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Conserved domains on  [gi|1084056276|gb|OGK61277|]
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hypothetical protein A3G65_04070 [Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_12_FULL_37_7b]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 5-221 1.65e-49

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 cd04188:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 211  Bit Score: 161.58  E-value: 1.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIQKGVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIKKrYLSEFP-KFRLVE-KNHQGKAFAVIEGIK 82
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARK-LARKNPaLIRVLTlPKNRGKGGAVRAGML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  83 DAHGDFVIFSDMDLATPLEEAYIFIDEFK-KGSKIVIGSR--KGKREGA--PFKRKLQSVGF-VIMRNMLVGlnGIQDTQ 156
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKtSGYDIAIGSRahLASAAVVkrSWLRNLLGRGFnFLVRLLLGL--GIKDTQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084056276 157 CGFKGFDRKAAIRIIEKLrvfHDERKArgssvsagFDLEFLFVARKLGYEIKEIPVHWRHAETKK 221
Cdd:cd04188   158 CGFKLFTRDAARRLFPRL---HLERWA--------FDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-221 1.65e-49

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: 161.58  E-value: 1.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIQKGVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIKKrYLSEFP-KFRLVE-KNHQGKAFAVIEGIK 82
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARK-LARKNPaLIRVLTlPKNRGKGGAVRAGML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  83 DAHGDFVIFSDMDLATPLEEAYIFIDEFK-KGSKIVIGSR--KGKREGA--PFKRKLQSVGF-VIMRNMLVGlnGIQDTQ 156
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKtSGYDIAIGSRahLASAAVVkrSWLRNLLGRGFnFLVRLLLGL--GIKDTQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084056276 157 CGFKGFDRKAAIRIIEKLrvfHDERKArgssvsagFDLEFLFVARKLGYEIKEIPVHWRHAETKK 221
Cdd:cd04188   158 CGFKLFTRDAARRLFPRL---HLERWA--------FDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-220 3.00e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 129.82  E-value: 3.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   1 MTISLIIPCYNEELNIQKgVLDKIGNFTAHDAqfkEVIIIDDGSTDSTVEIIKkRYLSEFPKFRLVE-KNHQGKAFAVIE 79
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEE-ALESLLAQTYPDF---EIIVVDDGSTDGTAEILR-ELAAKDPRIRVIRlERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  80 GIKDAHGDFVIFSDMDLATPLEEAYIFIDEFKKGSKIVIGSRKGKREGAPFKRKLQSVGFVIMRNMLvglnGIQDTQCGF 159
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLT----NLPDSTSGF 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084056276 160 KGFDRkaaiRIIEKLRVFHDerkargssvsAGFDLEFLFVARKlGYEIKEIPVHWRHAETK 220
Cdd:COG0463   153 RLFRR----EVLEELGFDEG----------FLEDTELLRALRH-GFRIAEVPVRYRAGESK 198
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 3-240 2.17e-35

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 128.35  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   3 ISLIIPCYNEELNIQKGVLDKIGNF---TAHDAQFK-EVIIIDDGSTDSTVEIIK---KRYLSEFPKFRLVE-KNHQGKA 74
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPKMLKETIKYLesrSRKDPKFKyEIIIVNDGSKDKTLKVAKdfwRQNINPNIDIRLLSlLRNKGKG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  75 FAVIEGIKDAHGDFVIFSDMDLATPLEE----AYIFIDEFKKGSKIVIGSRKGKREGA-----PFKRKLQSVGFVIMRNM 145
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGATDIDDfdklEDIMLKIEQNGLGIVFGSRNHLVDSDvvakrKWYRNILMYGFHFIVNT 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276 146 LVGLNgIQDTQCGFKGFDRKAAIRIiekLRVFHDERKArgssvsagFDLEFLFVARKLGYEIKEIPVHWRHAETKKVTFI 225
Cdd:PTZ00260  232 ICGTN-LKDTQCGFKLFTRETARII---FPSLHLERWA--------FDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVI 299

                         250
                  ....*....|....*
gi 1084056276 226 KDSVETITDLLRIKF 240
Cdd:PTZ00260  300 SASIQMARDILLVRS 314
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-169 4.48e-21

