NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|375366694|gb|EHS70680|]
View 

poly-beta-1,6 N-acetyl-D-glucosamine synthase [Staphylococcus aureus subsp. aureus IS-125]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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: 707.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694    3 FFNFLLFYPVFMSIYWIVGSIYFYFTREIRYSLNKKPDINVDELEGITFLLACYNESETIEDTLSNVLALKYEKKEIIII 82
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWPLPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   83 NDGSSDNTAELIYKIKENND-FIFVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKHDPKLGAVT 161
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPrLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  162 GNPRIRNKSSILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRI 241
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  242 KYEPLAMCWMLVPETLGGLWKQRVRWAQGGHEVLLRDFFSTMKTKRFPLYILMFEQIISILWVYIVLLYLGYLFITANFL 321
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  322 DYTFMTYSFSIFLLSSFTMTFINVIQFTVALFIDSRYEKKNMAGLIFVSWYPTVYWIINAAVVLVAFPKALKRKKGGYAT 401
Cdd:TIGR03937 321 PYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRAV 400

                  ....*..
gi 375366694  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: 707.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694    3 FFNFLLFYPVFMSIYWIVGSIYFYFTREIRYSLNKKPDINVDELEGITFLLACYNESETIEDTLSNVLALKYEKKEIIII 82
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWPLPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   83 NDGSSDNTAELIYKIKENND-FIFVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKHDPKLGAVT 161
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPrLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  162 GNPRIRNKSSILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRI 241
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  242 KYEPLAMCWMLVPETLGGLWKQRVRWAQGGHEVLLRDFFSTMKTKRFPLYILMFEQIISILWVYIVLLYLGYLFITANFL 321
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  322 DYTFMTYSFSIFLLSSFTMTFINVIQFTVALFIDSRYEKKNMAGLIFVSWYPTVYWIINAAVVLVAFPKALKRKKGGYAT 401
Cdd:TIGR03937 321 PYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRAV 400

                  ....*..
gi 375366694  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 5.58e-70

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: 218.64  E-value: 5.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  52 LLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELI--YKIKENNDFIFVDLQENRGKANALNQGIKQASYDY 129
Cdd:cd06423    2 IVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILeeLAALYIRRVLVVRDKENGGKAGALNAGLRHAKGDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 130 VMCLDADTIVDQDAPYYMIENFKHDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLF 208
Cdd:cd06423   82 VVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSeNLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAF 161
                        170
                 ....*....|....*....
gi 375366694 209 KKSAVVDVGYWDTDMITED 227
Cdd:cd06423  162 RREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
16-348 5.22e-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: 196.89  E-value: 5.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  16 IYWIVGSIYFYFTREIRYSLNKKPDinvdELEGITFLLACYNESETIEDTLSNVLALKY--EKKEIIIINDGSSDNTAEL 93
Cdd:COG1215    2 LLLLALLALLYLLLLALARRRRAPA----DLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  94 IYKIKENNDFI-FVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKhDPKLGAvtgnprirnkssi 172
Cdd:COG1215   78 ARELAAEYPRVrVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGA------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 173 lgkiqtieyasligcikrsqtlagavntiSGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIKYEPLAMCWML 252
Cdd:COG1215  144 -----------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 253 VPETLGGLWKQRVRWAQGGHEVLLRdFFSTMKTKRFPLYILMFeqIISILWVYIVL-LYLGYLFITANFLDYTFMTYSFS 331
Cdd:COG1215  195 APETLRALFRQRRRWARGGLQLLLK-HRPLLRPRRLLLFLLLL--LLPLLLLLLLLaLLALLLLLLPALLLALLLALRRR 271
                        330
                 ....*....|....*..
gi 375366694 332 IFLLSSFTMTFINVIQF 348
Cdd:COG1215  272 RLLLPLLHLLYGLLLLL 288
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
50-213 2.06e-31

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: 117.50  E-value: 2.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   50 TFLLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKI-KENNDFIFVDLQENRGKANALNQGIKQASYD 128
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYaKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  129 YVMCLDADTIVDQDAPYYMIENFKHDPKlGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLF 208
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA-DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159

                  ....*
gi 375366694  209 KKSAV 213
Cdd:pfam00535 160 RREAL 164
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-142 2.81e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 61.32  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   7 LLFYPVfmsIYW---------IVGSIYFYFTREIRYSLNKKPDINVDELEgITFLLACYNESETIEDTLSNVLA-----L 72
Cdd:PTZ00260  25 LLFYPY---ISWpdddkvirqVKSSVIHEKSKEVDKENYINNILKDSDVD-LSIVIPAYNEEDRLPKMLKETIKylesrS 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375366694  73 KYEKK---EIIIINDGSSDNTAEL-----IYKIKENNDFIFVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQD 142
Cdd:PTZ00260 101 RKDPKfkyEIIIVNDGSKDKTLKVakdfwRQNINPNIDIRLLSLLRNKGKGGAVRIGMLASRGKYILMVDADGATDID 178
 
