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Conserved domains on  [gi|496082723|ref|WP_008807230|]
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MULTISPECIES: poly-beta-1,6-N-acetyl-D-glucosamine synthase [Klebsiella]

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 ...
 30-438 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: 661.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723   30 ILDFVFFWPLFMSVLWITGGLYFWFQLERHWPwGEDTPPPTLPGNPLISILIPCFNEEKNARETISAALAQRYANLEVIA 109
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWP-LPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  110 INDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHYPHVGAV 189
Cdd:TIGR03937  80 INDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  190 TGNPRIRTRSTLIGRIQVGEFSSIIGLIKRTQRIYGRVFTVSGVIAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWD 269
Cdd:TIGR03937 160 TGNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  270 IFFEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLVNLRRLFHWEHHRMWPLFLEYACSTLWAFAYAVTILLFILSrLM 349
Cdd:TIGR03937 240 IRYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQ-VN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  350 PLPDNLAVHSLFPPEFTGMLLGVMCLLQFVASLYIERRYEKKVAKSLFWVIWFPMVYWMIGLLTTLVAFPKVMVKRQRSR 429
Cdd:TIGR03937 319 ILPYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKR 398


                  ....*....
gi 496082723  430 ARWVSPDRG 438
Cdd:TIGR03937 399 AVWVSPDRG 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 ...
 30-438 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: 661.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723   30 ILDFVFFWPLFMSVLWITGGLYFWFQLERHWPwGEDTPPPTLPGNPLISILIPCFNEEKNARETISAALAQRYANLEVIA 109
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWP-LPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  110 INDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHYPHVGAV 189
Cdd:TIGR03937  80 INDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  190 TGNPRIRTRSTLIGRIQVGEFSSIIGLIKRTQRIYGRVFTVSGVIAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWD 269
Cdd:TIGR03937 160 TGNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  270 IFFEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLVNLRRLFHWEHHRMWPLFLEYACSTLWAFAYAVTILLFILSrLM 349
Cdd:TIGR03937 240 IRYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQ-VN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  350 PLPDNLAVHSLFPPEFTGMLLGVMCLLQFVASLYIERRYEKKVAKSLFWVIWFPMVYWMIGLLTTLVAFPKVMVKRQRSR 429
Cdd:TIGR03937 319 ILPYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKR 398


                  ....*....
gi 496082723  430 ARWVSPDRG 438
Cdd:TIGR03937 399 AVWVSPDRG 407
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 79-256 4.35e-55

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: 180.89  E-value: 4.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEE-PRLRVIHLAANQGKAVALKAGAAAARGD 157
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYiRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 158 LLVCIDGDALLDRDTAAWLVAPLIHYPHVGAVTGNPRIR-TRSTLIGRIQVGEFSSIIGLIKRTQRIYGRVFTVSGVIAA 236
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRnGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGA 160

                        170       180
                 ....*....|....*....|
gi 496082723 237 FRRQALADVGYWSPDMITED 256
Cdd:cd06423  161 FRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 39-427 5.81e-53

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: 179.55  E-value: 5.81e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  39 LFMSVLWITGGLYFWFQLERHWPWGEDTPPptlpgnplISILIPCFNEEKNARETISAALAQRYA--NLEVIAINDGSSD 116
Cdd:COG1215    1 LLLLLALLALLYLLLLALARRRRAPADLPR--------VSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 117 NTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAvtgnprir 196
Cdd:COG1215   73 ETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAD-PGVGA-------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 197 trstligriqvgefssiiglikrtqriygrvftvSGVIAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWDIFFEPRA 276
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 277 LCWILMPETLKGLWKQRLRWAQGGAEVFLVNlRRLFHWehhrmwplfleyacSTLWAFAYAVTILLFILSRLMPLpdnla 356
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKH-RPLLRP--------------RRLLLFLLLLLLPLLLLLLLLAL----- 249

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082723 357 vhslfppeftgMLLGVMCLLQFVASLYierryeKKVAKSLFWVIWFPMVYWMIGLLTTLVAFPKVMVKRQR 427
Cdd:COG1215  250 -----------LALLLLLLPALLLALL------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 75-299 6.63e-31

