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Conserved domains on  [gi|492946731|ref|WP_006054817|]
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flippase-like domain-containing protein [Halogeometricum borinquense]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10302422)

glycosyltransferase family 2 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
5-218 1.53e-51

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


The actual alignment was detected with superfamily member cd06442:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 224  Bit Score: 176.57  E-value: 1.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSPPRFdhelEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKEGLST 84
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDY----EIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  85 ASGDIIIPFMGDLSDSPSDVPKLVEA-IEDGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLFGIRSKDVTNAFT 163
Cdd:cd06442   77 ARGDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492946731 164 AYRREVIEEIgVETLDSDSFDITAELPLRAHILGFTSTEVPVTWQSRDAGVSKLD 218
Cdd:cd06442  157 AYRREVLEKL-IDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLG 210
LPG_synthase_TM pfam03706
Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this ...
257-550 3.20e-34

Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this family of bacterial phosphatidylglycerol lysyltransferases. The function of the family is to add lysyl groups to membrane lipids, and this region is the transmembrane domain of 7xTMs. In order to counteract attack by membrane-damaging external cationic antimicrobial molecules - from host immune systems, bacteriocins, defensins, etc - bacteria modify their anionic membrane phosphatidylglycerol with positively-charged L-lysine; this results in repulsion of the foreign cationic peptides.


:

Pssm-ID: 461018  Cd Length: 302  Bit Score: 131.72  E-value: 3.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  257 IVGAAVFGIAILVGLFSLTGFEGVFQTLSDAQPAWILAAAGMYGSTFAFRTWRFRVLLRTAGHMASRGGVLRSIFTGWFV 336
Cdd:pfam03706   1 ILLGLLLSALLLWFLLRGFDLSELAELLRSADPGWLLLALLLALLSLLLRALRWRLLLRALGARISFRRAFRAYLIGYFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  337 NFLIPARA-GDVARGLALKSTEDVPFGVTSGLVVVERILDMLMLGLLMgIVTLMFLSNSQGRFLALAAFGLAL------- 408
Cdd:pfam03706  81 NNVTPGRLgGEVVRAYLLKRREGLSLSKALASVVLERLLDLLTLLLLG-LLALLLLLGLLLSGPAVLLTLALAlallall 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  409 --VLLVGLVVLVQLDERIADRFESRFPRIREGLAgLRHAVGSLLDNPYALALALFLSLPVWLLEASTLFLSARALGVSLD 486
Cdd:pfam03706 160 llLLLLLLRRRPRALARVLLRLAALLSRFRGRLR-SLERLLLSLSSPRRLLLAFLLSLLIWLLEALALYLLLRALGLDLS 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492946731  487 LIVGLTASVAAFLTQAVPVTPGGLGTYEAAIAGVLSLFSISTTLGTSIGLIDHFMRLAFVYILG 550
Cdd:pfam03706 239 LLLVLLLLLAATLAGALPPTPGGLGVREAAFVLLLGLLGVPAELALAAALLYRLITFWLILLLG 302
 
Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
5-218 1.53e-51

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 176.57  E-value: 1.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSPPRFdhelEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKEGLST 84
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDY----EIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  85 ASGDIIIPFMGDLSDSPSDVPKLVEA-IEDGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLFGIRSKDVTNAFT 163
Cdd:cd06442   77 ARGDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492946731 164 AYRREVIEEIgVETLDSDSFDITAELPLRAHILGFTSTEVPVTWQSRDAGVSKLD 218
Cdd:cd06442  157 AYRREVLEKL-IDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLG 210
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-221 1.72e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 148.70  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   1 MFVSLVVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKE 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD-----FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  81 GLSTASGDIIIPFMGDLSDSPSDVPKLVEAI-EDGYDVAYGSRFTEGGSVDGyppvKLLYNRSFnNLIRLLFGIrsKDVT 159
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALeEGPADLVYGSRLIREGESDL----RRLGSRLF-NLVRLLTNL--PDST 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492946731 160 NAFTAYRREVIEEIGVEtldsDSFDITAELpLRAHILGFTSTEVPVTWQSRDAGVSKLDATR 221
Cdd:COG0463  150 SGFRLFRREVLEELGFD----EGFLEDTEL-LRALRHGFRIAEVPVRYRAGESKLNLRDLLR 206
LPG_synthase_TM pfam03706
Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this ...
257-550 3.20e-34

Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this family of bacterial phosphatidylglycerol lysyltransferases. The function of the family is to add lysyl groups to membrane lipids, and this region is the transmembrane domain of 7xTMs. In order to counteract attack by membrane-damaging external cationic antimicrobial molecules - from host immune systems, bacteriocins, defensins, etc - bacteria modify their anionic membrane phosphatidylglycerol with positively-charged L-lysine; this results in repulsion of the foreign cationic peptides.


