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Conserved domains on  [gi|34369299|gb|AAN60065|]
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IcaA [Staphylococcus capitis]

Protein Classification

poly-beta-1,6 N-acetyl-D-glucosamine synthase( domain architecture ID 11499219)

poly-beta-1,6 N-acetyl-D-glucosamine synthase is a probable N-acetylglucosaminyltransferase that catalyzes the polymerization of single monomer units of UDP-N-acetylglucosamine to produce the linear homopolymer poly-beta-1,6-N-acetyl-D-glucosamine (PGA), a biofilm adhesin polysaccharide

CAZY:  GT2
EC:  2.4.1.-
Gene Ontology:  GO:0008375|GO:0042710|GO:0005886
PubMed:  15090514
TCDB:  4.D.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PgaC_IcaA TIGR03937
poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are ...
 3-408 0e+00

poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are biofilm-forming enzymes that polymerize N-acetyl-D-glucosamine residues in beta(1,6) linkage. One named members is IcaA (intercellular adhesin protein A), an enzyme that acts (with aid of subunit IcaD) in Polysaccharide Intercellular Adhesin (PIA) biosynthesis in Staphylococcus epidermis). The homologous member in E. coli is designated PgaC. Members are often encoded next to a polysaccharide deacetylase and involved in biofilm formation. Note that chitin, although also made from N-acetylglucosamine, is formed with beta-1,4 linkages.


:

Pssm-ID: 274866 [Multi-domain]  Cd Length: 407  Bit Score: 698.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299     3 FFNFLLFYPIFMSIYWIVGALYYFFTKELPFSKKKVISKNKDQIEGISFLLACYNESETVRDTLSNVLALNYPKKEIIII 82
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWPLPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    83 NDGSSDNTAEIIYEMKQHHD-FKFVDLQVNRGKANALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVT 161
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPrLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   162 GNPRIRNKSSILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADFRI 241
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   242 NYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLLRDFWATMKSKKLSLYILMFEQIVSIIWVYMILLYLAFLLMTANFL 321
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   322 DYTYLKYSFSIFFLSSFTMTFINIIQFTVALFIDSRYEKKNIAGLIFVSWYPTIYWIINAAVVIFAFPKALKRKKGGYAT 401
Cdd:TIGR03937 321 PYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRAV 400


                  ....*..
gi 34369299   402 WSSPDRG 408
Cdd:TIGR03937 401 WVSPDRG 407
 
Name Accession Description Interval E-value
PgaC_IcaA TIGR03937
poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are ...
 3-408 0e+00

poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are biofilm-forming enzymes that polymerize N-acetyl-D-glucosamine residues in beta(1,6) linkage. One named members is IcaA (intercellular adhesin protein A), an enzyme that acts (with aid of subunit IcaD) in Polysaccharide Intercellular Adhesin (PIA) biosynthesis in Staphylococcus epidermis). The homologous member in E. coli is designated PgaC. Members are often encoded next to a polysaccharide deacetylase and involved in biofilm formation. Note that chitin, although also made from N-acetylglucosamine, is formed with beta-1,4 linkages.


Pssm-ID: 274866 [Multi-domain]  Cd Length: 407  Bit Score: 698.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299     3 FFNFLLFYPIFMSIYWIVGALYYFFTKELPFSKKKVISKNKDQIEGISFLLACYNESETVRDTLSNVLALNYPKKEIIII 82
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWPLPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    83 NDGSSDNTAEIIYEMKQHHD-FKFVDLQVNRGKANALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVT 161
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPrLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   162 GNPRIRNKSSILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADFRI 241
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   242 NYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLLRDFWATMKSKKLSLYILMFEQIVSIIWVYMILLYLAFLLMTANFL 321
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   322 DYTYLKYSFSIFFLSSFTMTFINIIQFTVALFIDSRYEKKNIAGLIFVSWYPTIYWIINAAVVIFAFPKALKRKKGGYAT 401
Cdd:TIGR03937 321 PYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRAV 400


                  ....*..
gi 34369299   402 WSSPDRG 408
Cdd:TIGR03937 401 WVSPDRG 407
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 52-227 3.52e-72

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: 224.03  E-value: 3.52e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  52 LLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEM--KQHHDFKFVDLQVNRGKANALNEGVKHSSYDY 129
Cdd:cd06423   2 IVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELaaLYIRRVLVVRDKENGGKAGALNAGLRHAKGDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 130 VMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLF 208
Cdd:cd06423  82 VVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSeNLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAF 161

                       170
                ....*....|....*....
gi 34369299 209 KKSALKEVGYWDTDMITED 227
Cdd:cd06423 162 RREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-353 2.45e-60

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: 198.04  E-value: 2.45e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   3 FFNFLLFYPIFMSIYWIVGALYYFfTKELPFskkkvisknkdqiegISFLLACYNESETVRDTLSNVLALNYPKK--EII 80
Cdd:COG1215   1 LLLLLALLALLYLLLLALARRRRA-PADLPR---------------VSVIIPAYNEEAVIEETLRSLLAQDYPKEklEVI 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  81 IINDGSSDNTAEIIYEMK-QHHDFKFVDLQVNRGKANALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFkQDPKLGA 159
Cdd:COG1215  65 VVDDGSTDETAEIARELAaEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 160 vtgnprirnkssilgkiqtieyasligcikrsqslagaintiSGVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADF 239
Cdd:COG1215 144 ------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGY 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 240 RINYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLLRdFWATMKSKKLSLYILMFeqIVSIIWVYMILLYLAFLLMTAN 319
Cdd:COG1215 182 RIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLK-HRPLLRPRRLLLFLLLL--LLPLLLLLLLLALLALLLLLLP 258