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: 118.63  E-value: 6.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723   75 PLISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEP--RLRVIHLA---ANQGKAVALKA 149
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNArllGPTGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  150 GAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAVTGNPRIRTRSTLIGRIQVGEFSSIIGLIKRTQRiYGRVFT 229
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRL-ALGVLP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082723  230 VSGVIAAFRRQALADVGYWSPDMI-TEDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQG 299
Cdd:pfam13641 160 LSGAGSAIRREVLKELGLFDPFFLlGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 72-142 4.16e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 66.99  E-value: 4.16e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082723  72 PGNPLISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHlAANQG 142
Cdd:PRK10073   3 NSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAG 72
 
Name Accession Description Interval E-value
PgaC_IcaA TIGR03937
poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are ...
 30-438 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: 661.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723   30 ILDFVFFWPLFMSVLWITGGLYFWFQLERHWPwGEDTPPPTLPGNPLISILIPCFNEEKNARETISAALAQRYANLEVIA 109
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWP-LPRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  110 INDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHYPHVGAV 189
Cdd:TIGR03937  80 INDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  190 TGNPRIRTRSTLIGRIQVGEFSSIIGLIKRTQRIYGRVFTVSGVIAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWD 269
Cdd:TIGR03937 160 TGNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWN 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  270 IFFEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLVNLRRLFHWEHHRMWPLFLEYACSTLWAFAYAVTILLFILSrLM 349
Cdd:TIGR03937 240 IRYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQ-VN 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  350 PLPDNLAVHSLFPPEFTGMLLGVMCLLQFVASLYIERRYEKKVAKSLFWVIWFPMVYWMIGLLTTLVAFPKVMVKRQRSR 429
Cdd:TIGR03937 319 ILPYTPLVYSISLFQWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKR 398


                  ....*....
gi 496082723  430 ARWVSPDRG 438
Cdd:TIGR03937 399 AVWVSPDRG 407
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 79-256 4.35e-55

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: 180.89  E-value: 4.35e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEE-PRLRVIHLAANQGKAVALKAGAAAARGD 157
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYiRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 158 LLVCIDGDALLDRDTAAWLVAPLIHYPHVGAVTGNPRIR-TRSTLIGRIQVGEFSSIIGLIKRTQRIYGRVFTVSGVIAA 236
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRnGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGA 160

                        170       180
                 ....*....|....*....|
gi 496082723 237 FRRQALADVGYWSPDMITED 256
Cdd:cd06423  161 FRREALREVGGWDEDTLTED 180
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 39-427 5.81e-53

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: 179.55  E-value: 5.81e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  39 LFMSVLWITGGLYFWFQLERHWPWGEDTPPptlpgnplISILIPCFNEEKNARETISAALAQRYA--NLEVIAINDGSSD 116
Cdd:COG1215    1 LLLLLALLALLYLLLLALARRRRAPADLPR--------VSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 117 NTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAvtgnprir 196
Cdd:COG1215   73 ETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAD-PGVGA-------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 197 trstligriqvgefssiiglikrtqriygrvftvSGVIAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWDIFFEPRA 276
Cdd:COG1215  144 ----------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDA 189

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 277 LCWILMPETLKGLWKQRLRWAQGGAEVFLVNlRRLFHWehhrmwplfleyacSTLWAFAYAVTILLFILSRLMPLpdnla 356
Cdd:COG1215  190 VVYEEAPETLRALFRQRRRWARGGLQLLLKH-RPLLRP--------------RRLLLFLLLLLLPLLLLLLLLAL----- 249

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082723 357 vhslfppeftgMLLGVMCLLQFVASLYierryeKKVAKSLFWVIWFPMVYWMIGLLTTLVAFPKVMVKRQR 427
Cdd:COG1215  250 -----------LALLLLLLPALLLALL------LALRRRRLLLPLLHLLYGLLLLLAALRGKKVVWKKTPR 303
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 74-261 4.19e-32

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 121.35  E-value: 4.19e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  74 NPLISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAA 153
Cdd:COG0463    1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 154 ARGDLLVCIDGDALLDRDTAAWLVAPLIHYPhVGAVTGNPRIRTRSTLIGRIQVGEFSSIiglikrtqRIYGRVFTVSGV 233
Cdd:COG0463   81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSRLIREGESDLRRLGSRLFNLV--------RLLTNLPDSTSG 151

