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Conserved domains on  [gi|15219285|ref|NP_173105|]
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UDP-Glycosyltransferase superfamily protein [Arabidopsis thaliana]

Protein Classification

PLN02275 family protein( domain architecture ID 11476589)

PLN02275 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02275 PLN02275
transferase, transferring glycosyl groups
 1-417 0e+00

transferase, transferring glycosyl groups


:

Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 733.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285    1 MGKRGRACVVVLGDLGRSPRMQYHALSLARQASFQVDIVAYGGSIPHEAVLNHPSIHIHTMAQPRFIQYFPKILYPVTLL 80
Cdd:PLN02275   1 MGRRGRAAVVVLGDFGRSPRMQYHALSLARQASFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRVLYALALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   81 LKAFIQFTMLLWFLFVKVPAPDIFLVQNPPSVPTLIAVKWASSWRRAAFVVDWHNFGYTLLALSLGRNNLLVSLYRWSEN 160
Cdd:PLN02275  81 LKVAIQFLMLLWFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  161 HYGKMATGSLCVTKAMQHELDQNWGVRAKVLYDQPPEFFRPALLEerhelfcrvrkdlchpigvydfisrelenqelnet 240
Cdd:PLN02275 161 HYGKMADGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASLE----------------------------------- 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  241 lfttkfnadISLKQNRPALVVSSTSWTPDENFGILLEAAVMYDRRVAARSKGSETAeiSEEQHHYPNLLFIITGKGPEKE 320
Cdd:PLN02275 206 ---------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARLNESDSA--SGKQSLYPRLLFIITGKGPQKA 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  321 MYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNG 400
Cdd:PLN02275 275 MYEEKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNG 354

                        410
                 ....*....|....*..
gi 15219285  401 LLFSSSSELADQLLILF 417
Cdd:PLN02275 355 LLFSSSSELADQLLELL 371
 
Name Accession Description Interval E-value
PLN02275 PLN02275
transferase, transferring glycosyl groups
 1-417 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 733.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285    1 MGKRGRACVVVLGDLGRSPRMQYHALSLARQASFQVDIVAYGGSIPHEAVLNHPSIHIHTMAQPRFIQYFPKILYPVTLL 80
Cdd:PLN02275   1 MGRRGRAAVVVLGDFGRSPRMQYHALSLARQASFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRVLYALALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   81 LKAFIQFTMLLWFLFVKVPAPDIFLVQNPPSVPTLIAVKWASSWRRAAFVVDWHNFGYTLLALSLGRNNLLVSLYRWSEN 160
Cdd:PLN02275  81 LKVAIQFLMLLWFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  161 HYGKMATGSLCVTKAMQHELDQNWGVRAKVLYDQPPEFFRPALLEerhelfcrvrkdlchpigvydfisrelenqelnet 240
Cdd:PLN02275 161 HYGKMADGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASLE----------------------------------- 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  241 lfttkfnadISLKQNRPALVVSSTSWTPDENFGILLEAAVMYDRRVAARSKGSETAeiSEEQHHYPNLLFIITGKGPEKE 320
Cdd:PLN02275 206 ---------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARLNESDSA--SGKQSLYPRLLFIITGKGPQKA 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  321 MYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNG 400
Cdd:PLN02275 275 MYEEKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNG 354

