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Conserved domains on  [gi|1085344581|gb|OGV17282|]
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MAG: glycosyl transferase [Stygiobacter sp. RIFOXYA2_FULL_38_8]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 8-207 9.41e-37

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 127.51  E-value: 9.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   8 KPVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPPLSQ-NAGLLA 86
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAArNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  87 AAGEYISFLGSDDEYKPTYLEERVNFLRQNPqVDMIHgGVEIIGHPYVKDKNDLSREIHLSECVV------GGTFFGKRT 160
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVY-GSRLIREGESDLRRLGSRLFNLVRLLTnlpdstSGFRLFRRE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085344581 161 MFLELGgfHDLKYSDDSDFFERAEKYYRIEKVNfptyVYYRDTPDSI 207
Cdd:COG0463   159 VLEELG--FDEGFLEDTELLRALRHGFRIAEVP----VRYRAGESKL 199
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 8-207 9.41e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 127.51  E-value: 9.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   8 KPVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPPLSQ-NAGLLA 86
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAArNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  87 AAGEYISFLGSDDEYKPTYLEERVNFLRQNPqVDMIHgGVEIIGHPYVKDKNDLSREIHLSECVV------GGTFFGKRT 160
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVY-GSRLIREGESDLRRLGSRLFNLVRLLTnlpdstSGFRLFRRE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085344581 161 MFLELGgfHDLKYSDDSDFFERAEKYYRIEKVNfptyVYYRDTPDSI 207
Cdd:COG0463   159 VLEELG--FDEGFLEDTELLRALRHGFRIAEVP----VRYRAGESKL 199
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 13-189 1.18e-30

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: 110.29  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHEN-IRYMKHSNRRPPLSQNAGLLAAAGEY 91
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRvIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  92 ISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGgveiighpyvkdkndlsreihlsecvvGGTFFGKRTMFLELGGFHDL 171
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGG---------------------------PGNLLFRRELLEEIGGFDEA 133

                         170       180
                  ....*....|....*....|
gi 1085344581 172 KYS--DDSDFFERAEKYYRI 189
Cdd:cd00761   134 LLSgeEDDDFLLRLLRGGKV 153
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 12-171 3.46e-28

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: 104.01  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHS-NRRPPLSQNAGLLAAAGE 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  91 YISFLGSDDEYKPTYLEERVNFLRQNPqVDMIHGGVEIIghpyvkdkNDLSREIHLSECVVGGTFFGKRTMFLELGGFHD 170
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDG-ADVVVGSRYVI--------FGETGEYRRASRITLSRLPFFLGLRLLGLNLPF 151


                  .
gi 1085344581 171 L 171
Cdd:pfam00535 152 L 152
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 8-116 2.79e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 83.94  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   8 KPVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPPLSQNAGLLAA 87
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAVA 84

                          90       100
                  ....*....|....*....|....*....
gi 1085344581  88 AGEYISFLGSDDEYKPTYLEERVNFLRQN 116
Cdd:PRK10073   85 TGKYVAFPDADDVVYPTMYETLMTMALED 113
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 11-129 2.95e-03

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 37.28  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  11 VSIILPTFNREGLLSRAVDsVISQTFTDWELLIIDdgSLDETFPIVNSYLLKHE---NIRYMKHSNRRPPLSQN--AGLL 85
Cdd:TIGR04440   2 LTIIIPTYNRPEYLKRWLR-YYSDFGCDYRIIIAD--SSDEKFNENNLKVFKNYsnpNITYLHYPDLGVPFYEKllDALE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085344581  86 AAAGEYISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGGVEII 129
Cdd:TIGR04440  79 QVETPYVVICADDDFIIPSGLTECLSFLEANPDYSAAQGRYVYF 122
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 8-207 9.41e-37

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 127.51  E-value: 9.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   8 KPVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPPLSQ-NAGLLA 86
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAArNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  87 AAGEYISFLGSDDEYKPTYLEERVNFLRQNPqVDMIHgGVEIIGHPYVKDKNDLSREIHLSECVV------GGTFFGKRT 160
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVY-GSRLIREGESDLRRLGSRLFNLVRLLTnlpdstSGFRLFRRE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085344581 161 MFLELGgfHDLKYSDDSDFFERAEKYYRIEKVNfptyVYYRDTPDSI 207
Cdd:COG0463   159 VLEELG--FDEGFLEDTELLRALRHGFRIAEVP----VRYRAGESKL 199
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 13-189 1.18e-30

