPTGPSEIIedgenGL---LVPNGDVDALAEALLRLMEDEELRKKMGKNAR 334


                  ....*...
gi 2526276233 383 HQAMKFSW 390
Cdd:cd03820   335 KNAERFSI 342
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 211-347 1.76e-11

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: 66.93  E-value: 1.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 211 SAEAESELRKKYGLYHPFVM-YTGGIDHRKNIEGLIRSYAKLPQNLRASHqlaIVCSIQAENRRNLEALARKCGLEEDeL 289
Cdd:cd03812   175 NKEKRRKRRKLLILEDKLVLgHVGRFNEQKNHSFLIDIFEELKKKNPNVK---LVLVGEGELKEKIKEKVKELGLEDK-V 250

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2526276233 290 ILTGFVSeeDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGL 347
Cdd:cd03812   251 IFLGFRN--DVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN 306
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 270-389 3.30e-10

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: 62.85  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 270 ENRRNLEALARKCGLEeDELILTGFVSeeDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPE 349
Cdd:cd04951   229 PLRNELERLICNLNLV-DRVILLGQIS--NISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHN 305

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2526276233 350 ALFDPHSDDDFARLMERALNDED-FRARLVKHGKHQAMKFS 389
Cdd:cd04951   306 YVVPVSDPQLLAEKIKEIFDMSDeERDILGNKNEYIAKNFS 346
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 693-809 3.66e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 58.46  E-value: 3.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 693 RITGWADLD-LFRNYLAAADMGVQlrTLSRGETSGTVLDCMCHSLATIVNANGSMADLNEQAVW-MLSDEFSDEELITAL 770
Cdd:COG0438     3 RLVPRKGLDlLLEALLAAADVFVL--PSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETgLLVPPGDPEALAEAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2526276233 771 ETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQDAIE 809
Cdd:COG0438    81 LRLLEDPELRRRLGEAARERAEERFSWEAIAERLLALYE 119
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 19-399 4.42e-09

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: 59.71  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  19 GIGRYTMALVQEIvrNRGDHEVILAVngyFSDSIEpiRTAFDKLLPPENIQIWNtvtptakaetDNDWRRHAgellreAF 98
Cdd:cd03822    14 GIATYTDDLVEGL--RKGGPVVIVVI---VSPQDE--ILKDDDFEVPNEIKSWN----------SNEYFRLL------DH 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233  99 LASLKPDVVLVSSLFEGLTDNAVTSIAQFTRDFPTAVILydlipLIHHEIYLENPVVKAYYsekiefLRQADLWLAISES 178
Cdd:cd03822    71 LNFKKPDVVHIQHEFGIFGGKYGLYALGLLLHLRIPVIT-----TLHTVLDLSDPGKQALK------VLFRIATLSERVV 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 179 SRQEGISHL--DLSKDWSANISTDADGhfrkVPVSAEAESELRKKYGLYH--PFVMYTGGIDHRKNIEGLIRSYAKLpqn 254
Cdd:cd03822   140 VMAPISRFLlvRIKLIPAVNIEVIPHG----VPEVPQDPTTALKRLLLPEgkKVILTFGFIGPGKGLEILLEALPEL--- 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 255 lRASH---QLAIVCSIQAENRRN-----LEALARKCGLEEDELILTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPA--L 324
Cdd:cd03822   213 -KAEFpdvRLVIAGELHPSLARYegeryRKAAIEELGLQDHVDFHNNFLPEEEVPRYISAADVVVLPYLNTEQSSSGtlS 291

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2526276233 325 EAMRCGAPVIganTSSLP----EVIGLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMKFSWAESARRAIV 399
Cdd:cd03822   292 YAIACGKPVI---STPLRhaeeLLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADRYLR 367
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 302-396 6.43e-09

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 59.50  E-value: 6.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 302 RLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSL----PEVIGLPEA----LFDPHSDDDFARLMERAL---ND 370
Cdd:cd03791   364 RIYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLadtvFDYDPETGEgtgfVFEDYDAEALLAALRRALalyRN 443

                          90       100
                  ....*....|....*....|....*.
gi 2526276233 371 EDFRARLVKHGKHQAmkFSWAESARR 396
Cdd:cd03791   444 PELWRKLQKNAMKQD--FSWDKSAKE 467
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 628-790 9.06e-09