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: 86.68  E-value: 4.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   4 SLIIPCYNEELNIQKgVLDKIGNFTAhdaQFKEVIIIDDGSTDSTVEIIKKrYLSEFPKFRLVEKNH-QGKAFAVIEGIK 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLE-TLESLLNQTY---PNFEIIVVDDGSTDGTVEIAEE-YAKKDPRVRVIRLPEnRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  83 DAHGDFVIFSDMDLATPLEEAYIFIDEFKKGSK-IVIGSRKGKREGAPFKRKLQSVGFVIM---RNMLVGLNGIQDTQCG 158
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRITLSRLpffLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 1084056276 159 FKGFDRKAAIR 169
Cdd:pfam00535 156 FALYRREALEE 166
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-132 8.40e-09

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 54.80  E-value: 8.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   7 IPCYNEELNIQKgVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIkKRYLSEFPK---FRLVEKNHQGKAFAVIEGIKD 83
Cdd:NF038302    7 IPTYNGANRLPE-VLERLRSQIGTESLSWEIIVVDNNSTDNTAQVV-QEYQKNWPSpypLRYCFEPQQGAAFARQRAIQE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084056276  84 AHGDFVIFSDMD-LATP--LEEAYIFIDEFKK----GSKIvigsrKGKREGAP---FKR 132
Cdd:NF038302   85 AKGELIGFLDDDnLPAPnwVAAAYAFGQEHPQagayGSQI-----HGDFEVEPpenFER 138
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-91 9.12e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 50.97  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   3 ISLIIPCYNEELNIqkgvldkiGNFTAHDAQFK---EVIIIDDGSTDSTVEIIK----KRYLSEfpkfrlveknhQGKAF 75
Cdd:TIGR04283   1 LSIIIPVLNEAATL--------PELLADLQALRgdaEVIVVDGGSTDGTVEIARslgaKVIHSP-----------KGRAR 61

                          90
                  ....*....|....*.
gi 1084056276  76 AVIEGIKDAHGDFVIF 91
Cdd:TIGR04283  62 QMNAGAALAKGDILLF 77
 
Name Accession Description Interval E-value
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 5-221 1.65e-49

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: 161.58  E-value: 1.65e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIQKGVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIKKrYLSEFP-KFRLVE-KNHQGKAFAVIEGIK 82
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARK-LARKNPaLIRVLTlPKNRGKGGAVRAGML 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  83 DAHGDFVIFSDMDLATPLEEAYIFIDEFK-KGSKIVIGSR--KGKREGA--PFKRKLQSVGF-VIMRNMLVGlnGIQDTQ 156
Cdd:cd04188    80 AARGDYILFADADLATPFEELEKLEEALKtSGYDIAIGSRahLASAAVVkrSWLRNLLGRGFnFLVRLLLGL--GIKDTQ 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1084056276 157 CGFKGFDRKAAIRIIEKLrvfHDERKArgssvsagFDLEFLFVARKLGYEIKEIPVHWRHAETKK 221
Cdd:cd04188   158 CGFKLFTRDAARRLFPRL---HLERWA--------FDVELLVLARRLGYPIEEVPVRWVEIPGSK 211
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 5-176 1.02e-37

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: 130.39  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIQKgVLDKIGNFTAHDAQFkEVIIIDDGSTDSTVEIIKKrYLSEFPKFRLV--EKNhQGKAFAVIEGIK 82
Cdd:cd04179     1 VVIPAYNEEENIPE-LVERLLAVLEEGYDY-EIIVVDDGSTDGTAEIARE-LAARVPRVRVIrlSRN-FGKGAAVRAGFK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  83 DAHGDFVIFSDMDLATPLEEAYIFIDEF-KKGSKIVIGSR--KGKREGAPFKRKLQSVGFVIMRNMLVGLNgIQDTQCGF 159
Cdd:cd04179    77 AARGDIVVTMDADLQHPPEDIPKLLEKLlEGGADVVIGSRfvRGGGAGMPLLRRLGSRLFNFLIRLLLGVR-ISDTQSGF 155

