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Conserved domains on  [gi|446533092|ref|WP_000610438|]
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MULTISPECIES: poly-beta-1,6-N-acetyl-D-glucosamine synthase [Enterobacteriaceae]

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 ...
30-437 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: 708.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   30 MMRFVFFWPFFMSIMWIIGGVYFWVYRERHWPwGENAPAPQLKDNPSISIIIPCFNEEKNVEETIHAALAQRYENIEVIA 109
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWP-LPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  110 VNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAV 189
Cdd:TIGR03937  80 INDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  190 TGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWT 269
Cdd:TIGR03937 160 TGNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  270 IFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRMWPLFFEYCLTTIWAFTCLVGFIIYAVQLAG 349
Cdd:TIGR03937 240 IRYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  350 VPLNIELTHIAATHTAGILLCTLCLLQFIVSLVIENRYEHNLASSLFWIIWFPVIFWMLSLATTLVSFTRVMLMPKKQRA 429
Cdd:TIGR03937 320 LPYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRA 399

                  ....*...
gi 446533092  430 RWVSPDRG 437
Cdd:TIGR03937 400 VWVSPDRG 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 ...
30-437 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: 708.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   30 MMRFVFFWPFFMSIMWIIGGVYFWVYRERHWPwGENAPAPQLKDNPSISIIIPCFNEEKNVEETIHAALAQRYENIEVIA 109
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWP-LPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  110 VNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAV 189
Cdd:TIGR03937  80 INDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  190 TGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWT 269
Cdd:TIGR03937 160 TGNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  270 IFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRMWPLFFEYCLTTIWAFTCLVGFIIYAVQLAG 349
Cdd:TIGR03937 240 IRYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  350 VPLNIELTHIAATHTAGILLCTLCLLQFIVSLVIENRYEHNLASSLFWIIWFPVIFWMLSLATTLVSFTRVMLMPKKQRA 429
Cdd:TIGR03937 320 LPYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRA 399

                  ....*...
gi 446533092  430 RWVSPDRG 437
Cdd:TIGR03937 400 VWVSPDRG 407
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
79-256 2.12e-67

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: 212.86  E-value: 2.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAA-QIPRLRVIHLAQNQGKAIALKTGAAAAKSE 157
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAAlYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 158 YLVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTGNPRIR-TRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAA 236
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRnGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGA 160
                        170       180
                 ....*....|....*....|
gi 446533092 237 FRRSALAEVGYWSDDMITED 256
Cdd:cd06423  161 FRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
39-344 2.12e-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: 198.81  E-value: 2.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  39 FFMSIMWIIGGVYFWVYRERHWPwgenapapqlKDNPSISIIIPCFNEEKNVEETIHAALAQRY--ENIEVIAVNDGSTD 116
Cdd:COG1215    3 LLLALLALLYLLLLALARRRRAP----------ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 117 KTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLyNPRVGAvtgnprir 196
Cdd:COG1215   73 ETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGA-------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 197 trstlvgkiqvgeyssiiglikrtqriygnvftvSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFYEPRA 276
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446533092 277 LCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRMW-----PLFFEYCLTTIWAFTCLVGFIIYA 344
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLlllllPLLLLLLLLALLALLLLLLPALLL 262
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
78-244 5.42e-42

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: 146.00  E-value: 5.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   78 SIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSE 157
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  158 YLVCIDGDALLDRDAAAYIVEPMLyNPRVGAVTGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAAF 237
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALE-EDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159

                  ....*..
gi 446533092  238 RRSALAE 244
Cdd:pfam00535 160 RREALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
75-169 3.76e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 87.79  E-value: 3.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  75 PSISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHlAQNQGKAIALKTGAAAA 154
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVA 84
                         90
                 ....*....|....*
gi 446533092 155 KSEYLVCIDGDALLD 169
Cdd:PRK10073  85 TGKYVAFPDADDVVY 99
 
Name Accession Description Interval E-value
PgaC_IcaA TIGR03937
poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are ...
30-437 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: 708.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   30 MMRFVFFWPFFMSIMWIIGGVYFWVYRERHWPwGENAPAPQLKDNPSISIIIPCFNEEKNVEETIHAALAQRYENIEVIA 109
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWP-LPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  110 VNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAV 189
Cdd:TIGR03937  80 INDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  190 TGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWT 269
Cdd:TIGR03937 160 TGNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWN 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  270 IFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRMWPLFFEYCLTTIWAFTCLVGFIIYAVQLAG 349
Cdd:TIGR03937 240 IRYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNI 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  350 VPLNIELTHIAATHTAGILLCTLCLLQFIVSLVIENRYEHNLASSLFWIIWFPVIFWMLSLATTLVSFTRVMLMPKKQRA 429
Cdd:TIGR03937 320 LPYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRA 399

                  ....*...
gi 446533092  430 RWVSPDRG 437
Cdd:TIGR03937 400 VWVSPDRG 407
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
79-256 2.12e-67