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: 55.36  E-value: 9.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 628 DDFVVCSFGMLGPTKLNHRLLEAWlnSRLGADK-NCHLVFVGEnhpGTYGVELLEIIRNHRAEKNIRITGWADLDLFRNY 706
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAF--ALLKEKNpNLKLVIAGD---GEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 707 LAAADMGVQlrtLSRGETSGTV-LDCMCHSLATIVNANGSMADLNEQAVW-MLSDEFSDEELITALETLWQDGDKRQSLG 784
Cdd:pfam00534  76 LKIADVFVL---PSRYEGFGIVlLEAMACGLPVIASDVGGPPEVVKDGETgFLVKPNNAEALAEAIDKLLEDEELRERLG 152


                  ....*.
gi 2526276233 785 KRAREV 790
Cdd:pfam00534 153 ENARKR 158
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 283-377 1.32e-08

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: 58.14  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 283 GLEEDELILTGFVSEEDLVRLYNL--CHL-FVFP---SWhegfGLpaLEAMRCGAPVIGANTSSLPEVI-----GLPEAL 351
Cdd:cd03818   277 GVDLERVHFVGKVPYDQYVRLLQLsdAHVyLTYPfvlSW----SL--LEAMACGCPVIGSDTAPVREVIrdgrnGLLVDF 350

                          90       100
                  ....*....|....*....|....*.
gi 2526276233 352 FDPhsdDDFARLMERALNDEDFRARL 377
Cdd:cd03818   351 FDP---DALAAAVLELLEDPDRAAAL 373
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 293-345 1.54e-08

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: 57.68  E-value: 1.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2526276233 293 GFVSEEDLVRLYNLCHLFVFPS-WHEGFGLPALEAMRCGAPVIGANTSSLPEVI 345
Cdd:cd03802   226 GEVGHDEKQELLGGARALLFPInWDEPFGLVMIEAMACGTPVIAYRRGGLPEVI 279
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 227-377 3.26e-08

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: 56.69  E-value: 3.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 227 PFVMYTGGIDHRKNIEGLIRSYAKLpqnlRASH-QLAIVCSIQAENRRNLEALARKCGleedELILTGFVSEEDLVRLYN 305
Cdd:cd05844   190 PTILFVGRLVEKKGCDVLIEAFRRL----AARHpTARLVIAGDGPLRPALQALAAALG----RVRFLGALPHAEVQDWMR 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 306 LCHLFVFPSW------HEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEA--LFDPHSDDDFARLMERALNDEDFRARL 377
Cdd:cd05844   262 RAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETgfLVPEGDVDALADALQALLADRALADRM 341
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 422-804 5.43e-08

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: 56.20  E-value: 5.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 422 KLAYISP-LPPERSGIADYSAELLPELARH-YDIEVVVVQDNVTDEWINANC--------PIRTVQYFRDNASSYDRVLY 491
Cdd:cd03794     1 KILLISQyYPPPKGAAAARVYELAKELVRRgHEVTVLTPSPNYPLGRIFAGAtetkdgirVIRVKLGPIKKNGLIRRLLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 492 QFGNSAFHQHMFELLGTHPGVVVLHDFYLSgishymeahAIEPAFWTKELYHAHGYAAFYDRY--HSKDEVDVIWKYPCS 569
Cdd:cd03794    81 YLSFALAALLKLLVREERPDVIIAYSPPIT---------LGLAALLLKKLRGAPFILDVRDLWpeSLIALGVLKKGSLLK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 570 LSVVQNSL------GVIAHSQ-NSLRLAKRwyGDNGENWAVIPHMRDPH--VNKDRVLARQALGLGvDDFVVCSFGMLGP 640
Cdd:cd03794   152 LLKKLERKlyrladAIIVLSPgLKEYLLRK--GVPKEKIIVIPNWADLEefKPPPKDELRKKLGLD-DKFVVVYAGNIGK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 641 TKLNHRLLEAWlnSRLGADKNCHLVFVGenhPGTYGVELLEIIRNhRAEKNIRITGWADLDLFRNYLAAADMGVQlrTLS 720
Cdd:cd03794   229 AQGLETLLEAA--ERLKRRPDIRFLFVG---DGDEKERLKELAKA-RGLDNVTFLGRVPKEEVPELLSAADVGLV--PLK 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 721 RGETSGTV-----LDCMCHSLATIVNANGSMADLNEQA-VWMLSDEFSDEELITALETLWQDGDKRQSLGKRAREVILED 794
Cdd:cd03794   301 DNPANRGSspsklFEYMAAGKPILASDDGGSDLAVEINgCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEK 380