                        410
                 ....*....|....*..
gi 15219285  401 LLFSSSSELADQLLILF 417
Cdd:PLN02275 355 LLFSSSSELADQLLELL 371
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
 2-455 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 643.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   2 GKRGRACVVVLGDLGRSPRMQYHALSLARQaSFQVDIVAYGGSIPHEAVLNHPSIHIHTMAQPRfiqYFPKILYPVTLLL 81
Cdd:cd03816   1 PKKKRVCVLVLGDIGRSPRMQYHALSLARH-GWRVDLIGYLESPPHDELLSHPNITIHALPPPP---TKNKLPFLLFAPL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  82 KAFIQFTMLLWFLFvKVPAPDIFLVQNPPSVPTLIAVKWASSWRRAAFVVDWHNFGYTLLALSLGRNNLLVSLYRWSENH 161
Cdd:cd03816  77 KVLLQALSLLWLLY-ELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 162 YGKMATGSLCVTKAMQHELDQ--NWGVRAKVLYDQPPEFFRPALLEERHELFCRVrkdlchpigvydfisrelenqelne 239
Cdd:cd03816 156 FGRMADAHLCVTKAMQRDLQQfeNWNIRATVLYDRPPSHFRPIPLEEKHELFLEL------------------------- 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 240 TLFTTKFNADISLKQNRPALVVSSTSWTPDENFGILLEAAVMYDRRVAARSKgsetaeiseeqhHYPNLLFIITGKGPEK 319
Cdd:cd03816 211 ALFRELAEGAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPA------------LLPSLLCIITGKGPLK 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 320 EMYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKN 399
Cdd:cd03816 279 EMYLELIKELKLKKVTIRTPWLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVN 358

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15219285 400 GLLFSSSSELADQLLILFKGFpgNCDALMSLKAGAMETgSSGRWATEWEDCAKPLI 455
Cdd:cd03816 359 GLVFGDSEELAEQLIDLLSDF--DRGKLNVLKKGAQEE-SENRWDENWDRVAGPLF 411
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 305-418 5.34e-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: 54.97  E-value: 5.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   305 YPNLLFIITGKGPEKEMYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCGLPVCS 384
Cdd:pfam00534  31 NPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG---FGIVLLEAMACGLPVIA 107

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15219285   385 VSYSCIQELVKDGKNGLLFSSSS--ELADQLLILFK 418
Cdd:pfam00534 108 SDVGGPPEVVKDGETGFLVKPNNaeALAEAIDKLLE 143
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 349-418 3.61e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 46.14  E-value: 3.61e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219285 349 LLGSADlgVCLHTSSSGlDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNGLLF--SSSSELADQLLILFK 418
Cdd:COG0438  17 LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLE 85
 
Name Accession Description Interval E-value
PLN02275 PLN02275
transferase, transferring glycosyl groups
 1-417 0e+00

transferase, transferring glycosyl groups


Pssm-ID: 215155 [Multi-domain]  Cd Length: 371  Bit Score: 733.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285    1 MGKRGRACVVVLGDLGRSPRMQYHALSLARQASFQVDIVAYGGSIPHEAVLNHPSIHIHTMAQPRFIQYFPKILYPVTLL 80
Cdd:PLN02275   1 MGRRGRAAVVVLGDFGRSPRMQYHALSLARQASFQVDVVAYGGSEPIPALLNHPSIHIHLMVQPRLLQRLPRVLYALALL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   81 LKAFIQFTMLLWFLFVKVPAPDIFLVQNPPSVPTLIAVKWASSWRRAAFVVDWHNFGYTLLALSLGRNNLLVSLYRWSEN 160
Cdd:PLN02275  81 LKVAIQFLMLLWFLCVKIPRPDVFLVQNPPSVPTLAVVKLACWLRRAKFVIDWHNFGYTLLALSLGRSHPLVRLYRWYER 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  161 HYGKMATGSLCVTKAMQHELDQNWGVRAKVLYDQPPEFFRPALLEerhelfcrvrkdlchpigvydfisrelenqelnet 240
Cdd:PLN02275 161 HYGKMADGHLCVTKAMQHELDQNWGIRATVLYDQPPEFFRPASLE----------------------------------- 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  241 lfttkfnadISLKQNRPALVVSSTSWTPDENFGILLEAAVMYDRRVAARSKGSETAeiSEEQHHYPNLLFIITGKGPEKE 320
Cdd:PLN02275 206 ---------IRLRPNRPALVVSSTSWTPDEDFGILLEAAVMYDRRVAARLNESDSA--SGKQSLYPRLLFIITGKGPQKA 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  321 MYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNG 400
Cdd:PLN02275 275 MYEEKISRLNLRHVAFRTMWLEAEDYPLLLGSADLGVSLHTSSSGLDLPMKVVDMFGCGLPVCAVSYSCIGELVKDGKNG 354

