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Conserved domains on  [gi|663515936|gb|AIF06402|]
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glycosyl transferase family protein [uncultured marine group II/III euryarchaeote KM3_191_F05]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 13-362 1.54e-38

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.


The actual alignment was detected with superfamily member cd03794:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 391  Bit Score: 142.10  E-value: 1.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  13 DTRVWHEALSLVGAGYEVTVFCWARRDDS----LPAEELRDGVRVRRI--FASLDSWLPGRMLAFRSAMRQLASAA--AD 84
Cdd:cd03794   17 AARVYELAKELVRRGHEVTVLTPSPNYPLgrifAGATETKDGIRVIRVklGPIKKNGLIRRLLNYLSFALAALLKLlvRE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  85 ELPAVVHAH--DLETLPAACRAADVCDAKVVFDAHEDWPLLERVQGA----ALGAWFGWQQRRWLPRADTVVTVSPELAK 158
Cdd:cd03794   97 ERPDVIIAYspPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVlkkgSLLKLLKKLERKLYRLADAIIVLSPGLKE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 159 RLGGA-------EVLYNSEPLAVIEASVGEDLRAKLGLGG-VVAGYIGAL-RRRIIEQLLDAA---AQVPEVTLLVVG-G 225
Cdd:cd03794  177 YLLRKgvpkekiIVIPNWADLEEFKPPPKDELRKKLGLDDkFVVVYAGNIgKAQGLETLLEAAerlKRRPDIRFLFVGdG 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 226 PPKgragyaglQEQLEAHAAKVGARAVFTGPLAYGRMGDCYRACNLLLVgHYVAEPLRHAAVPKKLLDAMAYSIP-AVVG 304
Cdd:cd03794  257 DEK--------ERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLV-PLKDNPANRGSSPSKLFEYMAAGKPiLASD 327

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663515936 305 PYEARRSIVERNhCGLVAD-----DWVAPLRQLAGDDELRSEMGARGHVAWREKYCWDRMEER 362
Cdd:cd03794  328 DGGSDLAVEING-CGLVVEpgdpeALADAILELLDDPELRRAMGENGRELAEEKFSREKLADR 389
 
Name Accession Description Interval E-value
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 13-362 1.54e-38

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: 142.10  E-value: 1.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  13 DTRVWHEALSLVGAGYEVTVFCWARRDDS----LPAEELRDGVRVRRI--FASLDSWLPGRMLAFRSAMRQLASAA--AD 84
Cdd:cd03794   17 AARVYELAKELVRRGHEVTVLTPSPNYPLgrifAGATETKDGIRVIRVklGPIKKNGLIRRLLNYLSFALAALLKLlvRE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  85 ELPAVVHAH--DLETLPAACRAADVCDAKVVFDAHEDWPLLERVQGA----ALGAWFGWQQRRWLPRADTVVTVSPELAK 158
Cdd:cd03794   97 ERPDVIIAYspPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVlkkgSLLKLLKKLERKLYRLADAIIVLSPGLKE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 159 RLGGA-------EVLYNSEPLAVIEASVGEDLRAKLGLGG-VVAGYIGAL-RRRIIEQLLDAA---AQVPEVTLLVVG-G 225
Cdd:cd03794  177 YLLRKgvpkekiIVIPNWADLEEFKPPPKDELRKKLGLDDkFVVVYAGNIgKAQGLETLLEAAerlKRRPDIRFLFVGdG 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 226 PPKgragyaglQEQLEAHAAKVGARAVFTGPLAYGRMGDCYRACNLLLVgHYVAEPLRHAAVPKKLLDAMAYSIP-AVVG 304
Cdd:cd03794  257 DEK--------ERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLV-PLKDNPANRGSSPSKLFEYMAAGKPiLASD 327

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663515936 305 PYEARRSIVERNhCGLVAD-----DWVAPLRQLAGDDELRSEMGARGHVAWREKYCWDRMEER 362
Cdd:cd03794  328 DGGSDLAVEING-CGLVVEpgdpeALADAILELLDDPELRRAMGENGRELAEEKFSREKLADR 389
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
12-160 1.11e-12