                         410
                  ....*....|
gi 2526276233 795 HDPRYCAGQY 804
Cdd:cd03794   381 FSREKLADRL 390
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 578-806 1.85e-07

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: 54.25  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 578 GVIAHSQNSLRLAKRWYGDNgENWAVIPHMRDPHV----NKDRVLARQALGLGVDDFVVCSFGMLGPTKlNHRLLEAWLN 653
Cdd:cd03807   136 ATVANSSAVAEFHQEQGYAK-NKIVVIYNGIDLFKlspdDASRARARRRLGLAEDRRVIGIVGRLHPVK-DHSDLLRAAA 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 654 SRLGADKNCHLVFVGEnhpGTYGVELLEIIRNHRAEKNIRITGW-ADLdlfRNYLAAADMGVqLRTLSRGeTSGTVLDCM 732
Cdd:cd03807   214 LLVETHPDLRLLLVGR---GPERPNLERLLLELGLEDRVHLLGErSDV---PALLPAMDIFV-LSSRTEG-FPNALLEAM 285

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2526276233 733 CHSLATIVNANGSMADLNEQAVWMLSDEFSDEELITALETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQD 806
Cdd:cd03807   286 ACGLPVVATDVGGAAELVDDGTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANEFSIDAMVRRYET 359
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 239-389 1.31e-06

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: 51.82  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 239 KNIEGLIRSYAKLPQNLRASHQLAIVCS-----IQAENRRNLEALARKC----GLEEDELILTGFVSEEDLVRLYNLCHL 309
Cdd:cd03805   224 KNIALAIEAFAKLKQKLPEFENVRLVIAggydpRVAENVEYLEELQRLAeellNVEDQVLFLRSISDSQKEQLLSSALAL 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 310 FVFPSwHEGFGLPALEAMRCGAPVIGANT-----SSLPEVIGLpeaLFDPhSDDDFARLMERALNDEDFRARLVKHGKHQ 384
Cdd:cd03805   304 LYTPS-NEHFGIVPLEAMYAGKPVIACNSggpleTVVEGVTGF---LCEP-TPEAFAEAMLKLANDPDLADRMGAAGRKR 378


                  ....*.
gi 2526276233 385 AM-KFS 389
Cdd:cd03805   379 VKeKFS 384
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
229-402 1.73e-06

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 51.33  E-value: 1.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 229 VMYTGGIDHRKNIEGLIRSYAKLpQNLRASHQLAIVC-------SIQAENRRNLEALARKCGleeDELILTGFVSEEDLV 301
Cdd:PRK15484  196 LLYAGRISPDKGILLLMQAFEKL-ATAHSNLKLVVVGdptasskGEKAAYQKKVLEAAKRIG---DRCIMLGGQPPEKMH 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 302 RLYNLCHLFVFPS-WHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEA---LFDPHSDDDFARLMERALNDEDfRARL 377
Cdd:PRK15484  272 NYYPLADLVVVPSqVEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITgyhLAEPMTSDSIISDINRTLADPE-LTQI 350

                         170       180
                  ....*....|....*....|....*.
gi 2526276233 378 VKHGKHQAM-KFSWAESARRAIVQME 402
Cdd:PRK15484  351 AEQAKDFVFsKYSWEGVTQRFEEQIH 376
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 239-396 5.00e-06