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: 110.29  E-value: 1.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHEN-IRYMKHSNRRPPLSQNAGLLAAAGEY 91
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRvIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  92 ISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGgveiighpyvkdkndlsreihlsecvvGGTFFGKRTMFLELGGFHDL 171
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGG---------------------------PGNLLFRRELLEEIGGFDEA 133

                         170       180
                  ....*....|....*....|
gi 1085344581 172 KYS--DDSDFFERAEKYYRI 189
Cdd:cd00761   134 LLSgeEDDDFLLRLLRGGKV 153
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 12-206 5.45e-30

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: 109.94  E-value: 5.45e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHenIRYmkhsnrrppLSQ---------NA 82
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKI--TYW---------ISEpdkgiydamNK 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  83 GLLAAAGEYISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGGVEII----GHPYVKDKNDLSREIHLSECVVG--GTFF 156
Cdd:cd06433    70 GIALATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVdengRVIGRRRPPPFLDKFLLYGMPIChqATFF 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1085344581 157 gKRTMFLELGGF-HDLKYSDDSDFFERA-EKYYRIEKVNFPTyVYYRDTPDS 206
Cdd:cd06433   150 -RRSLFEKYGGFdESYRIAADYDLLLRLlLAGKIFKYLPEVL-AAFRLGGVS 199
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 9-192 1.31e-28

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: 106.13  E-value: 1.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   9 PVVSIILPTFNR-EGLLSRAVDSVISQTFTDWELLIIDDGSLD-ETFPIVNSYLLKHENIRYM-KHSNRRPPLSQNAGLL 85
Cdd:cd04184     1 PLISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDpEVKRVLKKYAAQDPRIKVVfREENGGISAATNSALE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  86 AAAGEYISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHG---GVEIIGH---PYVkdKNDLSREIHLSECVVGGTFFGKR 159
Cdd:cd04184    81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSdedKIDEGGKrsePFF--KPDWSPDLLLSQNYIGHLLVYRR 158

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1085344581 160 TMFLELGGFhDLKY--SDDSDFF----ERAEKYYRIEKV 192
Cdd:cd04184   159 SLVRQVGGF-REGFegAQDYDLVlrvsEHTDRIAHIPRV 196
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 12-171 3.46e-28

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: 104.01  E-value: 3.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHS-NRRPPLSQNAGLLAAAGE 90
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPeNRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  91 YISFLGSDDEYKPTYLEERVNFLRQNPqVDMIHGGVEIIghpyvkdkNDLSREIHLSECVVGGTFFGKRTMFLELGGFHD 170
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDG-ADVVVGSRYVI--------FGETGEYRRASRITLSRLPFFLGLRLLGLNLPF 151


                  .
gi 1085344581 171 L 171
Cdd:pfam00535 152 L 152
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 9-207 1.61e-25

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: 100.59  E-value: 1.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   9 PVVSIILPTFNREGLLSRAVDSVISQTF--TDWELLIIDDGSLDETFPIVNSYLLKHENIRYM-KHSNRRPPLSQNAGLL 85
Cdd:COG1215    29 PRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIeRPENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  86 AAAGEYISFLGSDDEYKPTYLEERVNFLrQNPQVDMihggveiighpyvkdkndlsreihlsecvVGGTFFGKRTMFLEL 165
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA-----------------------------SGANLAFRREALEEV 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1085344581 166 GGFHDLKYSDDSDFFERAEKY-YRIekVNFPTYVYYRDTPDSI 207
Cdd:COG1215   159 GGFDEDTLGEDLDLSLRLLRAgYRI--VYVPDAVVYEEAPETL 199
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
8-189 7.71e-21

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 85.81  E-value: 7.71e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   8 KPVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSylLKHENIRYMKHS-NRRPPLSQNAGLLA 86
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAA--LAFPRVRVIRNPeNLGFAAARNLGLRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  87 AAGEYISFLGSDDEYKPTYLEERVNFlrqnpqvdmihggveiighpyvkdkndlsreihlsecvvGGTFFgKRTMFLELG 166
Cdd:COG1216    80 AGGDYLLFLDDDTVVEPDWLERLLAA---------------------------------------ACLLI-RREVFEEVG 119