                        170       180
                 ....*....|....*....|....*...
gi 496082723 234 IAAFRRQALADVGYwsPDMITEDIDISW 261
Cdd:COG0463  152 FRLFRREVLEELGF--DEGFLEDTELLR 177
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 75-299 6.63e-31

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: 118.63  E-value: 6.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723   75 PLISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEP--RLRVIHLA---ANQGKAVALKA 149
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNArllGPTGKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  150 GAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAVTGNPRIRTRSTLIGRIQVGEFSSIIGLIKRTQRiYGRVFT 229
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTPVFSLNRSTMLSALGALEFALRHLRMMSLRL-ALGVLP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082723  230 VSGVIAAFRRQALADVGYWSPDMI-TEDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQG 299
Cdd:pfam13641 160 LSGAGSAIRREVLKELGLFDPFFLlGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 78-244 3.43e-30

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: 114.80  E-value: 3.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723   78 SILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGD 157
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  158 LLVCIDGDALLDRDTAAWLVAPLIHYPHVGAVTGNPRIRTRSTLIGRIQvGEFSSIIGLIKRTQRIYGRVFTVSGVIAAF 237
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRAS-RITLSRLPFFLGLRLLGLNLPFLIGGFALY 159


                  ....*..
gi 496082723  238 RRQALAD 244
Cdd:pfam00535 160 RREALEE 166
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 76-316 3.51e-30

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: 117.33  E-value: 3.51e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  76 LISILIPCFNEEKNARETISAALAQRY--ANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIH-LAANQGKavALKAGAA 152
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLIDnPKRIQSA--GLNIGIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 153 AARGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAVTGNPRIRTRSTLIGRIQVGEfSSIIGLIKRTQR--IYGRVFTV 230
Cdd:cd02525   79 NSRGDIIIRVDAHAVYPKDYILELVEALKR-TGADNVGGPMETIGESKFQKAIAVAQ-SSPLGSGGSAYRggAVKIGYVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 231 SGVIAAFRRQALADVGYWSPDMIT-EDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLVNlR 309
Cdd:cd02525  157 TVHHGAYRREVFEKVGGFDESLVRnEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRARTLRKH-R 235


                 ....*..
gi 496082723 310 RLFHWEH 316
Cdd:cd02525  236 KSLSLRH 242
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 60-300 3.44e-27

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: 109.21  E-value: 3.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  60 WPWGEDTPPPTLPGN----PLISILIPCFNEEKNARETISAALAQRYAN--LEVIAINDGSSDNTAQVLQQLAQEepRLR 133
Cdd:cd06439   10 KLLARLRPKPPSLPDpaylPTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYADK--GVK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 134 VIHLAANQGKAVALKAGAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAVTGNPRIRTRstligriqvGEFSSI 213
Cdd:cd06439   88 LLRFPERRGKAAALNRALALATGEIVVFTDANALLDPDALRLLVRHFAD-PSVGAVSGELVIVDG---------GGSGSG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 214 IGL-------IKRTQRIYGRVFTVSGVIAAFRRQALADvgyWSPDMITEDIDISWKLQLRHWDIFFEPRALCWILMPETL 286
Cdd:cd06439  158 EGLywkyenwLKRAESRLGSTVGANGAIYAIRRELFRP---LPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDG 234

                        250
                 ....*....|....
gi 496082723 287 KGLWKQRLRWAQGG 300
Cdd:cd06439  235 SEEFRRRVRIAAGN 248
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 79-194 9.67e-24

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: 96.81  E-value: 9.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGDL 158
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 496082723 159 LVCIDGDALLDRDTAAWLVAPLIHYPHVGAVTGNPR 194
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGN 116
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 79-165 8.19e-21

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: 89.46  E-value: 8.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARET---ISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAAR 155
Cdd:cd04187    1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHAR 80

                         90
                 ....*....|
gi 496082723 156 GDLLVCIDGD 165
Cdd:cd04187   81 GDAVITMDAD 90
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 158-349 8.37e-21