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: 707.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694    3 FFNFLLFYPVFMSIYWIVGSIYFYFTREIRYSLNKKPDINVDELEGITFLLACYNESETIEDTLSNVLALKYEKKEIIII 82
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWPLPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   83 NDGSSDNTAELIYKIKENND-FIFVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKHDPKLGAVT 161
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPrLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  162 GNPRIRNKSSILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRI 241
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  242 KYEPLAMCWMLVPETLGGLWKQRVRWAQGGHEVLLRDFFSTMKTKRFPLYILMFEQIISILWVYIVLLYLGYLFITANFL 321
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIL 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  322 DYTFMTYSFSIFLLSSFTMTFINVIQFTVALFIDSRYEKKNMAGLIFVSWYPTVYWIINAAVVLVAFPKALKRKKGGYAT 401
Cdd:TIGR03937 321 PYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRAV 400

                  ....*..
gi 375366694  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 5.58e-70

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: 218.64  E-value: 5.58e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  52 LLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELI--YKIKENNDFIFVDLQENRGKANALNQGIKQASYDY 129
Cdd:cd06423    2 IVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILeeLAALYIRRVLVVRDKENGGKAGALNAGLRHAKGDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 130 VMCLDADTIVDQDAPYYMIENFKHDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLF 208
Cdd:cd06423   82 VVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSeNLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGAF 161
                        170
                 ....*....|....*....
gi 375366694 209 KKSAVVDVGYWDTDMITED 227
Cdd:cd06423  162 RREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
16-348 5.22e-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: 196.89  E-value: 5.22e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  16 IYWIVGSIYFYFTREIRYSLNKKPDinvdELEGITFLLACYNESETIEDTLSNVLALKY--EKKEIIIINDGSSDNTAEL 93
Cdd:COG1215    2 LLLLALLALLYLLLLALARRRRAPA----DLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  94 IYKIKENNDFI-FVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKhDPKLGAvtgnprirnkssi 172
Cdd:COG1215   78 ARELAAEYPRVrVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGA------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 173 lgkiqtieyasligcikrsqtlagavntiSGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIKYEPLAMCWML 252
Cdd:COG1215  144 -----------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEE 194
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 253 VPETLGGLWKQRVRWAQGGHEVLLRdFFSTMKTKRFPLYILMFeqIISILWVYIVL-LYLGYLFITANFLDYTFMTYSFS 331
Cdd:COG1215  195 APETLRALFRQRRRWARGGLQLLLK-HRPLLRPRRLLLFLLLL--LLPLLLLLLLLaLLALLLLLLPALLLALLLALRRR 271
                        330
                 ....*....|....*..
gi 375366694 332 IFLLSSFTMTFINVIQF 348
Cdd:COG1215  272 RLLLPLLHLLYGLLLLL 288
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
37-271 1.12e-40

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: 144.65  E-value: 1.12e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  37 KKPDINVDE--LEGITFLLACYNESETIEDTLSNVLALKY--EKKEIIIINDGSSDNTAELIYKIKENNdFIFVDLQENR 112
Cdd:cd06439   17 PKPPSLPDPayLPTVTIIIPAYNEEAVIEAKLENLLALDYprDRLEIIVVSDGSTDGTAEIAREYADKG-VKLLRFPERR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 113 GKANALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKhDPKLGAVTGNPRIRNKssilGKIQTIE--YASLIGCIKR 190
Cdd:cd06439   96 GKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHFA-DPSVGAVSGELVIVDG----GGSGSGEglYWKYENWLKR 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 191 SQTLAGAVNTISGVFTLFKKSAVVDvgyWDTDMITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQG 270
Cdd:cd06439  171 AESRLGSTVGANGAIYAIRRELFRP---LPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVRIAAG 247

                 .
gi 375366694 271 G 271
Cdd:cd06439  248 N 248
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
52-275 9.20e-36

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: 131.16  E-value: 9.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  52 LLACYNES-ETIEDTLSNVLALKY--EKKEIIIINDGSSDNTAELIYKIKENNDFIFVDLQENRG-KANALNQGIKQASY 127
Cdd:cd06421    6 FIPTYNEPlEIVRKTLRAALAIDYphDKLRVYVLDDGRRPELRALAAELGVEYGYRYLTRPDNRHaKAGNLNNALAHTTG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 128 DYVMCLDADTIVDQD-----APYymienFKHDPKLGAVTGNPRIRNKSSILGKIQTIEYASLI--GCIKRSQTLAGAVnT 200
Cdd:cd06421   86 DFVAILDADHVPTPDflrrtLGY-----FLDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELfyGVIQPGRDRWGAA-F 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375366694 201 ISGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQGGHEVL 275
Cdd:cd06421  160 CCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
50-213 2.06e-31

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: 117.50  E-value: 2.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   50 TFLLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKI-KENNDFIFVDLQENRGKANALNQGIKQASYD 128
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYaKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  129 YVMCLDADTIVDQDAPYYMIENFKHDPKlGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLF 208
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGA-DVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159

                  ....*
gi 375366694  209 KKSAV 213
Cdd:pfam00535 160 RREAL 164
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
49-245 4.26e-31