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 65.63  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936   12 VDTRVWHEALSLVGAGYEVTVFCwaRRDDSLPAEELRDGVRVRRIFASLDsWLPGRMLAFRSAMRQLASAAAdelPAVVH 91
Cdd:pfam13439   3 VERYVLELARALARRGHEVTVVT--PGGPGPLAEEVVRVVRVPRVPLPLP-PRLLRSLAFLRRLRRLLRRER---PDVVH 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663515936   92 AHDLETL-PAACRAADVCDAKVVFDAHEDWPLLERVQGA--ALGAWFGWQQRRWLPRADTVVTVSPELAKRL 160
Cdd:pfam13439  77 AHSPFPLgLAALAARLRLGIPLVVTYHGLFPDYKRLGARlsPLRRLLRRLERRLLRRADRVIAVSEAVADEL 148
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 266-362 3.20e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 57.31  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 266 YRACNLLLVghyvaePLRHAAVPKKLLDAMAYSIPAVVGPYEARRSIVERNHCGLV-----ADDWVAPLRQLAGDDELRS 340
Cdd:COG0438   18 LAAADVFVL------PSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLvppgdPEALAEAILRLLEDPELRR 91

                         90       100
                 ....*....|....*....|..
gi 663515936 341 EMGARGHVAWREKYCWDRMEER 362
Cdd:COG0438   92 RLGEAARERAEERFSWEAIAER 113
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
20-230 1.01e-03

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 40.73  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  20 ALSLVGAGYEVTVFC-------WaRRDDSLPAE----ELRDGVRVRRifASLdsWLPGRMLAFRSaMRQLASAAADELPA 88
Cdd:PRK10307  25 AEWLAARGHEVRVITappyypqW-RVGEGYSAWryrrESEGGVTVWR--CPL--YVPKQPSGLKR-LLHLGSFALSSFFP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  89 VVH------------AHDLETLPAACRAADVCDAKVVF-------DAHEDWPLLERVQGAALGAWFgwqQRRWLPRADTV 149
Cdd:PRK10307  99 LLAqrrwrpdrvigvVPTLFCAPGARLLARLSGARTWLhiqdyevDAAFGLGLLKGGKVARLATAF---ERSLLRRFDNV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 150 VTVSPELAKRLGGAEV-------LYN-SEPLAVIEASVGED--LRAKLGL--GGVVAGYIGAL-RRRIIEQLLDAAAQV- 215
Cdd:PRK10307 176 STISRSMMNKAREKGVaaekvifFPNwSEVARFQPVADADVdaLRAQLGLpdGKKIVLYSGNIgEKQGLELVIDAARRLr 255

                        250
                 ....*....|....*...
gi 663515936 216 --PEVTLLVVG-GPPKGR 230
Cdd:PRK10307 256 drPDLIFVICGqGGGKAR 273
 
Name Accession Description Interval E-value
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 13-362 1.54e-38

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: 142.10  E-value: 1.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  13 DTRVWHEALSLVGAGYEVTVFCWARRDDS----LPAEELRDGVRVRRI--FASLDSWLPGRMLAFRSAMRQLASAA--AD 84
Cdd:cd03794   17 AARVYELAKELVRRGHEVTVLTPSPNYPLgrifAGATETKDGIRVIRVklGPIKKNGLIRRLLNYLSFALAALLKLlvRE 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  85 ELPAVVHAH--DLETLPAACRAADVCDAKVVFDAHEDWPLLERVQGA----ALGAWFGWQQRRWLPRADTVVTVSPELAK 158
Cdd:cd03794   97 ERPDVIIAYspPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVlkkgSLLKLLKKLERKLYRLADAIIVLSPGLKE 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 159 RLGGA-------EVLYNSEPLAVIEASVGEDLRAKLGLGG-VVAGYIGAL-RRRIIEQLLDAA---AQVPEVTLLVVG-G 225
Cdd:cd03794  177 YLLRKgvpkekiIVIPNWADLEEFKPPPKDELRKKLGLDDkFVVVYAGNIgKAQGLETLLEAAerlKRRPDIRFLFVGdG 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 226 PPKgragyaglQEQLEAHAAKVGARAVFTGPLAYGRMGDCYRACNLLLVgHYVAEPLRHAAVPKKLLDAMAYSIP-AVVG 304
Cdd:cd03794  257 DEK--------ERLKELAKARGLDNVTFLGRVPKEEVPELLSAADVGLV-PLKDNPANRGSSPSKLFEYMAAGKPiLASD 327

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663515936 305 PYEARRSIVERNhCGLVAD-----DWVAPLRQLAGDDELRSEMGARGHVAWREKYCWDRMEER 362
Cdd:cd03794  328 DGGSDLAVEING-CGLVVEpgdpeALADAILELLDDPELRRAMGENGRELAEEKFSREKLADR 389
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 2-362 1.58e-32