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


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 89.70  E-value: 8.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  158 LLVCIDGDALLDRDTAAwLVAPLIHYPHVGAVTGNPRIRTRSTLIGRIQVGEFSSIIGLIKRTQRIYGRVFTVSGVIAAF 237
Cdd:pfam13632   1 WILLLDADTVLPPDCLL-GIANEMASPEVAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  238 RRQALADVGYWSPDMITEDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLVNLRRLFhwehh 317
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILLIRLLGYL----- 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 496082723  318 rmWPLFLEY-ACSTLWAFAYAVTILLFILSRLM 349
Cdd:pfam13632 155 --GTLLWSGlPLALLLLLLFSISSLALVLLLLA 185
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 75-304 1.57e-19

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: 87.24  E-value: 1.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  75 PLISILIPCFNEEKNA-RETISAALAQRYAN--LEVIAINDGSSDNTAQVLQQLAqEEPRLRVIHLAANQG-KAVALKAG 150
Cdd:cd06421    1 PTVDVFIPTYNEPLEIvRKTLRAALAIDYPHdkLRVYVLDDGRRPELRALAAELG-VEYGYRYLTRPDNRHaKAGNLNNA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 151 AAAARGDLLVCIDGDALLDRDTAAWLVAPLIHYPHVGAVTG-----NPRIRTRSTLIGRIQVGEFSSIIglikrtQRIYG 225
Cdd:cd06421   80 LAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTpqffyNPDPFDWLADGAPNEQELFYGVI------QPGRD 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 226 R----VFTVSGviAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQGGA 301
Cdd:cd06421  154 RwgaaFCCGSG--AVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGML 231


                 ...
gi 496082723 302 EVF 304
Cdd:cd06421  232 QIL 234
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 79-165 2.46e-19

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: 85.32  E-value: 2.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALA--QRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARG 156
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80


                 ....*....
gi 496082723 157 DLLVCIDGD 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 3.00e-19

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: 86.19  E-value: 3.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALAQRY--ANLEVIAINDGSSDNTAQVLQ-QLAQEEPRLRVIHLAA--NQGKAVALKAGAAA 153
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEfAAAKPNFQLKILNNSRvsISGKKNALTTAIKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 154 ARGDLLVCIDGDALLDRDtaaWLVAplIHYPH--------VGAVTGnpriRTRSTLIGRIQVGEFSSIIGLIKRTQrIYG 225
Cdd:cd04192   81 AKGDWIVTTDADCVVPSN---WLLT--FVAFIqkeqiglvAGPVIY----FKGKSLLAKFQRLDWLSLLGLIAGSF-GLG 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496082723 226 RVFTVSGVIAAFRRQALADVGYWS--PDMITEDIDISWKLQLRHWD-IFFE--PRALCWILMPETLKGLWKQRLRWAQG 299
Cdd:cd04192  151 KPFMCNGANMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYPkVAYLknPEALVTTQPVTSWKELLNQRKRWASK 229
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 77-300 4.67e-19

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 85.77  E-value: 4.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  77 ISILIPCFNEEKNA-RETISAALAQRyaNLEVIAINDGSSDntaQVLQQLAQEEPRLRVIHLAANQ-GKAVALKAGAAAA 154
Cdd:cd06434    2 VTVIIPVYDEDPDVfRECLRSILRQK--PLEIIVVTDGDDE---PYLSILSQTVKYGGIFVITVPHpGKRRALAEGIRHV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 155 RGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAVTGNPRI-RTRSTLIGRIQVGEFSSIIGLIKRTQRIYGRVFTVSGV 233
Cdd:cd06434   77 TTDIVVLLDSDTVWPPNALPEMLKPFED-PKVGGVGTNQRIlRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGR 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 496082723 234 IAAFRRQALADVGYwSPD-----------MITEDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQGG 300
Cdd:cd06434  156 TAAYRTEILKDFLF-LEEftnetfmgrrlNAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSN 232
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 75-300 1.78e-18

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: 83.90  E-value: 1.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  75 PLISILIPCFNEEKNARETISAALAQRY-ANLEVIAINDGSSDNTAQVLQQLAQEEPRLRV----IHLAANQG-KAVALK 148
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAACALDYpKDRLEIQVLDDSTDETVRLAREIVEEYAAQGVnikhVRRADRTGyKAGALA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 149 AGAAAARGDLLVCIDGDALLDRDtaaWL--VAPLIHYPHVGAV-TGNPRIRTRSTLIGRIQVGEFSSIIGLIKRTQRIYG 225
Cdd:cd06437   81 EGMKVAKGEYVAIFDADFVPPPD---FLqkTPPYFADPKLGFVqTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSSTG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496082723 226 RVFTVSGVIAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQGG 300
Cdd:cd06437  158 LFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 78-314 1.83e-16