Pssm-ID: 461018  Cd Length: 302  Bit Score: 131.72  E-value: 3.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  257 IVGAAVFGIAILVGLFSLTGFEGVFQTLSDAQPAWILAAAGMYGSTFAFRTWRFRVLLRTAGHMASRGGVLRSIFTGWFV 336
Cdd:pfam03706   1 ILLGLLLSALLLWFLLRGFDLSELAELLRSADPGWLLLALLLALLSLLLRALRWRLLLRALGARISFRRAFRAYLIGYFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  337 NFLIPARA-GDVARGLALKSTEDVPFGVTSGLVVVERILDMLMLGLLMgIVTLMFLSNSQGRFLALAAFGLAL------- 408
Cdd:pfam03706  81 NNVTPGRLgGEVVRAYLLKRREGLSLSKALASVVLERLLDLLTLLLLG-LLALLLLLGLLLSGPAVLLTLALAlallall 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  409 --VLLVGLVVLVQLDERIADRFESRFPRIREGLAgLRHAVGSLLDNPYALALALFLSLPVWLLEASTLFLSARALGVSLD 486
Cdd:pfam03706 160 llLLLLLLRRRPRALARVLLRLAALLSRFRGRLR-SLERLLLSLSSPRRLLLAFLLSLLIWLLEALALYLLLRALGLDLS 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492946731  487 LIVGLTASVAAFLTQAVPVTPGGLGTYEAAIAGVLSLFSISTTLGTSIGLIDHFMRLAFVYILG 550
Cdd:pfam03706 239 LLLVLLLLLAATLAGALPPTPGGLGVREAAFVLLLGLLGVPAELALAAALLYRLITFWLILLLG 302
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-172 4.98e-30

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 115.96  E-value: 4.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731    4 SLVVPAHNEVGNLERLVDSVTsELSPPRFdhelEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKEGLS 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLL-NQTYPNF----EIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   84 TASGDIIIPFMGDLSDSPSDVPKLVEAIE-DGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLF-GIRSKDVTNA 161
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEeDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLlGLNLPFLIGG 155
                         170
                  ....*....|.
gi 492946731  162 FTAYRREVIEE 172
Cdd:pfam00535 156 FALYRREALEE 166
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-236 9.81e-30

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 117.49  E-value: 9.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   1 MFVSLVVPAHNEVGNLERLVDSVTSELSPPRfdhELEILLVDDNSTDETPGLCDQLEREY--SSVTVVHRHDNPGFGNAV 78
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKALQDVK---DFEIIVVDDGSPDGTQDVVKQLQKVYgeDRILLRPRPGKLGLGTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  79 KEGLSTASGDIIIPFMGDLSDSPSDVPKLVEA-IEDGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLFGIRSKD 157
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKqRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492946731 158 VTNAFTAYRREVIEEIgVETLDSDSFDITAELPLRAHILGFTSTEVPVTWQSRDAGVSKLDATRKgPVYLKRLSDLFVT 236
Cdd:PLN02726 166 LTGSFRLYKRSALEDL-VSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEI-VQYLKGLLYLLLT 242
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
284-563 6.72e-28

Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440161  Cd Length: 289  Bit Score: 113.51  E-value: 6.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 284 LSDAQPAWILAAAGMYGSTFAFRTWRFRVLLRTAGHMASRGGVLRSIFTGWFVNFLIP-ARAGDVARGLALKStEDVPFG 362
Cdd:COG0392    1 LRAANPWWLLLALLLTLLSYLLLALRWRLLLRALGVKLPFRRLFLVSFIGYFGNNIGPgALGGEAVRARLLSR-RGVPAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 363 VTSGLVVVERILDMLMLGLLMGIV------TLMFLSNSQGRFLALAAFGLALVLLVGLVVLVQLDERIADRF--ESRFPR 434
Cdd:COG0392   80 KAAAIVALERLTDLLGLLLLAGLGllfgpgALPGLGNLPGALLLLLLGLALLAAVLLYLLLLAFRPRLLLRLrrWKLLRK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 435 IREGLAGLRHAVGSLLDNPYALALALFLSLPVWLLEASTLFLSARALGVSLDLIVGLTASVAAFLTQAVPVTPGGLGTYE 514
Cdd:COG0392  160 IREKLERFLEGLRRLRLSPRLLLLQLLLSLLDWLLAALILYFLLPALGVDVSFLAVLAVFLLASLAGLLPPTPGGLGVFE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 492946731 515 AAIAGVLSLFSISTTLGTSIGLIDHFMRLAFVYILGAISTVHIGFRSRS 563
Cdd:COG0392  240 AALLLLLSLFGVPAAAALAALLLYRLIYYLLPLLLGLLLLLLLELRRRR 288
TIGR00374 TIGR00374
conserved hypothetical protein; This model is built on a superfamily of proteins in the ...
262-558 1.35e-15

conserved hypothetical protein; This model is built on a superfamily of proteins in the Archaea and in Aquifex aeolicus. The authenticity of homology can be seen in the presence of motifs in the alignment that include residues relatively rare among these sequences, even though the alignment includes long regions of low-complexity hydrophobic sequences. One apparent fusion protein contains a Glycos_transf_2 region in the N-terminal half of the protein and a region homologous to this superfamily in the C-terminal region. [Unknown function, General]