                       330       340       350
                ....*....|....*....|....*....|....
gi 34369299 320 FLDYTYLKYSFSIFFLSSFTMTFINIIQFTVALF 353
Cdd:COG1215 259 ALLLALLLALRRRRLLLPLLHLLYGLLLLLAALR 292
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 50-215 4.25e-33

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: 122.12  E-value: 4.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    50 SFLLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYE-MKQHHDFKFVDLQVNRGKANALNEGVKHSSYD 128
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEyAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   129 YVMCLDADTIVNQDAPYYMMDNFKQDPKlGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLF 208
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA-DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159


                  ....*..
gi 34369299   209 KKSALKE 215
Cdd:pfam00535 160 RREALEE 166
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 7-136 5.40e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 60.17  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    7 LLFYPIfmsIYW---------IVGALYYFFTKELPFSKKKVISKNKDQIEgISFLLACYNESETVRDTLSNVLAL--NYP 75
Cdd:PTZ00260  25 LLFYPY---ISWpdddkvirqVKSSVIHEKSKEVDKENYINNILKDSDVD-LSIVIPAYNEEDRLPKMLKETIKYleSRS 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34369299   76 KK------EIIIINDGSSDNTAEI-----IYEMKQHHDFKFVDLQVNRGKANALNEGVKHSSYDYVMCLDAD 136
Cdd:PTZ00260 101 RKdpkfkyEIIIVNDGSKDKTLKVakdfwRQNINPNIDIRLLSLLRNKGKGGAVRIGMLASRGKYILMVDAD 172
 
Name Accession Description Interval E-value
PgaC_IcaA TIGR03937
poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are ...
 3-408 0e+00

poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are biofilm-forming enzymes that polymerize N-acetyl-D-glucosamine residues in beta(1,6) linkage. One named members is IcaA (intercellular adhesin protein A), an enzyme that acts (with aid of subunit IcaD) in Polysaccharide Intercellular Adhesin (PIA) biosynthesis in Staphylococcus epidermis). The homologous member in E. coli is designated PgaC. Members are often encoded next to a polysaccharide deacetylase and involved in biofilm formation. Note that chitin, although also made from N-acetylglucosamine, is formed with beta-1,4 linkages.


Pssm-ID: 274866 [Multi-domain]  Cd Length: 407  Bit Score: 698.62  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299     3 FFNFLLFYPIFMSIYWIVGALYYFFTKELPFSKKKVISKNKDQIEGISFLLACYNESETVRDTLSNVLALNYPKKEIIII 82
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWPLPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    83 NDGSSDNTAEIIYEMKQHHD-FKFVDLQVNRGKANALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVT 161
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPrLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   162 GNPRIRNKSSILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADFRI 241
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   242 NYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLLRDFWATMKSKKLSLYILMFEQIVSIIWVYMILLYLAFLLMTANFL 321
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   322 DYTYLKYSFSIFFLSSFTMTFINIIQFTVALFIDSRYEKKNIAGLIFVSWYPTIYWIINAAVVIFAFPKALKRKKGGYAT 401
Cdd:TIGR03937 321 PYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRAV 400


                  ....*..
gi 34369299   402 WSSPDRG 408
Cdd:TIGR03937 401 WVSPDRG 407
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 52-227 3.52e-72

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: 224.03  E-value: 3.52e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  52 LLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEM--KQHHDFKFVDLQVNRGKANALNEGVKHSSYDY 129
Cdd:cd06423   2 IVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELaaLYIRRVLVVRDKENGGKAGALNAGLRHAKGDI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 130 VMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLF 208
Cdd:cd06423  82 VVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSeNLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAF 161

                       170
                ....*....|....*....
gi 34369299 209 KKSALKEVGYWDTDMITED 227
Cdd:cd06423 162 RREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-353 2.45e-60

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: 198.04  E-value: 2.45e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   3 FFNFLLFYPIFMSIYWIVGALYYFfTKELPFskkkvisknkdqiegISFLLACYNESETVRDTLSNVLALNYPKK--EII 80
Cdd:COG1215   1 LLLLLALLALLYLLLLALARRRRA-PADLPR---------------VSVIIPAYNEEAVIEETLRSLLAQDYPKEklEVI 64

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  81 IINDGSSDNTAEIIYEMK-QHHDFKFVDLQVNRGKANALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFkQDPKLGA 159
Cdd:COG1215  65 VVDDGSTDETAEIARELAaEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 160 vtgnprirnkssilgkiqtieyasligcikrsqslagaintiSGVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADF 239
Cdd:COG1215 144 ------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGY 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 240 RINYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLLRdFWATMKSKKLSLYILMFeqIVSIIWVYMILLYLAFLLMTAN 319
Cdd:COG1215 182 RIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLK-HRPLLRPRRLLLFLLLL--LLPLLLLLLLLALLALLLLLLP 258