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: 125.34  E-value: 1.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936   2 LLGHDLLEPT--VDTRVWHEALSLVGAGYEVTVFCwaRRDDSLPAEELRDGVRVRRIFASLDSWLPGRMLafrsamRQLA 79
Cdd:cd03801    4 LLSPELPPPVggAERHVRELARALAARGHDVTVLT--PADPGEPPEELEDGVIVPLLPSLAALLRARRLL------RELR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  80 SAAADELPAVVHAHDLETLPAACRAADVCDAKVVFDAHEDWPLLERVQGAALGAWFGwQQRRWLPRADTVVTVSPELAKR 159
Cdd:cd03801   76 PLLRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRLLA-RAEALLRRADAVIAVSEALRDE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 160 LGGAEVLYNSE----PLAVIEASVGEDLRAKLGL--GGVVAGYIGALRRR-IIEQLLDAAAQV----PEVTLLVVGGPPK 228
Cdd:cd03801  155 LRALGGIPPEKivviPNGVDLERFSPPLRRKLGIppDRPVLLFVGRLSPRkGVDLLLEALAKLlrrgPDVRLVIVGGDGP 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 229 gragyagLQEQLEAHAAKVGARAVFTGPLAYGRMGDCYRACNLLLVghyvaePLRHAAVPKKLLDAMAYSIPAVVGPYEA 308
Cdd:cd03801  235 -------LRAELEELELGLGDRVRFLGFVPDEELPALYAAADVFVL------PSRYEGFGLVVLEAMAAGLPVVATDVGG 301

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 663515936 309 RRSIVERNHCGLVAD-----DWVAPLRQLAGDDELRSEMGARGHVAWREKYCWDRMEER 362
Cdd:cd03801  302 LPEVVEDGEGGLVVPpddveALADALLRLLADPELRARLGRAARERVAERFSWERVAER 360
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 20-362 3.05e-14

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: 73.18  E-value: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  20 ALSLVGAGYEVTVFC---WARRDDSLPAEELRDGVRVRRIFASLDSWLPGRMLAFR--SAMRQLASAAADELPAVVHAH- 93
Cdd:cd03798   24 VRALSRRGVDVEVLApapWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLraPSLAKLLKRRRRGPPDLIHAHf 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  94 DLETLPAACRAADVCDAKVVFDAHEdwpllERVQGAALGAWFGWQQRRWLPRADTVVTVSPELA---KRLGG----AEVL 166
Cdd:cd03798  104 AYPAGFAAALLARLYGVPYVVTEHG-----SDINVFPPRSLLRKLLRWALRRAARVIAVSKALAeelVALGVprdrVDVI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 167 YNSEPLAVIEasvGEDLRAKLGLGGVVAGYIGALRRRI-IEQLLDA----AAQVPEVTLLVVGGPPKGRAGYAglqeqlE 241
Cdd:cd03798  179 PNGVDPARFQ---PEDRGLGLPLDAFVILFVGRLIPRKgIDLLLEAfarlAKARPDVVLLIVGDGPLREALRA------L 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 242 AHAAKVGARAVFTGPLAYGRMGDCYRACNLLlvghyvAEPLRHAAVPKKLLDAMAYSIPAVVGPYEARRSIVERNHCGLV 321
Cdd:cd03798  250 AEDLGLGDRVTFTGRLPHEQVPAYYRACDVF------VLPSRHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLL 323

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 663515936 322 ADDW-----VAPLRQLAGDDELRSEM-GARGHVA----WREKycWDRMEER 362
Cdd:cd03798  324 VPPGdadalAAALRRALAEPYLRELGeAARARVAerfsWVKA--ADRIAAA 372
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 20-362 7.69e-13