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: 212.86  E-value: 2.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAA-QIPRLRVIHLAQNQGKAIALKTGAAAAKSE 157
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAAlYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 158 YLVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTGNPRIR-TRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAA 236
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRnGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGA 160
                        170       180
                 ....*....|....*....|
gi 446533092 237 FRRSALAEVGYWSDDMITED 256
Cdd:cd06423  161 FRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
39-344 2.12e-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: 198.81  E-value: 2.12e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  39 FFMSIMWIIGGVYFWVYRERHWPwgenapapqlKDNPSISIIIPCFNEEKNVEETIHAALAQRY--ENIEVIAVNDGSTD 116
Cdd:COG1215    3 LLLALLALLYLLLLALARRRRAP----------ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTD 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 117 KTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLyNPRVGAvtgnprir 196
Cdd:COG1215   73 ETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGA-------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 197 trstlvgkiqvgeyssiiglikrtqriygnvftvSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFYEPRA 276
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446533092 277 LCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRMW-----PLFFEYCLTTIWAFTCLVGFIIYA 344
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKHRPLLRPRRLLLFLlllllPLLLLLLLLALLALLLLLLPALLL 262
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
78-244 5.42e-42

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: 146.00  E-value: 5.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   78 SIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSE 157
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  158 YLVCIDGDALLDRDAAAYIVEPMLyNPRVGAVTGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAAF 237
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALE-EDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159

                  ....*..
gi 446533092  238 RRSALAE 244
Cdd:pfam00535 160 RREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
74-261 1.72e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 146.39  E-value: 1.72e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  74 NPSISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAA 153
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 154 AKSEYLVCIDGDALLDRDAAAYIVEPMLYNPrVGAVTGNPRIRTRSTLvgkiqvgeYSSIIGLIKRTQRIYGNVFTVSGV 233
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLIREGESD--------LRRLGSRLFNLVRLLTNLPDSTSG 151
                        170       180
                 ....*....|....*....|....*...
gi 446533092 234 IAAFRRSALAEVGYwsDDMITEDIDISW 261
Cdd:COG0463  152 FRLFRREVLEELGF--DEGFLEDTELLR 177
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
60-300 4.35e-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: 141.18  E-value: 4.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  60 WPWGENAPAPQLKDN----PSISIIIPCFNEEKNVEETIHAALAQRY--ENIEVIAVNDGSTDKTRAILDHMAAQipRLR 133
Cdd:cd06439   10 KLLARLRPKPPSLPDpaylPTVTIIIPAYNEEAVIEAKLENLLALDYprDRLEIIVVSDGSTDGTAEIAREYADK--GVK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 134 VIHLAQNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPmLYNPRVGAVTGNPRIRTRSTLVGkiqvGE--YS 211
Cdd:cd06439   88 LLRFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRH-FADPSVGAVSGELVIVDGGGSGS----GEglYW 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 212 SIIGLIKRTQRIYGNVFTVSGVIAAFRRSALAEvgyWSDDMITEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWK 291
Cdd:cd06439  163 KYENWLKRAESRLGSTVGANGAIYAIRRELFRP---LPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFR 239

                 ....*....
gi 446533092 292 QRLRWAQGG 300
Cdd:cd06439  240 RRVRIAAGN 248
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
76-324 1.69e-38

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: 139.67  E-value: 1.69e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  76 SISIIIPCFNEEKNVEETIHAALAQRY--ENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIH-LAQNQgkAIALKTGAA 152
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDnPKRIQ--SAGLNIGIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 153 AAKSEYLVCIDGDALLDRDAAAYIVEpMLYNPRVGAVTGNPRIRTRSTLVGKIQVGeYSSIIGLIKRTQR--IYGNVFTV 230
Cdd:cd02525   79 NSRGDIIIRVDAHAVYPKDYILELVE-ALKRTGADNVGGPMETIGESKFQKAIAVA-QSSPLGSGGSAYRggAVKIGYVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 231 SGVIAAFRRSALAEVGYWSDDMIT-EDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMT 309
Cdd:cd02525  157 TVHHGAYRREVFEKVGGFDESLVRnEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRARTLRKHRK 236
                        250
                 ....*....|....*.
gi 446533092 310 RL-WRKenfrMWPLFF 324
Cdd:cd02525  237 SLsLRH----LLPLAF 248
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
75-299 1.70e-33

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: 125.56  E-value: 1.70e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   75 PSISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIP--RLRVIHLAQNQG---KAIALKT 149
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNARLLGptgKSRGLNH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  150 GAAAAKSEYLVCIDGDALLDRDAAAYIVePMLYNPRVGAVTGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRiYGNVFT 229
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYV-QYFDSPKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRL-ALGVLP 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446533092  230 VSGVIAAFRRSALAEVGYWSDDMI-TEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQG 299
Cdd:pfam13641 160 LSGAGSAIRREVLKELGLFDPFFLlGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
79-194 3.43e-31

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: 117.22  E-value: 3.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSEY 158
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446533092 159 LVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTGNPR 194
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGN 116
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
79-165 2.50e-28