                       330       340       350
                ....*....|....*....|....*....|....
gi 34369299 320 FLDYTYLKYSFSIFFLSSFTMTFINIIQFTVALF 353
Cdd:COG1215 259 ALLLALLLALRRRRLLLPLLHLLYGLLLLLAALR 292
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 16-271 8.54e-39

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: 139.64  E-value: 8.54e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  16 IYWIVGALYYFFTKelpFSKKKVISKNKDQIEGISFLLACYNESETVRDTLSNVLALNYPKK--EIIIINDGSSDNTAEI 93
Cdd:cd06439   1 TYFGYPLLLKLLAR---LRPKPPSLPDPAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDrlEIIVVSDGSTDGTAEI 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  94 IYEMKQhHDFKFVDLQVNRGKANALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFkQDPKLGAVTGNPRIRNKssil 173
Cdd:cd06439  78 AREYAD-KGVKLLRFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHF-ADPSVGAVSGELVIVDG---- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 174 GKIQTIE--YASLIGCIKRSQSLAGAINTISGVFTLFKKSAlkeVGYWDTDMITEDIAVSWKLHLADFRINYEPRAMCWM 251
Cdd:cd06439 152 GGSGSGEglYWKYENWLKRAESRLGSTVGANGAIYAIRREL---FRPLPADTINDDFVLPLRIARQGYRVVYEPDAVAYE 228

                       250       260
                ....*....|....*....|
gi 34369299 252 LVPETVGGLWKQRVRWAQGG 271
Cdd:cd06439 229 EVAEDGSEEFRRRVRIAAGN 248
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 52-275 4.80e-35

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 129.23  E-value: 4.80e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  52 LLACYNES-ETVRDTLSNVLALNYP--KKEIIIINDGSSDNTAEIIYEMKQHHDFKFVDLQVNRG-KANALNEGVKHSSY 127
Cdd:cd06421   6 FIPTYNEPlEIVRKTLRAALAIDYPhdKLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHaKAGNLNNALAHTTG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 128 DYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTGNPRIRNKSSILGKIQTIEYASLI--GCIKRSQSLAGAInTISGVF 205
Cdd:cd06421  86 DFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELfyGVIQPGRDRWGAA-FCCGSG 164

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 206 TLFKKSALKEVGYWDTDMITEDIAVSWKLHLADFRINYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVL 275
Cdd:cd06421 165 AVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 50-215 4.25e-33

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: 122.12  E-value: 4.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    50 SFLLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYE-MKQHHDFKFVDLQVNRGKANALNEGVKHSSYD 128
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEyAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   129 YVMCLDADTIVNQDAPYYMMDNFKQDPKlGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLF 208
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA-DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159


                  ....*..
gi 34369299   209 KKSALKE 215
Cdd:pfam00535 160 RREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 49-245 6.70e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.50  E-value: 6.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEM-KQHHDFKFVDLQVNRGKANALNEGVKHSSY 127
Cdd:COG0463   4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELaAKDPRIRVIRLERNRGKGAARNAGLAAARG 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 128 DYVMCLDADTIVNQDAPYYMMDNFKQDPkLGAVTGNPRIRNkssilGKIQTIEYASLIGCIKRsqsLAGAINTISGVFTL 207
Cdd:COG0463  84 DYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLIRE-----GESDLRRLGSRLFNLVR---LLTNLPDSTSGFRL 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 34369299 208 FKKSALKEVGY-----WDTDMItediavswKLHLADFRINYEP 245
Cdd:COG0463 155 FRREVLEELGFdegflEDTELL--------RALRHGFRIAEVP 189
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 52-270 9.93e-28

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: 109.30  E-value: 9.93e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  52 LLACYNESETVRDTLSNVLALNYPKK--EIIIINDGSSDNTAEIIYEMKQHHDFKFVDLQVNR----GKANALNEGVKHS 125
Cdd:cd04192   2 VIAARNEAENLPRLLQSLSALDYPKEkfEVILVDDHSTDGTVQILEFAAAKPNFQLKILNNSRvsisGKKNALTTAIKAA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 126 SYDYVMCLDADTIVNQDAPYYMMdNFKQDPKLGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKrSQSLAGAINTISGVF 205
Cdd:cd04192  82 KGDWIVTTDADCVVPSNWLLTFV-AFIQKEQIGLVAGPVIYFKGKSLLAKFQRLDWLSLLGLIA-GSFGLGKPFMCNGAN 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34369299 206 TLFKKSALKEVGYWDT--DMITED------IAVSwklHLADFRINYEPRAMCWMLVPETVGGLWKQRVRWAQG 270
Cdd:cd04192 160 MAYRKEAFFEVGGFEGndHIASGDdelllaKVAS---KYPKVAYLKNPEALVTTQPVTSWKELLNQRKRWASK 229
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 55-165 1.18e-26

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: 104.51  E-value: 1.18e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  55 CYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEM-KQHHDFKFVDLQVNRGKANALNEGVKHSSYDYVMCL 133
Cdd:cd00761   5 AYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYaKKDPRVIRVINEENQGLAAARNAGLKAARGEYILFL 84

                        90       100       110
                ....*....|....*....|....*....|..
gi 34369299 134 DADTIVNQDAPYYMMDNFKQDPKLGAVTGNPR 165
Cdd:cd00761  85 DADDLLLPDWLERLVAELLADPEADAVGGPGN 116
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 50-277 1.44e-25