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: 69.19  E-value: 7.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  20 ALSLVGAGYEVTVFCWARRDDSLPAEELRDGVRVRRI----FASLDS-WLPGRMLAFRSAMRQlASAAADELPAVVHAHD 94
Cdd:cd03800   31 ARALAELGYQVDIFTRRISPADPEVVEIAPGARVIRVpagpPEYLPKeELWPYLEEFADGLLR-FIAREGGRYDLIHSHY 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  95 LETLPAACRAADVCDAKVVFDAHEdwplLERVQGAALGAwfGWQ---------QRRWLPRADTVVTVSP----ELAKRLG 161
Cdd:cd03800  110 WDSGLVGALLARRLGVPLVHTFHS----LGRVKYRHLGA--QDTyhpslritaEEQILEAADRVIASTPqeadELISLYG 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 162 GAEVLYNSEPLAV-----IEASVGEDLRAKLGLG--GVVAGYIGAL-RRRIIEQLLDAAAQVPE----VTLLVVGGP-PK 228
Cdd:cd03800  184 ADPSRINVVPPGVdlerfFPVDRAEARRARLLLPpdKPVVLALGRLdPRKGIDTLVRAFAQLPElrelANLVLVGGPsDD 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 229 GRAGYAGLQEQLeAHAAKVGARAVFTGPLAYGRMGDCYRACNLLLVGHYVaEPLRHAAVpkkllDAMAYSIP----AVVG 304
Cdd:cd03800  264 PLSMDREELAEL-AEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLY-EPFGLTAI-----EAMACGTPvvatAVGG 336

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663515936 305 PyearRSIVERNHCGLVAD-----DWVAPLRQLAGDDELRSEMGARGHVAWREKYCWDRMEER 362
Cdd:cd03800  337 L----QDIVRDGRTGLLVDphdpeALAAALRRLLDDPALWQRLSRAGLERARAHYTWESVADQ 395
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
12-160 1.11e-12

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 65.63  E-value: 1.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936   12 VDTRVWHEALSLVGAGYEVTVFCwaRRDDSLPAEELRDGVRVRRIFASLDsWLPGRMLAFRSAMRQLASAAAdelPAVVH 91
Cdd:pfam13439   3 VERYVLELARALARRGHEVTVVT--PGGPGPLAEEVVRVVRVPRVPLPLP-PRLLRSLAFLRRLRRLLRRER---PDVVH 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 663515936   92 AHDLETL-PAACRAADVCDAKVVFDAHEDWPLLERVQGA--ALGAWFGWQQRRWLPRADTVVTVSPELAKRL 160
Cdd:pfam13439  77 AHSPFPLgLAALAARLRLGIPLVVTYHGLFPDYKRLGARlsPLRRLLRRLERRLLRRADRVIAVSEAVADEL 148
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
14-160 3.43e-12

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 63.96  E-value: 3.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936   14 TRVWHEALSLVGAGYEVTVFCwaRRDDSLPAEELRDGVRVRRIFASLDSWLPGRMlafrSAMRQLASAAADELPAVVHAH 93
Cdd:pfam13579   5 VYVLELARALAALGHEVRVVT--PGGPPGRPELVGDGVRVHRLPVPPRPSPLADL----AALRRLRRLLRAERPDVVHAH 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 663515936   94 DLETLPAACRAADVCDAKVVFDAHEDWPlleRVQGAALGAWFGWQQRRWLPRADTVVTVSPELAKRL 160
Cdd:pfam13579  79 SPTAGLAARLARRRRGVPLVVTVHGLAL---DYGSGWKRRLARALERRLLRRADAVVVVSEAEAELL 142
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 22-358 9.35e-12

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: 65.85  E-value: 9.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  22 SLVGAGYEVTVFCWARRDDSLPAEELRDGVRVRRIFASLDSWLPG-RMLAFRSAMRQLASAAADElPAVVHAHDLETLP- 99
Cdd:cd03821   26 ALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIPLLRQGaGRTDFSPGLPNWLRRNLRE-YDVVHIHGVWTYTs 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 100 -AACRAADVCDAKVVFDAHEDWPLLERVQGAALGAWFG-WQQRRWLPRADTVVTVSPELAKRLggaEVLYNSEPLAVIEA 177
Cdd:cd03821  105 lAACKLARRRGIPYVVSPHGMLDPWALQQKHWKKRIALhLIERRNLNNAALVHFTSEQEADEL---RRFGLEPPIAVIPN 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 178 SVGEDLRAKlGLGGVVAGYIGALRRRI-----------IEQLLDAAAQVPEVTL---LVVGGPPKGragyAGLQEQLEAH 243
Cdd:cd03821  182 GVDIPEFDP-GLRDRRKHNGLEDRRIIlflgrihpkkgLDLLIRAARKLAEQGRdwhLVIAGPDDG----AYPAFLQLQS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 244 AAKVGARAVFTGPLAYGRMGDCYRACNLLLVghyvaePLRHAAVPKKLLDAMAYSIPAVVGPYEARRSIVERNhCGLVAD 323
Cdd:cd03821  257 SLGLGDRVTFTGPLYGEAKWALYASADLFVL------PSYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVD 329