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: 110.36  E-value: 2.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALA--QRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAKS 156
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                 ....*....
gi 446533092 157 EYLVCIDGD 165
Cdd:cd04179   81 DIVVTMDAD 89
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
79-299 1.04e-27

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: 109.69  E-value: 1.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRY--ENIEVIAVNDGSTDKTRAILDHMAA-QIPRLRVIHLAQ--NQGKAIALKTGAAA 153
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAkPNFQLKILNNSRvsISGKKNALTTAIKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 154 AKSEYLVCIDGDALLDRDAAAYIVEPMLYNPrVGAVTGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQrIYGNVFTVSGV 233
Cdd:cd04192   81 AKGDWIVTTDADCVVPSNWLLTFVAFIQKEQ-IGLVAGPVIYFKGKSLLAKFQRLDWLSLLGLIAGSF-GLGKPFMCNGA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446533092 234 IAAFRRSALAEVGYWS--DDMITEDIDISWKLQLNQWTIFY---EPRALCWILMPETLKGLWKQRLRWAQG 299
Cdd:cd04192  159 NMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYPKVAylkNPEALVTTQPVTSWKELLNQRKRWASK 229
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
79-165 5.37e-27

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: 106.41  E-value: 5.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEET---IHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAK 155
Cdd:cd04187    1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80
                         90
                 ....*....|
gi 446533092 156 SEYLVCIDGD 165
Cdd:cd04187   81 GDAVITMDAD 90
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
75-304 1.33e-25

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: 104.19  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  75 PSISIIIPCFNEEKN-VEETIHAALAQRY--ENIEVIAVNDGSTDKTRAILDHMAAQIPRlRVIHLAQNQG-KAIALKTG 150
Cdd:cd06421    1 PTVDVFIPTYNEPLEiVRKTLRAALAIDYphDKLRVYVLDDGRRPELRALAAELGVEYGY-RYLTRPDNRHaKAGNLNNA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 151 AAAAKSEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTG-----NPRIRTRSTLVGKIQVGEYSSIIGLIKrtQRIYG 225
Cdd:cd06421   80 LAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTpqffyNPDPFDWLADGAPNEQELFYGVIQPGR--DRWGA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446533092 226 NVFTVSGviAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVF 304
Cdd:cd06421  158 AFCCGSG--AVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
73-323 1.42e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 103.15  E-value: 1.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  73 DNPSISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDhmAAQIPRLRVIHLAQNQGKAIALKTGAA 152
Cdd:COG1216    1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLA--ALAFPRVRVIRNPENLGFAAARNLGLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 153 AAKSEYLVCIDGDALLDRDAAAYIVEpmlynprvgavtgnprirtrstlvgkiqvgeyssiiglikrtqriYGNVFtvsg 232
Cdd:COG1216   79 AAGGDYLLFLDDDTVVEPDWLERLLA---------------------------------------------AACLL---- 109
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 233 viaaFRRSALAEVGYWSDDMIT--EDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLrwaqggaevFLKNMTR 310
Cdd:COG1216  110 ----IRREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYY---------LGRNRLL 176
                        250
                 ....*....|...
gi 446533092 311 LWRKENFRMWPLF 323
Cdd:COG1216  177 FLRKHGPRPLLRL 189
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
78-306 7.02e-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: 102.09  E-value: 7.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  78 SIIIPCFNEEKN-VEETIHAALAQRYENIEVIAVNDGSTDKT--RAILDHMAAQIPRLRVIHLAQNQG-KAIALKTG--A 151
Cdd:cd06435    1 SIHVPCYEEPPEmVKETLDSLAALDYPNFEVIVIDNNTKDEAlwKPVEAHCAQLGERFRFFHVEPLPGaKAGALNYAleR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 152 AAAKSEYLVCIDGDALLDRDAAAYIVePMLYNPRVGAVTGNPRIRT-RSTLVGKIQVGEYSSI--IGLIKRTQRiygNVF 228
Cdd:cd06435   81 TAPDAEIIAVIDADYQVEPDWLKRLV-PIFDDPRVGFVQAPQDYRDgEESLFKRMCYAEYKGFfdIGMVSRNER---NAI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446533092 229 TVSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLK 306
Cdd:cd06435  157 IQHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKK 234
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
76-300 5.35e-24

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: 99.64  E-value: 5.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  76 SISIIIPCFNEEKNV-EETIHAALAQryENIEVIAVNDGSTDKTRAILDHMAAQIPRlrVIHLAQNQGKAIALKTGAAAA 154
Cdd:cd06434    1 DVTVIIPVYDEDPDVfRECLRSILRQ--KPLEIIVVTDGDDEPYLSILSQTVKYGGI--FVITVPHPGKRRALAEGIRHV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 155 KSEYLVCIDGDALLDRDAAAYIVEPMLyNPRVGAVTGNPRI-RTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGV 233
Cdd:cd06434   77 TTDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRIlRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGR 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446533092 234 IAAFRRSALAEVGYWSDDM----------ITEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQGG 300
Cdd:cd06434  156 TAAYRTEILKDFLFLEEFTnetfmgrrlnAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSN 232
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
79-279 1.07e-23