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 117.88  E-value: 4.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITFLLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENNDFI-FVDLQENRGKANALNQGIKQASY 127
Cdd:COG0463    4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIrVIRLERNRGKGAARNAGLAAARG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 128 DYVMCLDADtivDQDAPYY---MIENFKHDPkLGAVTGNPRIRNkssilGKIQTIEYASLIGCIKRsqtLAGAVNTISGV 204
Cdd:COG0463   84 DYIAFLDAD---DQLDPEKleeLVAALEEGP-ADLVYGSRLIRE-----GESDLRRLGSRLFNLVR---LLTNLPDSTSG 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 375366694 205 FTLFKKSAVVDVGY-----WDTDMItediavswKLHLRGYRIKYEP 245
Cdd:COG0463  152 FRLFRREVLEELGFdegflEDTELL--------RALRHGFRIAEVP 189
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
55-165 8.70e-28

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: 107.59  E-value: 8.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  55 CYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENND-FIFVDLQENRGKANALNQGIKQASYDYVMCL 133
Cdd:cd00761    5 AYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPrVIRVINEENQGLAAARNAGLKAARGEYILFL 84
                         90       100       110
                 ....*....|....*....|....*....|..
gi 375366694 134 DADTIVDQDAPYYMIENFKHDPKLGAVTGNPR 165
Cdd:cd00761   85 DADDLLLPDWLERLVAELLADPEADAVGGPGN 116
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
52-270 1.65e-26

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: 106.22  E-value: 1.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  52 LLACYNESETIEDTLSNVLALKY--EKKEIIIINDGSSDNTAELIYKIKENNDF----IFVDLQENRGKANALNQGIKQA 125
Cdd:cd04192    2 VIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAKPNFqlkiLNNSRVSISGKKNALTTAIKAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 126 SYDYVMCLDADTIVDQD-APYYMIENFKHDPKL--GAVTGnpriRNKSSILGKIQTIEYASLIGCIKrSQTLAGAVNTIS 202
Cdd:cd04192   82 KGDWIVTTDADCVVPSNwLLTFVAFIQKEQIGLvaGPVIY----FKGKSLLAKFQRLDWLSLLGLIA-GSFGLGKPFMCN 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 375366694 203 GVFTLFKKSAVVDVGYWDT--DMITED----IAvswKLHLRGYRIKYE--PLAMCWMLVPETLGGLWKQRVRWAQG 270
Cdd:cd04192  157 GANMAYRKEAFFEVGGFEGndHIASGDdellLA---KVASKYPKVAYLknPEALVTTQPVTSWKELLNQRKRWASK 229
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
49-271 9.92e-26

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: 103.93  E-value: 9.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITFLLACYNESETIEDTLSNVLALKYEKKEIII-INDGSSDNTAELIYKIKEN-----NDFIFVDLQENRG-KANALNQG 121
Cdd:cd06437    3 VTVQLPVFNEKYVVERLIEAACALDYPKDRLEIqVLDDSTDETVRLAREIVEEyaaqgVNIKHVRRADRTGyKAGALAEG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 122 IKQASYDYVMCLDADTIVDQD----APYYMienfkHDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQTLAG 196
Cdd:cd06437   83 MKVAKGEYVAIFDADFVPPPDflqkTPPYF-----ADPKLGFVQTRWGHINANySLLTRVQAMSLDYHFTIEQVARSSTG 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375366694 197 AVNTISGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQGG 271
Cdd:cd06437  158 LFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
56-250 2.62e-24

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: 98.40  E-value: 2.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  56 YNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKikENNDFIFVDLQENRGKANALNQGIKQASYDYVMCLDA 135
Cdd:cd04186    6 YNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRE--LFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLLNP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 136 DTIVDQDAPYYMIENFKHDPKLGAVTGnprirnkssilgkiqtieyasligcikrsqtlagavnTISGVFTLFKKSAVVD 215
Cdd:cd04186   84 DTVVEPGALLELLDAAEQDPDVGIVGP-------------------------------------KVSGAFLLVRREVFEE 126
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 375366694 216 VGYWDTD--MITEDIAVSWKLHLRGYRIKYEPLAMCW 250
Cdd:cd04186  127 VGGFDEDffLYYEDVDLCLRARLAGYRVLYVPQAVIY 163
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
49-277 3.31e-24

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: 100.38  E-value: 3.31e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITFLLACYNESETIEDTLSNVLALKYEKK--EIIIINDGSSDNTAELIYKIKENNDFIFVDLQENRGKANALNQGIKQAS 126
Cdd:cd02525    2 VSIIIPVRNEEKYIEELLESLLNQSYPKDliEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDNPKRIQSAGLNIGIRNSR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 127 YDYVMCLDADTIVDQDapyYMIENFKHDPKLGA--VTGNPRIRNKSSilgKIQTIEYASL----IGCIKRSQTLAGAVNT 200
Cdd:cd02525   82 GDIIIRVDAHAVYPKD---YILELVEALKRTGAdnVGGPMETIGESK---FQKAIAVAQSsplgSGGSAYRGGAVKIGYV 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375366694 201 ISGVFTLFKKSAVVDVGYWDTDMIT-EDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQGGHEVLLR 277
Cdd:cd02525  156 DTVHHGAYRREVFEKVGGFDESLVRnEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRARTLRK 233
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
49-264 1.52e-23