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: 78.21  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  78 SILIPCFNEEKN-ARETISAALAQRYANLEVIAINDGSSD-NTAQVLQQLAQE-EPRLRVIHLAANQG-KAVALKAGAAA 153
Cdd:cd06435    1 SIHVPCYEEPPEmVKETLDSLAALDYPNFEVIVIDNNTKDeALWKPVEAHCAQlGERFRFFHVEPLPGaKAGALNYALER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 154 ARGD--LLVCIDGDALLDRDtaaWL--VAPLIHYPHVGAVTGNPRIRT-RSTLIGRIQVGEFSSI--IGLIKRTQRiyGR 226
Cdd:cd06435   81 TAPDaeIIAVIDADYQVEPD---WLkrLVPIFDDPRVGFVQAPQDYRDgEESLFKRMCYAEYKGFfdIGMVSRNER--NA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 227 VFTVsGVIAAFRRQALADVGYWSPDMITEDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQGGAEVFLV 306
Cdd:cd06435  156 IIQH-GTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKK 234


                 ....*...
gi 496082723 307 nlrrlfHW 314
Cdd:cd06435  235 ------HW 236
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
74-326 1.97e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 77.34  E-value: 1.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  74 NPLISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAqeEPRLRVIHLAANQGKAVALKAGAAA 153
Cdd:COG1216    2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLGLRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 154 ARGDLLVCIDGDALLDRDTAAWLVAplihyphvgavTGNprirtrstligriqvgefssiiglikrtqriygrvftvsgv 233
Cdd:COG1216   80 AGGDYLLFLDDDTVVEPDWLERLLA-----------AAC----------------------------------------- 107

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 234 iAAFRRQALADVGYWSPDMIT--EDIDISWKLQLRHWDIFFEPRALCWILMPETLKGLWKQRLRWAQggaevflvnlRRL 311
Cdd:COG1216  108 -LLIRREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYLGRN----------RLL 176

                        250
                 ....*....|....*
gi 496082723 312 FHWEHHRMWPLFLEY 326
Cdd:COG1216  177 FLRKHGPRPLLRLAL 191
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 79-279 4.31e-15

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: 72.59  E-value: 4.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLaqeEPRLRVIHLAANQGKAVALKAGAAAARGDL 158
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLREL---FPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 159 LVCIDGDALLDRDTAAWLVAPLIHYPHVGAVTGnprirtrstligriqvgefssiiglikrtqriygrvfTVSGVIAAFR 238
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAAEQDPDVGIVGP-------------------------------------KVSGAFLLVR 120

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 496082723 239 RQALADVGYWSPD--MITEDIDISWKLQLRHWDIFFEPRALCW 279
Cdd:cd04186  121 REVFEEVGGFDEDffLYYEDVDLCLRARLAGYRVLYVPQAVIY 163
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 72-142 4.16e-12

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 66.99  E-value: 4.16e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496082723  72 PGNPLISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHlAANQG 142
Cdd:PRK10073   3 NSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLH-QANAG 72
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 79-165 2.29e-11

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: 62.97  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEK-------NARETISAALAQRYanlEVIAINDGSSDNTAQVLQQLAQEEPRL-RVIHLAANQGKAVALKAG 150
Cdd:cd04188    1 VVIPAYNEEKrlpptleEAVEYLEERPSFSY---EIIVVDDGSKDGTAEVARKLARKNPALiRVLTLPKNRGKGGAVRAG 77

                         90
                 ....*....|....*
gi 496082723 151 AAAARGDLLVCIDGD 165
Cdd:cd04188   78 MLAARGDYILFADAD 92
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 75-184 3.76e-11

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: 62.22  E-value: 3.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  75 PLISILIPCFN-EEKNARETISAALAQRYANLEVIAINDGSSDN-TAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAA 152
Cdd:cd04184    1 PLISIVMPVYNtPEKYLREAIESVRAQTYPNWELCIADDASTDPeVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 496082723 153 AARGDLLVCIDGDALLDRDTAAWLVAPLIHYP 184
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALNEHP 112
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 155-297 4.48e-10