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 663515936 324 ----DWVAPLRQLAGDDELRSEMGARGH--VAWREKYCWDR 358
Cdd:cd03821  330 pnvsSLAEALAEALRDPADRKRLGEMARraRQVEENFSWEA 370
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 193-346 1.03e-11

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: 62.68  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  193 VAGYIGALRRRI-IEQLLDAAAQV----PEVTLLVVGGPPKgragyaglQEQLEAHAAKVGARA--VFTGPLAYGRMGDC 265
Cdd:pfam00534   4 IILFVGRLEPEKgLDLLIKAFALLkeknPNLKLVIAGDGEE--------EKRLKKLAEKLGLGDnvIFLGFVSDEDLPEL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  266 YRACNLLLVghyvaePLRHAAVPKKLLDAMAYSIPAVVGPYEARRSIVERNHCGLV-----ADDWVAPLRQLAGDDELRS 340
Cdd:pfam00534  76 LKIADVFVL------PSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLvkpnnAEALAEAIDKLLEDEELRE 149


                  ....*.
gi 663515936  341 EMGARG 346
Cdd:pfam00534 150 RLGENA 155
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 27-303 4.89e-11

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: 63.45  E-value: 4.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  27 GYEVTVFCwARRDDSLPAEElrdgVRVRRIFASLDSWLPGRMLAF---RSAMRQLASAAADelpaVVHAHD---LETLpa 100
Cdd:cd03817   31 GHEVYVIT-PSDPGAEDEEE----VVRYRSFSIPIRKYHRQHIPFpfkKAVIDRIKELGPD----IIHTHTpfsLGKL-- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 101 ACRAADVCDAKVVFDAH---EDWpLLERVQGAALGAWFG-WQQRRWLPRADTVVTVSPELAKRL------GGAEVLYNSE 170
Cdd:cd03817  100 GLRIARKLKIPIVHTYHtmyEDY-LHYIPKGKLLVKAVVrKLVRRFYNHTDAVIAPSEKIKDTLreygvkGPIEVIPNGI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 171 PLAVIEASVGEDLRAKLGL--GGVVAGYIGalrrRI-----IEQLLDAAAQV---PEVTLLVVG-GPPKgragyaglqEQ 239
Cdd:cd03817  179 DLDKFEKPLNTEERRKLGLppDEPILLYVG----RLakeknIDFLLRAFAELkkePNIKLVIVGdGPER---------EE 245

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 240 LEAHA--AKVGARAVFTGPLAYGRMGDCYRACNLLLvghyvaeplrHAAV----PKKLLDAMAYSIPAVV 303
Cdd:cd03817  246 LKELAreLGLADKVIFTGFVPREELPEYYKAADLFV----------FASTtetqGLVYLEAMAAGLPVVA 305
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 266-362 3.20e-10

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 57.31  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 266 YRACNLLLVghyvaePLRHAAVPKKLLDAMAYSIPAVVGPYEARRSIVERNHCGLV-----ADDWVAPLRQLAGDDELRS 340
Cdd:COG0438   18 LAAADVFVL------PSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLvppgdPEALAEAILRLLEDPELRR 91

                         90       100
                 ....*....|....*....|..
gi 663515936 341 EMGARGHVAWREKYCWDRMEER 362
Cdd:COG0438   92 RLGEAARERAEERFSWEAIAER 113
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 69-358 3.29e-10

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 60.77  E-value: 3.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  69 LAFRSAMRQLASAAAdelPAVVHAHDLETLP-AACRAADVCDAKVVFDAHEDWPLLERVQGAALGAWFGWQQRRWL-PRA 146
Cdd:cd03814   70 LPLPRRVRRLIKEFQ---PDIIHIATPGPLGlAALRAARRLGLPVVTSYHTDFPEYLSYYTLGPLSWLAWAYLRWFhNPF 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 147 DTVVTVSPELAKRLGGAEVlynsEPLAVIEASV----------GEDLRAKLGLGG-VVAGYIGAL-RRRIIEQLLDAA-- 212
Cdd:cd03814  147 DTTLVPSPSIARELEGHGF----ERVRLWPRGVdtelfhpsrrDAALRRRLGPPGrPLLLYVGRLaPEKNLEALLDADlp 222

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 213 -AQVPEVTLLVVG-GPPKGRAGYAGLQeqleahaakvgarAVFTGPLAYGRMGDCYRACNLLLVghyvaePLRHAAVPKK 290
Cdd:cd03814  223 lAASPPVRLVVVGdGPARAELEARGPD-------------VIFTGFLTGEELARAYASADVFVF------PSRTETFGLV 283