                         170       180
                  ....*....|....*....|....*..
gi 1085344581 167 GFhDLK---YSDDSDFFERA-EKYYRI 189
Cdd:COG1216   120 GF-DERfflYGEDVDLCLRLrKAGYRI 145
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 8-116 2.79e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 83.94  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   8 KPVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPPLSQNAGLLAA 87
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAVA 84

                          90       100
                  ....*....|....*....|....*....
gi 1085344581  88 AGEYISFLGSDDEYKPTYLEERVNFLRQN 116
Cdd:PRK10073   85 TGKYVAFPDADDVVYPTMYETLMTMALED 113
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 11-189 6.38e-18

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: 79.20  E-value: 6.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  11 VSIILPTFNREGLLSRAVDSVISQTF--TDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPPLSQNAGLLAAA 88
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRNSR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  89 GEYISFLGSDDEYKPTYLEERVNFLRQnPQVDMIHGGVEIIG------------HPYVKDKNDLSREIHLSECVVGGTFF 156
Cdd:cd02525    82 GDIIIRVDAHAVYPKDYILELVEALKR-TGADNVGGPMETIGeskfqkaiavaqSSPLGSGGSAYRGGAVKIGYVDTVHH 160

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1085344581 157 G--KRTMFLELGGF-HDLKYSDDSDFFERAEKY-YRI 189
Cdd:cd02525   161 GayRREVFEKVGGFdESLVRNEDAELNYRLRKAgYKI 197
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 13-189 2.20e-16

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: 73.36  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYmkHSNRRPPLSQNAGLLAAAGEYI 92
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRN--GENLGFGAGNNQGIREAKGDYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  93 SFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGgveiighpyvkdkndlsreihlseCVVGGTFFGKRTMFLELGGFHD-- 170
Cdd:cd04186    79 LLLNPDTVVEPGALLELLDAAEQDPDVGIVGP------------------------KVSGAFLLVRREVFEEVGGFDEdf 134

                         170       180
                  ....*....|....*....|
gi 1085344581 171 LKYSDDSDFFERAEKY-YRI 189
Cdd:cd04186   135 FLYYEDVDLCLRARLAgYRV 154
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-129 3.40e-16

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: 73.82  E-value: 3.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPPLSQN--AGLLAAAG 89
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNGKNLGVARNfeSLLQAADG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1085344581  90 EYISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGGVEII 129
Cdd:cd04196    81 DYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELV 120
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 13-176 2.71e-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: 70.72  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYM--KHSNRRPPLSQNAGLLAAAGE 90
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVvrDKENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  91 YISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGGVeiigHPYVKDKNDLSREIHL-----------------SECVVGG 153
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRV----RVRNGSENLLTRLQAIeylsifrlgrraqsalgGVLVLSG 156

                         170       180
                  ....*....|....*....|....
gi 1085344581 154 TFFG-KRTMFLELGGFHDLKYSDD 176
Cdd:cd06423   157 AFGAfRREALREVGGWDEDTLTED 180
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
6-182 3.03e-14

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 69.64  E-value: 3.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   6 TFKPVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSldETFPIVNSYL--LKHENIRYMKHS-NRRPPLSQNA 82
Cdd:PRK10018    2 KDNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCS--TSWEQLQQYVtaLNDPRITYIHNDiNSGACAVRNQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  83 GLLAAAGEYISFLGSDDEYKPTYL------EERVN---FLRQNpqvDMIHGGvEIIGHPY---VKDKNDLSREIHLSECV 150
Cdd:PRK10018   80 AIMLAQGEYITGIDDDDEWTPNRLsvflahKQQLVthaFLYAN---DYVCQG-EVYSQPAslpLYPKSPYSRRLFYKRNI 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1085344581 151 VGGTFFGKRTMFLELGGFHDLKYSDDSDFFER 182
Cdd:PRK10018  156 IGNQVFTWAWRFKECLFDTELKAAQDYDIFLR 187
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 13-98 5.29e-11

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: 59.03  E-value: 5.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNRE---GLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKhsnrrppLSQN-------- 81
Cdd:cd04187     1 IVVPVYNEEenlPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIR-------LSRNfgqqaall 73

                          90
                  ....*....|....*..
gi 1085344581  82 AGLLAAAGEYISFLGSD 98
Cdd:cd04187    74 AGLDHARGDAVITMDAD 90
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 13-98 9.76e-11