                        410
                 ....*....|....*..
gi 15219285  401 LLFSSSSELADQLLILF 417
Cdd:PLN02275 355 LLFSSSSELADQLLELL 371
GT33_ALG1-like cd03816
chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is ...
 2-455 0e+00

chitobiosyldiphosphodolichol beta-mannosyltransferase and similar proteins; This family is most closely related to the GT33 family of glycosyltransferases. The yeast gene ALG1 has been shown to function as a mannosyltransferase that catalyzes the formation of dolichol pyrophosphate (Dol-PP)-GlcNAc2Man from GDP-Man and Dol-PP-Glc-NAc2, and participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. In humans ALG1 has been associated with the congenital disorders of glycosylation (CDG) designated as subtype CDG-Ik.


Pssm-ID: 340843 [Multi-domain]  Cd Length: 411  Bit Score: 643.94  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   2 GKRGRACVVVLGDLGRSPRMQYHALSLARQaSFQVDIVAYGGSIPHEAVLNHPSIHIHTMAQPRfiqYFPKILYPVTLLL 81
Cdd:cd03816   1 PKKKRVCVLVLGDIGRSPRMQYHALSLARH-GWRVDLIGYLESPPHDELLSHPNITIHALPPPP---TKNKLPFLLFAPL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  82 KAFIQFTMLLWFLFvKVPAPDIFLVQNPPSVPTLIAVKWASSWRRAAFVVDWHNFGYTLLALSLGRNNLLVSLYRWSENH 161
Cdd:cd03816  77 KVLLQALSLLWLLY-ELRPADYILVQNPPSIPTLAIAWLYCRLRRTKLIIDWHNFGYTILALKLGENHPLVRLAKWYEKT 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 162 YGKMATGSLCVTKAMQHELDQ--NWGVRAKVLYDQPPEFFRPALLEERHELFCRVrkdlchpigvydfisrelenqelne 239
Cdd:cd03816 156 FGRMADAHLCVTKAMQRDLQQfeNWNIRATVLYDRPPSHFRPIPLEEKHELFLEL------------------------- 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 240 TLFTTKFNADISLKQNRPALVVSSTSWTPDENFGILLEAAVMYDRRVAARSKgsetaeiseeqhHYPNLLFIITGKGPEK 319
Cdd:cd03816 211 ALFRELAEGAVSYKEGRPALLVSSTSWTPDEDFSILLDALKAYESSAATEPA------------LLPSLLCIITGKGPLK 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 320 EMYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKN 399
Cdd:cd03816 279 EMYLELIKELKLKKVTIRTPWLSAEDYPRLLASADLGVCLHTSSSGLDLPMKVVDMFGCGLPVCAMDFKCIGELVKHGVN 358

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15219285 400 GLLFSSSSELADQLLILFKGFpgNCDALMSLKAGAMETgSSGRWATEWEDCAKPLI 455
Cdd:cd03816 359 GLVFGDSEELAEQLIDLLSDF--DRGKLNVLKKGAQEE-SENRWDENWDRVAGPLF 411
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 13-416 7.20e-11