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 663515936 291 LLDAMAYSIPAVVGPYEARRSIVERNHCGLVADD-----WVAPLRQLAGDDELRSEMGARGHvAWREKYCWDR 358
Cdd:cd03814  284 VLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPgdaaaFAAALRALLEDPELRRRMAARAR-AEAERYSWEA 355
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 20-345 1.91e-09

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: 58.49  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  20 ALSLVGAGYEVTVFCWARRdDSLPAEELRDGVRVRRIFASLDSWLPGRMLAFRS------AMRQLASAAADELPAVVHAH 93
Cdd:cd03823   25 AEALVAEGHEVAVLTAGVG-PPGQATVARSVVRYRRAPDETLPLALKRRGYELFetynpgLRRLLARLLEDFRPDVVHTH 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  94 DLETLPaaCRAADVC---DAKVVFDAHEDWPLLERvqgaalgawfgwqQRRWLPRADTVVTVSPELAKRLGgaEVLYNSE 170
Cdd:cd03823  104 NLSGLG--ASLLDAArdlGIPVVHTLHDYWLLCPR-------------QFLFKKGGDAVLAPSRFTANLHE--ANGLFSA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 171 PLAVI----EASVGEDLRAKLGLGGVVAGYIGALRR-RIIEQLLDAAAQVP--EVTLLVVGGPPKGRAGYAGLQEQLEAH 243
Cdd:cd03823  167 RISVIpnavEPDLAPPPRRRPGTERLRFGYIGRLTEeKGIDLLVEAFKRLPreDIELVIAGHGPLSDERQIEGGRRIAFL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 244 aakvgaravftGPLAYGRMGDCYRACNLLLVGHYVAEPLrhaavPKKLLDAMAYSIPAVVGPYEARRSIVERNHCGLV-- 321
Cdd:cd03823  247 -----------GRVPTDDIKDFYEKIDVLVVPSIWPEPF-----GLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLfa 310

                        330       340
                 ....*....|....*....|....*..
gi 663515936 322 ---ADDWVAPLRQLAGDDELRSEMGAR 345
Cdd:cd03823  311 pgdAEDLAAAMRRLLTDPALLERLRAG 337
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
191-335 4.78e-09

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 54.44  E-value: 4.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  191 GVVAGYIGALRRRI--IEQLLDAAAQV----PEVTLLVVGGppkgragyaGLQEQLEAHAAKVGARAVFTGPLAygRMGD 264
Cdd:pfam13692   1 RPVILFVGRLHPNVkgVDYLLEAVPLLrkrdNDVRLVIVGD---------GPEEELEELAAGLEDRVIFTGFVE--DLAE 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 663515936  265 CYRACNLLLVghyvaePLRHAAVPKKLLDAMAYSIPAVVGPYEARRSIVERNHCGLV----ADDWVAPLRQLAGD 335
Cdd:pfam13692  70 LLAAADVFVL------PSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGENGLLVppgdPEALAEAILRLLED 138
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 20-359 1.18e-08

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: 56.06  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  20 ALSLVGAGYEVTVFCwaRRDDSLPAEELRDGVRVRRIfasldSWLPGRMLAFR--SAMRQLASAAADELPAVVHAHdleT 97
Cdd:cd03808   20 IKALVKKGYEVHVIA--PDGDKLSDELKELGVKVIDI-----PILRRGINPLKdlKALFKLYKLLKKEKPDIVHCH---T 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  98 LPA------ACRAADVCdaKVVFDAHEdwplLERVQGAALGAWFGWQQ--RRWLPRADTVVTVSP---ELAKRLGgaevL 166
Cdd:cd03808   90 PKPgilgrlAARLAGVP--KVIYTVHG----LGFVFTEGKLLRLLYLLleKLALLFTDKVIFVNEddrDLAIKKG----I 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 167 YNSEPLAVIE-ASVGEDLRAK----LGLGGVVAGYIG-ALRRRIIEQLLDAAAQV----PEVTLLVVGGPPKgRAGYAGL 236
Cdd:cd03808  160 IKKKKTVLIPgSGVDLDRFQYspesLPSEKVVFLFVArLLKDKGIDELIEAAKILkkkgPNVRFLLVGDGEL-ENPSEIL 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 237 QEQLEAhaakvGARAVFTG----PLAYgrmgdcYRACNLLLVghyvaePLRHAAVPKKLLDAMAYSIPA----VVGPyea 308
Cdd:cd03808  239 IEKLGL-----EGRIEFLGfrsdVPEL------LAESDVFVL------PSYREGLPRSLLEAMAAGRPVittdVPGC--- 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 663515936 309 rRSIVERNHCGLV-----ADDWVAPLRQLAGDDELRSEMGARGHVAWREKYCWDRM 359
Cdd:cd03808  299 -RELVIDGVNGFLvppgdVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKV 353
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 134-362 4.46e-06

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: 48.13  E-value: 4.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 134 WFGWQQRRWLPRADTVVTVSP----ELAKRLGGAE----VLYN-SEPLAVIEASVGEDLRAKLGLGGVVAgYIGALRRRI 204
Cdd:cd03809  127 YYRLLLPISLRRADAIITVSEatrdDIIKFYGVPPekivVIPLgVDPSFFPPESAAVLIAKYLLPEPYFL-YVGTLEPRK 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 205 -IEQLLDAAAQVPEVT----LLVVGGPPKGRAGYAGLQEQLEAhaakvGARAVFTGPLAYGRMGDCYRACNLLLV-GHYv 278
Cdd:cd03809  206 nHERLLKAFALLKKQGgdlkLVIVGGKGWEDEELLDLVKKLGL-----GGRVRFLGYVSDEDLPALYRGARAFVFpSLY- 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 279 aE----PlrhaavpkkLLDAMAYSIPAVVGPYEARRSIVErNHCGLV----ADDWVAPLRQLAGDDELRSEMGARGHvAW 350
Cdd:cd03809  280 -EgfglP---------VLEAMACGTPVIASNISVLPEVAG-DAALYFdpldPESIADAILRLLEDPSLREELIRKGL-ER 347

                        250
                 ....*....|..
gi 663515936 351 REKYCWDRMEER 362
Cdd:cd03809  348 AKKFSWEKTAEK 359
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 134-358 2.62e-05

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: 45.69  E-value: 2.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 134 WFGWQQRRWLPRADTVVTVS---PELAKRLGGA--EVLYNSEPLAVIEASvgEDLRAKLglggVVAgyIGalrrRIIEQ- 207
Cdd:cd03820  127 RRLLLRRLLYKRADKIVVLTeadKLKKYKQPNSnvVVIPNPLSFPSEEPS--TNLKSKR----ILA--VG----RLTYQk 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 208 ----LLDAAAQV----PEVTLLVVG-GPPKGRagyagLQEQLEAHaaKVGARAVFTGPLayGRMGDCYRACNLLLVghyv 278
Cdd:cd03820  195 gfdlLIEAWALIakkhPDWKLRIYGdGPEREE-----LEKLIDKL--GLEDRVKLLGPT--KNIAEEYANSSIFVL---- 261

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 279 aePLRHAAVPKKLLDAMAYSIPAV-----VGPYEarrsIVERNHCGLV-----ADDWVAPLRQLAGDDELRSEMGARGHV 348
Cdd:cd03820  262 --SSRYEGFPMVLLEAMAYGLPIIsfdcpTGPSE----IIEDGENGLLvpngdVDALAEALLRLMEDEELRKKMGKNARK 335

                        250
                 ....*....|
gi 663515936 349 AwREKYCWDR 358
Cdd:cd03820  336 N-AERFSIEK 344
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 32-362 4.07e-05

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: 45.14  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  32 VFCWARRDDSLPAeelrDGVRVRRIFASLDSwLPGRMLAFRSAMRQ--LASAAADELPAVVHAH----DLETLPAAcRAA 105
Cdd:cd05844   30 TFVGCRRLAPAPF----DGVALRALGGSGPL-RWLRQMAQRLLGWSapRLGGAAGLAPALVHAHfgrdGVYALPLA-RAL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 106 DVcdaKVVFDAHEDWPLLERVQGAALGAWFGWQQRRWLP---RADTVVTVSPELAKRL-------GGAEVLY-NSEPLAV 174
Cdd:cd05844  104 GV---PLVVTFHGFDITTSRAWLAASPGWPSQFQRHRRAlqrPAALFVAVSGFIRDRLlarglpaERIHVHYiGIDPAKF 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 175 IEASVGEDLRAKLGLGGVVagyigalRRRIIEQLLDA----AAQVPEVTLLVVGGPPkgragyagLQEQLEAHAAKVGaR 250
Cdd:cd05844  181 APRDPAERAPTILFVGRLV-------EKKGCDVLIEAfrrlAARHPTARLVIAGDGP--------LRPALQALAAALG-R 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 251 AVFTGPLAYGRMGDCYRACNLLLVGHYVAEPLRHAAVPKKLLDAMAYSIPAVVGPYEARRSIVERNHCGLV-----ADDW 325
Cdd:cd05844  245 VRFLGALPHAEVQDWMRRAEIFCLPSVTAASGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLvpegdVDAL 324

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 663515936 326 VAPLRQLAGDDELRSEMGARGHVAWREKYCWDRMEER 362
Cdd:cd05844  325 ADALQALLADRALADRMGGAARAFVCEQFDIRVQTAK 361
PRK10307 PRK10307
colanic acid biosynthesis glycosyltransferase WcaI;
20-230 1.01e-03

colanic acid biosynthesis glycosyltransferase WcaI;


Pssm-ID: 236670 [Multi-domain]  Cd Length: 412  Bit Score: 40.73  E-value: 1.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  20 ALSLVGAGYEVTVFC-------WaRRDDSLPAE----ELRDGVRVRRifASLdsWLPGRMLAFRSaMRQLASAAADELPA 88
Cdd:PRK10307  25 AEWLAARGHEVRVITappyypqW-RVGEGYSAWryrrESEGGVTVWR--CPL--YVPKQPSGLKR-LLHLGSFALSSFFP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936  89 VVH------------AHDLETLPAACRAADVCDAKVVF-------DAHEDWPLLERVQGAALGAWFgwqQRRWLPRADTV 149
Cdd:PRK10307  99 LLAqrrwrpdrvigvVPTLFCAPGARLLARLSGARTWLhiqdyevDAAFGLGLLKGGKVARLATAF---ERSLLRRFDNV 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 150 VTVSPELAKRLGGAEV-------LYN-SEPLAVIEASVGED--LRAKLGL--GGVVAGYIGAL-RRRIIEQLLDAAAQV- 215
Cdd:PRK10307 176 STISRSMMNKAREKGVaaekvifFPNwSEVARFQPVADADVdaLRAQLGLpdGKKIVLYSGNIgEKQGLELVIDAARRLr 255

                        250
                 ....*....|....*...
gi 663515936 216 --PEVTLLVVG-GPPKGR 230
Cdd:PRK10307 256 drPDLIFVICGqGGGKAR 273
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 139-359 3.27e-03

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: 39.18  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 139 QRRWLPRADTVVTVSPELAKR---LGGAEVLYNSEPLAV--IEASVGEDLRAKLGL---GGVVAGYIGALRR-RIIEQLL 209
Cdd:cd03795  131 MTRFLRRADRIIATSPNYVETsptLREFKNKVRVIPLGIdkNVYNIPRVDFENIKRekkGKKIFLFIGRLVYyKGLDYLI 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 210 DAAAQVPEVTLLVVGGPpkgragyagLQEQLEAHAAKVGARAVFTgplaYGRMGDCYRACnLLLVGHYVAEP--LRHAAV 287
Cdd:cd03795  211 EAAQYLNYPIVIGGEGP---------LKPDLEAQIELNLLDNVKF----LGRVDDEEKVI-YLHLCDVFVFPsvLRSEAF 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 663515936 288 PKKLLDAMAYSIPAVV------GPYearrsIVERNHCGLV-----ADDWVAPLRQLAGDDELRSEMGARGHVAWREKYCW 356
Cdd:cd03795  277 GIVLLEAMMCGKPVIStnigtgVPY-----VNNNGETGLVvppkdPDALAEAIDKLLSDEELRESYGENAKKRFEELFTA 351


                 ...
gi 663515936 357 DRM 359
Cdd:cd03795  352 EKM 354
Glyco_trans_4_2 pfam13477
Glycosyl transferase 4-like;
20-93 8.12e-03

Glycosyl transferase 4-like;


Pssm-ID: 433241 [Multi-domain]  Cd Length: 139  Bit Score: 36.53  E-value: 8.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 663515936   20 ALSLVGAGYEVTVFCwarRDDSLPAEELRDGVRVRRIfaSLDSWLPGRMLafrsAMRQLASAAADELPAVVHAH 93
Cdd:pfam13477  17 ADALADRGYDVHVIS---SKGPAKDELIAEGIHVHRL--KVPRKGPLGYL----KAFRLKKLIKKIKPDVVHVH 81
 
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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