                         170
                  ....*....|....*..
gi 1084056276 160 KGFDRKAAIRIIEKLRV 176
Cdd:cd04179   156 RLFRREVLEALLSLLES 172
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-220 3.00e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 129.82  E-value: 3.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   1 MTISLIIPCYNEELNIQKgVLDKIGNFTAHDAqfkEVIIIDDGSTDSTVEIIKkRYLSEFPKFRLVE-KNHQGKAFAVIE 79
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEE-ALESLLAQTYPDF---EIIVVDDGSTDGTAEILR-ELAAKDPRIRVIRlERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  80 GIKDAHGDFVIFSDMDLATPLEEAYIFIDEFKKGSKIVIGSRKGKREGAPFKRKLQSVGFVIMRNMLvglnGIQDTQCGF 159
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLGSRLFNLVRLLT----NLPDSTSGF 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1084056276 160 KGFDRkaaiRIIEKLRVFHDerkargssvsAGFDLEFLFVARKlGYEIKEIPVHWRHAETK 220
Cdd:COG0463   153 RLFRR----EVLEELGFDEG----------FLEDTELLRALRH-GFRIAEVPVRYRAGESK 198
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 3-240 2.17e-35

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 128.35  E-value: 2.17e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   3 ISLIIPCYNEELNIQKGVLDKIGNF---TAHDAQFK-EVIIIDDGSTDSTVEIIK---KRYLSEFPKFRLVE-KNHQGKA 74
Cdd:PTZ00260   72 LSIVIPAYNEEDRLPKMLKETIKYLesrSRKDPKFKyEIIIVNDGSKDKTLKVAKdfwRQNINPNIDIRLLSlLRNKGKG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  75 FAVIEGIKDAHGDFVIFSDMDLATPLEE----AYIFIDEFKKGSKIVIGSRKGKREGA-----PFKRKLQSVGFVIMRNM 145
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGATDIDDfdklEDIMLKIEQNGLGIVFGSRNHLVDSDvvakrKWYRNILMYGFHFIVNT 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276 146 LVGLNgIQDTQCGFKGFDRKAAIRIiekLRVFHDERKArgssvsagFDLEFLFVARKLGYEIKEIPVHWRHAETKKVTFI 225
Cdd:PTZ00260  232 ICGTN-LKDTQCGFKLFTRETARII---FPSLHLERWA--------FDIEIVMIAQKLNLPIAEVPVNWTEVEGSKLNVI 299

                         250
                  ....*....|....*
gi 1084056276 226 KDSVETITDLLRIKF 240
Cdd:PTZ00260  300 SASIQMARDILLVRS 314
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 5-212 5.39e-27

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: 103.77  E-value: 5.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIqKGVLDKIGN-FTAHDAqfkEVIIIDDGSTDSTVEIIKKrYLSEFPKFRL-VEKNHQGKAFAVIEGIK 82
Cdd:cd06442     1 IIIPTYNERENI-PELIERLDAaLKGIDY---EIIVVDDNSPDGTAEIVRE-LAKEYPRVRLiVRPGKRGLGSAYIEGFK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  83 DAHGDFVIFSDMDLATPleEAYI--FIDEFKKGSK-IVIGSR---KGKREGAPFKRKLQSVGFVIMrNMLVGLNGIQDTQ 156
Cdd:cd06442    76 AARGDVIVVMDADLSHP--PEYIpeLLEAQLEGGAdLVIGSRyveGGGVEGWGLKRKLISRGANLL-ARLLLGRKVSDPT 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1084056276 157 CGFKGFDRKAAIRIIEKLRVfhderkaRGSSvsagFDLEFLFVARKLGYEIKEIPV 212
Cdd:cd06442   153 SGFRAYRREVLEKLIDSLVS-------KGYK----FQLELLVRARRLGYRIVEVPI 197
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 5-172 4.67e-24

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: 94.85  E-value: 4.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIQ------KGVLDKIGNftahdaQFkEVIIIDDGSTDSTVEIIKkRYLSEFPKFRLVE--KNhQGKAFA 76
Cdd:cd04187     1 IVVPVYNEEENLPelyerlKAVLESLGY------DY-EIIFVDDGSTDRTLEILR-ELAARDPRVKVIRlsRN-FGQQAA 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  77 VIEGIKDAHGDFVIFSDMDLATPLEEAYIFIDEFKKGSKIVIGSRKGKREgaPFKRKLQSVGFVIMRNMLVGLNgIQDTQ 156
Cdd:cd04187    72 LLAGLDHARGDAVITMDADLQDPPELIPEMLAKWEEGYDVVYGVRKNRKE--SWLKRLTSKLFYRLINKLSGVD-IPDNG 148