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 97.37  E-value: 1.52e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITFLLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKeNNDFIFVDLQENRGKANALNQGIKQASYD 128
Cdd:COG1216    5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALA-FPRVRVIRNPENLGFAAARNLGLRAAGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 129 YVMCLDADTIVDQDApyymIENFkhdpklgavtgnprirnkssilgkiqtIEYASLigcikrsqtlagavntisgvftLF 208
Cdd:COG1216   84 YLLFLDDDTVVEPDW----LERL---------------------------LAAACL----------------------LI 110
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 375366694 209 KKSAVVDVGYWDTDMIT--EDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQR 264
Cdd:COG1216  111 RREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAY 168
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
129-316 4.62e-23

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: 95.48  E-value: 4.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  129 YVMCLDADTIVDQDAPYYmIENFKHDPKLGAVTGNPRIRNKSSILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFTLF 208
Cdd:pfam13632   1 WILLLDADTVLPPDCLLG-IANEMASPEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  209 KKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQGGHEVLL-RDFFSTMKTKR 287
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLiRLLGYLGTLLW 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 375366694  288 FPL---YILMFEQIISILWVYIVLLYLGYLFI 316
Cdd:pfam13632 160 SGLplaLLLLLLFSISSLALVLLLLALLAGLL 191
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
53-277 2.69e-22

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: 94.77  E-value: 2.69e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  53 LACYNES-ETIEDTLSNVLALKYEKKEIIIINDGSSDntaELIYKIKE------NNDFIFVDLQENRG-KANALNQGIKQ 124
Cdd:cd06435    4 VPCYEEPpEMVKETLDSLAALDYPNFEVIVIDNNTKD---EALWKPVEahcaqlGERFRFFHVEPLPGaKAGALNYALER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 125 ASYD--YVMCLDADTIVDQDAPYYMIENFKhDPKLGAVTGNPRIRN-KSSILGKIQTIEYASL--IGCIKRSQTLAGAVN 199
Cdd:cd06435   81 TAPDaeIIAVIDADYQVEPDWLKRLVPIFD-DPRVGFVQAPQDYRDgEESLFKRMCYAEYKGFfdIGMVSRNERNAIIQH 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375366694 200 tisGVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQGGHEVLLR 277
Cdd:cd06435  160 ---GTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKK 234
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
49-271 1.09e-21

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: 93.09  E-value: 1.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITFLLACYNESETI-EDTLSNVLALKyeKKEIIIINDGSsDNTAELIYKIKENNDFIFVDLQENRGKANALNQGIKQASY 127
Cdd:cd06434    2 VTVIIPVYDEDPDVfRECLRSILRQK--PLEIIVVTDGD-DEPYLSILSQTVKYGGIFVITVPHPGKRRALAEGIRHVTT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 128 DYVMCLDADTIVDQDAPYYMIENFKhDPKLGAVTGNPRIRNK-SSILGKIQTIEYASLIGCIKRSQTLAGAVNTISGVFT 206
Cdd:cd06434   79 DIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRPrDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRTA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 375366694 207 LFKKSAVVDVGY-WD----TDM-----ITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQGG 271
Cdd:cd06434  158 AYRTEILKDFLFlEEftneTFMgrrlnAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSN 232
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
49-270 4.81e-20

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: 88.20  E-value: 4.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   49 ITFLLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENNDFIFVDLQEN------RGKANALNQGI 122
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRLRVIRNarllgpTGKSRGLNHGF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  123 KQASYDYVMCLDADTIVDQDAPYYMIENFKHdPKLGAVTGNPRIRNKSSILGKIQTIEYAsLIGCIKRSQTLAGAVNTIS 202
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTPVFSLNRSTMLSALGALEFA-LRHLRMMSLRLALGVLPLS 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375366694  203 GVFTLFKKSAVVDVGYWDTDMI-TEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQG 270
Cdd:pfam13641 162 GAGSAIRREVLKELGLFDPFFLlGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
55-213 4.88e-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: 86.86  E-value: 4.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  55 CYNESETIEDTLSNVLALKYEKK--EIIIINDGSSDNTAELIYKI-KENNDFIFVDLQENRGKANALNQGIKQASYDYVM 131
Cdd:cd04179    5 AYNEEENIPELVERLLAVLEEGYdyEIIVVDDGSTDGTAEIARELaARVPRVRVIRLSRNFGKGAAVRAGFKAARGDIVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 132 CLDADtivDQDAPYY---MIENFKHDpklGA--VTGNPRIRNKSSILGKIQtieyasLIGcikrSQTLAGAVNTISGV-- 204
Cdd:cd04179   85 TMDAD---LQHPPEDipkLLEKLLEG---GAdvVIGSRFVRGGGAGMPLLR------RLG----SRLFNFLIRLLLGVri 148
                        170
                 ....*....|....*
gi 375366694 205 ------FTLFKKSAV 213
Cdd:cd04179  149 sdtqsgFRLFRREVL 163
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
52-267 4.33e-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: 83.13  E-value: 4.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  52 LLACYNESET-IEDTLSNVLALKY----------EKKEIIIINDGssdntaelIYKIkenndfifvdlqeNRGKAN---- 116
Cdd:cd04190    2 CVTMYNEDEEeLARTLDSILKNDYpfcarggdswKKIVVCVIFDG--------AIKK-------------NRGKRDsqlw 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 117 ---ALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKHDPKLGAVTGNPRIRNKS-SILGKIQTIEYASLIGCIKRSQ 192
Cdd:cd04190   61 ffnYFCRVLFPDDPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKqGPLVMYQVFEYAISHWLDKAFE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 193 TLAGAVNTISGVFTLFKKSAVVDV-GYW-------------DTDMIT------EDIAVSWKLHLRGYRIK--YEPLAMCW 250
Cdd:cd04190  141 SVFGFVTCLPGCFSMYRIEALKGDnGGKgplldyayltntvDSLHKKnnldlgEDRILCTLLLKAGPKRKylYVPGAVAE 220
                        250
                 ....*....|....*..
gi 375366694 251 MLVPETLGGLWKQRVRW 267
Cdd:cd04190  221 TDVPETFVELLSQRRRW 237
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
55-136 4.40e-17