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: 96.86  E-value: 1.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILdhmAAQIPRLRVIHLAQNQGKAIALKTGAAAAKSEY 158
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELL---RELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 159 LVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTGnprirtrstlvgkiqvgeyssiiglikrtqriygnvfTVSGVIAAFR 238
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAAEQDPDVGIVGP-------------------------------------KVSGAFLLVR 120
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446533092 239 RSALAEVGYWSDD--MITEDIDISWKLQLNQWTIFYEPRALCW 279
Cdd:cd04186  121 REVFEEVGGFDEDffLYYEDVDLCLRARLAGYRVLYVPQAVIY 163
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
75-300 4.71e-23

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: 97.00  E-value: 4.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  75 PSISIIIPCFNEEKNVEETIHAALAQRY--ENIEvIAVNDGSTDKT----RAILDHMAAQIPRLRVIHLAQNQG-KAIAL 147
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAACALDYpkDRLE-IQVLDDSTDETvrlaREIVEEYAAQGVNIKHVRRADRTGyKAGAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 148 KTGAAAAKSEYLVCIDGDALLDRDAAAYIVePMLYNPRVGAV-TGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGN 226
Cdd:cd06437   80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTP-PYFADPKLGFVqTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSSTGL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446533092 227 VFTVSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQGG 300
Cdd:cd06437  159 FFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
158-342 5.28e-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: 90.09  E-value: 5.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  158 YLVCIDGDALLDRDAAAYIVEPMLYnPRVGAVTGNPRIRTRSTLVGKIQVGEYSSIIGLIKRTQRIYGNVFTVSGVIAAF 237
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  238 RRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFYEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKEN- 316
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYLGTLLw 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 446533092  317 ------FRMWPLF-FEYCLTTIWAFTCLVGFII 342
Cdd:pfam13632 160 sglplaLLLLLLFsISSLALVLLLLALLAGLLL 192
PRK10073 PRK10073
putative glycosyl transferase; Provisional
75-169 3.76e-19

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 87.79  E-value: 3.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  75 PSISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHlAQNQGKAIALKTGAAAA 154
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLAVA 84
                         90
                 ....*....|....*
gi 446533092 155 KSEYLVCIDGDALLD 169
Cdd:PRK10073  85 TGKYVAFPDADDVVY 99
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
79-165 9.79e-19

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: 84.16  E-value: 9.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEK----NVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRL-RVIHLAQNQGKAIALKTGAAA 153
Cdd:cd04188    1 VVIPAYNEEKrlppTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALiRVLTLPKNRGKGGAVRAGMLA 80
                         90
                 ....*....|..
gi 446533092 154 AKSEYLVCIDGD 165
Cdd:cd04188   81 ARGDYILFADAD 92
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
75-185 6.81e-16

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: 76.09  E-value: 6.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  75 PSISIIIPCFN-EEKNVEETIHAALAQRYENIEVIAVNDGSTD-KTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAA 152
Cdd:cd04184    1 PLISIVMPVYNtPEKYLREAIESVRAQTYPNWELCIADDASTDpEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80
                         90       100       110
                 ....*....|....*....|....*....|...
gi 446533092 153 AAKSEYLVCIDGDALLDRDAAAYIVEPMLYNPR 185
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALNEHPD 113
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
77-270 9.92e-16

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


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 76.01  E-value: 9.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   77 ISIIIPCFNEEKNVEETIHAALAQRyENIEVIAVNDGSTDKTRAILDHMAAQiprlrVIHLAqnQGKAIALKTGAAAAKS 156
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALR-GDAEVIVVDGGSTDGTVEIARSLGAK-----VIHSP--KGRARQMNAGAALAKG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  157 EYLVCIDGDALLDRDAAAYIvEPMLYNPrvGAVTGNPRIRTRSTlvgkiqvGEYSSIIGLI-----KRTQRIYGN--VFt 229
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEAI-RRALAKP--GYVAGAFDLRFDGP-------GLLLRLIEWGvnlrsRLTGIPYGDqgLF- 141
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 446533092  230 vsgviaaFRRSALAEVGYWSDDMITEDIDISWKL-QLNQWTI 270
Cdd:TIGR04283 142 -------VRRSLFEQIGGFPDIPLMEDIELSRRLrRLGRLAI 176
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
77-263 5.23e-15