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 103.63  E-value: 1.44e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  50 SFLLACYNES-ETVRDTLSNVLALNYPKKEIIIINDGSSD-NTAEIIYEMKQHHD--FKFVDLQVNRG-KANALNEGVKH 124
Cdd:cd06435   1 SIHVPCYEEPpEMVKETLDSLAALDYPNFEVIVIDNNTKDeALWKPVEAHCAQLGerFRFFHVEPLPGaKAGALNYALER 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 125 SSYD--YVMCLDADTIVNQDAPYYMMDNFKqDPKLGAVTGNPRIRN-KSSILGKIQTIEYASL--IGCIKRSQslAGAIN 199
Cdd:cd06435  81 TAPDaeIIAVIDADYQVEPDWLKRLVPIFD-DPRVGFVQAPQDYRDgEESLFKRMCYAEYKGFfdIGMVSRNE--RNAII 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34369299 200 TIsGVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADFRINYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLLR 277
Cdd:cd06435 158 QH-GTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKK 234
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 49-271 4.97e-25

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: 102.00  E-value: 4.97e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESETVRDTLSNVLALNYPKKEIII-INDGSSDNTAEIIYEMKQHHDFKFVDLQ-VNRG-----KANALNEG 121
Cdd:cd06437   3 VTVQLPVFNEKYVVERLIEAACALDYPKDRLEIqVLDDSTDETVRLAREIVEEYAAQGVNIKhVRRAdrtgyKAGALAEG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 122 VKHSSYDYVMCLDADTIVNQD----APYYmmdnFKqDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQSLAG 196
Cdd:cd06437  83 MKVAKGEYVAIFDADFVPPPDflqkTPPY----FA-DPKLGFVQTRWGHINANySLLTRVQAMSLDYHFTIEQVARSSTG 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 34369299 197 AINTISGVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADFRINYEPRAMCWMLVPETVGGLWKQRVRWAQGG 271
Cdd:cd06437 158 LFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 49-277 1.64e-23

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: 98.46  E-value: 1.64e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESETVRDTLSNVLALNYPKK--EIIIINDGSSDNTAEIIYEMKQHHD-FKFVDlqvNRGK--ANALNEGVK 123
Cdd:cd02525   2 VSIIIPVRNEEKYIEELLESLLNQSYPKDliEIIVVDGGSTDGTREIVQEYAAKDPrIRLID---NPKRiqSAGLNIGIR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 124 HSSYDYVMCLDADTIVNQDapyYMMDNFK--QDPKLGAVTGNPRIRNKSSilgKIQTIEYASL----IGCIKRSQSLAGA 197
Cdd:cd02525  79 NSRGDIIIRVDAHAVYPKD---YILELVEalKRTGADNVGGPMETIGESK---FQKAIAVAQSsplgSGGSAYRGGAVKI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 198 INTISGVFTLFKKSALKEVGYWDTDMIT-EDIAVSWKLHLADFRINYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLL 276
Cdd:cd02525 153 GYVDTVHHGAYRREVFEKVGGFDESLVRnEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRARTLR 232


                .
gi 34369299 277 R 277
Cdd:cd02525 233 K 233
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
49-264 3.83e-23

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 96.22  E-value: 3.83e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMkQHHDFKFVDLQVNRGKANALNEGVKHSSYD 128
Cdd:COG1216   5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL-AFPRVRVIRNPENLGFAAARNLGLRAAGGD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 129 YVMCLDADTIVNQDApyymmdnfkqdpklgavtgnprirnkssiLGKIqtIEYASLigcikrsqslagaintisgvftLF 208
Cdd:COG1216  84 YLLFLDDDTVVEPDW-----------------------------LERL--LAAACL----------------------LI 110

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 34369299 209 KKSALKEVGYWDTDMIT--EDIAVSWKLHLADFRINYEPRAMCWMLVPETVGGLWKQR 264
Cdd:COG1216 111 RREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY 168
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 56-250 3.15e-21

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: 89.93  E-value: 3.15e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  56 YNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMKQhhDFKFVDLQVNRGKANALNEGVKHSSYDYVMCLDA 135
Cdd:cd04186   6 YNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFP--EVRLIRNGENLGFGAGNNQGIREAKGDYVLLLNP 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 136 DTIVNQDAPYYMMDNFKQDPKLGAVTGnprirnkssilgkiqtieyasligcikrsqslagainTISGVFTLFKKSALKE 215
Cdd:cd04186  84 DTVVEPGALLELLDAAEQDPDVGIVGP-------------------------------------KVSGAFLLVRREVFEE 126

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 34369299 216 VGYWDTD--MITEDIAVSWKLHLADFRINYEPRAMCW 250
Cdd:cd04186 127 VGGFDEDffLYYEDVDLCLRARLAGYRVLYVPQAVIY 163
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 49-270 4.05e-21

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: 91.28  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    49 ISFLLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMKQHHDFKFVDLQVN------RGKANALNEGV 122
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNarllgpTGKSRGLNHGF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   123 KHSSYDYVMCLDADTIVNQDA-PYYMmdNFKQDPKLGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRSQsLAGAINTI 201
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTlKKYV--QYFDSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLR-LALGVLPL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   202 SGVFTLFKKSALKEVGYWDTDMI-TEDIAVSWKLHLADFRINYEPRAMCWMLVPETVGGLWKQRVRWAQG 270
Cdd:pfam13641 161 SGAGSAIRREVLKELGLFDPFFLlGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 129-316 9.68e-21

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 89.32  E-value: 9.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   129 YVMCLDADTIVNQDAPYYMMDNFKqDPKLGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFTLF 208
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMA-SPEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   209 KKSALKEVGYWDTDMITEDIAVSWKLHLADFRINYEPRAMCWMLVPETVGGLWKQRVRWAQGGHEVLLRD--------FW 280
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRllgylgtlLW 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 34369299   281 ATMkskKLSLYILMFEQIVSIIWVYMILLYLAFLLM 316
Cdd:pfam13632 160 SGL---PLALLLLLLFSISSLALVLLLLALLAGLLL 192
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 55-216 1.18e-20

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: 88.78  E-value: 1.18e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  55 CYNESETVRDTLSNVLAL--NYPKKEIIIINDGSSDNTAEIIYEM-KQHHDFKFVDLQVNRGKANALNEGVKHSSYDYVM 131
Cdd:cd04179   5 AYNEEENIPELVERLLAVleEGYDYEIIVVDDGSTDGTAEIARELaARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 132 CLDADtivNQDAPYY---MMDNFKQDpklGA--VTGNPRIRNKSSILGKIQTIeyASLIgcikrsqsLAGAINTISGV-- 204
Cdd:cd04179  85 TMDAD---LQHPPEDipkLLEKLLEG---GAdvVIGSRFVRGGGAGMPLLRRL--GSRL--------FNFLIRLLLGVri 148

                       170
                ....*....|....*...
gi 34369299 205 ------FTLFKKSALKEV 216
Cdd:cd04179 149 sdtqsgFRLFRREVLEAL 166
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 49-271 4.38e-19

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: 85.77  E-value: 4.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESETV-RDTLSNVLALNypKKEIIIINDGSSDNTAEIIYEMKQHHDfKFVDLQVNRGKANALNEGVKHSSY 127
Cdd:cd06434   2 VTVIIPVYDEDPDVfRECLRSILRQK--PLEIIVVTDGDDEPYLSILSQTVKYGG-IFVITVPHPGKRRALAEGIRHVTT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 128 DYVMCLDADTIVNQDAPYYMMDNFKqDPKLGAVTGNPRIRNK-SSILGKIQTIEYASLIGCIKRSQSLAGAINTISGVFT 206
Cdd:cd06434  79 DIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRPrDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTA 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34369299 207 LFKKSALKEVGYwdTDMITEDIAVSWKLHLAD------------FRINYEPRAMCWMLVPETVGGLWKQRVRWAQGG 271
Cdd:cd06434 158 AYRTEILKDFLF--LEEFTNETFMGRRLNAGDdrfltryvlshgYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSN 232
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
 52-267 9.86e-18

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 81.97  E-value: 9.86e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  52 LLACYNESET-VRDTLSNVLALNYP----------KKEIIIINDGSsdntaeiiyemkqhhdfkfvdLQVNRGKAN---- 116
Cdd:cd04190   2 CVTMYNEDEEeLARTLDSILKNDYPfcarggdswkKIVVCVIFDGA---------------------IKKNRGKRDsqlw 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 117 ---ALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQ 192
Cdd:cd04190  61 ffnYFCRVLFPDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKqGPLVMYQVFEYAISHWLDKAFE 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 193 SLAGAINTISGVFTLFKKSALKEV-GYW----DTDMITEDIAVSWK---LHLADFRI--------------NYEPRAMCW 250
Cdd:cd04190 141 SVFGFVTCLPGCFSMYRIEALKGDnGGKgpllDYAYLTNTVDSLHKknnLDLGEDRIlctlllkagpkrkyLYVPGAVAE 220

                       250
                ....*....|....*..
gi 34369299 251 MLVPETVGGLWKQRVRW 267
Cdd:cd04190 221 TDVPETFVELLSQRRRW 237
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 55-144 2.09e-16

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: 76.75  E-value: 2.09e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  55 CYNESETVRDT---LSNVLALNYPKKEIIIINDGSSDNTAEIIYEM-KQHHDFKFVDLQVNRGKANALNEGVKHSSYDYV 130
Cdd:cd04187   5 VYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELaARDPRVKVIRLSRNFGQQAALLAGLDHARGDAV 84

                        90
                ....*....|....
gi 34369299 131 MCLDADTivnQDAP 144
Cdd:cd04187  85 ITMDADL---QDPP 95
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 55-136 1.80e-15

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: 74.91  E-value: 1.80e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  55 CYNES-------ETVRDTLSNVLALNYpkkEIIIINDGSSDNTAEIIYEMKQHH--DFKFVDLQVNRGKANALNEGVKHS 125
Cdd:cd04188   5 AYNEEkrlpptlEEAVEYLEERPSFSY---EIIVVDDGSKDGTAEVARKLARKNpaLIRVLTLPKNRGKGGAVRAGMLAA 81

                        90
                ....*....|.
gi 34369299 126 SYDYVMCLDAD 136
Cdd:cd04188  82 RGDYILFADAD 92
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 51-229 2.17e-15