Pssm-ID: 129470  Cd Length: 319  Bit Score: 78.19  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  262 VFGIAILVGLFSLTGFEGVFQTLSDAQPAWILAAAGMYGSTFAFRTWRFRVLLRTAGHMASRGGVLRSIFTGWFVNFLIP 341
Cdd:TIGR00374   2 VLSILFLLAIILYIGPGEILRALGNANPFYLLLAFLLQFLVLALWTLRWKLISNALGIKYSFRHLFMLLFVGMFINNITP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  342 ARAGD-VARGLALKSTEDVPFGVTSGLVVVERILDMLMLGLLMGIVTLMFLSNSQGRFLALAAFGLALVLLVGLVVLVQL 420
Cdd:TIGR00374  82 SAAGGePMRAYMLKKKEGISASLGFSTVLAERVFDLVIFILLLPLSAIMVFVLSIPKLFIYLILILITLLLFLIILYIFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  421 DERIADRFES---RFP------------RIREGLAGLRHAVGSLLDNPYALALALFLSLPVWLLEASTLFLSARALGVSL 485
Cdd:TIGR00374 162 NKKILQKIASkilKAVvkffsrknelesKLRSFLVRFLGATKFFLKDTAELVVLILLSLGMWLLEILRLYLIFLAFGVEV 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492946731  486 DLIVGLTASVAAFLTQAVPVTPGGLGTYEAAIAGVLSLFSISTTLGTSIGLIDHFMRLAFVYILGAISTVHIG 558
Cdd:TIGR00374 242 SFLEIIIIQLIALLVGLLPLTPGGLGVAEVSMIYLFSVFGVPPSVAGAVVLLDRLISYWMITFLGAIAFFIYL 314
 
Name Accession Description Interval E-value
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
5-218 1.53e-51

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 176.57  E-value: 1.53e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSPPRFdhelEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKEGLST 84
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGIDY----EIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  85 ASGDIIIPFMGDLSDSPSDVPKLVEA-IEDGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLFGIRSKDVTNAFT 163
Cdd:cd06442   77 ARGDVIVVMDADLSHPPEYIPELLEAqLEGGADLVIGSRYVEGGGVEGWGLKRKLISRGANLLARLLLGRKVSDPTSGFR 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492946731 164 AYRREVIEEIgVETLDSDSFDITAELPLRAHILGFTSTEVPVTWQSRDAGVSKLD 218
Cdd:cd06442  157 AYRREVLEKL-IDSLVSKGYKFQLELLVRARRLGYRIVEVPITFVDREHGESKLG 210
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
5-193 5.75e-50

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 170.83  E-value: 5.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSPprfDHELEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKEGLST 84
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLEE---GYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  85 ASGDIIIPFMGDLSDSPSDVPKLVEAI-EDGYDVAYGSRFTEGGSVdGYPPVKLLYNRSFNNLIRLLFGIRSKDVTNAFT 163
Cdd:cd04179   78 ARGDIVVTMDADLQHPPEDIPKLLEKLlEGGADVVIGSRFVRGGGA-GMPLLRRLGSRLFNFLIRLLLGVRISDTQSGFR 156
                        170       180       190
                 ....*....|....*....|....*....|
gi 492946731 164 AYRREVIEEIgVETLDSDSFDITAELPLRA 193
Cdd:cd04179  157 LFRREVLEAL-LSLLESNGFEFGLELLVGA 185
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-221 1.72e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 148.70  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   1 MFVSLVVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKE 80
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD-----FEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  81 GLSTASGDIIIPFMGDLSDSPSDVPKLVEAI-EDGYDVAYGSRFTEGGSVDGyppvKLLYNRSFnNLIRLLFGIrsKDVT 159
Cdd:COG0463   77 GLAAARGDYIAFLDADDQLDPEKLEELVAALeEGPADLVYGSRLIREGESDL----RRLGSRLF-NLVRLLTNL--PDST 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492946731 160 NAFTAYRREVIEEIGVEtldsDSFDITAELpLRAHILGFTSTEVPVTWQSRDAGVSKLDATR 221
Cdd:COG0463  150 SGFRLFRREVLEELGFD----EGFLEDTEL-LRALRHGFRIAEVPVRYRAGESKLNLRDLLR 206
LPG_synthase_TM pfam03706
Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this ...
257-550 3.20e-34

Lysylphosphatidylglycerol synthase TM region; LPG_synthase_TM is the N-terminal region of this family of bacterial phosphatidylglycerol lysyltransferases. The function of the family is to add lysyl groups to membrane lipids, and this region is the transmembrane domain of 7xTMs. In order to counteract attack by membrane-damaging external cationic antimicrobial molecules - from host immune systems, bacteriocins, defensins, etc - bacteria modify their anionic membrane phosphatidylglycerol with positively-charged L-lysine; this results in repulsion of the foreign cationic peptides.