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: 73.76  E-value: 5.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  77 ISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAIldhmaAQIPRLRVIHLAqnQGKAIALKTGAAAAKS 156
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAI-----ARSAGVVVISSP--KGRARQMNAGAAAARG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 157 EYLVCIDGDALLDRDAAAYIVEPMLYNPRVgAVTGNPRIRTRSTLvgkiqvgeYSSIIGLIK----RTQRIYGN--VFtv 230
Cdd:cd02522   74 DWLLFLHADTRLPPDWDAAIIETLRADGAV-AGAFRLRFDDPGPR--------LRLLELGANlrsrLFGLPYGDqgLF-- 142
                        170       180       190
                 ....*....|....*....|....*....|...
gi 446533092 231 sgviaaFRRSALAEVGYWSDDMITEDIDISWKL 263
Cdd:cd02522  143 ------IRRELFEELGGFPELPLMEDVELVRRL 169
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
79-256 4.79e-13

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: 67.41  E-value: 4.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRyENIEVIAVNDGSTDKTRAILDhMAAQIPRLRVI--HLAQ-NQGKAIALKTGAA--- 152
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNK-PNFLVLVIDDASDDDTAGIVR-LAITDSRVHLLrrHLPNaRTGKGDALNAAYDqir 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 153 -------AAKSEYLVC-IDGDALLDRDAAAYiVEPMLYNPRVGAVTGNPRIRTRST-LVGKIQVGEYSSIIGLIKRTQRI 223
Cdd:cd06436   79 qilieegADPERVIIAvIDADGRLDPNALEA-VAPYFSDPRVAGTQSRVRMYNRHKnLLTILQDLEFFIIIAATQSLRAL 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446533092 224 YGNVfTVSGVIAAFRRSALAEV---GYWSDDMiTED 256
Cdd:cd06436  158 TGTV-GLGGNGQFMRLSALDGLigeEPWSDSL-LED 191
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
79-165 7.16e-13

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: 67.56  E-value: 7.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEET---IHAALAQryENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAAAAK 155
Cdd:cd06442    1 IIIPTYNERENIPELierLDAALKG--IDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78
                         90
                 ....*....|
gi 446533092 156 SEYLVCIDGD 165
Cdd:cd06442   79 GDVIVVMDAD 88
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
79-171 2.84e-12

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: 64.91  E-value: 2.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPrLRVIHLAQ-NQG--KAIALKTGAAAAK 155
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFP-IPIKHVWQeDEGfrKAKIRNKAIAAAK 79
                         90
                 ....*....|....*.
gi 446533092 156 SEYLVCIDGDALLDRD 171
Cdd:cd06420   80 GDYLIFIDGDCIPHPD 95
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
78-279 1.01e-11

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: 63.72  E-value: 1.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  78 SIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIprLRVI--------HlAQNqgKAIALKT 149
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKI--TYWIsepdkgiyD-AMN--KGIALAT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 150 GaaaaksEYLVCI-DGDALLDRDAAAYIVEPMLyNPRVGAVTGNPRIRTRSTLVGKIQVGEYSSIIGLikrtqrIYGNVF 228
Cdd:cd06433   76 G------DIIGFLnSDDTLLPGALLAVVAAFAE-HPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFL------LYGMPI 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446533092 229 TVSGVIaaFRRSALAEVGYWSDD-MITEDIDISWKLQLNQWTIFYEPRALCW 279
Cdd:cd06433  143 CHQATF--FRRSLFEKYGGFDESyRIAADYDLLLRLLLAGKIFKYLPEVLAA 192
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
77-181 5.73e-11

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 63.63  E-value: 5.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  77 ISIIIPCFNEE----KNVEETIhAALAQRYE-----NIEVIAVNDGSTDKTRAI-LDHMAAQIPR---LRVIHLAQNQGK 143
Cdd:PTZ00260  72 LSIVIPAYNEEdrlpKMLKETI-KYLESRSRkdpkfKYEIIIVNDGSKDKTLKVaKDFWRQNINPnidIRLLSLLRNKGK 150
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 446533092 144 AIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPML 181
Cdd:PTZ00260 151 GGAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIML 188
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
143-297 8.45e-11

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: 60.37  E-value: 8.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  143 KAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLyNPRVGAVTGNPRIRTRSTLVGKIqvgEYSSIIGLIKRTQR 222
Cdd:pfam13506  18 KVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLA-DPKVGLVTSPPVGSDPKGLAAAL---EAAFFNTLAGVLQA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  223 IYGNVFTVSGVIAAFRRSALAEVG---YWSDDmITEDIDISWKLQLNQWTIFYEPRALCWILMPE--TLKGLWKQRLRWA 297
Cdd:pfam13506  94 ALSGIGFAVGMSMAFRRADLERIGgfeALADY-LAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFRAFMARQLRWA 172
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
79-296 3.58e-10