                         170
                  ....*....|....*.
gi 1084056276 157 CGFKGFDRKAAIRIIE 172
Cdd:cd04187   149 GDFRLMDRKVVDALLL 164
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 4-169 4.48e-21

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: 86.68  E-value: 4.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   4 SLIIPCYNEELNIQKgVLDKIGNFTAhdaQFKEVIIIDDGSTDSTVEIIKKrYLSEFPKFRLVEKNH-QGKAFAVIEGIK 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLE-TLESLLNQTY---PNFEIIVVDDGSTDGTVEIAEE-YAKKDPRVRVIRLPEnRGKAGARNAGLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  83 DAHGDFVIFSDMDLATPLEEAYIFIDEFKKGSK-IVIGSRKGKREGAPFKRKLQSVGFVIM---RNMLVGLNGIQDTQCG 158
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGAdVVVGSRYVIFGETGEYRRASRITLSRLpffLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 1084056276 159 FKGFDRKAAIR 169
Cdd:pfam00535 156 FALYRREALEE 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 1-93 1.12e-18

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: 82.87  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   1 MTISLIIPCYNEELNIQkgvlDKIGNFTAHD--AQFKEVIIIDDGSTDSTVEIIkKRYLSEFPKFRLVEK-NHQGKAFAV 77
Cdd:COG1215    29 PRVSVIIPAYNEEAVIE----ETLRSLLAQDypKEKLEVIVVDDGSTDETAEIA-RELAAEYPRVRVIERpENGGKAAAL 103

                          90
                  ....*....|....*.
gi 1084056276  78 IEGIKDAHGDFVIFSD 93
Cdd:COG1215   104 NAGLKAARGDIVVFLD 119
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-123 2.92e-17

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: 76.39  E-value: 2.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   6 IIPCYNEELNIQKgVLDKIgnfTAHDAQFKEVIIIDDGSTDSTVEIIKKRYLSEFPKFRLVEKNHQGKAFAVIEGIKDAH 85
Cdd:cd00761     2 IIPAYNEEPYLER-CLESL---LAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAAR 77

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1084056276  86 GDFVIFSDMDLATPLEEAYIFIDEFKKGSKIVIGSRKG 123
Cdd:cd00761    78 GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPG 115
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-212 7.04e-17

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 77.05  E-value: 7.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   1 MTISLIIPCYNEELNIqkGVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIKK-RYLSEFPKFRLVEKNHQ-GKAFAVI 78
Cdd:PLN02726    9 MKYSIIVPTYNERLNI--ALIVYLIFKALQDVKDFEIIVVDDGSPDGTQDVVKQlQKVYGEDRILLRPRPGKlGLGTAYI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  79 EGIKDAHGDFVIFSDMDLATplEEAYI--FIDEFK-KGSKIVIGSR---KGKREGAPFKRKLQSVGFVIMRNMLVGlNGI 152
Cdd:PLN02726   87 HGLKHASGDFVVIMDADLSH--HPKYLpsFIKKQReTGADIVTGTRyvkGGGVHGWDLRRKLTSRGANVLAQTLLW-PGV 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084056276 153 QDTQCGFKGFDRKAAIRIIEklrvfhderkargSSVSAG--FDLEFLFVARKLGYEIKEIPV 212
Cdd:PLN02726  164 SDLTGSFRLYKRSALEDLVS-------------SVVSKGyvFQMEIIVRASRKGYRIEEVPI 212
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 2-93 1.00e-16

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: 76.89  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   2 TISLIIPCYNEELNIQKgVLDKIGNFTAHDAQFkEVIIIDDGSTDSTVEIIkKRYLSEFPKFRLVEKNHQGKAFAVIEGI 81
Cdd:cd02525     1 FVSIIIPVRNEEKYIEE-LLESLLNQSYPKDLI-EIIVVDGGSTDGTREIV-QEYAAKDPRIRLIDNPKRIQSAGLNIGI 77