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: 63.52  E-value: 7.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  13 GDLGRSPRMQYHALSLARQAsFQVDIVA-----YGGSIPHEAVLNHPSIHIHtmaqpRFIQYFPKILYPVTLLLKAFIQF 87
Cdd:cd03794  12 PKGAAAARVYELAKELVRRG-HEVTVLTpspnyPLGRIFAGATETKDGIRVI-----RVKLGPIKKNGLIRRLLNYLSFA 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  88 TMLLWFLFVKVPAPDIFLVQNPPsvPTL-IAVKWASSWRRAAFVVD----WHNfgyTLLALSLGRNNLLVSLYRWSENHY 162
Cdd:cd03794  86 LAALLKLLVREERPDVIIAYSPP--ITLgLAALLLKKLRGAPFILDvrdlWPE---SLIALGVLKKGSLLKLLKKLERKL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 163 GKMATGSLCVTKAMQheldqnwgvrakvlydqppEFFRPAlleerhelfcRVRKDLCH--PIGVydfisrelenqELNET 240
Cdd:cd03794 161 YRLADAIIVLSPGLK-------------------EYLLRK----------GVPKEKIIviPNWA-----------DLEEF 200

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 241 LFTTKFNADISLKQNRPALVVSSTSWTPDENFGILLEAAvmydrrvaarskgsetaeisEEQHHYPNLLFIITGKGPEKE 320
Cdd:cd03794 201 KPPPKDELRKKLGLDDKFVVVYAGNIGKAQGLETLLEAA--------------------ERLKRRPDIRFLFVGDGDEKE 260

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 321 MYEEKIKRLNLRHVAFRTmWLAAEDYPLLLGSADLG-VCLHTS-SSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGK 398
Cdd:cd03794 261 RLKELAKARGLDNVTFLG-RVPKEEVPELLSAADVGlVPLKDNpANRGSSPSKLFEYMAAGKPILASDDGGSDLAVEING 339

                       410       420
                ....*....|....*....|
gi 15219285 399 NGLLF--SSSSELADQLLIL 416
Cdd:cd03794 340 CGLVVepGDPEALADAILEL 359
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 244-403 4.65e-10

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


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 59.73  E-value: 4.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 244 TKFNADISLKQNRPALVVSSTSWTPDENFGILLEAAvmydRRVAARskgsetaeiseeqhHYPNLLFIITGKGPEKEMYE 323
Cdd:cd01635  97 ELLALARLLVSLPLADKVSVGRLVPEKGIDLLLEAL----ALLKAR--------------LPDLVLVLVGGGGEREEEEA 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 324 EKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNGLLF 403
Cdd:cd01635 159 LAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEG---FGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 296-415 1.43e-09

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: 59.60  E-value: 1.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 296 AEISEEqhhyPNLLFIITGKGPEKEMYEEKIKRLNL-RHVAFrTMWLAAEDYPLLLGSADLGVclHTSSSGLdLPMKVVD 374
Cdd:cd03817 224 AELKKE----PNIKLVIVGDGPEREELKELARELGLaDKVIF-TGFVPREELPEYYKAADLFV--FASTTET-QGLVYLE 295

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15219285 375 MFGCGLPVCSVSYSCIQELVKDGKNGLLFSSSSELADQLLI 415
Cdd:cd03817 296 AMAAGLPVVAAKDPAASELVEDGENGFLFEPNDETLAEKLL 336
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 305-418 5.34e-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: 54.97  E-value: 5.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   305 YPNLLFIITGKGPEKEMYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCGLPVCS 384
Cdd:pfam00534  31 NPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPSRYEG---FGIVLLEAMACGLPVIA 107

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 15219285   385 VSYSCIQELVKDGKNGLLFSSSS--ELADQLLILFK 418
Cdd:pfam00534 108 SDVGGPPEVVKDGETGFLVKPNNaeALAEAIDKLLE 143
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 34-410 1.96e-08