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: 60.01  E-value: 3.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNE-EKNVEETIH----------AALAQRYENIEVIAVNDGSTDKTRAILD----HMAAQiprLRVIHLAQNqgk 143
Cdd:cd04190    1 VCVTMYNEdEEELARTLDsilkndypfcARGGDSWKKIVVCVIFDGAIKKNRGKRDsqlwFFNYF---CRVLFPDDP--- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 144 aialktgaaaaksEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTG--NPRIRTRSTLVgKIQVGEYSSIIGLIKRTQ 221
Cdd:cd04190   75 -------------EFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGeiHPMGKKQGPLV-MYQVFEYAISHWLDKAFE 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 222 RIYGNVFTVSGVIAAFRRSALAEV-GYWSDDM----ITEDIDISW-KLQLNQwtifYEPRALCWILM------------- 282
Cdd:cd04190  141 SVFGFVTCLPGCFSMYRIEALKGDnGGKGPLLdyayLTNTVDSLHkKNNLDL----GEDRILCTLLLkagpkrkylyvpg 216
                        250       260
                 ....*....|....*....|.
gi 446533092 283 -------PETLKGLWKQRLRW 296
Cdd:cd04190  217 avaetdvPETFVELLSQRRRW 237
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
78-259 2.27e-07

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 51.89  E-value: 2.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092   78 SIIIPCFNEEKN--VEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQ-GKAIALKTGAAAA 154
Cdd:pfam10111   1 SVVIPVYNGEKThwIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYYPNAPDTTySLAASRNRGTSHA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  155 KSEYLVCIDGDALLDRDaaayIVEPMLYNPRVGAVTGNPRIRTRSTLVGKIQV-------GEYSSIIGLIKRTQRIYGNV 227
Cdd:pfam10111  81 IGEYISFIDGDCLWSPD----KFEKQLKIATSLALQENIQAAVVLPVTDLNDEssnflrrGGDLTASGDVLRDLLVFYSP 156
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 446533092  228 ----FTVSGVIAAFRRSALAEVGYWSDDMI---TEDIDI 259
Cdd:pfam10111 157 laifFAPNSSNALINRQAFIEVGGFDESFRghgAEDFDI 195
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
78-245 2.48e-07

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


Pssm-ID: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 51.09  E-value: 2.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  78 SIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLA-QNQGKAIALKTGAAAAKS 156
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNgKNLGVARNFESLLQAADG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 157 EYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAVTGNPRIrtrstlvgkiqVGEYSSIIGL-IKRTQRIYGNVF------- 228
Cdd:cd04196   81 DYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLEL-----------VDENGNPIGEsFFEYQKIKPGTSfnnllfq 149
                        170
                 ....*....|....*...
gi 446533092 229 -TVSGVIAAFRRSALAEV 245
Cdd:cd04196  150 nVVTGCTMAFNRELLELA 167
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
77-178 6.30e-07

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


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 49.98  E-value: 6.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  77 ISIIIPCFNEEKNVEETIHAALAQryeNIEVIAVNDGSTDKTRAIldhmaAQIPRLRVIHLAqNQGKAIALKTGAAAAKS 156
Cdd:cd02511    2 LSVVIITKNEERNIERCLESVKWA---VDEIIVVDSGSTDRTVEI-----AKEYGAKVYQRW-WDGFGAQRNFALELATN 72
                         90       100
                 ....*....|....*....|..
gi 446533092 157 EYLVCIDGDALLDRDAAAYIVE 178
Cdd:cd02511   73 DWVLSLDADERLTPELADEILA 94
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
72-165 8.50e-07

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 50.38  E-value: 8.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  72 KDNPSISIIIPCFNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGA 151
Cdd:PRK10018   2 KDNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSWEQLQQYVTALNDPRITYIHNDINSGACAVRNQAI 81
                         90
                 ....*....|....
gi 446533092 152 AAAKSEYLVCIDGD 165
Cdd:PRK10018  82 MLAQGEYITGIDDD 95
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
78-183 4.58e-06

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


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 48.35  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  78 SIIIPCFNEEKNV-EETIHAALAQ--RYENIEVIAVNDGSTD--KTRAILDHMAAQIPRLRVIHLAQNQGKAIALKTGAA 152
Cdd:cd02510    1 SVIIIFHNEALSTlLRTVHSVINRtpPELLKEIILVDDFSDKpeLKLLLEEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 446533092 153 AAKSEYLVCIDG---------DALLDRDAAAY--IVEPMLYN 183
Cdd:cd02510   81 AATGDVLVFLDShcevnvgwlEPLLARIAENRktVVCPIIDV 122
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
79-169 9.80e-06

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: 46.30  E-value: 9.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRYEN-IEVIAVNDGSTDKTRAILDHMAAQIPRLRVIHLAQN------QGKAIALKTGA 151
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGShnspspKGVGYAKNQAI 80
                         90
                 ....*....|....*...
gi 446533092 152 AAAKSEYLVCIDGDALLD 169
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMM 98
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
71-191 1.40e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 46.83  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  71 LKDNPSISIIIPCFNEEKNVEETIHAALAQRYENI--EVIAVNDGSTDKTRAILDHMAAqiprlRVIH-------LAQNQ 141
Cdd:PRK13915  27 AKAGRTVSVVLPALNEEETVGKVVDSIRPLLMEPLvdELIVIDSGSTDATAERAAAAGA-----RVVSreeilpeLPPRP 101
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446533092 142 GKAIALKTGAAAAKSEYLVCIDGDaLLDRDA--AAYIVEPMLYNPRVGAVTG 191
Cdd:PRK13915 102 GKGEALWRSLAATTGDIVVFVDAD-LINFDPmfVPGLLGPLLTDPGVHLVKA 152
PLN02189 PLN02189
cellulose synthase
244-337 1.81e-05