                          90
                  ....*....|..
gi 1084056276  82 KDAHGDFVIFSD 93
Cdd:cd02525    78 RNSRGDIIIRVD 89
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-95 1.29e-16

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: 76.47  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   2 TISLIIPCYNEELNIQKgvldKIGNFTAHD--AQFKEVIIIDDGSTDSTVEIIkKRYLSEFPKfRLVEKNHQGKAFAVIE 79
Cdd:cd06439    30 TVTIIIPAYNEEAVIEA----KLENLLALDypRDRLEIIVVSDGSTDGTAEIA-REYADKGVK-LLRFPERRGKAAALNR 103

                          90
                  ....*....|....*.
gi 1084056276  80 GIKDAHGDFVIFSDMD 95
Cdd:cd06439   104 ALALATGEIVVFTDAN 119
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-139 1.13e-14

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: 70.78  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIqKGVLDKIGNFTAHDAQFkEVIIIDDGSTDSTVEIIKKRYLSEFPKFRLVEkNHQ----GKAFAVIEG 80
Cdd:cd04192     1 VVIAARNEAENL-PRLLQSLSALDYPKEKF-EVILVDDHSTDGTVQILEFAAAKPNFQLKILN-NSRvsisGKKNALTTA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084056276  81 IKDAHGDFVIFSDMDLATP---LEEAYIFIdeFKKGSKIVIGSRKGKREGApFKRKLQSVGF 139
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPsnwLLTFVAFI--QKEQIGLVAGPVIYFKGKS-LLAKFQRLDW 136
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 5-95 2.77e-14

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: 68.79  E-value: 2.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIqKGVLDKIGNFTAHDaqfKEVIIIDDGSTDSTVEIIKKRY-LSEFPKFRLVEKNHQGKAFAVIEGIKD 83
Cdd:cd06423     1 IIVPAYNEEAVI-ERTIESLLALDYPK---LEVIVVDDGSTDDTLEILEELAaLYIRRVLVVRDKENGGKAGALNAGLRH 76

                          90
                  ....*....|..
gi 1084056276  84 AHGDFVIFSDMD 95
Cdd:cd06423    77 AKGDIVVVLDAD 88
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-95 7.20e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.91  E-value: 7.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   3 ISLIIPCYNEELNIQKGvldkIGNFTAHDAQFKEVIIIDDGSTDSTVEIIKkRYLSEFPKFRLVEKNHQGKAFAVIEGIK 82
Cdd:PRK10073    8 LSIIIPLYNAGKDFRAF----MESLIAQTWTALEIIIVNDGSTDNSVEIAK-HYAENYPHVRLLHQANAGVSVARNTGLA 82

                          90
                  ....*....|...
gi 1084056276  83 DAHGDFVIFSDMD 95
Cdd:PRK10073   83 VATGKYVAFPDAD 95
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-95 4.38e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 60.39  E-value: 4.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   1 MTISLIIPCYNEELNIQKgVLDKIGNFTAHDAqfkEVIIIDDGSTDSTVEIIKKRylsEFPKFRLVEKNH-QGKAFAVIE 79
Cdd:COG1216     3 PKVSVVIPTYNRPELLRR-CLESLLAQTYPPF---EVIVVDNGSTDGTAELLAAL---AFPRVRVIRNPEnLGFAAARNL 75

                          90
                  ....*....|....*.
gi 1084056276  80 GIKDAHGDFVIFSDMD 95
Cdd:COG1216    76 GLRAAGGDYLLFLDDD 91
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 36-95 2.02e-10

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: 58.80  E-value: 2.02e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084056276  36 EVIIIDDGSTDSTVEIIkKRYLSEFPKFRLVEKNHQGKAFAV--IEGIKDAHGDFVIFSDMD 95
Cdd:cd04196    29 ELIISDDGSTDGTVEII-KEYIDKDPFIIILIRNGKNLGVARnfESLLQAADGDYVFFCDQD 89
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 2-54 2.99e-09

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: 55.37  E-value: 2.99e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1084056276   2 TISLIIPCYNEELNIqKGVLDKIGNFTahdaqfKEVIIIDDGSTDSTVEIIKK 54
Cdd:cd02511     1 TLSVVIITKNEERNI-ERCLESVKWAV------DEIIVVDSGSTDRTVEIAKE 46
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
7-132 8.40e-09