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: 58.36  E-value: 9.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHE-NIRYMKHSNR--RPPLSQNAGLLAAAG 89
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPiPIKHVWQEDEgfRKAKIRNKAIAAAKG 80


                  ....*....
gi 1085344581  90 EYISFLGSD 98
Cdd:cd06420    81 DYLIFIDGD 89
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 12-201 1.16e-10

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 58.48  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNREG--LLSRAVDSVISQTFTDWELLIIDDGSL-DETFPIVNSYLLKHENIRYMKHSNRRPPLSQNAGLLAAA 88
Cdd:cd04195     1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPVtQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  89 GEYISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGGVEIIGH---PYVKDKNDLSR-EIHL---SECVVG-GTFFGKRT 160
Cdd:cd04195    81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSdgnDIGKRRLPTSHdDILKfarRRSPFNhPTVMFRKS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1085344581 161 MFLELGGFHDLKYSDDSDFFERA-EKYYRIEkvNFP-TYVYYR 201
Cdd:cd04195   161 KVLAVGGYQDLPLVEDYALWARMlANGARFA--NLPeILVKAR 201
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 13-124 1.75e-10

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: 57.58  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVIS--QTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHsnrrpplSQN--------A 82
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRL-------SRNfgkgaavrA 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1085344581  83 GLLAAAGEYISFLGSDDEYKPTYLEERVNFLRQNPqVDMIHG 124
Cdd:cd04179    74 GFKAARGDIVVTMDADLQHPPEDIPKLLEKLLEGG-ADVVIG 114
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 13-213 1.50e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 55.76  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVISQTFTD--WELLIIDDGSLDETFPIVNSYLLKheNIRYMKHS-NRRPPLS--QNA---GL 84
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKekFEVILVDDHSTDGTVQILEFAAAK--PNFQLKILnNSRVSISgkKNAlttAI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  85 LAAAGEYISFLGSDDEYKPTYLEERVNFlRQNPQVDMIHGGVeiighPYVKDKNDLSREIHLSECVVGGT---FFG---- 157
Cdd:cd04192    79 KAAKGDWIVTTDADCVVPSNWLLTFVAF-IQKEQIGLVAGPV-----IYFKGKSLLAKFQRLDWLSLLGLiagSFGlgkp 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344581 158 ----------KRTMFLELGGF--HDLKYSDDSDFFeraekyyrIEKVNFPTY-VYYRDTPDSICSTIEE 213
Cdd:cd04192   153 fmcnganmayRKEAFFEVGGFegNDHIASGDDELL--------LAKVASKYPkVAYLKNPEALVTTQPV 213
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 13-201 3.19e-09

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 54.77  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVISQTFTD-WELLIIDDGSLDETFPIVNSYLLKHENIR---YMKHSNRRPP----LSQNAGL 84
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKLEDSGvivLVGSHNSPSPkgvgYAKNQAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  85 LAAAGEYISFLGSDDEYKPTYLEERVNFLRQNPQVDMihgGVEIIGHP------YVKDKNDLSREIHLSE-------CVV 151
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNSII---GCQVRRIPedsterYTRWINTLTREQLLTQvytshgpTVI 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344581 152 GGTFFGKRTMFLELGGFHDLKYSDDSD--FF----ERAEKYYRIEKVnfptYVYYR 201
Cdd:cd06913   158 MPTWFCSREWFSHVGPFDEGGKGVPEDllFFyehlRKGGGVYRVDRC----LLLYR 209
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 13-168 6.18e-08

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: 50.99  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFN-RE--GLLSRAVDSVISQTftDWELLIIDDGSLDETFPIVNSYLLKHENIRyMKHSNRRPPLSQN--AGLLAA 87
Cdd:cd06442     1 IIIPTYNeREniPELIERLDAALKGI--DYEIIVVDDNSPDGTAEIVRELAKEYPRVR-LIVRPGKRGLGSAyiEGFKAA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  88 AGEYISFLGSDDEYKPTYLEErvnFLRQnpqvdMIHGGVEI-IGHPYVKDKN----DLSREIhLSecvVGGTFFGKRTMF 162
Cdd:cd06442    78 RGDVIVVMDADLSHPPEYIPE---LLEA-----QLEGGADLvIGSRYVEGGGvegwGLKRKL-IS---RGANLLARLLLG 145