cellulose synthase


Pssm-ID: 215121 [Multi-domain]  Cd Length: 1040  Bit Score: 47.31  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  244 EVGyWSDDMITEDIDISWKLQLNQW-TIFYEP-RALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLW--RKENFRM 319
Cdd:PLN02189  729 ELG-WIYGSITEDILTGFKMHCRGWrSIYCMPkRAAFKGSAPINLSDRLNQVLRWALGSVEIFFSRHSPLLygYKGGNLK 807
                          90
                  ....*....|....*...
gi 446533092  320 WPLFFEYCLTTIWAFTCL 337
Cdd:PLN02189  808 WLERFAYVNTTIYPFTSL 825
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
77-165 2.03e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 46.27  E-value: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  77 ISIIIPCFNEEKNVEETIH---AALAQRYENIEVIAVNDGSTDKTRAILDHmAAQIPRLRVIH--LAQNQGKAIALKTGA 151
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIRrttAACESLGKEYEILLIDDGSSDNSAEMLVE-AAQAPDSHIVAilLNRNYGQHSAIMAGF 86
                         90
                 ....*....|....
gi 446533092 152 AAAKSEYLVCIDGD 165
Cdd:PRK10714  87 SHVTGDLIITLDAD 100
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
80-267 1.47e-04

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: 43.04  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  80 IIPCFN-EEKNVEETIHAALAQryenIEVIAVNDGSTDKTRAILDHMAAQipRLRVIHLAQNQGKAIALKTGAAAAKS-- 156
Cdd:cd02526    2 VVVTYNpDLSKLKELLAALAEQ----VDKVVVVDNSSGNDIELRLRLNSE--KIELIHLGENLGIAKALNIGIKAALEng 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 157 -EYLVCIDGDALLDRDAAA-YIVEPMLY--NPRVGAVTgnPRIRTRSTlvgkiqvGEYSSIIGLIKRTQRIY---GNVFT 229
Cdd:cd02526   76 aDYVLLFDQDSVPPPDMVEkLLAYKILSdkNSNIGAVG--PRIIDRRT-------GENSPGVRKSGYKLRIQkegEEGLK 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446533092 230 -VSGVIA---AFRRSALAEVGYWSDDMITEDIDISWKLQLNQ 267
Cdd:cd02526  147 eVDFLITsgsLISLEALEKVGGFDEDLFIDYVDTEWCLRARS 188
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
78-256 1.65e-04

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: 42.69  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  78 SIIIPCFNEEK--NVEETIHAALAQRYENIEVIAVNDGS-TDKTRAILDHMAAQIPrLRVIHLAQNQGKAIALKTGAAAA 154
Cdd:cd04195    1 SVLMSVYIKEKpeFLREALESILKQTLPPDEVVLVKDGPvTQSLNEVLEEFKRKLP-LKVVPLEKNRGLGKALNEGLKHC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 155 KSEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAV---------TGNPRIRTRSTLVGKiQVGEYSsiiglIKRTQRIYG 225
Cdd:cd04195   80 TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVgggvlefdsDGNDIGKRRLPTSHD-DILKFA-----RRRSPFNHP 153
                        170       180       190
                 ....*....|....*....|....*....|.
gi 446533092 226 NVftvsgviaAFRRSALAEVGYWSDDMITED 256
Cdd:cd04195  154 TV--------MFRKSKVLAVGGYQDLPLVED 176
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
84-172 1.76e-04

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 42.62  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  84 FNEEKNVEETIHAALAQRYENIEVIAVNDGSTDKTRAILDHMAAQIPrLRVIHLAQNQGKA--------IALKTGAAaak 155
Cdd:cd04185    6 YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDN-IVYLRLPENLGGAggfyegvrRAYELGYD--- 81
                         90
                 ....*....|....*..
gi 446533092 156 seYLVCIDGDALLDRDA 172
Cdd:cd04185   82 --WIWLMDDDAIPDPDA 96
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
71-165 2.06e-04

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 42.76  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  71 LKDNPSISIIIPCFNEEKNVE---ETIHAALaQRYENIEVIAVNDGSTDKTRAILDHMAAQI--PRLRVIHLAQNQGKAI 145
Cdd:PLN02726   5 GEGAMKYSIIVPTYNERLNIAlivYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLQKVYgeDRILLRPRPGKLGLGT 83
                         90       100
                 ....*....|....*....|
gi 446533092 146 ALKTGAAAAKSEYLVCIDGD 165
Cdd:PLN02726  84 AYIHGLKHASGDFVVIMDAD 103
PLN02915 PLN02915
cellulose synthase A [UDP-forming], catalytic subunit
244-415 2.46e-04