Pssm-ID: 461018  Cd Length: 302  Bit Score: 131.72  E-value: 3.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  257 IVGAAVFGIAILVGLFSLTGFEGVFQTLSDAQPAWILAAAGMYGSTFAFRTWRFRVLLRTAGHMASRGGVLRSIFTGWFV 336
Cdd:pfam03706   1 ILLGLLLSALLLWFLLRGFDLSELAELLRSADPGWLLLALLLALLSLLLRALRWRLLLRALGARISFRRAFRAYLIGYFA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  337 NFLIPARA-GDVARGLALKSTEDVPFGVTSGLVVVERILDMLMLGLLMgIVTLMFLSNSQGRFLALAAFGLAL------- 408
Cdd:pfam03706  81 NNVTPGRLgGEVVRAYLLKRREGLSLSKALASVVLERLLDLLTLLLLG-LLALLLLLGLLLSGPAVLLTLALAlallall 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  409 --VLLVGLVVLVQLDERIADRFESRFPRIREGLAgLRHAVGSLLDNPYALALALFLSLPVWLLEASTLFLSARALGVSLD 486
Cdd:pfam03706 160 llLLLLLLRRRPRALARVLLRLAALLSRFRGRLR-SLERLLLSLSSPRRLLLAFLLSLLIWLLEALALYLLLRALGLDLS 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492946731  487 LIVGLTASVAAFLTQAVPVTPGGLGTYEAAIAGVLSLFSISTTLGTSIGLIDHFMRLAFVYILG 550
Cdd:pfam03706 239 LLLVLLLLLAATLAGALPPTPGGLGVREAAFVLLLGLLGVPAELALAAALLYRLITFWLILLLG 302
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
5-173 3.43e-33

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 124.90  E-value: 3.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSPPRFDHEleILLVDDNSTDETPGLCDQLEREYSSVTVVH--RhdNPGFGNAVKEGL 82
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYE--IIFVDDGSTDRTLEILRELAARDPRVKVIRlsR--NFGQQAALLAGL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  83 STASGDIIIPFMGDLSDSPSDVPKLVEAIEDGYDVAYGSRFTEGGSvdgypPVKLLYNRSFNNLIRLLFGIRSKDVTNAF 162
Cdd:cd04187   77 DHARGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKES-----WLKRLTSKLFYRLINKLSGVDIPDNGGDF 151
                        170
                 ....*....|.
gi 492946731 163 TAYRREVIEEI 173
Cdd:cd04187  152 RLMDRKVVDAL 162
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
4-172 4.98e-30

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 115.96  E-value: 4.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731    4 SLVVPAHNEVGNLERLVDSVTsELSPPRFdhelEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKEGLS 83
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLL-NQTYPNF----EIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   84 TASGDIIIPFMGDLSDSPSDVPKLVEAIE-DGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLF-GIRSKDVTNA 161
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEeDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLlGLNLPFLIGG 155
                         170
                  ....*....|.
gi 492946731  162 FTAYRREVIEE 172
Cdd:pfam00535 156 FALYRREALEE 166
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
5-216 5.59e-30

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 117.28  E-value: 5.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSP-PRFDHEleILLVDDNSTDETPGLCDQLEREYSS-VTVVHRHDNPGFGNAVKEGL 82
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEErPSFSYE--IIVVDDGSKDGTAEVARKLARKNPAlIRVLTLPKNRGKGGAVRAGM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  83 STASGDIIIpFM-GDLSDSPSDVPKLVEAIE-DGYDVAYGSR-FTEGGSVDGYPPVKLLYNRSFNNLIRLLFGIRSKDVT 159
Cdd:cd04188   79 LAARGDYIL-FAdADLATPFEELEKLEEALKtSGYDIAIGSRaHLASAAVVKRSWLRNLLGRGFNFLVRLLLGLGIKDTQ 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492946731 160 NAFTAYRREVIEEI-GVETLDSDSFDItaELPLRAHILGFTSTEVPVTWqsRDAGVSK 216
Cdd:cd04188  158 CGFKLFTRDAARRLfPRLHLERWAFDV--ELLVLARRLGYPIEEVPVRW--VEIPGSK 211
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-236 9.81e-30

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 117.49  E-value: 9.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   1 MFVSLVVPAHNEVGNLERLVDSVTSELSPPRfdhELEILLVDDNSTDETPGLCDQLEREY--SSVTVVHRHDNPGFGNAV 78
Cdd:PLN02726   9 MKYSIIVPTYNERLNIALIVYLIFKALQDVK---DFEIIVVDDGSPDGTQDVVKQLQKVYgeDRILLRPRPGKLGLGTAY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  79 KEGLSTASGDIIIPFMGDLSDSPSDVPKLVEA-IEDGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLFGIRSKD 157
Cdd:PLN02726  86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKKqRETGADIVTGTRYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPGVSD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492946731 158 VTNAFTAYRREVIEEIgVETLDSDSFDITAELPLRAHILGFTSTEVPVTWQSRDAGVSKLDATRKgPVYLKRLSDLFVT 236
Cdd:PLN02726 166 LTGSFRLYKRSALEDL-VSSVVSKGYVFQMEIIVRASRKGYRIEEVPITFVDRVYGESKLGGSEI-VQYLKGLLYLLLT 242
AglD2 COG0392
Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis] ...
284-563 6.72e-28