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 73.79  E-value: 2.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  51 FLLACYNESETVRDTLSNVLALNYPKK--EIIIINDGSSDNTAEI-------IYEmkqHHDfkfvdlQVNRGKANALNEG 121
Cdd:cd06438   1 ILIPAHNEEAVIGNTVRSLKAQDYPRElyRIFVVADNCTDDTAQVaraagatVLE---RHD------PERRGKGYALDFG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 122 VKHS-----SYDYVMCLDADTIVNQDAPYYMMDNFKQDPKlgAVTGNPRIRN-KSSILGKIQTIEYASLIGCIKRSQSLA 195
Cdd:cd06438  72 FRHLlnladDPDAVVVFDADNLVDPNALEELNARFAAGAR--VVQAYYNSKNpDDSWITRLYAFAFLVFNRLRPLGRSNL 149

                       170       180       190
                ....*....|....*....|....*....|....
gi 34369299 196 GAINTISGVFTLFKKSALKEVGyWDTDMITEDIA 229
Cdd:cd06438 150 GLSCQLGGTGMCFPWAVLRQAP-WAAHSLTEDLE 182
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 114-268 5.76e-15

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 72.32  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   114 KANALNEGVKHSSYDYVMCLDADTIVNQDAPYYMMDNFKqDPKLGAVTGNPRIRNKSSILGkiqTIEYASLIGCIKRSQS 193
Cdd:pfam13506  18 KVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLA-DPKVGLVTSPPVGSDPKGLAA---ALEAAFFNTLAGVLQA 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 34369299   194 LAGAINTISGVFTLFKKSALKEVGYWDT--DMITEDIAVSWKLHLADFRINYEPRAMCWMLVPE--TVGGLWKQRVRWA 268
Cdd:pfam13506  94 ALSGIGFAVGMSMAFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFRAFMARQLRWA 172
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 54-222 1.66e-13

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: 68.73  E-value: 1.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  54 ACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIyemKQHHD--FKFV---DlqvnRGKANALNEGVKHSSYD 128
Cdd:cd06433   5 PTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDII---KKYEDkiTYWIsepD----KGIYDAMNKGIALATGD 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 129 YVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRsqslagaiNTISGVFTLF 208
Cdd:cd06433  78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYG--------MPICHQATFF 149

                       170
                ....*....|....
gi 34369299 209 KKSALKEVGYWDTD 222
Cdd:cd06433 150 RRSLFEKYGGFDES 163
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 49-270 6.60e-13

CESA_like_2 is a member of 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: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 68.05  E-value: 6.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESETVRDTLSNVLALNYPKK--EIIIINDGSSDNTAEII--YEMKQHHDFKFVDLQVNRGKANALNEGVKH 124
Cdd:cd06427   3 YTILVPLYKEAEVLPQLIASLSALDYPRSklDVKLLLEEDDEETIAAAraLRLPSIFRVVVVPPSQPRTKPKACNYALAF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 125 SSYDYVMCLDADTIVNQDAPYYMMDNF-KQDPKLGAVTGNPRIRNKSS-ILGKIQTIEYASLIGCIKRSQSLAGAINTIS 202
Cdd:cd06427  83 ARGEYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPLNYYNAREnWLTRMFALEYAAWFDYLLPGLARLGLPIPLG 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 34369299 203 GVFTLFKKSALKEVGYWDTDMITEDIAVSWKLHLADFRINYEPRAMcWMLVPETVGGLWKQRVRWAQG 270
Cdd:cd06427 163 GTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTT-LEEANNALGNWIRQRSRWIKG 229
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
 121-267 1.84e-12

Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).


Pssm-ID: 367353 [Multi-domain]  Cd Length: 527  Bit Score: 68.63  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   121 GVKHSSYDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTGNPRIRNK-SSILGKIQTIEYASLIGCIKRSQSLAGAIN 199
Cdd:pfam03142 196 GVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKrQSWVTAIQVFEYYISHHLSKAFESVFGGVT 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   200 TISGVFTLFK-KSALKEVGYWDTDMITEDIAVSWK------------LHLAD--------------FRINYEPRAMCWML 252
Cdd:pfam03142 276 CLPGCFSMYRiKAPKGGDGYWVPILASPDIVEHYSenvvdtlhkknlLLLGEdrylttlmlktfpkRKTVFVPQAVCKTI 355

                         170
                  ....*....|....*
gi 34369299   253 VPETVGGLWKQRVRW 267
Cdd:pfam03142 356 APDTFKVLLSQRRRW 370
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 50-162 7.60e-12

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: 63.87  E-value: 7.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  50 SFLLACY-NES-ETVRDTLSNVLALNYPKKEIIIINDGS-SDNTAEIIYEMKQHHDFKFVDLQVNRGKANALNEGVKHSS 126
Cdd:cd04195   1 SVLMSVYiKEKpEFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCT 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 34369299 127 YDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTG 162
Cdd:cd04195  81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGG 116
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 56-270 1.49e-11