                         170
                  ....*....|
gi 1085344581 163 LEL----GGF 168
Cdd:cd06442   146 RKVsdptSGF 155
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 9-184 2.08e-07

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: 49.62  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   9 PVVSIILPTFNREGLLSRAVDSVISqtfTDW--ELLIID--DGSLDETF----PIVNSYLLKHENIRYMKHSNRRpplSQ 80
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACA---LDYpkDRLEIQvlDDSTDETVrlarEIVEEYAAQGVNIKHVRRADRT---GY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  81 NAGLLAAA-----GEYISFLGSDDEYKPTYLeERVNFLRQNPQVDMIHGGVEIIGhpyvKDKNDLSR--EIHLS-----E 148
Cdd:cd06437    75 KAGALAEGmkvakGEYVAIFDADFVPPPDFL-QKTPPYFADPKLGFVQTRWGHIN----ANYSLLTRvqAMSLDyhftiE 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1085344581 149 CVVG---GTFFG--------KRTMFLELGGFHDLKYSDDSDFFERAE 184
Cdd:cd06437   150 QVARsstGLFFNfngtagvwRKECIEDAGGWNHDTLTEDLDLSYRAQ 196
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 12-202 3.13e-07

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: 49.58  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNREGLlSRAVDSVISQTF---TDWELLIIDDGSLDETFPIVNSyLLKHENIRYMKHSNRR---PPLSQNAGLL 85
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFqydPEFELIIINDGSTDKTLEEVSS-IKDHNLQVYYPNAPDTtysLAASRNRGTS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  86 AAAGEYISFLGSDDEYKPTYLEERVNF-----LRQNPQVDMIHGGVEII--GHPYVKDKNDLSREIHLSECVV------- 151
Cdd:pfam10111  79 HAIGEYISFIDGDCLWSPDKFEKQLKIatslaLQENIQAAVVLPVTDLNdeSSNFLRRGGDLTASGDVLRDLLvfyspla 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581 152 ------GGTFFGKRTMFLELGGFHD---LKYSDDSDFFERAEKYYRIEKVnFPTYVYYRD 202
Cdd:pfam10111 159 iffapnSSNALINRQAFIEVGGFDEsfrGHGAEDFDIFLRLAARYPFVAV-MPPQLLYRL 217
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 11-189 4.46e-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: 48.72  E-value: 4.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  11 VSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHenirymKHSNRRPPLSQNAGLLAAAGE 90
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVV------ISSPKGRARQMNAGAAAARGD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  91 YISFLGSDdeykpTYLEerVNFLRQNPQVDMIHGgvEIIGH--PYVKDKNDLSREIHLSE---CVVGGTFFG------KR 159
Cdd:cd02522    75 WLLFLHAD-----TRLP--PDWDAAIIETLRADG--AVAGAfrLRFDDPGPRLRLLELGAnlrSRLFGLPYGdqglfiRR 145

                         170       180       190
                  ....*....|....*....|....*....|
gi 1085344581 160 TMFLELGGFHDLKYSDDSDFFERAEKYYRI 189
Cdd:cd02522   146 ELFEELGGFPELPLMEDVELVRRLRRRGRP 175
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 13-98 5.89e-07

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: 48.33  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  13 IILPTFNREGLLSRAVDSVIS-----QTFTdWELLIIDDGSLDETFPIVNSYLLKH-ENIRYMKHSNRR-PPLSQNAGLL 85
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEyleerPSFS-YEIIVVDDGSKDGTAEVARKLARKNpALIRVLTLPKNRgKGGAVRAGML 79

                          90
                  ....*....|...
gi 1085344581  86 AAAGEYISFLGSD 98
Cdd:cd04188    80 AARGDYILFADAD 92
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 9-127 7.66e-06

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: 45.05  E-value: 7.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   9 PVVSIILPTFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSNRRPP------LSQNA 82
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLgptgksRGLNH 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1085344581  83 GLLAAAGEYISFLGSDDEYKPTYLEERVNFLrQNPQVDMIHGGVE 127
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTPVF 125
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 6-131 2.96e-05