Predicted membrane flippase AglD2/YbhN, UPF0104 family [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440161  Cd Length: 289  Bit Score: 113.51  E-value: 6.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 284 LSDAQPAWILAAAGMYGSTFAFRTWRFRVLLRTAGHMASRGGVLRSIFTGWFVNFLIP-ARAGDVARGLALKStEDVPFG 362
Cdd:COG0392    1 LRAANPWWLLLALLLTLLSYLLLALRWRLLLRALGVKLPFRRLFLVSFIGYFGNNIGPgALGGEAVRARLLSR-RGVPAG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 363 VTSGLVVVERILDMLMLGLLMGIV------TLMFLSNSQGRFLALAAFGLALVLLVGLVVLVQLDERIADRF--ESRFPR 434
Cdd:COG0392   80 KAAAIVALERLTDLLGLLLLAGLGllfgpgALPGLGNLPGALLLLLLGLALLAAVLLYLLLLAFRPRLLLRLrrWKLLRK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 435 IREGLAGLRHAVGSLLDNPYALALALFLSLPVWLLEASTLFLSARALGVSLDLIVGLTASVAAFLTQAVPVTPGGLGTYE 514
Cdd:COG0392  160 IREKLERFLEGLRRLRLSPRLLLLQLLLSLLDWLLAALILYFLLPALGVDVSFLAVLAVFLLASLAGLLPPTPGGLGVFE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 492946731 515 AAIAGVLSLFSISTTLGTSIGLIDHFMRLAFVYILGAISTVHIGFRSRS 563
Cdd:COG0392  240 AALLLLLSLFGVPAAAALAALLLYRLIYYLLPLLLGLLLLLLLELRRRR 288
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
3-274 2.00e-18

undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 86.71  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   3 VSLVVPAHNEVGNLERLVDSVTSELSppRFDHELEILLVDDNSTDETPG-LCDQLEREYSSVTVVHRHDNPGFGNAVKEG 81
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRRTTAACE--SLGKEYEILLIDDGSSDNSAEmLVEAAQAPDSHIVAILLNRNYGQHSAIMAG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  82 LSTASGDIIIPFMGDLSDSPSDVPKLVEAIEDGYDVAYGSRFTEGGSVdgyppVKLLYNRSFNNLIRLLFGIRSKDVTNA 161
Cdd:PRK10714  86 FSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDVVGTVRQNRQDSW-----FRKTASKMINRLIQRTTGKAMGDYGCM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 162 FTAYRREVIEEIgVETLDSDSFditaeLPLRAHILGFTSTEVPVTWQSRDAGVSKLDatrkgpvyLKRLSDLfvtgnlvg 241
Cdd:PRK10714 161 LRAYRRHIVDAM-LHCHERSTF-----IPILANTFARRAIEIPVHHAEREFGDSKYS--------FMRLINL-------- 218
                        250       260       270
                 ....*....|....*....|....*....|...
gi 492946731 242 LRDLLSAITSgGPLRIVgaAVFGIAILVGLFSL 274
Cdd:PRK10714 219 MYDLVTCLTT-TPLRLL--SLLGSIIAIGGFSL 248
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
1-311 1.34e-17

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 83.64  E-value: 1.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   1 MFVSLVVPAHNEVGNLERLVDSVTSELSPPrfdHELEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKE 80
Cdd:COG1215   29 PRVSVIIPAYNEEAVIEETLRSLLAQDYPK---EKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  81 GLSTASGDIIIPFMGDLSDSPSDVPKLVEAIEDGYDVAYGsrfteggsvdgyppvkllynrsfnnlirllfgirskdvtn 160
Cdd:COG1215  106 GLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASG---------------------------------------- 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 161 AFTAYRREVIEEIGveTLDSDSF--DItaELPLRAHILGF---------TSTEVPVTWqsRDAGVSKLDATRKGPVYLKR 229
Cdd:COG1215  146 ANLAFRREALEEVG--GFDEDTLgeDL--DLSLRLLRAGYrivyvpdavVYEEAPETL--RALFRQRRRWARGGLQLLLK 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731 230 LSDLFVTGNLVGLrdllsAITSGGPLrIVGAAVFGIAILVGLFSLTGFEGVFQTLSDAQPAWILAAAgMYGSTFAFRTWR 309
Cdd:COG1215  220 HRPLLRPRRLLLF-----LLLLLLPL-LLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHL-LYGLLLLLAALR 292

                 ..
gi 492946731 310 FR 311
Cdd:COG1215  293 GK 294
TIGR00374 TIGR00374
conserved hypothetical protein; This model is built on a superfamily of proteins in the ...
262-558 1.35e-15

conserved hypothetical protein; This model is built on a superfamily of proteins in the Archaea and in Aquifex aeolicus. The authenticity of homology can be seen in the presence of motifs in the alignment that include residues relatively rare among these sequences, even though the alignment includes long regions of low-complexity hydrophobic sequences. One apparent fusion protein contains a Glycos_transf_2 region in the N-terminal half of the protein and a region homologous to this superfamily in the C-terminal region. [Unknown function, General]