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: 79.53  E-value: 4.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  55 CYNESETIEDTLSNVLALKYEKK----EIIIINDGSSDNTAELIYKIKENNDFIF--VDLQENRGKANALNQGIKQASYD 128
Cdd:cd04188    5 AYNEEKRLPPTLEEAVEYLEERPsfsyEIIVVDDGSKDGTAEVARKLARKNPALIrvLTLPKNRGKGGAVRAGMLAARGD 84

                 ....*...
gi 375366694 129 YVMCLDAD 136
Cdd:cd04188   85 YILFADAD 92
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
55-151 1.01e-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: 77.52  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  55 CYNESETIEDT---LSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENNDFI-FVDLQENRGKANALNQGIKQASYDYV 130
Cdd:cd04187    5 VYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVkVIRLSRNFGQQAALLAGLDHARGDAV 84
                         90       100
                 ....*....|....*....|.
gi 375366694 131 MCLDADTivdQDAPyYMIENF 151
Cdd:cd04187   85 ITMDADL---QDPP-ELIPEM 101
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
114-268 2.18e-16

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: 76.55  E-value: 2.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  114 KANALNQGIKQASYDYVMCLDADTIVDQDAPYYMIENFKhDPKLGAVTGNPRIRNKSSILGkiqTIEYASLIGCIKRSQT 193
Cdd:pfam13506  18 KVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLA-DPKVGLVTSPPVGSDPKGLAA---ALEAAFFNTLAGVLQA 93
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 375366694  194 LAGAVNTISGVFTLFKKSAVVDVGYWDT--DMITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPE--TLGGLWKQRVRWA 268
Cdd:pfam13506  94 ALSGIGFAVGMSMAFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFRAFMARQLRWA 172
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
51-227 1.74e-14

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: 71.65  E-value: 1.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  51 FLLACYNESETIEDTLSNVLALKyEKKEIIIINDGSSDNTAELIYKIKENNDFIFV--DLQENR-GKANALNQGIKQ--- 124
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNK-PNFLVLVIDDASDDDTAGIVRLAITDSRVHLLrrHLPNARtGKGDALNAAYDQirq 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 125 --------ASYDYVMCLDADTIVDQDApYYMIENFKHDPKLGAVTGNPRIRNK-SSILGKIQTIEYASLIGCIKRSQTLA 195
Cdd:cd06436   80 ilieegadPERVIIAVIDADGRLDPNA-LEAVAPYFSDPRVAGTQSRVRMYNRhKNLLTILQDLEFFIIIAATQSLRALT 158
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 375366694 196 GAVnTISGVFTLFKKSAVVDV---GYWdTDMITED 227
Cdd:cd06436  159 GTV-GLGGNGQFMRLSALDGLigeEPW-SDSLLED 191
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
49-169 1.41e-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: 69.11  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITfllACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENNDFIFVdlQENRGKANALNQGIKQASYD 128
Cdd:cd06433    3 IT---PTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWIS--EPDKGIYDAMNKGIALATGD 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 375366694 129 YVMCLDADTIVDQDAPYYMIENFKHDPKLGAVTGNPRIRNK 169
Cdd:cd06433   78 IIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDE 118
Chitin_synth_2 pfam03142
Chitin synthase; Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They ...
121-318 3.39e-13

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: 70.94  E-value: 3.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  121 GIKQASYDYVMCLDADTIVDQDAPYYMIENFKHDPKLGAVTGNPRIRNK-SSILGKIQTIEYASLIGCIKRSQTLAGAVN 199
Cdd:pfam03142 196 GVSPDFYEYVLMVDADTKVFPDSLTRMVACMVDDPEIMGLCGETKIANKrQSWVTAIQVFEYYISHHLSKAFESVFGGVT 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  200 TISGVFTLFK-KSAVVDVGYWDTDMITEDIA------VSWKLHLRG--------------------YRIKYEPLAMCWML 252
Cdd:pfam03142 276 CLPGCFSMYRiKAPKGGDGYWVPILASPDIVehysenVVDTLHKKNllllgedrylttlmlktfpkRKTVFVPQAVCKTI 355
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 375366694  253 VPETLGGLWKQRVRWAQGG-HE----VLLRDFFSTMKtkrFPLYILMFEQIISILWVYIVLLYLGYLFITA 318
Cdd:pfam03142 356 APDTFKVLLSQRRRWINSTvHNlmelVLVRDLCGTFC---FSMQFVVFIELIGTVVLPAAIAFTVYLIVIS 423
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
61-241 9.35e-13