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 54.80  E-value: 8.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   7 IPCYNEELNIQKgVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIkKRYLSEFPK---FRLVEKNHQGKAFAVIEGIKD 83
Cdd:NF038302    7 IPTYNGANRLPE-VLERLRSQIGTESLSWEIIVVDNNSTDNTAQVV-QEYQKNWPSpypLRYCFEPQQGAAFARQRAIQE 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1084056276  84 AHGDFVIFSDMD-LATP--LEEAYIFIDEFKK----GSKIvigsrKGKREGAP---FKR 132
Cdd:NF038302   85 AKGELIGFLDDDnLPAPnwVAAAYAFGQEHPQagayGSQI-----HGDFEVEPpenFER 138
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 3-91 9.12e-08

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 50.97  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   3 ISLIIPCYNEELNIqkgvldkiGNFTAHDAQFK---EVIIIDDGSTDSTVEIIK----KRYLSEfpkfrlveknhQGKAF 75
Cdd:TIGR04283   1 LSIIIPVLNEAATL--------PELLADLQALRgdaEVIVVDGGSTDGTVEIARslgaKVIHSP-----------KGRAR 61

                          90
                  ....*....|....*.
gi 1084056276  76 AVIEGIKDAHGDFVIF 91
Cdd:TIGR04283  62 QMNAGAALAKGDILLF 77
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 3-147 1.26e-07

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 51.66  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   3 ISLIIPCYNEELNIQKgVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIKKRylSEFPKFR----LVEKNHqGKAFAVI 78
Cdd:PRK10714    8 VSVVIPVYNEQESLPE-LIRRTTAACESLGKEYEILLIDDGSSDNSAEMLVEA--AQAPDSHivaiLLNRNY-GQHSAIM 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084056276  79 EGIKDAHGDFVIFSDMDLATPLEEAYIFIDEFKKGSKiVIGSRKGKREGAPFkRKLQSVgfviMRNMLV 147
Cdd:PRK10714   84 AGFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYD-VVGTVRQNRQDSWF-RKTASK----MINRLI 146
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 3-54 1.54e-07

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: 50.65  E-value: 1.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1084056276   3 ISLIIPCYNEELNIQKGvldkIGNFTAHDAQFKEVIIIDDGSTDSTVEIIKK 54
Cdd:cd02522     1 LSIIIPTLNEAENLPRL----LASLRRLNPLPLEIIVVDGGSTDGTVAIARS 48
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 4-91 3.10e-06

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 46.38  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   4 SLIIPCYNEELNIQKG---VLD-KIGNFtahdaqfkEVIIIDDGSTDSTVEIIKKrylSEFPKFRLVEKNHQGKAFAVIE 79
Cdd:cd06433     1 SIITPTYNQAETLEETidsVLSqTYPNI--------EYIVIDGGSTDGTVDIIKK---YEDKITYWISEPDKGIYDAMNK 69

                          90
                  ....*....|..
gi 1084056276  80 GIKDAHGDFVIF 91
Cdd:cd06433    70 GIALATGDIIGF 81
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 5-179 3.77e-06

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 46.22  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYNEELNIQKGVldkiGNFTAHDAQFKeVIIIDDGSTDSTVEIIkkRYLSEFPKFRLV----EKNHQGK------A 74
Cdd:cd06436     1 VLVPCLNEEAVIQRTL----ASLLRNKPNFL-VLVIDDASDDDTAGIV--RLAITDSRVHLLrrhlPNARTGKgdalnaA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  75 FAVIEGIKDAHG-DF--VIFSDMDLATPLEEAYI------FIDEFKKGSKIVIgsrKGKREGAPFKRKLQSVGFVIMRNM 145
Cdd:cd06436    74 YDQIRQILIEEGaDPerVIIAVIDADGRLDPNALeavapyFSDPRVAGTQSRV---RMYNRHKNLLTILQDLEFFIIIAA 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1084056276 146 L---------VGLngiqdtqCGFKGFDRKAAIRIIEKLRVFHD 179
Cdd:cd06436   151 TqslraltgtVGL-------GGNGQFMRLSALDGLIGEEPWSD 186
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 5-95 1.05e-05