cellulose synthase A [UDP-forming], catalytic subunit


Pssm-ID: 215494 [Multi-domain]  Cd Length: 1044  Bit Score: 43.77  E-value: 2.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  244 EVGyWSDDMITEDIDISWKLQLNQW-TIFYEP-RALCWILMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRM-W 320
Cdd:PLN02915  732 EIG-WIYGSVTEDILTGFKMHCRGWkSVYCMPkRPAFKGSAPINLSDRLHQVLRWALGSVEIFMSRHCPLWYAYGGKLkW 810
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  321 PLFFEYCLTTIWAFTclvgfiiyavqlaGVPLnielthiaathtagILLCTL---CLL--QFIVSLVienryeHNLASsl 395
Cdd:PLN02915  811 LERLAYINTIVYPFT-------------SIPL--------------LAYCTIpavCLLtgKFIIPTL------NNLAS-- 855
                         170       180
                  ....*....|....*....|
gi 446533092  396 fwiIWFPVIFwmLSLATTLV 415
Cdd:PLN02915  856 ---IWFLALF--LSIIATSV 870
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
75-191 2.78e-04

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: 41.81  E-value: 2.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  75 PSISIIIPCFNEEKNVEETIHAALAQRYENIEVI-AVNDGsTDKTRAILDHMAAQIPRLRVIHLAQNQGKAIALK----- 148
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILfCVQDE-DDPAIPVVRKLIAKYPNVDARLLIGGEKVGINPKvnnli 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446533092 149 TGAAAAKSEYLVCIDGDALLDRDAAAYIVEPmLYNPRVGAVTG 191
Cdd:cd02520   80 KGYEEARYDILVISDSDISVPPDYLRRMVAP-LMDPGVGLVTC 121
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
79-172 3.00e-04

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: 41.43  E-value: 3.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  79 IIIPCFNEEKNVEETIHAALAQRY--ENIEVIAVNDGSTDKTraildhmaAQIPR---LRVI--HLAQNQGKAIALKTGA 151
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYprELYRIFVVADNCTDDT--------AQVARaagATVLerHDPERRGKGYALDFGF 72
                         90       100
                 ....*....|....*....|....*.
gi 446533092 152 AAAKSEY-----LVCIDGDALLDRDA 172
Cdd:cd06438   73 RHLLNLAddpdaVVVFDADNLVDPNA 98
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
51-304 5.53e-04

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 42.32  E-value: 5.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  51 YFWV-----YRERHWPWgENAPAPQLKDN---PSISIIIPCFNEEKNV-EETIHAALAQRY--ENIEVIAVNDGSTDKTR 119
Cdd:PRK11498 229 YAWIvlvlgYFQVVWPL-NRQPVPLPKDMslwPTVDIFVPTYNEDLNVvKNTIYASLGIDWpkDKLNIWILDDGGREEFR 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 120 AILDHMAAQIPRlRVIHlaqNQGKAIALKTGAAAAKSEYLVCIDGDALLDRDAAAYIVEPMLYNPRVGAV-------TGN 192
Cdd:PRK11498 308 QFAQEVGVKYIA-RPTH---EHAKAGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMqtphhffSPD 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092 193 PRIRTRSTLvGKIQvGEYSSIIGLIKRTQRIYGNVFtVSGVIAAFRRSALAEVGYWSDDMITEDIDISWKLQLNQWTIFY 272
Cdd:PRK11498 384 PFERNLGRF-RKTP-NEGTLFYGLVQDGNDMWDATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAY 460
                        250       260       270
                 ....*....|....*....|....*....|..
gi 446533092 273 EPRALCWILMPETLKGLWKQRLRWAQGGAEVF 304
Cdd:PRK11498 461 MRIPQAAGLATESLSAHIGQRIRWARGMVQIF 492
PLN02638 PLN02638
cellulose synthase A (UDP-forming), catalytic subunit
244-413 1.45e-03

cellulose synthase A (UDP-forming), catalytic subunit


Pssm-ID: 215343 [Multi-domain]  Cd Length: 1079  Bit Score: 41.06  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  244 EVGyWSDDMITEDIDISWKLQLNQW-TIFYEPRALCWI-LMPETLKGLWKQRLRWAQGGAEVFLKNMTRLWRKENFRM-W 320
Cdd:PLN02638  768 EIG-WIYGSVTEDILTGFKMHARGWrSIYCMPKRPAFKgSAPINLSDRLNQVLRWALGSVEILFSRHCPIWYGYGGRLkW 846
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446533092  321 PLFFEYCLTTIWAFTclvgfiiyavqlaGVPLnielthiaathtagILLCTL---CLL--QFIVSLVienryeHNLASsl 395
Cdd:PLN02638  847 LERFAYVNTTIYPIT-------------SIPL--------------LLYCTLpavCLLtgKFIIPQI------SNIAS-- 891
                         170
                  ....*....|....*...
gi 446533092  396 fwiIWFPVIFwmLSLATT 413
Cdd:PLN02638  892 ---IWFISLF--LSIFAT 904
 
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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