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: 58.45  E-value: 4.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  155 RGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAVTGNPRIRTRSTLIGRIQVGEFSsiiGLIKRTQRIYGRVFTVSGVI 234
Cdd:pfam13506  30 KYDLLVISDSDIRVPPDYLRDLLAPLAD-PKVGLVTSPPVGSDPKGLAAALEAAFFN---TLAGVLQAALSGIGFAVGMS 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496082723  235 AAFRRQALADVGYWSP--DMITEDIDISWKLQLRHWDIFFEPRALCWILMPE--TLKGLWKQRLRWA 297
Cdd:pfam13506 106 MAFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFRAFMARQLRWA 172
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 79-256 5.19e-10

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: 58.55  E-value: 5.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALAQRyANLEVIAINDGSSDNTAQVLqQLAQEEPRLRVI--HLA-ANQGK----------AV 145
Cdd:cd06436    1 VLVPCLNEEAVIQRTLASLLRNK-PNFLVLVIDDASDDDTAGIV-RLAITDSRVHLLrrHLPnARTGKgdalnaaydqIR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 146 ALKAGAAAARGDLLVC-IDGDALLDrDTAAWLVAPLIHYPHVGAVTGNPRIRTRST-LIGRIQVGEFSSIIGLIKRTQRI 223
Cdd:cd06436   79 QILIEEGADPERVIIAvIDADGRLD-PNALEAVAPYFSDPRVAGTQSRVRMYNRHKnLLTILQDLEFFIIIAATQSLRAL 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 496082723 224 YGRVfTVSGVIAAFRRQALADV---GYWsPDMITED 256
Cdd:cd06436  158 TGTV-GLGGNGQFMRLSALDGLigeEPW-SDSLLED 191
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
74-165 9.45e-09

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 56.15  E-value: 9.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  74 NPLISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSdnTAQVLQQLAQE--EPRLRVIHLAANQGKAVALKAGA 151
Cdd:PRK10018   4 NPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTAlnDPRITYIHNDINSGACAVRNQAI 81

                         90
                 ....*....|....
gi 496082723 152 AAARGDLLVCIDGD 165
Cdd:PRK10018  82 MLAQGEYITGIDDD 95
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 79-165 1.24e-07

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 52.15  E-value: 1.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  79 ILIPCFNEEKNARETISAALAQ-RYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIHLAANQGKAVALKAGAAAARGD 157
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAAlKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80


                 ....*...
gi 496082723 158 LLVCIDGD 165
Cdd:cd06442   81 VIVVMDAD 88
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 78-209 1.89e-07

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: 51.39  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  78 SILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQeeprlRVIHL----------AANQGkaval 147
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYED-----KITYWisepdkgiydAMNKG----- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496082723 148 kagAAAARGDLLVCI-DGDALLDRDTAAWLVAPLIHyPHVGAVTGNPRIRTRSTLIGRIQVGE 209
Cdd:cd06433   71 ---IALATGDIIGFLnSDDTLLPGALLAVVAAFAEH-PEVDVVYGDVLLVDENGRVIGRRRPP 129
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 77-165 1.64e-06

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 49.73  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  77 ISILIPCFNEEKNARETI---SAALAQRYANLEVIAINDGSSDNTAQVLQQLAQ-EEPRLRVIHLAANQGKAVALKAGAA 152
Cdd:PRK10714   8 VSVVIPVYNEQESLPELIrrtTAACESLGKEYEILLIDDGSSDNSAEMLVEAAQaPDSHIVAILLNRNYGQHSAIMAGFS 87

                         90
                 ....*....|...
gi 496082723 153 AARGDLLVCIDGD 165
Cdd:PRK10714  88 HVTGDLIITLDAD 100
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 78-136 3.25e-06

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: 48.01  E-value: 3.25e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 496082723  78 SILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPRLRVIH 136
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILI 59
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 77-165 5.54e-06

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 48.22  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  77 ISILIPCFNEE----KNARETI----SAALAQRYANLEVIAINDGSSDNTAQVLQQLAQEEPR----LRVIHLAANQGKA 144
Cdd:PTZ00260  72 LSIVIPAYNEEdrlpKMLKETIkyleSRSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSLLRNKGKG 151