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: 44.88  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   5 LIIPCYN--EELNIqkgVLDKIGNFTAHDAqfkEVIIIDDGSTDSTVEIIKKrYLSEFPkFRLVEKNHQGKAF--AVI-- 78
Cdd:cd06420     1 LIITTYNrpEALEL---VLKSVLNQSILPF---EVIIADDGSTEETKELIEE-FKSQFP-IPIKHVWQEDEGFrkAKIrn 72

                          90
                  ....*....|....*..
gi 1084056276  79 EGIKDAHGDFVIFSDMD 95
Cdd:cd06420    73 KAIAAAKGDYLIFIDGD 89
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 2-95 1.15e-05

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 45.32  E-value: 1.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   2 TISLIIPCYNEELNIQKGVLDKIgnftaHDAQFKEVIIIDDGSTDSTVEIIKKRYLseFPKFRLVEKNHQGKAFAVIEGI 81
Cdd:cd06434     1 DVTVIIPVYDEDPDVFRECLRSI-----LRQKPLEIIVVTDGDDEPYLSILSQTVK--YGGIFVITVPHPGKRRALAEGI 73

                          90
                  ....*....|....
gi 1084056276  82 KDAHGDFVIFSDMD 95
Cdd:cd06434    74 RHVTTDIVVLLDSD 87
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-95 1.32e-05

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: 44.50  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   3 ISLIIPCYNEELNIQKGVLDKIGNFTAHDAqfkEVIIIDDGSTDSTVEIIKKRYLSEFPKFRLV--EKNhQGKAFAVIEG 80
Cdd:cd04184     3 ISIVMPVYNTPEKYLREAIESVRAQTYPNW---ELCIADDASTDPEVKRVLKKYAAQDPRIKVVfrEEN-GGISAATNSA 78

                          90
                  ....*....|....*
gi 1084056276  81 IKDAHGDFVIFSDMD 95
Cdd:cd04184    79 LELATGEFVALLDHD 93
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-179 3.23e-04

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 41.11  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   4 SLIIPCYNEELNiqKGVLDKIGNFTAHDAQFKEVIIIDDGSTDSTVEIIK-------KRYLSEFPkfrlveKNHQGKAFA 76
Cdd:pfam10111   1 SVVIPVYNGEKT--HWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSsikdhnlQVYYPNAP------DTTYSLAAS 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276  77 VIEGIKDAHGDFVIFSDMDlatpleeAYIFIDEFKKGSKIVIgsrkgkregapfKRKLQSVGFVIMRNMLVGLNGiQDTQ 156
Cdd:pfam10111  73 RNRGTSHAIGEYISFIDGD-------CLWSPDKFEKQLKIAT------------SLALQENIQAAVVLPVTDLND-ESSN 132

                         170       180
                  ....*....|....*....|...
gi 1084056276 157 CGFKGFDRKAAIRIIEKLRVFHD 179
Cdd:pfam10111 133 FLRRGGDLTASGDVLRDLLVFYS 155
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 1-99 3.89e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.06  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084056276   1 MTISLIIPCYNEELNIQKgVLDKIGNFTAHDAqFKEVIIIDDGSTDSTVEIIK---------KRYLSEFPKFRlveknhq 71
Cdd:PRK13915   31 RTVSVVLPALNEEETVGK-VVDSIRPLLMEPL-VDELIVIDSGSTDATAERAAaagarvvsrEEILPELPPRP------- 101

                          90       100
                  ....*....|....*....|....*...
gi 1084056276  72 GKAFAVIEGIKDAHGDFVIFSDMDLATP 99
Cdd:PRK13915  102 GKGEALWRSLAATTGDIVVFVDADLINF 129
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 36-95 3.75e-03

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: 37.15  E-value: 3.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1084056276  36 EVIIIDDGSTDSTVEIIKKrylsEFPKFRLVEkNHQGKAFAVI--EGIKDAHGDFVIFSDMD 95
Cdd:cd04186    28 EVIVVDNASTDGSVELLRE----LFPEVRLIR-NGENLGFGAGnnQGIREAKGDYVLLLNPD 84
 
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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