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: 55.83  E-value: 1.96e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  34 FQVDIVAYGGSIPHEAVLNhpSIHIHTMAQPRFIQYFPKILYPVTLLLKAFI---QFTMLLWFLFvkvPAPDIFLVQNPP 110
Cdd:cd03811  30 YDVTLVLLRDEGDLDKQLN--GDVKLIRLLIRVLKLIKLGLLKAILKLKRILkraKPDVVISFLG---FATYIVAKLAAA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 111 SVPTLIavkwassWRR-AAFVVDWHNFGYTLLALSLGRNNLLVslyrwsenhygkmatgslCVTKAMQHELDQN-WGVRA 188
Cdd:cd03811 105 RSKVIA-------WIHsSLSKLYYLKKKLLLKLKLYKKADKIV------------------CVSKGIKEDLIRLgPSPPE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 189 KVLYdqppeffrpalleerhelfcrvrkdlchpigVYDFISRELENQELNETLFTTKFNADIslkqnrpalVVSSTSWTP 268
Cdd:cd03811 160 KIEV-------------------------------IYNPIDIDRIRALAKEPILNEPEDGPV---------ILAVGRLDP 199

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 269 DENFGILLEAAvmydrrvaarskgsetAEISEeqhHYPNLLFIITGKGPEKEMYEEKIKRLNLRHvafRTMWLAAED--Y 346
Cdd:cd03811 200 QKGHDLLIEAF----------------AKLRK---KYPDVKLVILGDGPLREELEKLAKELGLAE---RVIFLGFQSnpY 257

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219285 347 PlLLGSADLGVclHTSSS-GldLPMKVVDMFGCGLPVcsVSYSC--IQELVKDGKNGLLFSSSSELA 410
Cdd:cd03811 258 P-YLKKADLFV--LSSRYeG--FPNVLLEAMALGTPV--VSTDCpgPREILDDGENGLLVPDGDAAA 317
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 24-414 2.17e-08

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: 56.01  E-value: 2.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285  24 HALSLARQ-ASFQVDIVAYGGSIPHEAVLNHPSIHIHTM-AQPRFIQYFPKILYPVTLLLKAFiqftmllwflfvkvpAP 101
Cdd:cd03801  19 HVRELARAlAARGHDVTVLTPADPGEPPEELEDGVIVPLlPSLAALLRARRLLRELRPLLRLR---------------KF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 102 DIFLVQNPPSVPTLIAVKWAsswRRAAFVVDWHNFGYTLLALSLGRNNLLVSLYRWsenhYGKMATGSLCVTKAMQHELD 181
Cdd:cd03801  84 DVVHAHGLLAALLAALLALL---LGAPLVVTLHGAEPGRLLLLLAAERRLLARAEA----LLRRADAVIAVSEALRDELR 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 182 QNWGV---RAKVLydqppeffrpalleerhelfcrvrkdlchPIGVydfisrelenqelNETLFTTKFNADISLKQNRPa 258
Cdd:cd03801 157 ALGGIppeKIVVI-----------------------------PNGV-------------DLERFSPPLRRKLGIPPDRP- 193

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 259 LVVSSTSWTPDENFGILLEAAvmydRRVAARskgsetaeiseeqhhYPNLLFIITGK-GPEKEMYEEKIKRLNlRHVAFr 337
Cdd:cd03801 194 VLLFVGRLSPRKGVDLLLEAL----AKLLRR---------------GPDVRLVIVGGdGPLRAELEELELGLG-DRVRF- 252

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15219285 338 TMWLAAEDYPLLLGSADLGVCLHTSSSgldLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNGLLFS--SSSELADQLL 414
Cdd:cd03801 253 LGFVPDEELPALYAAADVFVLPSRYEG---FGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPpdDVEALADALL 328
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
310-418 2.53e-06

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 46.74  E-value: 2.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285   310 FIITGKGPEKEmYEEKIKRLNlRHVAFRTMwlaAEDYPLLLGSADLGVClhtSSSGLDLPMKVVDMFGCGLPVcsVSYSC 389
Cdd:pfam13692  36 LVIVGDGPEEE-LEELAAGLE-DRVIFTGF---VEDLAELLAAADVFVL---PSLYEGFGLKLLEAMAAGLPV--VATDV 105