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: 67.31  E-value: 9.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  61 TIEDTLSNVLALKYEKKEIIIInDGSSDNTAElIYKIKENNDFIFVDLQENRGKANALNQGIKQA---SYDYVMCLDADT 137
Cdd:cd02526    9 DLSKLKELLAALAEQVDKVVVV-DNSSGNDIE-LRLRLNSEKIELIHLGENLGIAKALNIGIKAAlenGADYVLLFDQDS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 138 IVDQDapyyMIENFKH-------DPKLGAVTgnPRI--RNKSSILGKIQTIEYASLI------GCIKRSQTLAgavntiS 202
Cdd:cd02526   87 VPPPD----MVEKLLAykilsdkNSNIGAVG--PRIidRRTGENSPGVRKSGYKLRIqkegeeGLKEVDFLIT------S 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 375366694 203 GvfTLFKKSAVVDVGYWDTDMITE--DIAVSWKLHLRGYRI 241
Cdd:cd02526  155 G--SLISLEALEKVGGFDEDLFIDyvDTEWCLRARSKGYKI 193
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
49-270 3.89e-12

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: 65.74  E-value: 3.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITFLLACYNESETIEDTLSNVLALKY--EKKEIIIINDGSSDNTAELI--YKIKENNDFIFVDLQENRGKANALNQGIKQ 124
Cdd:cd06427    3 YTILVPLYKEAEVLPQLIASLSALDYprSKLDVKLLLEEDDEETIAAAraLRLPSIFRVVVVPPSQPRTKPKACNYALAF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 125 ASYDYVMCLDADTIVDQDAPYYMIENF-KHDPKLGAVTGNPRIRNKSS-ILGKIQTIEYASLIGCIKRSQTLAGAVNTIS 202
Cdd:cd06427   83 ARGEYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPLNYYNAREnWLTRMFALEYAAWFDYLLPGLARLGLPIPLG 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375366694 203 GVFTLFKKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIK------YEPlamcwmlVPETLGGLWKQRVRWAQG 270
Cdd:cd06427  163 GTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGvlnsttLEE-------ANNALGNWIRQRSRWIKG 229
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
56-238 3.05e-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: 62.59  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  56 YNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIykikenNDFIFVDLQENRGKANALNQGIKQASYDYVMCLDA 135
Cdd:cd02522    8 LNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIA------RSAGVVVISSPKGRARQMNAGAAAARGDWLLFLHA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 136 DTIVDQDAPYYMIENFkHDPKLGAVTGNPRIRNKSSILgkiQTIEYAS-----LIGCIKRSQTLagavntisgvftLFKK 210
Cdd:cd02522   82 DTRLPPDWDAAIIETL-RADGAVAGAFRLRFDDPGPRL---RLLELGAnlrsrLFGLPYGDQGL------------FIRR 145
                        170       180
                 ....*....|....*....|....*...
gi 375366694 211 SAVVDVGYWDTDMITEDIAVSWKLHLRG 238
Cdd:cd02522  146 ELFEELGGFPELPLMEDVELVRRLRRRG 173
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
51-229 6.11e-11

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: 61.08  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  51 FLLACYNESETIEDTLSNVLALKY--EKKEIIIINDGSSDNTAEL-------IYkikENNDfifvdlQENRGKANALNQG 121
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYprELYRIFVVADNCTDDTAQVaraagatVL---ERHD------PERRGKGYALDFG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 122 IKQA-----SYDYVMCLDADTIVDQDApyymIENFKHDPKLGA--VTGNPRIRN-KSSILGKIQTIEYASLIGCIKRSQT 193
Cdd:cd06438   72 FRHLlnladDPDAVVVFDADNLVDPNA----LEELNARFAAGArvVQAYYNSKNpDDSWITRLYAFAFLVFNRLRPLGRS 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 375366694 194 LAGAVNTISGVFTLFKKSAVVDVGyWDTDMITEDIA 229
Cdd:cd06438  148 NLGLSCQLGGTGMCFPWAVLRQAP-WAAHSLTEDLE 182
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
55-143 1.29e-10

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: 61.15  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  55 CYNESETIEDTLSNVLALKyekKEIIIINDGSSDNTAELIykiKENNDFIFVdlQENRGKANALNQGIKQASYDYVMCLD 134
Cdd:cd02511    8 TKNEERNIERCLESVKWAV---DEIIVVDSGSTDRTVEIA---KEYGAKVYQ--RWWDGFGAQRNFALELATNDWVLSLD 79

                 ....*....
gi 375366694 135 ADTIVDQDA 143
Cdd:cd02511   80 ADERLTPEL 88
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
56-143 2.77e-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: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  56 YNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENNDFIFVDLQENRGKANALNQGIKQAS---YDYVMC 132
Cdd:cd04185    6 YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDNIVYLRLPENLGGAGGFYEGVRRAYelgYDWIWL 85
                         90
                 ....*....|.
gi 375366694 133 LDADTIVDQDA 143
Cdd:cd04185   86 MDDDAIPDPDA 96
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
7-142 2.81e-10