Pssm-ID: 129470  Cd Length: 319  Bit Score: 78.19  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  262 VFGIAILVGLFSLTGFEGVFQTLSDAQPAWILAAAGMYGSTFAFRTWRFRVLLRTAGHMASRGGVLRSIFTGWFVNFLIP 341
Cdd:TIGR00374   2 VLSILFLLAIILYIGPGEILRALGNANPFYLLLAFLLQFLVLALWTLRWKLISNALGIKYSFRHLFMLLFVGMFINNITP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  342 ARAGD-VARGLALKSTEDVPFGVTSGLVVVERILDMLMLGLLMGIVTLMFLSNSQGRFLALAAFGLALVLLVGLVVLVQL 420
Cdd:TIGR00374  82 SAAGGePMRAYMLKKKEGISASLGFSTVLAERVFDLVIFILLLPLSAIMVFVLSIPKLFIYLILILITLLLFLIILYIFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  421 DERIADRFES---RFP------------RIREGLAGLRHAVGSLLDNPYALALALFLSLPVWLLEASTLFLSARALGVSL 485
Cdd:TIGR00374 162 NKKILQKIASkilKAVvkffsrknelesKLRSFLVRFLGATKFFLKDTAELVVLILLSLGMWLLEILRLYLIFLAFGVEV 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492946731  486 DLIVGLTASVAAFLTQAVPVTPGGLGTYEAAIAGVLSLFSISTTLGTSIGLIDHFMRLAFVYILGAISTVHIG 558
Cdd:TIGR00374 242 SFLEIIIIQLIALLVGLLPLTPGGLGVAEVSMIYLFSVFGVPPSVAGAVVLLDRLISYWMITFLGAIAFFIYL 314
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
5-174 1.59e-15

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 74.96  E-value: 1.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGF-GNAVKEGLS 83
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPK-----LEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGkAGALNAGLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  84 TASGDIIIPFMGDLSDSPSDVPKLVEAIEDGYDVaygsrftegGSVDGYPPVkllYNRSFNNLIRL---------LFGIR 154
Cdd:cd06423   76 HAKGDIVVVLDADTILEPDALKRLVVPFFADPKV---------GAVQGRVRV---RNGSENLLTRLqaieylsifRLGRR 143
                        170       180
                 ....*....|....*....|....*..
gi 492946731 155 SKDVTN-------AFTAYRREVIEEIG 174
Cdd:cd06423  144 AQSALGgvlvlsgAFGAFRREALREVG 170
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
1-218 4.90e-15

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 76.34  E-value: 4.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   1 MFVSLVVPAHNEVGNLERLVDSVTSELS-----PPRFDHEleILLVDDNSTDETPGLCDQLEREY----SSVTVVHRHDN 71
Cdd:PTZ00260  70 VDLSIVIPAYNEEDRLPKMLKETIKYLEsrsrkDPKFKYE--IIIVNDGSKDKTLKVAKDFWRQNinpnIDIRLLSLLRN 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  72 PGFGNAVKEGLSTASGDIIIPFMGDLSDSPSDVPKLVEAI----EDGYDVAYGSR--FTEGGSVDGYPPVKLLYNRSFNN 145
Cdd:PTZ00260 148 KGKGGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMlkieQNGLGIVFGSRnhLVDSDVVAKRKWYRNILMYGFHF 227
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492946731 146 LIRLLFGIRSKDVTNAFTAYRREVIEEI-GVETLDSDSFDItaELPLRAHILGFTSTEVPVTWQSRDAgvSKLD 218
Cdd:PTZ00260 228 IVNTICGTNLKDTQCGFKLFTRETARIIfPSLHLERWAFDI--EIVMIAQKLNLPIAEVPVNWTEVEG--SKLN 297
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-120 1.16e-13

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that 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. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 68.69  E-value: 1.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   6 VVPAHNEVGNLERLVDSVTsELSPPRFdhelEILLVDDNSTDETPGLCDQLEREYSSVTVVHRHDNPGFGNAVKEGLSTA 85
Cdd:cd00761    2 IIPAYNEEPYLERCLESLL-AQTYPNF----EVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAA 76
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 492946731  86 SGDIIIPFMGDLSDSPSDVPKLVEA--IEDGYDVAYG 120
Cdd:cd00761   77 RGEYILFLDADDLLLPDWLERLVAEllADPEADAVGG 113
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-91 3.93e-12

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 65.40  E-value: 3.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   1 MFVSLVVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPGLCDQLerEYSSVTVVHRHDNPGFGNAVKE 80
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPP-----FEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNL 75
                         90
                 ....*....|.
gi 492946731  81 GLSTASGDIII 91
Cdd:COG1216   76 GLRAAGGDYLL 86
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
2-174 1.99e-11