                          90       100       110
                  ....*....|....*....|....*....|...
gi 15219285   390 --IQELVkDGKNGLLFS--SSSELADQLLILFK 418
Cdd:pfam13692 106 ggIPELV-DGENGLLVPpgDPEALAEAILRLLE 137
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 349-418 3.61e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 46.14  E-value: 3.61e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15219285 349 LLGSADlgVCLHTSSSGlDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNGLLF--SSSSELADQLLILFK 418
Cdd:COG0438  17 LLAAAD--VFVLPSRSE-GFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVppGDPEALAEAILRLLE 85
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 305-418 1.48e-05

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: 46.82  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 305 YPNLLFIITGKGPEKEMYEEKIKRLNLRHvafRTMWLAA-EDYPLLLGSADLgVCLHTSSSGLdlPMKVVDMFGCGLPVc 383
Cdd:cd03808 218 GPNVRFLLVGDGELENPSEILIEKLGLEG---RIEFLGFrSDVPELLAESDV-FVLPSYREGL--PRSLLEAMAAGRPV- 290

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15219285 384 sVSYSC--IQELVKDGKNGLLFS--SSSELADQLLILFK 418
Cdd:cd03808 291 -ITTDVpgCRELVIDGVNGFLVPpgDVEALADAIEKLIE 328
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
21-189 4.06e-05

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 44.06  E-value: 4.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285    21 MQYHALSLAR---QASFQVDIVAYGGSIPHEAVLNHpsIHIHTMAQPRFIQYFPKILYPVTLLLKAFIQFtmllwflfvk 97
Cdd:pfam13439   3 VERYVLELARalaRRGHEVTVVTPGGPGPLAEEVVR--VVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRE---------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285    98 vpAPDIFLVQNPPsvPTLIAVKWASSWRRAAFVVDWHNfGYTLLALSLGRNNLLVSLYRWSENHYGKMATGSLCVTKAMQ 177
Cdd:pfam13439  71 --RPDVVHAHSPF--PLGLAALAARLRLGIPLVVTYHG-LFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVA 145

                         170
                  ....*....|..
gi 15219285   178 HELDQNWGVRAK 189
Cdd:pfam13439 146 DELRRLYGVPPE 157
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
21-188 3.52e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 40.85  E-value: 3.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285    21 MQYHALSLAR---QASFQVDIVAYGGSIPHEAvLNHPSIHIHTMAQPRFIQYFPKILYPVTLLlkafiqfTMLLWFlfvk 97
Cdd:pfam13579   3 IGVYVLELARalaALGHEVRVVTPGGPPGRPE-LVGDGVRVHRLPVPPRPSPLADLAALRRLR-------RLLRAE---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285    98 vpAPDIFLVQNPPSvptLIAVKWASSWRRAAFVVDWHNFGYTLLALSLGRnnllvsLYRWSENHYGKMATGSLCVTKAMQ 177
Cdd:pfam13579  71 --RPDVVHAHSPTA---GLAARLARRRRGVPLVVTVHGLALDYGSGWKRR------LARALERRLLRRADAVVVVSEAEA 139

                         170
                  ....*....|.
gi 15219285   178 HELdQNWGVRA 188
Cdd:pfam13579 140 ELL-RALGVPA 149
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 275-416 3.71e-04

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: 42.44  E-value: 3.71e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 275 LLEAAvmydRRVAARskgsetaeiseeqhhYPNLLFIITGKGPEKEMYEEKIKRLNlrHVAFRTMWLAAEDYPLLLGSAD 354
Cdd:cd05844 207 LIEAF----RRLAAR---------------HPTARLVIAGDGPLRPALQALAAALG--RVRFLGALPHAEVQDWMRRAEI 265

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219285 355 LGVCLHTSSSGlD---LPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNGLLFSS--SSELADQLLIL 416
Cdd:cd05844 266 FCLPSVTAASG-DsegLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEgdVDALADALQAL 331
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 305-402 5.50e-04

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


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 42.05  E-value: 5.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 305 YPNLLFIITGKGPEKEMYEEKIKRLNLRHVAFRTMWLAAEDYPLLLGSADLGVCLHTSSSGLD---LPMKVVDMFGCGLP 381
Cdd:cd03799 203 YPNIEYQIIGDGDLKEQLQQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGDqdgPPNTLKEAMAMGLP 282