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


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 50.11  E-value: 5.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 239 KNIEGLIRSYAKLPQNLR-ASHQLAIVCSIQAENRRNLEALARKCGLEEdeliLTGFVSEE-DLVRLYNLCHLFVFPSWH 316
Cdd:TIGR03088 207 KDQPTLVRAFALLVRQLPeGAERLRLVIVGDGPARGACEQMVRAAGLAH----LVWLPGERdDVPALMQALDLFVLPSLA 282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 317 EGFGLPALEAMRCGAPVIGANTSSLPEVI--GLPEALFDPHSDDDFARLMERALNDedfRARLVKHGKHQ----AMKFSW 390
Cdd:TIGR03088 283 EGISNTILEAMASGLPVIATAVGGNPELVqhGVTGALVPPGDAVALARALQPYVSD---PAARRAHGAAGraraEQQFSI 359


                  ....*.
gi 2526276233 391 AESARR 396
Cdd:TIGR03088 360 NAMVAA 365
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 273-345 3.31e-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: 47.45  E-value: 3.31e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526276233 273 RNLEALARKCgLEEDELILTGFVSEEDLVRLY--NLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVI 345
Cdd:cd04946   270 ERLEKLAENK-LENVKVNFTGEVSNKEVKQLYkeNDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIV 343
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 603-807 3.93e-05

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: 46.89  E-value: 3.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 603 VIPHMRDPHV--NKDRVLARQALGLGVDDFVVCSFGMLGPTKLNHRLLEAWlnSRLGADKNCHLVFVGEnhpGTYGVELL 680
Cdd:cd03817   173 VIPNGIDLDKfeKPLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAF--AELKKEPNIKLVIVGD---GPEREELK 247

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 681 EIIRNHRAEKNIRITGWADLDLFRNYLAAADMGVqlrTLSRGETSG-TVLDCMCHSLATIVNANGSMADLNEQAV-WMLS 758
Cdd:cd03817   248 ELARELGLADKVIFTGFVPREELPEYYKAADLFV---FASTTETQGlVYLEAMAAGLPVVAAKDPAASELVEDGEnGFLF 324

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2526276233 759 DEfSDEELITALETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQDA 807
Cdd:cd03817   325 EP-NDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLYEEV 372
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
317-396 8.98e-05

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 42.21  E-value: 8.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 317 EGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEALFDPHSDDDFARLMERALNDEDFRARLVKHGKHQAMK-FSWAESAR 395
Cdd:pfam13524  10 DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRERVLAeHTYAHRAE 89


                  .
gi 2526276233 396 R 396
Cdd:pfam13524  90 Q 90
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 278-388 2.40e-04

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: 44.63  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 278 LARKCGLEeDELILTGFVSEEDLVRLYNLchlFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVIGLPEALFD---- 353
Cdd:cd03813   346 LVASLGLE-NKVKFLGFQNIKEYYPKLGL---LVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADDALGqagl 421

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2526276233 354 ---PHSDDDFARLMERALNDEDFRARLVKHGKHQAMKF 388
Cdd:cd03813   422 vvpPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 291-430 4.43e-04

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: 43.77  E-value: 4.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 291 LTGFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVigLPEALF---DPHSDDDFARLMERA 367
Cdd:cd03796   254 LLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVGGIPEV--LPPDMIllaEPDPEDIVRKLEEAI 331

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2526276233 368 LNDEdfRARLVKHGKHQAMK--FSWAESARRAivqmERLVAHQKSHSTNSVPDRRLKLAYISPLP 430
Cdd:cd03796   332 SILR--TGKHDPWSFHNRVKkmYSWEDVARRT----EKVYDRILSTPNRPFLERLKRYYNCGPIA 390
PHA01633 PHA01633
putative glycosyl transferase group 1
 293-334 1.04e-03

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 42.27  E-value: 1.04e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2526276233 293 GFVSEEDLVRLYNLCHLFVFPSWHEGFGLPALEAMRCGAPVI 334
Cdd:PHA01633  210 GHNSREYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMGTPVI 251
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 269-377 1.44e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 42.67  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 269 AENRRNLEALARKCGLEEDELILTGFVSEEDLVRLYNLCHLFV--FPswHEGfGLPALEAMRCGAPVI--------GANT 338
Cdd:COG3914   510 PEARERLRAAAAARGVDPDRLIFLPRLPRAEHLARYALADLFLdtFP--YNG-GTTTLEALWMGVPVVtlagetfaSRVG 586

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2526276233 339 SSLPEVIGLPE--AlfdpHSDDDFarlMERAL---NDEDFRARL 377
Cdd:COG3914   587 ASLLTALGLPEliA----TSEEEY---VALAValaTDPELLAAL 623
PLN00142 PLN00142
sucrose synthase
 235-364 1.56e-03