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 64.56  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   2 FVSLVVPAHNEVGNLERLVDSVtSELSPPRFDheLEILLVDDNSTDETPGLCDQLEREYSSVTVVHrhdNPG--FGNAVK 79
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESL-LNQSYPKDL--IEIIVVDGGSTDGTREIVQEYAAKDPRIRLID---NPKriQSAGLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  80 EGLSTASGDIIIPFMGDlSDSPSD-VPKLVEAIED-GYDVAYGSRFTEGGSVDGYpPVKLLYNRSFNNLIRLLFGIRSKD 157
Cdd:cd02525   75 IGIRNSRGDIIIRVDAH-AVYPKDyILELVEALKRtGADNVGGPMETIGESKFQK-AIAVAQSSPLGSGGSAYRGGAVKI 152
                        170       180
                 ....*....|....*....|
gi 492946731 158 V---TNAFTAYRREVIEEIG 174
Cdd:cd02525  153 GyvdTVHHGAYRREVFEKVG 172
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
3-91 2.08e-10

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 61.44  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   3 VSLVVPAHNEVGNLERLVDSVTSeLSPPRfdHELEILLVDDNSTDETpglcDQLEREYS--SVTVVHRHDNPGFGNAVKE 80
Cdd:cd06439   31 VTIIIPAYNEEAVIEAKLENLLA-LDYPR--DRLEIIVVSDGSTDGT----AEIAREYAdkGVKLLRFPERRGKAAALNR 103
                         90
                 ....*....|.
gi 492946731  81 GLSTASGDIII 91
Cdd:cd06439  104 ALALATGEIVV 114
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
3-198 6.19e-10

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 59.69  E-value: 6.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731    3 VSLVVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPGLCDQLEREYS--SVTVVHRHDNPGFGNAV-- 78
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPP-----VEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNARLLGPTGKSrg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   79 -KEGLSTASGDIIIPFMGDLSDSPSDVPKLVE-AIEDGYDVAYGSRFTEGGSVDGYPPVKLLYNRSFNNLIRLLFGIRSK 156
Cdd:pfam13641  79 lNHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQyFDSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRLALGVL 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 492946731  157 DVTNAFTAYRREVIEEIGVETLDSDSFDiTAELPLRAHILGF 198
Cdd:pfam13641 159 PLSGAGSAIRREVLKELGLFDPFFLLGD-DKSLGRRLRRHGW 199
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-198 5.54e-09

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 55.64  E-value: 5.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   6 VVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPglcDQLEREYSSVTVVHRHDNPGFGNAVKEGLSTA 85
Cdd:cd04186    2 IIVNYNSLEYLKACLDSLLAQTYPD-----FEVIVVDNASTDGSV---ELLRELFPEVRLIRNGENLGFGAGNNQGIREA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  86 SGDIIIPFMGDLSDSPSDVPKLVEAIEDGYDVAygsrfteggsvdgyppvkllynrsfnnlirlLFGIRskdVTNAFTAY 165
Cdd:cd04186   74 KGDYVLLLNPDTVVEPGALLELLDAAEQDPDVG-------------------------------IVGPK---VSGAFLLV 119
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 492946731 166 RREVIEEIGVetLDSDSF----DItaELPLRAHILGF 198
Cdd:cd04186  120 RREVFEEVGG--FDEDFFlyyeDV--DLCLRARLAGY 152
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
3-119 1.27e-07

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 52.68  E-value: 1.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   3 VSLVVPAHNEVGNLERLVDSVTselspprfDHELEILLVDDNSTDETPGLCdqlerEYSSVTVVHrHDNPGFGNAVKEGL 82
Cdd:cd02511    2 LSVVIITKNEERNIERCLESVK--------WAVDEIIVVDSGSTDRTVEIA-----KEYGAKVYQ-RWWDGFGAQRNFAL 67
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492946731  83 STASGDIIipFMGDlSD---SPSDVPKLVEAIEDGYDVAY 119
Cdd:cd02511   68 ELATNDWV--LSLD-ADerlTPELADEILALLATDDYDGY 104
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
3-144 1.32e-07

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 53.38  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   3 VSLVVPAHNEVGNLERLVDSVTSELSPPRFDhelEILLVDDNSTDETPGLCdqleREYSSvTVVHRHD-------NPGFG 75
Cdd:PRK13915  33 VSVVLPALNEEETVGKVVDSIRPLLMEPLVD---ELIVIDSGSTDATAERA----AAAGA-RVVSREEilpelppRPGKG 104
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  76 NAVKEGLSTASGDIIIPFMGDLSD-SPSDVPKLVEAIEDGYDVAYgsrfteggsvdgyppVKLLYNRSFN 144
Cdd:PRK13915 105 EALWRSLAATTGDIVVFVDADLINfDPMFVPGLLGPLLTDPGVHL---------------VKAFYRRPLR 159
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-91 6.46e-07

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 50.75  E-value: 6.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVtSELSPPrfDHELEILLVDDNSTDETpglCDQLEREYSSVTV------VHRHDNPGFGNAV 78
Cdd:cd04192    1 VVIAARNEAENLPRLLQSL-SALDYP--KEKFEVILVDDHSTDGT---VQILEFAAAKPNFqlkilnNSRVSISGKKNAL 74
                         90
                 ....*....|...
gi 492946731  79 KEGLSTASGDIII 91
Cdd:cd04192   75 TTAIKAAKGDWIV 87
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
3-152 1.17e-06