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: 43.73  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   6 TFKPVVSIILPTFNREGLLSRAVDSVISQtftDW-----ELLIIDDGSLDETFPIVNSYlLKHENIRYMKHSNRRPPLSQ 80
Cdd:cd06439    26 AYLPTVTIIIPAYNEEAVIEAKLENLLAL---DYprdrlEIIVVSDGSTDGTAEIAREY-ADKGVKLLRFPERRGKAAAL 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1085344581  81 NAGLLAAAGEYISFLGSDDEYKPTYLEERV-NFlrQNPQVDMIHGGVEIIGH 131
Cdd:cd06439   102 NRALALATGEIVVFTDANALLDPDALRLLVrHF--ADPSVGAVSGELVIVDG 151
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 17-66 3.76e-05

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 43.01  E-value: 3.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344581  17 TFNREGLLSRAVDSVISQTFTDWELLIIDDGSLDET-------FPIVN-SYLLKHENI 66
Cdd:cd04185     5 TYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTaewltslGDLDNiVYLRLPENL 62
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-108 6.10e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 42.76  E-value: 6.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581   1 MQVYKTFKPVVSIILPTFN-REG------LLSRAVDSVisqtfTDWELLIIDDGSLDETFPIVNSYLLKHENIRYMKHSn 73
Cdd:PLN02726    1 MEAPGEGAMKYSIIVPTYNeRLNialivyLIFKALQDV-----KDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRP- 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1085344581  74 rRPP-----LSQNAGLLAAAGEYISFLGSDDEYKPTYLEE 108
Cdd:PLN02726   75 -RPGklglgTAYIHGLKHASGDFVVIMDADLSHHPKYLPS 113
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 12-98 1.53e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 41.68  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNREGLLSRAVDSVIS--------QTFTDWELLIIDDGSLDETFPIVNSYLLKHEN-------IRYMKhsNRRP 76
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKylesrsrkDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnidirlLSLLR--NKGK 150

                          90       100
                  ....*....|....*....|..
gi 1085344581  77 PLSQNAGLLAAAGEYISFLGSD 98
Cdd:PTZ00260  151 GGAVRIGMLASRGKYILMVDAD 172
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 11-190 1.06e-03

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: 38.81  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  11 VSIILPTFNREGLLSRAVDSVisQTFTDwELLIIDDGSLDETFPIVNSY---LLKHENIRYMKHsnrrpplsQNAGLLAA 87
Cdd:cd02511     2 LSVVIITKNEERNIERCLESV--KWAVD-EIIVVDSGSTDRTVEIAKEYgakVYQRWWDGFGAQ--------RNFALELA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  88 AGEYISFLGSDDEYKPTYLEERVNFLRQNPQVD-------------MIHGGVEIIGHP--YVKDKNDLS-REIHLSECVV 151
Cdd:cd02511    71 TNDWVLSLDADERLTPELADEILALLATDDYDGyyvprrnfflgrwIRHGGWYPDRQLrlFRRGKARFEdGRVHEQVVVD 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1085344581 152 GGTFFGkrtmflELGGFHDLKYSDDSDFFERAEKYYRIE 190
Cdd:cd02511   151 GGVGIV------LKGDILHYGYKSLEEFLEKHNRYSSLE 183
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 12-122 1.96e-03

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: 38.34  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  12 SIILPTFNrEGL--LSRAVDSVISQTFTDW--ELLIIDDGSLDETFPIVNSYLLKH--ENIRYMKHSNR----RpplSQN 81
Cdd:cd02510     1 SVIIIFHN-EALstLLRTVHSVINRTPPELlkEIILVDDFSDKPELKLLLEEYYKKylPKVKVLRLKKRegliR---ARI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1085344581  82 AGLLAAAGEYISFLGSDDEYKPTYLEERVNFLRQN------PQVDMI 122
Cdd:cd02510    77 AGARAATGDVLVFLDSHCEVNVGWLEPLLARIAENrktvvcPIIDVI 123
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 11-129 2.95e-03

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 37.28  E-value: 2.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344581  11 VSIILPTFNREGLLSRAVDsVISQTFTDWELLIIDdgSLDETFPIVNSYLLKHE---NIRYMKHSNRRPPLSQN--AGLL 85
Cdd:TIGR04440   2 LTIIIPTYNRPEYLKRWLR-YYSDFGCDYRIIIAD--SSDEKFNENNLKVFKNYsnpNITYLHYPDLGVPFYEKllDALE 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1085344581  86 AAAGEYISFLGSDDEYKPTYLEERVNFLRQNPQVDMIHGGVEII 129
Cdd:TIGR04440  79 QVETPYVVICADDDFIIPSGLTECLSFLEANPDYSAAQGRYVYF 122
 
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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