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 61.32  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   7 LLFYPVfmsIYW---------IVGSIYFYFTREIRYSLNKKPDINVDELEgITFLLACYNESETIEDTLSNVLA-----L 72
Cdd:PTZ00260  25 LLFYPY---ISWpdddkvirqVKSSVIHEKSKEVDKENYINNILKDSDVD-LSIVIPAYNEEDRLPKMLKETIKylesrS 100
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 375366694  73 KYEKK---EIIIINDGSSDNTAEL-----IYKIKENNDFIFVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQD 142
Cdd:PTZ00260 101 RKDPKfkyEIIIVNDGSKDKTLKVakdfwRQNINPNIDIRLLSLLRNKGKGGAVRIGMLASRGKYILMVDADGATDID 178
PRK10073 PRK10073
putative glycosyl transferase; Provisional
54-140 4.82e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 57.36  E-value: 4.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  54 ACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENNDFIFVDLQENRGKANALNQGIKQASYDYVMCL 133
Cdd:PRK10073  13 PLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQANAGVSVARNTGLAVATGKYVAFP 92

                 ....*..
gi 375366694 134 DADTIVD 140
Cdd:PRK10073  93 DADDVVY 99
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
52-138 1.06e-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: 54.94  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  52 LLACYNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELI--YKIKENNDFIFVDLQENRGKANALNQGIKQASYDY 129
Cdd:cd04196    3 LMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIkeYIDKDPFIIILIRNGKNLGVARNFESLLQAADGDY 82

                 ....*....
gi 375366694 130 VMCLDADTI 138
Cdd:cd04196   83 VFFCDQDDI 91
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
43-136 9.06e-08

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 53.59  E-value: 9.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  43 VDELEGITFLLACYNESET----IEDTLS--NVLALKYEkkeIIIINDGSSDNTAELIYKIKE--NNDFIFVDLQENRGK 114
Cdd:PRK10714   2 IHPIKKVSVVIPVYNEQESlpelIRRTTAacESLGKEYE---ILLIDDGSSDNSAEMLVEAAQapDSHIVAILLNRNYGQ 78
                         90       100
                 ....*....|....*....|..
gi 375366694 115 ANALNQGIKQASYDYVMCLDAD 136
Cdd:PRK10714  79 HSAIMAGFSHVTGDLIITLDAD 100
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
49-160 1.37e-07

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: 51.43  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  49 ITFLLACYNESET-IEDTLSNVLALKYEKKEIIIINDGSSDN-TAELIYKIKENNDFIFVD-LQENRGKANALNQGIKQA 125
Cdd:cd04184    3 ISIVMPVYNTPEKyLREAIESVRAQTYPNWELCIADDASTDPeVKRVLKKYAAQDPRIKVVfREENGGISAATNSALELA 82
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 375366694 126 SYDYVMCLDADTIVDQDAPYYMIENFKHDPKLGAV 160
Cdd:cd04184   83 TGEFVALLDHDDELAPHALYEVVKALNEHPDADLI 117
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
78-240 1.46e-07

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: 51.55  E-value: 1.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  78 EIIIINDGS-SDNTAELIYKIKENNDFIFVDLQENRGKANALNQGIKQASYDYVMCLDADTIVDQD-----APYYM---- 147
Cdd:cd04195   31 EVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCTYDWVARMDTDDISLPDrfekqLDFIEknpe 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 148 -------IENFKHDPKLGAVTGNPRIRNKssilgkiqTIEYAsligcIKRSQTLAGAVntisgvftLFKKSAVVDVGYWD 220
Cdd:cd04195  111 idivgggVLEFDSDGNDIGKRRLPTSHDD--------ILKFA-----RRRSPFNHPTV--------MFRKSKVLAVGGYQ 169
                        170       180
                 ....*....|....*....|
gi 375366694 221 TDMITEDIAVSWKLHLRGYR 240
Cdd:cd04195  170 DLPLVEDYALWARMLANGAR 189
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
56-156 1.58e-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: 51.77  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  56 YNESETIEDTLSNVLA-LKYEKKEIIIINDGSSDNTAELIYKIKENNDFIFVDL-QENRGKANALNQGIKQASYDYVMCL 133
Cdd:cd06442    6 YNERENIPELIERLDAaLKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVrPGKRGLGSAYIEGFKAARGDVIVVM 85
                         90       100
                 ....*....|....*....|...
gi 375366694 134 DADtivdqdapyymienFKHDPK 156
Cdd:cd06442   86 DAD--------------LSHPPE 94
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
56-142 1.67e-07