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: 63.74  E-value: 1.49e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  56 YNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIyemKQHHdfkFVDLQVNRGKANALNEGVKHSSYDYVMCLDA 135
Cdd:cd02522   8 LNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIA---RSAG---VVVISSPKGRARQMNAGAAAARGDWLLFLHA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 136 DTIVNQDAP-YYMMDNFKQDPKLGAvtGNPRIRNKSSILgkiQTIEYAS-----LIGCIKRSQSLagaintisgvftLFK 209
Cdd:cd02522  82 DTRLPPDWDaAIIETLRADGAVAGA--FRLRFDDPGPRL---RLLELGAnlrsrLFGLPYGDQGL------------FIR 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34369299 210 KSALKEVGYWDTDMITEDIAVSWKLHladfrinyepRAMCWMLVPETVG---------GLWKQ-------RVRWAQG 270
Cdd:cd02522 145 RELFEELGGFPELPLMEDVELVRRLR----------RRGRPALLPSPVTtsarrwernGWLRTtllnwllLLLYLLG 211
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 56-143 2.72e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 59.57  E-value: 2.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  56 YNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMKQHHDFKFVDLQVNRGKANALNEGVKH---SSYDYVMC 132
Cdd:cd04185   6 YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYEGVRRayeLGYDWIWL 85

                        90
                ....*....|.
gi 34369299 133 LDADTIVNQDA 143
Cdd:cd04185  86 MDDDAIPDPDA 96
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 7-136 5.40e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 60.17  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    7 LLFYPIfmsIYW---------IVGALYYFFTKELPFSKKKVISKNKDQIEgISFLLACYNESETVRDTLSNVLAL--NYP 75
Cdd:PTZ00260  25 LLFYPY---ISWpdddkvirqVKSSVIHEKSKEVDKENYINNILKDSDVD-LSIVIPAYNEEDRLPKMLKETIKYleSRS 100

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 34369299   76 KK------EIIIINDGSSDNTAEI-----IYEMKQHHDFKFVDLQVNRGKANALNEGVKHSSYDYVMCLDAD 136
Cdd:PTZ00260 101 RKdpkfkyEIIIVNDGSKDKTLKVakdfwRQNINPNIDIRLLSLLRNKGKGGAVRIGMLASRGKYILMVDAD 172
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 51-227 1.62e-09

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: 57.01  E-value: 1.62e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  51 FLLACYNESETVRDTLSNVLAlNYPKKEIIIINDGSSDNTAEIIyeMKQHHDFKFVDL-----QVNRGKANALNEGVKH- 124
Cdd:cd06436   1 VLVPCLNEEAVIQRTLASLLR-NKPNFLVLVIDDASDDDTAGIV--RLAITDSRVHLLrrhlpNARTGKGDALNAAYDQi 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 125 ----------SSYDYVMCLDADTIVNQDApYYMMDNFKQDPKLGAVTGNPRIRNK-SSILGKIQTIEYASLIGCIKRSQS 193
Cdd:cd06436  78 rqilieegadPERVIIAVIDADGRLDPNA-LEAVAPYFSDPRVAGTQSRVRMYNRhKNLLTILQDLEFFIIIAATQSLRA 156

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 34369299 194 LAGAInTISGVFTLFKKSALKEV---GYWdTDMITED 227
Cdd:cd06436 157 LTGTV-GLGGNGQFMRLSALDGLigeEPW-SDSLLED 191
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 61-241 2.03e-08

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 54.60  E-value: 2.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  61 TVRDTLSNVLALNYPKKEIIIInDGSSDNTAEIIYEmKQHHDFKFVDLQVNRGKANALNEGVKHS---SYDYVMCLDADT 137
Cdd:cd02526   9 DLSKLKELLAALAEQVDKVVVV-DNSSGNDIELRLR-LNSEKIELIHLGENLGIAKALNIGIKAAlenGADYVLLFDQDS 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299 138 IVNQDA---PYYMMDNFKQDPKLGAVTgnPRI--RNKSSILGKIQTIEYASLIGCikrsQSLAGAINT----ISGvfTLF 208
Cdd:cd02526  87 VPPPDMvekLLAYKILSDKNSNIGAVG--PRIidRRTGENSPGVRKSGYKLRIQK----EGEEGLKEVdfliTSG--SLI 158

                       170       180       190
                ....*....|....*....|....*....|....*
gi 34369299 209 KKSALKEVGYWDTDMITE--DIAVSWKLHLADFRI 241
Cdd:cd02526 159 SLEALEKVGGFDEDLFIDyvDTEWCLRARSKGYKI 193
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 49-160 2.10e-08

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: 54.13  E-value: 2.10e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESET-VRDTLSNVLALNYPKKEIIIINDGSSDN-TAEIIYEMKQHHD-FKFVDLQVNRGKANALNEGVKHS 125
Cdd:cd04184   3 ISIVMPVYNTPEKyLREAIESVRAQTYPNWELCIADDASTDPeVKRVLKKYAAQDPrIKVVFREENGGISAATNSALELA 82

                        90       100       110
                ....*....|....*....|....*....|....*
gi 34369299 126 SYDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAV 160
Cdd:cd04184  83 TGEFVALLDHDDELAPHALYEVVKALNEHPDADLI 117
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 44-136 3.19e-08

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 54.74  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   44 DQIEGISFLLACYNESET----VRDTLS--NVLALNYpkkEIIIINDGSSDNTAEIIYEMKQHHDFKFVDLQVNR--GKA 115
Cdd:PRK10714   3 HPIKKVSVVIPVYNEQESlpelIRRTTAacESLGKEY---EILLIDDGSSDNSAEMLVEAAQAPDSHIVAILLNRnyGQH 79