                         90       100
                 ....*....|....*....|.
gi 496082723 145 VALKAGAAAARGDLLVCIDGD 165
Cdd:PTZ00260 152 GAVRIGMLASRGKYILMVDAD 172
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 77-191 2.49e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 46.06  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  77 ISILIPCFNEEKNARETISAALAQRYANL--EVIAINDGSSDNTAQVLQQ-----LAQEEPRLRvihLAANQGKAVALKA 149
Cdd:PRK13915  33 VSVVLPALNEEETVGKVVDSIRPLLMEPLvdELIVIDSGSTDATAERAAAagarvVSREEILPE---LPPRPGKGEALWR 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496082723 150 GAAAARGDLLVCIDGDaLLDRDT--AAWLVAPLIHYPHVGAVTG 191
Cdd:PRK13915 110 SLAATTGDIVVFVDAD-LINFDPmfVPGLLGPLLTDPGVHLVKA 152
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 77-126 3.69e-05

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: 44.87  E-value: 3.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082723  77 ISILIPCFNEEKNARETISAALAQRYANLEVIAINDGSSDNTAQVLQQLA 126
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAG 50
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 73-165 4.48e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 44.69  E-value: 4.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  73 GNPLISILIPCFNEEKN-------ARETIsaalaQRYANLEVIAINDGSSDNTAQVLQQLAQ--EEPRLRVIHLAANQGK 143
Cdd:PLN02726   7 GAMKYSIIVPTYNERLNialivylIFKAL-----QDVKDFEIIVVDDGSPDGTQDVVKQLQKvyGEDRILLRPRPGKLGL 81

                         90       100
                 ....*....|....*....|..
gi 496082723 144 AVALKAGAAAARGDLLVCIDGD 165
Cdd:PLN02726  82 GTAYIHGLKHASGDFVVIMDAD 103
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 75-191 1.01e-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: 42.97  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723  75 PLISILIPCFNEEKNARETISAALAQRYANLEVI-AINDGsSDNTAQVLQQLAQEEPRLRVI------HLAANqGKAVAL 147
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILfCVQDE-DDPAIPVVRKLIAKYPNVDARlliggeKVGIN-PKVNNL 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 496082723 148 KAGAAAARGDLLVCIDGDALLDRDTAAWLVAPLIHyPHVGAVTG 191
Cdd:cd02520   79 IKGYEEARYDILVISDSDISVPPDYLRRMVAPLMD-PGVGLVTC 121
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 91-142 6.74e-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: 40.70  E-value: 6.74e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496082723  91 RETISAALAQRYANLEVIAINDGSSDNTAQVLQQLAQeEPRLRVIHLAANQG 142
Cdd:cd04185   13 KECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGD-LDNIVYLRLPENLG 63
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 79-121 2.43e-03

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: 38.74  E-value: 2.43e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 496082723  79 ILIPCFNEEKNARETISAALAQRY--ANLEVIAINDGSSDNTAQV 121
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYprELYRIFVVADNCTDDTAQV 45
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
 159-296 2.44e-03

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: 39.60  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 159 LVCIDGDALLDRDTAAWLVAPLIHYPHVGAVTG--NPRIRTRSTLIgRIQVGEFSSIIGLIKRTQRIYGRVFTVSGVIAA 236
Cdd:cd04190   77 ILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGeiHPMGKKQGPLV-MYQVFEYAISHWLDKAFESVFGFVTCLPGCFSM 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496082723 237 FRRQALADV-GYWSPDM----ITEDIDISWKLQLRHwdiFFEPRALCWILM--------------------PETLKGLWK 291
Cdd:cd04190  156 YRIEALKGDnGGKGPLLdyayLTNTVDSLHKKNNLD---LGEDRILCTLLLkagpkrkylyvpgavaetdvPETFVELLS 232


                 ....*
gi 496082723 292 QRLRW 296
Cdd:cd04190  233 QRRRW 237
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 77-125 9.97e-03

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


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 37.27  E-value: 9.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496082723  77 ISILIPCFNEEKNARETI-SAALAQRyanlEVIAINDGSSDNTAQVLQQL 125
Cdd:cd02511    2 LSVVIITKNEERNIERCLeSVKWAVD----EIIVVDSGSTDRTVEIAKEY 47
 
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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