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 49.88  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   3 VSLVVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPGLCDQLEreyssvtVVHRHDNPGFGNAVKEGL 82
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLP-----LEIIVVDGGSTDGTVAIARSAG-------VVVISSPKGRARQMNAGA 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492946731  83 STASGDIIIpFmgdL-SDS--PSDVPKLV--EAIEDGYDVAYGS-RFTEGGsvdgyPPVKLLYNRSF--NNLIRLLFG 152
Cdd:cd02522   69 AAARGDWLL-F---LhADTrlPPDWDAAIieTLRADGAVAGAFRlRFDDPG-----PRLRLLELGANlrSRLFGLPYG 137
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
2-101 2.57e-06

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 48.85  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   2 FVSLVVPAHNEVGNLERLVDSVtSELSPPRfdHELEILLVDDnSTDETPGLCDQLEREYSS----VTVVHRHDNPGF-GN 76
Cdd:cd06437    2 MVTVQLPVFNEKYVVERLIEAA-CALDYPK--DRLEIQVLDD-STDETVRLAREIVEEYAAqgvnIKHVRRADRTGYkAG 77
                         90       100
                 ....*....|....*....|....*
gi 492946731  77 AVKEGLSTASGDIIIPFMGDLSDSP 101
Cdd:cd06437   78 ALAEGMKVAKGEYVAIFDADFVPPP 102
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-118 4.22e-06

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 48.89  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   3 VSLVVPAHNEVGNLERLVDSvtseLSPPRFDhELEILLVDDNSTDETPGLCDQLEREYSSVTVVHRhDNPGFGNAVKEGL 82
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMES----LIAQTWT-ALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQ-ANAGVSVARNTGL 81
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 492946731  83 STASGD-IIIPFMGDLSDsPSDVPKLVE-AIEDGYDVA 118
Cdd:PRK10073  82 AVATGKyVAFPDADDVVY-PTMYETLMTmALEDDLDVA 118
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
4-94 1.46e-05

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 47.20  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   4 SLVVPAHNEvgNLERLVDSVTS--ELSPPRFDHEleILLVDDNSTDETpgLCDQLEREYSS----VTVVHRHDNPGFGNA 77
Cdd:cd02510    1 SVIIIFHNE--ALSTLLRTVHSviNRTPPELLKE--IILVDDFSDKPE--LKLLLEEYYKKylpkVKVLRLKKREGLIRA 74
                         90
                 ....*....|....*..
gi 492946731  78 VKEGLSTASGDIIIpFM 94
Cdd:cd02510   75 RIAGARAATGDVLV-FL 90
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
6-75 4.88e-05

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 44.51  E-value: 4.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   6 VVPAHNEVGNLERLVDSVTSELSPprfDHELEILLVDDNSTDETPglcdQLEREySSVTVVHRHDNPGFG 75
Cdd:cd06438    2 LIPAHNEEAVIGNTVRSLKAQDYP---RELYRIFVVADNCTDDTA----QVARA-AGATVLERHDPERRG 63
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
3-174 1.38e-04

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 43.35  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   3 VSLVVPAHN-EVGNLERLVDSVTSELSPprfdhELEILLVDDNSTDETPGLcdqLEREYSS----VTVVHRHDNPGFGNA 77
Cdd:cd04184    3 ISIVMPVYNtPEKYLREAIESVRAQTYP-----NWELCIADDASTDPEVKR---VLKKYAAqdprIKVVFREENGGISAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731  78 VKEGLSTASGDIIIpFMgDLSD--SPSDVPKLVEAI--EDGYDVAYGS--RFTEGGSVdgyppvkllYNRSFN---NLIR 148
Cdd:cd04184   75 TNSALELATGEFVA-LL-DHDDelAPHALYEVVKALneHPDADLIYSDedKIDEGGKR---------SEPFFKpdwSPDL 143
                        170       180
                 ....*....|....*....|....*.
gi 492946731 149 LLfgirSKDVTNAFTAYRREVIEEIG 174
Cdd:cd04184  144 LL----SQNYIGHLLVYRRSLVRQVG 165
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
37-99 5.81e-04

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 41.46  E-value: 5.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492946731  37 EILLVDDNSTDETPGLCDQLEREYSSVTVVHRHD-NPGFGNAVKEGLSTASGDIIIpfmgdLSD 99
Cdd:cd04196   29 ELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGkNLGVARNFESLLQAADGDYVF-----FCD 87
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
5-123 3.27e-03

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 38.71  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492946731   5 LVVPAHNEVGNLERLVDSVTSELSPPrfdheLEILLVDDNSTDETPGLCDQLeREYSSVTVVH-RHDNPGF--GNAVKEG 81
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILP-----FEVIIADDGSTEETKELIEEF-KSQFPIPIKHvWQEDEGFrkAKIRNKA 74
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 492946731  82 LSTASGDIIIPFMGDLSDSPSDVPKLVEAIEDGYDVaYGSRF 123
Cdd:cd06420   75 IAAAKGDYLIFIDGDCIPHPDFIADHIELAEPGVFL-SGSRV 115
 
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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