                         90       100
                 ....*....|....*....|.
gi 34369299  116 NALNEGVKHSSYDYVMCLDAD 136
Cdd:PRK10714  80 SAIMAGFSHVTGDLIITLDAD 100
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 52-138 3.51e-08

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: 53.40  E-value: 3.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  52 LLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMKQHHDF--KFVDLQVNRGKANALNEGVKHSSYDY 129
Cdd:cd04196   3 LMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFiiILIRNGKNLGVARNFESLLQAADGDY 82


                ....*....
gi 34369299 130 VMCLDADTI 138
Cdd:cd04196  83 VFFCDQDDI 91
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 50-216 3.86e-08

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 53.93  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   50 SFLLACYNESETV-------RDTLSNVlalnyPKKEIIIINDGSSDNTAEIIYEMKQHHDFKFVDLQVNRGK---ANALN 119
Cdd:PLN02726  12 SIIVPTYNERLNIalivyliFKALQDV-----KDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKlglGTAYI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  120 EGVKHSSYDYVMCLDADTivnQDAPYYMMDNFKQDPKLGA--VTGNpRIRNKSSILGKIQTIEYASLIGCIKRSQSLAGA 197
Cdd:PLN02726  87 HGLKHASGDFVVIMDADL---SHHPKYLPSFIKKQRETGAdiVTGT-RYVKGGGVHGWDLRRKLTSRGANVLAQTLLWPG 162

                        170
                 ....*....|....*....
gi 34369299  198 INTISGVFTLFKKSALKEV 216
Cdd:PLN02726 163 VSDLTGSFRLYKRSALEDL 181
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 49-139 4.01e-08

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 54.67  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299   49 ISFLLACYNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMKQHH-DFKFVDlQVNRGKANALNEGVKHSSY 127
Cdd:PRK10073   8 LSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYpHVRLLH-QANAGVSVARNTGLAVATG 86

                         90
                 ....*....|..
gi 34369299  128 DYVMCLDADTIV 139
Cdd:PRK10073  87 KYVAFPDADDVV 98
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 49-143 5.21e-08

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: 53.45  E-value: 5.21e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  49 ISFLLACYNESETVRDTLSNVLALnypKKEIIIINDGSSDNTAEIIYEMKQH-HDFKFvdlqvnRGKANALNEGVKHSSY 127
Cdd:cd02511   2 LSVVIITKNEERNIERCLESVKWA---VDEIIVVDSGSTDRTVEIAKEYGAKvYQRWW------DGFGAQRNFALELATN 72

                        90
                ....*....|....*.
gi 34369299 128 DYVMCLDADTIVNQDA 143
Cdd:cd02511  73 DWVLSLDADERLTPEL 88
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 56-142 5.62e-08

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: 52.19  E-value: 5.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  56 YNESETVRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMKQHHDFKFVDL-QVNRG--KANALNEGVKHSSYDYVMC 132
Cdd:cd06420   6 YNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIPIKHVwQEDEGfrKAKIRNKAIAAAKGDYLIF 85

                        90
                ....*....|
gi 34369299 133 LDADTIVNQD 142
Cdd:cd06420  86 IDGDCIPHPD 95
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 56-136 5.02e-07

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: 50.22  E-value: 5.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299  56 YNESETVRDTLSNVLALNYPKK-EIIIINDGSSDNTAEIIYEMKQHHDFKFVDLQVN-RGKANALNEGVKHSSYDYVMCL 133
Cdd:cd06442   6 YNERENIPELIERLDAALKGIDyEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGkRGLGSAYIEGFKAARGDVIVVM 85


                ...
gi 34369299 134 DAD 136
Cdd:cd06442  86 DAD 88
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 50-142 2.87e-05

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: 45.35  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34369299    50 SFLLACYNESET--VRDTLSNVLALNYPKKEIIIINDGSSDNTAEIIYEMKQH--HDFKFVDLQVNRGKANALNEGVKHS 125
Cdd:pfam10111   1 SVVIPVYNGEKThwIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHnlQVYYPNAPDTTYSLAASRNRGTSHA 80

                          90
                  ....*....|....*..
gi 34369299   126 SYDYVMCLDADTIVNQD 142
Cdd:pfam10111  81 IGEYISFIDGDCLWSPD 97
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
 125-177 1.75e-03

Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane.


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 39.95  E-value: 1.75e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 34369299 125 SSYDYVMCLDADTIVNQDAPYYMMDNFKQDPKLGAVTGNPRIRNKSSILGKIQ 177
Cdd:cd04191  94 SRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGAETLFARLQ 146
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
 77-136 3.53e-03

Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative glucosyltransferases,


Pssm-ID: 433416 [Multi-domain]  Cd Length: 97  Bit Score: 36.45  E-value: 3.53e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34369299    77 KEIIIINDGSSDNTAEIIYEMKQ------HHDFKFVDLQVNRgkANALNEGVKHssYDYVMCLDAD 136
Cdd:pfam13704  20 DHIYVYDNGSDDGTAEILARLPDvsilrsDLSYKDARFQVDW--RNALLARYAE--ADWVLVVDAD 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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