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 42.27  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 235 IDHRKNIEGLIRSYAKLPQnLRASHQLAIVC-SIQAENRRNLEALA--RKCgleeDELI----LTG----FVSEEDLVR- 302
Cdd:PLN00142  582 LDRVKNLTGLVEWYGKNKR-LRELVNLVVVGgFIDPSKSKDREEIAeiKKM----HSLIekynLKGqfrwIAAQTNRVRn 656

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 303 --LYN-LCH---LFVFPSWHEGFGLPALEAMRCGAPVIGANTSSLPEVI--GLPEALFDPHSDDDFARLM 364
Cdd:PLN00142  657 geLYRyIADtkgAFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIvdGVSGFHIDPYHGDEAANKI 726
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 605-789 1.69e-03

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: 41.90  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 605 PHMRDPHvnkdrvlARQALGLGvDDFVVCSFGMLGPTKLNHRLLEAWLnsRLGADKNCHLVFVGENhPGTYGVElleiir 684
Cdd:cd03814   182 PSRRDAA-------LRRRLGPP-GRPLLLYVGRLAPEKNLEALLDADL--PLAASPPVRLVVVGDG-PARAELE------ 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 685 nhRAEKNIRITGWADLDLFRNYLAAADMGVQlrtLSRGETSG-TVLDCMCHSLATIVNANGSMADL-NEQAVWMLSDEFS 762
Cdd:cd03814   245 --ARGPDVIFTGFLTGEELARAYASADVFVF---PSRTETFGlVVLEAMASGLPVVAADAGGPRDIvRPGGTGALVEPGD 319

                         170       180
                  ....*....|....*....|....*..
gi 2526276233 763 DEELITALETLWQDGDKRQSLGKRARE 789
Cdd:cd03814   320 AAAFAAALRALLEDPELRRRMAARARA 346
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 236-383 1.70e-03

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


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 41.92  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 236 DHRKNIEGLIRSYAKLPQnlRASH-QLAIVCSIQA---ENRRNLEALARKCGLEEDELILTGFVSEEDLVRLYNLCHLFV 311
Cdd:cd03792   207 DPSKDPLGVIDAYKLFKR--RAEEpQLVICGHGAVddpEGSVVYEEVMEYAGDDHDIHVLRLPPSDQEINALQRAATVVL 284

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2526276233 312 FPSWHEGFGLPALEAMRCGAPVIGANTSSLP-EVIGLPEALFDPHSDDDFARLMeRALNDEDFRARLVKHGKH 383
Cdd:cd03792   285 QLSTREGFGLTVSEALWKGKPVIATPAGGIPlQVIDGETGFLVNSVEGAAVRIL-RLLTDPELRRKMGLAARE 356
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 291-334 5.99e-03

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: 39.96  E-value: 5.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2526276233 291 LTGFVSEEDLVRLYNLCHLFVFPSwHEGFGLPALEAMRCGAPVI 334
Cdd:cd03804   250 FLGYQPDEVLKELLSKARAFVFAA-EEDFGIVPVEAQACGTPVI 292
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
761-806 7.19e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 36.81  E-value: 7.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2526276233 761 FSD-EELITALETLWQDGDKRQSLGKRAREVILEDHDPRYCAGQYQD 806
Cdd:pfam13524  47 YRDpEELAEKIRYLLEHPEERRAIAAAGRERVLAEHTYAHRAEQLLD 93
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
293-381 7.36e-03

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


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 39.53  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2526276233 293 GFVSEEDLVRLYNlCHLFV--FPSWHEGFGLPA---LEAMRCGAPVIGANTSSLpeviglpEALFDP-------HSDDDF 360
Cdd:COG4641   186 GHLPGEEHPAAYA-SSKITlnVNRMAASPDSPTrrtFEAAACGAFLLSDPWEGL-------EELFEPgeevlvfRDGEEL 257

                          90       100
                  ....*....|....*....|.
gi 2526276233 361 ARLMERALNDEDFRARLVKHG 381
Cdd:COG4641   258 AEKLRYLLADPEERRAIAEAG 278
 
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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