                        90       100
                ....*....|....*....|.
gi 15219285 382 VCSVSYSCIQELVKDGKNGLL 402
Cdd:cd03799 283 VISTEHGGIPELVEDGVSGFL 303
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
357-413 1.65e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 37.58  E-value: 1.65e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15219285   357 VCLHTSSSGLDLPMKVVDMFGCGLPVCSVSYSCIQELVKDGKNGLLFSSSSELADQL 413
Cdd:pfam13524   1 IVLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKI 57
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 297-403 2.08e-03

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: 40.03  E-value: 2.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 297 EISEEQHHYPNLLFIITGKGPEKEMYEEKIKRLNLRH----VAFRtmwlaaEDYPLLLGSADLGVclhTSSSGLDLPMKV 372
Cdd:cd03819 202 DAAAELKDEPDFRLLVAGDGPERDEIRRLVERLGLRDrvtfTGFR------EDVPAALAASDVVV---LPSLHEEFGRVA 272

                        90       100       110
                ....*....|....*....|....*....|.
gi 15219285 373 VDMFGCGLPVCSVSYSCIQELVKDGKNGLLF 403
Cdd:cd03819 273 LEAMACGTPVVATDVGGAREIVVHGRTGLLV 303
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 268-442 3.48e-03

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: 39.61  E-value: 3.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 268 PDENFGILLEAAvmydRRVAArskgsetaeiseeqhHYPNLLFIITGKGPEKEMYEEKIKRLNLRHVAFrtmwLAAE--D 345
Cdd:cd03807 201 PVKDHSDLLRAA----ALLVE---------------THPDLRLLLVGRGPERPNLERLLLELGLEDRVH----LLGErsD 257

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 346 YPLLLGSADLGvCLHTSSSGldLPMKVVDMFGCGLPVCSVSYSCIQELVkDGKNGLLFS--SSSELADQLLilfkgfpgn 423
Cdd:cd03807 258 VPALLPAMDIF-VLSSRTEG--FPNALLEAMACGLPVVATDVGGAAELV-DDGTGFLVPagDPQALADAIR--------- 324

                       170
                ....*....|....*....
gi 15219285 424 cdALMSLKAGAMETGSSGR 442
Cdd:cd03807 325 --ALLEDPEKRARLGRAAR 341
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 306-418 7.28e-03

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


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 38.44  E-value: 7.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 306 PNLLFIITGKGPEKEMYEEKIKRLNL-RHVAFR--TMWLAAE--DYPLLLgsadlgvclhTSSSGLDLPMKVVDMFGCGL 380
Cdd:cd04949 190 PEITLDIYGYGEEREKLKKLIEELHLeDNVFLKgyHSNLDQEyqDAYLSL----------LTSQMEGFGLTLMEAIGHGL 259

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15219285 381 PVCS--VSYScIQELVKDGKNGLLFSSS--SELADQLLILFK 418
Cdd:cd04949 260 PVVSydVKYG-PSELIEDGENGYLIEKNniDALADKIIELLN 300
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 311-414 7.65e-03

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: 38.49  E-value: 7.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219285 311 IITGKGPEKEMYEEKIKRLNLRHvafRTMWLA-AEDYPLLLGSADLGVCLHTSSS-GLDLpmkvVDMFGCGLPVCSVSYS 388
Cdd:cd04962 230 LLVGDGPERVPAEELARELGVED---RVLFLGkQDDVEELLSIADLFLLPSEKESfGLAA----LEAMACGVPVVSSNAG 302

                        90       100       110
                ....*....|....*....|....*....|.
gi 15219285 389 CIQELVKDGKNGLLF-----SSSSELADQLL 414
Cdd:cd04962 303 GIPEVVKHGETGFLSdvgdvDAMAKSALSIL 333
 
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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