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: 51.04  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  56 YNESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKEnnDFIFvDL----QENRG--KANALNQGIKQASYDY 129
Cdd:cd06420    6 YNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKS--QFPI-PIkhvwQEDEGfrKAKIRNKAIAAAKGDY 82
                         90
                 ....*....|...
gi 375366694 130 VMCLDADTIVDQD 142
Cdd:cd06420   83 LIFIDGDCIPHPD 95
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
58-142 5.06e-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: 44.58  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   58 ESETIEDTLSNVLALKYEKKEIIIINDGSSDNTAELIYKIKENNDFIFV--DLQENRGKANALNQGIKQASYDYVMCLDA 135
Cdd:pfam10111  11 KTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYpnAPDTTYSLAASRNRGTSHAIGEYISFIDG 90

                  ....*..
gi 375366694  136 DTIVDQD 142
Cdd:pfam10111  91 DCLWSPD 97
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
56-216 5.42e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 44.30  E-value: 5.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  56 YNESETIedTLSNVLALKYEKK----EIIIINDGSSDNTAELIYKIKENNDFIFVDLQENRGK---ANALNQGIKQASYD 128
Cdd:PLN02726  18 YNERLNI--ALIVYLIFKALQDvkdfEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPRPGKlglGTAYIHGLKHASGD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 129 YVMCLDADTivdQDAPYYMIENFKHDPKLGA--VTGNpRIRNKSSILG-----KIqTIEYASLIgcikrSQTLAGA-VNT 200
Cdd:PLN02726  96 FVVIMDADL---SHHPKYLPSFIKKQRETGAdiVTGT-RYVKGGGVHGwdlrrKL-TSRGANVL-----AQTLLWPgVSD 165
                        170
                 ....*....|....*.
gi 375366694 201 ISGVFTLFKKSAVVDV 216
Cdd:PLN02726 166 LTGSFRLYKRSALEDL 181
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
56-142 5.06e-04

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: 41.29  E-value: 5.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  56 YNESETIEDTLSNVLALKYEKK-EIIIINDGSSDNTAELIYKIK---ENNDFIFVDLQEN----RGKANALNQGIKQASY 127
Cdd:cd06913    6 HNGEQWLDECLESVLQQDFEGTlELSVFNDASTDKSAEIIEKWRkklEDSGVIVLVGSHNspspKGVGYAKNQAIAQSSG 85
                         90
                 ....*....|....*
gi 375366694 128 DYVMCLDADTIVDQD 142
Cdd:cd06913   86 RYLCFLDSDDVMMPQ 100
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
39-138 6.92e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.44  E-value: 6.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  39 PDINVDELEG------ITFLLACYNESETIEDTLSNVLALKYEK--KEIIIINDGSSDNTAEL-------IYkikeNNDF 103
Cdd:PRK13915  17 PDWTIEELVAakagrtVSVVLPALNEEETVGKVVDSIRPLLMEPlvDELIVIDSGSTDATAERaaaagarVV----SREE 92
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 375366694 104 IFVDLQENRGKANALNQGIKQASYDYVMCLDADTI 138
Cdd:PRK13915  93 ILPELPPRPGKGEALWRSLAATTGDIVVFVDADLI 127
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
127-177 1.79e-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: 1.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 375366694 127 YDYVMCLDADTIVDQDAPYYMIENFKHDPKLGAVTGNPRIRNKSSILGKIQ 177
Cdd:cd04191   96 YDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGAETLFARLQ 146
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
209-270 1.95e-03

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 40.39  E-value: 1.95e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 375366694 209 KKSAVVDVGYWDTDMITEDIAVSWKLHLRGYRIKY--EPLAMCwmLVPETLGGLWKQRVRWAQG 270
Cdd:PRK11498 426 RRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYmrIPQAAG--LATESLSAHIGQRIRWARG 487
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
65-269 3.01e-03

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 38.73  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694  65 TLSNVLALKYEKKEIIIINDGSSDNTAELIYK-IKENNDF---IFVDlQENRG---KANALNQGIKQASYDYVMCLDADT 137
Cdd:cd02520   19 NLESFFQQDYPKYEILFCVQDEDDPAIPVVRKlIAKYPNVdarLLIG-GEKVGinpKVNNLIKGYEEARYDILVISDSDI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694 138 IVDQDAPYYMIENFKhDPKLGAVTGNPrirnkssILGKiqtieyasliGCIKRSQTLAGAvntisGVFTLFKksavvdvg 217
Cdd:cd02520   98 SVPPDYLRRMVAPLM-DPGVGLVTCLC-------AFGK----------SMALRREVLDAI-----GGFEAFA-------- 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 375366694 218 ywdtDMITEDIAVSWKLHLRGYRIKYEPLAMCWMLVPETLGGLWKQRVRWAQ 269
Cdd:cd02520  147 ----DYLAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWSR 194
Glyco_tranf_2_4 pfam13704
Glycosyl transferase family 2; Members of this family of prokaryotic proteins include putative ...
56-136 4.73e-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: 4.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375366694   56 YNESETIEDTLSNVLALKYEkkEIIIINDGSSDNTAELiykIKENNDFIFVDLQENRGKA-------NALNQGIKQAsyD 128
Cdd:pfam13704   1 RNEADILPQWLAHHLALGFD--HIYVYDNGSDDGTAEI---LARLPDVSILRSDLSYKDArfqvdwrNALLARYAEA--D 73

                  ....*...
gi 375366694  129 YVMCLDAD 136
Cdd:pfam13704  74 WVLVVDAD 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH