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Conserved domains on  [gi|1320716433|gb|AUL14929|]
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poly-beta-1,6 N-acetyl-D-glucosamine synthase [Bordetella bronchiseptica]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PgaC_IcaA super family cl37350
poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are ...
 9-411 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.


The actual alignment was detected with superfamily member TIGR03937:

Pssm-ID: 274866 [Multi-domain]  Cd Length: 407  Bit Score: 584.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433   9 LSSFVFYYPFFMSYFWIVGGLLHFFLFEQGR---KHRATLLPRVPRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAV 85
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWplpRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  86 NDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVT 165
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 166 GNPRIRNRSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTL 245
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 246 RYEPRALTWILMPETFRGLFKQRYRWARGGIETALKYAPRMLNPRQILMWPIFLEFSLSVLWAYAMLFLICMAVLGQFV- 324
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIl 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 325 -ALPPAWQFEIFpRWHGTLLFLTCLAQLFAGCIVDRAYDYRIFRYFADAVWYPIAFWIIGMITTVFALPRVLFRRAQSRA 403
Cdd:TIGR03937 321 pYTPLVYSISLF-QWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRA 399


                  ....*...
gi 1320716433 404 RWVSPDRG 411
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 ...
 9-411 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: 584.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433   9 LSSFVFYYPFFMSYFWIVGGLLHFFLFEQGR---KHRATLLPRVPRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAV 85
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWplpRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  86 NDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVT 165
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 166 GNPRIRNRSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTL 245
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 246 RYEPRALTWILMPETFRGLFKQRYRWARGGIETALKYAPRMLNPRQILMWPIFLEFSLSVLWAYAMLFLICMAVLGQFV- 324
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIl 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 325 -ALPPAWQFEIFpRWHGTLLFLTCLAQLFAGCIVDRAYDYRIFRYFADAVWYPIAFWIIGMITTVFALPRVLFRRAQSRA 403
Cdd:TIGR03937 321 pYTPLVYSISLF-QWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRA 399


                  ....*...
gi 1320716433 404 RWVSPDRG 411
Cdd:TIGR03937 400 VWVSPDRG 407
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 18-352 3.76e-61

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: 200.35  E-value: 3.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  18 FFMSYFWIVGGLLHFFLFEQGRKHRATLlprvPRVAIVVPCYNEGENVAEVIAHLDRMHYP--NYRIIAVNDGSRDNTGA 95
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRRAPADL----PRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  96 LLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGhVGAvtgnprirnrst 175
Cdd:COG1215    77 IARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG-VGA------------ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 176 vlgrmqvgefssivglikrtqqlygklmtvSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWI 255
Cdd:COG1215   144 ------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYE 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 256 LMPETFRGLFKQRYRWARGGIETALKYaPRMLNPRQILMWPIFLEFSLSVLWAYAMLFLICMAVLGQFVAlppAWQFEIF 335
Cdd:COG1215   194 EAPETLRALFRQRRRWARGGLQLLLKH-RPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLL---ALLLALR 269

                         330
                  ....*....|....*..
gi 1320716433 336 PRWHGTLLFLTCLAQLF 352
Cdd:COG1215   270 RRRLLLPLLHLLYGLLL 286
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 54-231 1.43e-59

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: 192.06  E-value: 1.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQY-PRLLVVHQSRNEGKAIGLNTAAQLSDAE 132
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYiRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 133 FLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTGNPRIRNRS-TVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTM 211
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSeNLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGA 160

                         170       180
                  ....*....|....*....|
gi 1320716433 212 FRKQALHQVGYWSPDMQTED 231
Cdd:cd06423   161 FRREALREVGGWDEDTLTED 180
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 54-219 3.15e-36

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: 130.59  E-value: 3.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEF 133
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGDY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 134 LLCIDGDSLPHPDSITYMLTHFLHAGHVGAVtGNPRIRNRSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTMFR 213
Cdd:pfam00535  82 IAFLDADDEVPPDWLEKLVEALEEDGADVVV-GSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALYR 160


                  ....*.
gi 1320716433 214 KQALHQ 219
Cdd:pfam00535 161 REALEE 166
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 50-146 9.26e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 62.76  E-value: 9.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSrNEGKAIGLNTAAQLS 129
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQA-NAGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1320716433 130 DAEFLLCIDGDSLPHPD 146
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
 
Name Accession Description Interval E-value
PgaC_IcaA TIGR03937
poly-beta-1,6 N-acetyl-D-glucosamine synthase; Members of this protein family are ...
 9-411 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: 584.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433   9 LSSFVFYYPFFMSYFWIVGGLLHFFLFEQGR---KHRATLLPRVPRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAV 85
Cdd:TIGR03937   1 LFNFVFFYPLFMSIYWIVGGVYYYFHWERKWplpRTRPPPLDEYPGVSILVPCYNEGANVEETISHLLALRYPNFEIIAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  86 NDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVT 165
Cdd:TIGR03937  81 NDGSKDNTAEILDRLAAQDPRLRVIHLAENQGKANALNTGLLAAKYEYLVCIDGDALLDPDAAYWMVEHFLSNPRVGAVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 166 GNPRIRNRSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTL 245
Cdd:TIGR03937 161 GNPRIRNRSTILGKIQVGEFSSIIGLIKRAQRVYGTIFTVSGVITAFRKSALHDVGYWSTDMITEDIDISWKLQLAGWNI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 246 RYEPRALTWILMPETFRGLFKQRYRWARGGIETALKYAPRMLNPRQILMWPIFLEFSLSVLWAYAMLFLICMAVLGQFV- 324
Cdd:TIGR03937 241 RYEPRALCWILMPETLRGLWKQRLRWAQGGAEVLLKYFRQLWRWRNRRLWPLLFEYIVSVIWAYSVLLLLILWLIQVNIl 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 325 -ALPPAWQFEIFpRWHGTLLFLTCLAQLFAGCIVDRAYDYRIFRYFADAVWYPIAFWIIGMITTVFALPRVLFRRAQSRA 403
Cdd:TIGR03937 321 pYTPLVYSISLF-QWSGLLLTFICLLQFTVSLFIDSRYEKGLLRYLFWCIWYPTVYWLLNAATTVVAFPKALLRKKGKRA 399


                  ....*...
gi 1320716433 404 RWVSPDRG 411
Cdd:TIGR03937 400 VWVSPDRG 407
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 18-352 3.76e-61

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: 200.35  E-value: 3.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  18 FFMSYFWIVGGLLHFFLFEQGRKHRATLlprvPRVAIVVPCYNEGENVAEVIAHLDRMHYP--NYRIIAVNDGSRDNTGA 95
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRRAPADL----PRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  96 LLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGhVGAvtgnprirnrst 175
Cdd:COG1215    77 IARELAAEYPRVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG-VGA------------ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 176 vlgrmqvgefssivglikrtqqlygklmtvSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWI 255
Cdd:COG1215   144 ------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYE 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 256 LMPETFRGLFKQRYRWARGGIETALKYaPRMLNPRQILMWPIFLEFSLSVLWAYAMLFLICMAVLGQFVAlppAWQFEIF 335
Cdd:COG1215   194 EAPETLRALFRQRRRWARGGLQLLLKH-RPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLL---ALLLALR 269

                         330
                  ....*....|....*..
gi 1320716433 336 PRWHGTLLFLTCLAQLF 352
Cdd:COG1215   270 RRRLLLPLLHLLYGLLL 286
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 54-231 1.43e-59

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: 192.06  E-value: 1.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQY-PRLLVVHQSRNEGKAIGLNTAAQLSDAE 132
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYiRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 133 FLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTGNPRIRNRS-TVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTM 211
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSeNLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGAFGA 160

                         170       180
                  ....*....|....*....|
gi 1320716433 212 FRKQALHQVGYWSPDMQTED 231
Cdd:cd06423   161 FRREALREVGGWDEDTLTED 180
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 54-219 3.15e-36

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: 130.59  E-value: 3.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEF 133
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGDY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 134 LLCIDGDSLPHPDSITYMLTHFLHAGHVGAVtGNPRIRNRSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTMFR 213
Cdd:pfam00535  82 IAFLDADDEVPPDWLEKLVEALEEDGADVVV-GSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALYR 160


                  ....*.
gi 1320716433 214 KQALHQ 219
Cdd:pfam00535 161 REALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 50-249 8.77e-36

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 130.59  E-value: 8.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLS 129
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 130 DAEFLLCIDGDSLPHPDSITYMLtHFLHAGHVGAVTGNPRIRNRSTVLGRMQVGEFSSIvglikrtqQLYGKLMTVSGVM 209
Cdd:COG0463    82 RGDYIAFLDADDQLDPEKLEELV-AALEEGPADLVYGSRLIREGESDLRRLGSRLFNLV--------RLLTNLPDSTSGF 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1320716433 210 TMFRKQALHQVGYWSPDMqtEDIDISWkLQLAGWTLRYEP 249
Cdd:COG0463   153 RLFRREVLEELGFDEGFL--EDTELLR-ALRHGFRIAEVP 189
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 50-279 1.35e-29

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: 114.98  E-value: 1.35e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAE--VIAHLDrMHYPN--YRIIAVNDGSRDNTGALLNELAEQYPRLLVvHQSRNEG-KAIGLNT 124
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRktLRAALA-IDYPHdkLRVYVLDDGRRPELRALAAELGVEYGYRYL-TRPDNRHaKAGNLNN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 125 AAQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTG------NPRIRNRSTVLGRMQvgefssivGLIKRTQQL 198
Cdd:cd06421    79 ALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTpqffynPDPFDWLADGAPNEQ--------ELFYGVIQP 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 199 YGKLMTVS---GVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARGG 275
Cdd:cd06421   151 GRDRWGAAfccGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGM 230


                  ....
gi 1320716433 276 IETA 279
Cdd:cd06421   231 LQIL 234
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 50-274 1.71e-29

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: 114.39  E-value: 1.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYP--RLLVVHQSRNEG---KAIGLNT 124
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPdvRLRVIRNARLLGptgKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 125 AAQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGhVGAVTGNPRIRNRSTVLGRMQVGEFsSIVGLIKRTQQLYGKLMT 204
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPK-VGAVGTPVFSLNRSTMLSALGALEF-ALRHLRMMSLRLALGVLP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1320716433 205 VSGVMTMFRKQALHQVGYWSPD-MQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARG 274
Cdd:pfam13641 160 LSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
50-299 2.44e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 113.16  E-value: 2.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELaeQYPRLLVVHQSRNEGKAIGLNTAAQLS 129
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAAL--AFPRVRVIRNPENLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 130 DAEFLLCIDGDSLPHPDSITYMLTHFlhaghvgavtgnprirnrstvlgrmqvgefssivglikrtqqlygklmtvsgvM 209
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAAA-----------------------------------------------------C 107

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 210 TMFRKQALHQVGYWSPD--MQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKqRYRWARGGIETALKYAPRML 287
Cdd:COG1216   108 LLIRREVFEEVGGFDERffLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLR-AYYLGRNRLLFLRKHGPRPL 186

                         250
                  ....*....|..
gi 1320716433 288 NPRQILMWPIFL 299
Cdd:COG1216   187 LRLALLRGLRLR 198
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 50-278 6.73e-28

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: 110.75  E-value: 6.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPN--YRIIAVNDGSRDNTgallNELAEQYP--RLLVVHQSRNEGKAIGLNTA 125
Cdd:cd06439    29 PTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGT----AEIAREYAdkGVKLLRFPERRGKAAALNRA 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 126 AQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGhVGAVTGNPRIRNRstvlgrmqvGEFSSIVGL-------IKRTQQL 198
Cdd:cd06439   105 LALATGEIVVFTDANALLDPDALRLLVRHFADPS-VGAVSGELVIVDG---------GGSGSGEGLywkyenwLKRAESR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 199 YGKLMTVSGVMTMFRKQALHQvgyWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARGGIET 278
Cdd:cd06439   175 LGSTVGANGAIYAIRRELFRP---LPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVRIAAGNLQA 251
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 51-293 1.73e-26

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: 106.55  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  51 RVAIVVPCYNEGENVAEVIAHLDRMHYP--NYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHqsrNEGK--AIGLNTAA 126
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYAAKDPRIRLID---NPKRiqSAGLNIGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 127 QLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGhVGAVTGNPRIRNRS---TVLGRMQVGEFSSIVGLIKRTQQLYGKLM 203
Cdd:cd02525    78 RNSRGDIIIRVDAHAVYPKDYILELVEALKRTG-ADNVGGPMETIGESkfqKAIAVAQSSPLGSGGSAYRGGAVKIGYVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 204 TVsgVMTMFRKQALHQVGYWSPDM-QTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARGGIETALKY 282
Cdd:cd02525   157 TV--HHGAYRREVFEKVGGFDESLvRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKWRARTLRKH 234

                         250
                  ....*....|.
gi 1320716433 283 aPRMLNPRQIL 293
Cdd:cd02525   235 -RKSLSLRHLL 244
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 54-283 4.67e-26

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: 105.18  E-value: 4.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEG-ENVAEVIAHLDRMHYPNYRIIAVNDGSRDNT-----GALLNELAEqypRLLVVHQSRNEG-KAIGLNTAA 126
Cdd:cd06435     2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVIVIDNNTKDEAlwkpvEAHCAQLGE---RFRFFHVEPLPGaKAGALNYAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 127 QL--SDAEFLLCIDGDSLPHPDSITYMLTHFLHAgHVGAVTGNPRIRN-RSTVLGRMQVGEFSSI--VGLIKRTQqlYGK 201
Cdd:cd06435    79 ERtaPDAEIIAVIDADYQVEPDWLKRLVPIFDDP-RVGFVQAPQDYRDgEESLFKRMCYAEYKGFfdIGMVSRNE--RNA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 202 LMTVsGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARGGIETALK 281
Cdd:cd06435   156 IIQH-GTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKK 234


                  ..
gi 1320716433 282 YA 283
Cdd:cd06435   235 HW 236
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 54-169 1.53e-25

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: 101.43  E-value: 1.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEF 133
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1320716433 134 LLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTGNPR 169
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGN 116
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 50-275 4.88e-25

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 102.39  E-value: 4.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYR-IIAVNDGSRDNTGALLNELAEQYPR--LLVVHQSRNEG---KAIGLN 123
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRlEIQVLDDSTDETVRLAREIVEEYAAqgVNIKHVRRADRtgyKAGALA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 124 TAAQLSDAEFLLCIDGDSLPHPDSITYMLTHFlHAGHVGAVTGNPRIRNRST-VLGRMQVGEFSSIVGLIKRTQQLYGKL 202
Cdd:cd06437    81 EGMKVAKGEYVAIFDADFVPPPDFLQKTPPYF-ADPKLGFVQTRWGHINANYsLLTRVQAMSLDYHFTIEQVARSSTGLF 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1320716433 203 MTVSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARGG 275
Cdd:cd06437   160 FNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 133-324 1.03e-23

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


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 97.41  E-value: 1.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 133 FLLCIDGDSLPHPDSITYMLTHFLHAGhVGAVTGNPRIRNRSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVMTMF 212
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPE-VAIIQGPILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 213 RKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARGGIETAlkYAPRMLNPRQI 292
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLIL--LIRLLGYLGTL 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1320716433 293 LMWPIFLEFSLSVL--WAYAMLFLICMAVLGQFV 324
Cdd:pfam13632 158 LWSGLPLALLLLLLfsISSLALVLLLLALLAGLL 191
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 54-254 2.44e-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: 95.70  E-value: 2.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTgalLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDAEF 133
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGS---VELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 134 LLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTGnprirnrstvlgrmqvgefssivglikrtqqlygklmTVSGVMTMFR 213
Cdd:cd04186    78 VLLLNPDTVVEPGALLELLDAAEQDPDVGIVGP-------------------------------------KVSGAFLLVR 120

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1320716433 214 KQALHQVGYWSPD--MQTEDIDISWKLQLAGWTLRYEPRALTW 254
Cdd:cd04186   121 REVFEEVGGFDEDffLYYEDVDLCLRARLAGYRVLYVPQAVIY 163
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 54-274 5.83e-22

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: 93.51  E-value: 5.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYP--NYRIIAVNDGSRDNTGALL-NELAEQYPRLLVVHQSR--NEGKAIGLNTAAQL 128
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPkeKFEVILVDDHSTDGTVQILeFAAAKPNFQLKILNNSRvsISGKKNALTTAIKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 129 SDAEFLLCIDGDSLPHPDSI-TYMLTHFLH--AGHVGAVTGnprIRNRStVLGRMQVGEFSSIVGLIKRTQQLyGKLMTV 205
Cdd:cd04192    81 AKGDWIVTTDADCVVPSNWLlTFVAFIQKEqiGLVAGPVIY---FKGKS-LLAKFQRLDWLSLLGLIAGSFGL-GKPFMC 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1320716433 206 SGVMTMFRKQALHQVGYWS--PDMQTEDIDISWKLQLAGWT-LRYE--PRALTWILMPETFRGLFKQRYRWARG 274
Cdd:cd04192   156 NGANMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYPkVAYLknPEALVTTQPVTSWKELLNQRKRWASK 229
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 54-172 9.98e-22

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: 91.87  E-value: 9.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRM--HYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLSDA 131
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVleEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1320716433 132 EFLLCIDGDsLPH-PDSITYMLTHfLHAGHVGAVTGNPRIRN 172
Cdd:cd04179    81 DIVVTMDAD-LQHpPEDIPKLLEK-LLEGGADVVIGSRFVRG 120
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 54-145 2.40e-18

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: 82.14  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGEN----VAEVIAHLDRMHYpNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQLS 129
Cdd:cd04187     1 IVVPVYNEEENlpelYERLKAVLESLGY-DYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGQQAALLAGLDHA 79

                          90
                  ....*....|....*.
gi 1320716433 130 DAEFLLCIDGDsLPHP 145
Cdd:cd04187    80 RGDAVITMDAD-LQDP 94
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 50-289 6.02e-17

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 79.61  E-value: 6.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYR---IIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAA 126
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKldvKLLLEEDDEETIAAARALRLPSIFRVVVVPPSQPRTKPKACNYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 127 QLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAG-HVGAVTGNPRIRN-RSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMT 204
Cdd:cd06427    81 AFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDdKLACVQAPLNYYNaRENWLTRMFALEYAAWFDYLLPGLARLGLPIP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 205 VSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRAlTWILMPETFRGLFKQRYRWARGGIETalkYAP 284
Cdd:cd06427   161 LGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNST-TLEEANNALGNWIRQRSRWIKGYMQT---WLV 236


                  ....*
gi 1320716433 285 RMLNP 289
Cdd:cd06427   237 HMRNP 241
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 54-140 4.98e-16

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: 76.45  E-value: 4.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGE----NVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLL-VVHQSRNEGKAIGLNTAAQL 128
Cdd:cd04188     1 VVIPAYNEEKrlppTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIrVLTLPKNRGKGGAVRAGMLA 80

                          90
                  ....*....|..
gi 1320716433 129 SDAEFLLCIDGD 140
Cdd:cd04188    81 ARGDYILFADAD 92
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 54-160 3.80e-15

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: 74.11  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDR-MHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHqsrNEGKAiGLNTA----AQL 128
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAaLKGIDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIV---RPGKR-GLGSAyiegFKA 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1320716433 129 SDAEFLLCIDGDSLPHPDSITYMLTHFLHAGH 160
Cdd:cd06442    77 ARGDVIVVMDADLSHPPEYIPELLEAQLEGGA 108
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 52-275 5.51e-14

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: 71.13  E-value: 5.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  52 VAIVVPCYNEGENV-AEVIAHLDRMHypNYRIIAVNDGsRDNTGALLNELAEQYPRLLVVHQSRnEGKAIGLNTAAQLSD 130
Cdd:cd06434     2 VTVIIPVYDEDPDVfRECLRSILRQK--PLEIIVVTDG-DDEPYLSILSQTVKYGGIFVITVPH-PGKRRALAEGIRHVT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 131 AEFLLCIDGDSLPHPDSITYMLTHFLhAGHVGAVTGNPRIRN-RSTVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGVM 209
Cdd:cd06434    78 TDIVVLLDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRpRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLSGRT 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1320716433 210 TMFRKQALHQVGYwSPDMQTE-----------DIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARGG 275
Cdd:cd06434   157 AAYRTEILKDFLF-LEEFTNEtfmgrrlnagdDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQLRWSRSN 232
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
 130-271 8.52e-12

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: 64.64  E-value: 8.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 130 DAEFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTGNPRIRNRS-TVLGRMQVGEFSSIVGLIKRTQQLYGKLMTVSGV 208
Cdd:cd04190    73 DPEFILLVDADTKFDPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKqGPLVMYQVFEYAISHWLDKAFESVFGFVTCLPGC 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 209 MTMFRKQALHQV-GYWSPDMQ----TEDIDISWK---LQLAgwtlryEPRALTWILM--------------------PET 260
Cdd:cd04190   153 FSMYRIEALKGDnGGKGPLLDyaylTNTVDSLHKknnLDLG------EDRILCTLLLkagpkrkylyvpgavaetdvPET 226

                         170
                  ....*....|.
gi 1320716433 261 FRGLFKQRYRW 271
Cdd:cd04190   227 FVELLSQRRRW 237
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 50-146 9.26e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 62.76  E-value: 9.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSrNEGKAIGLNTAAQLS 129
Cdd:PRK10073    6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRLLHQA-NAGVSVARNTGLAVA 84

                          90
                  ....*....|....*..
gi 1320716433 130 DAEFLLCIDGDSLPHPD 146
Cdd:PRK10073   85 TGKYVAFPDADDVVYPT 101
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 48-153 1.18e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 58.56  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  48 RVPRVAIVVPCYNEGENVAeVIAHLDRMHYP---NYRIIAVNDGSRDNTGALLNELAEQYPRLLVVHQSRneGKAIGLNT 124
Cdd:PLN02726    7 GAMKYSIIVPTYNERLNIA-LIVYLIFKALQdvkDFEIIVVDDGSPDGTQDVVKQLQKVYGEDRILLRPR--PGKLGLGT 83

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1320716433 125 A--AQLSDA--EFLLCIDGDSLPHPDSITYMLT 153
Cdd:PLN02726   84 AyiHGLKHAsgDFVVIMDADLSHHPKYLPSFIK 116
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 54-158 1.17e-08

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 54.51  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYP-RLLVVHQsRNEG--KAIGLNTAAQLSD 130
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPiPIKHVWQ-EDEGfrKAKIRNKAIAAAK 79

                          90       100
                  ....*....|....*....|....*...
gi 1320716433 131 AEFLLCIDGDSLPHPDSITymlTHFLHA 158
Cdd:cd06420    80 GDYLIFIDGDCIPHPDFIA---DHIELA 104
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 134-273 8.52e-08

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: 51.51  E-value: 8.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 134 LLCI-DGDSLPHPDSITYMLTHFLHAGhVGAVTGNPRIRNRSTVLGRMQVGEFSSIVGLIkrtqqlygkLMTVSGV---- 208
Cdd:pfam13506  33 LLVIsDSDIRVPPDYLRDLLAPLADPK-VGLVTSPPVGSDPKGLAAALEAAFFNTLAGVL---------QAALSGIgfav 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1320716433 209 -MTM-FRKQALHQVGYWSP--DMQTEDIDISWKLQLAGWTLRYEPRALTWILMPE--TFRGLFKQRYRWAR 273
Cdd:pfam13506 103 gMSMaFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFRAFMARQLRWAR 173
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 53-170 1.68e-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: 51.48  E-value: 1.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  53 AIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQYPRLLVVH-QSRNEGKAIGLNTAAQLSDA 131
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIrNGKNLGVARNFESLLQAADG 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1320716433 132 EFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTGNPRI 170
Cdd:cd04196    81 DYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLEL 119
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 52-238 1.92e-07

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily of unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 51.42  E-value: 1.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  52 VAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAeqyprllVVHQSRNEGKAIGLNTAAQLSDA 131
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAG-------VVVISSPKGRARQMNAGAAAARG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 132 EFLLCIDGDSLPHPDSITyMLTHFLHAGHVGAVTGNPRIRNRSTVLGRMQVGEF--SSIVGLIKRTQQLygklmtvsgvm 209
Cdd:cd02522    74 DWLLFLHADTRLPPDWDA-AIIETLRADGAVAGAFRLRFDDPGPRLRLLELGANlrSRLFGLPYGDQGL----------- 141

                         170       180
                  ....*....|....*....|....*....
gi 1320716433 210 tMFRKQALHQVGYWSPDMQTEDIDISWKL 238
Cdd:cd02522   142 -FIRRELFEELGGFPELPLMEDVELVRRL 169
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 50-146 3.16e-07

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 50.66  E-value: 3.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYN-EGENVAEVIAHLDRMHYPNYRIIAVNDGSRDN-TGALLNELAEQYPRLLVVHQSRNEGKAIGLNTAAQ 127
Cdd:cd04184     1 PLISIVMPVYNtPEKYLREAIESVRAQTYPNWELCIADDASTDPeVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80

                          90
                  ....*....|....*....
gi 1320716433 128 LSDAEFLLCIDGDSLPHPD 146
Cdd:cd04184    81 LATGEFVALLDHDDELAPH 99
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 53-140 5.77e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 50.92  E-value: 5.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  53 AIVVPCYNE----GENVAEVIAHLDRMHYPN----YRIIAVNDGSRDNTGALLNELAEQYPR----LLVVHQSRNEGKAI 120
Cdd:PTZ00260   73 SIVIPAYNEedrlPKMLKETIKYLESRSRKDpkfkYEIIIVNDGSKDKTLKVAKDFWRQNINpnidIRLLSLLRNKGKGG 152

                          90       100
                  ....*....|....*....|
gi 1320716433 121 GLNTAAQLSDAEFLLCIDGD 140
Cdd:PTZ00260  153 AVRIGMLASRGKYILMVDAD 172
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 53-243 6.44e-07

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: 49.97  E-value: 6.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  53 AIVVpCYNEgeNVAEVIAHLDRMHYPNYRIIAVndgsrDNTGALLNELAEQYP--RLLVVHQSRNEGKAIGLNT---AAQ 127
Cdd:cd02526     1 AVVV-TYNP--DLSKLKELLAALAEQVDKVVVV-----DNSSGNDIELRLRLNseKIELIHLGENLGIAKALNIgikAAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 128 LSDAEFLLCIDGDSLPHPDSITYMLTHFLH---AGHVGAVTgnPRIRNRSTvlgrmqvGEFSSIVGLIKRTQQLYGKLMT 204
Cdd:cd02526    73 ENGADYVLLFDQDSVPPPDMVEKLLAYKILsdkNSNIGAVG--PRIIDRRT-------GENSPGVRKSGYKLRIQKEGEE 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1320716433 205 ----VSGVMT---MFRKQALHQVGYwspdMQTE------DIDISWKLQLAGW 243
Cdd:cd02526   144 glkeVDFLITsgsLISLEALEKVGG----FDEDlfidyvDTEWCLRARSKGY 191
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
 54-206 1.06e-06

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: 48.92  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMhYPNYRIIAVNDGSRDNTGALLnELAEQYPRLLVVHQSRNE---GKAIGLNTA-AQLS 129
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRN-KPNFLVLVIDDASDDDTAGIV-RLAITDSRVHLLRRHLPNartGKGDALNAAyDQIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 130 --------DAE--FLLCIDGDSLPHPDSITyMLTHFLHAGHVGAVTGNPRIRNRST-VLGRMQVGEFSSIvglIKRTQQL 198
Cdd:cd06436    79 qilieegaDPErvIIAVIDADGRLDPNALE-AVAPYFSDPRVAGTQSRVRMYNRHKnLLTILQDLEFFII---IAATQSL 154


                  ....*...
gi 1320716433 199 YGKLMTVS 206
Cdd:cd06436   155 RALTGTVG 162
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 53-155 3.15e-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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 47.63  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  53 AIVVpCYNEGENVAEVIAHLDRMHYPNYRIIAVNDGSRDNTGALLNELAEQyPRLLVVHQSRNEGKAIGLNTAAQL---S 129
Cdd:cd04185     1 AVVV-TYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDL-DNIVYLRLPENLGGAGGFYEGVRRayeL 78

                          90       100
                  ....*....|....*....|....*.
gi 1320716433 130 DAEFLLCIDGDSLPHPDSITYMLTHF 155
Cdd:cd04185    79 GYDWIWLMDDDAIPDPDALEKLLAYA 104
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
50-154 1.58e-05

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 46.14  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAHLDRMHYPNYRIIAVND--GSRDNTGALLNELAEqyPRLLVVHQSRNEGKAIGLNTAAQ 127
Cdd:PRK10018    5 PLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDcsTSWEQLQQYVTALND--PRITYIHNDINSGACAVRNQAIM 82

                          90       100
                  ....*....|....*....|....*..
gi 1320716433 128 LSDAEFLLCIDGDSLPHPDSITYMLTH 154
Cdd:PRK10018   83 LAQGEYITGIDDDDEWTPNRLSVFLAH 109
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 47-103 6.76e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 44.73  E-value: 6.76e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  47 PRVPRVAIVVPCYNEGENVAEVIAHLD---RMHYPNYRIIAVNDGSRDNTGALLNELAEQ 103
Cdd:PRK10714    3 HPIKKVSVVIPVYNEQESLPELIRRTTaacESLGKEYEILLIDDGSSDNSAEMLVEAAQA 62
PRK14716 PRK14716
glycosyl transferase family protein;
50-336 1.08e-03

glycosyl transferase family protein;


Pssm-ID: 237800 [Multi-domain]  Cd Length: 504  Bit Score: 41.20  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENVAEVIAH-LDRMHYPNYRIIAvndGSRDNTGALLNE---LAEQYPRL-LVVHQsrNEG---KAIG 121
Cdd:PRK14716   66 KRIAIFVPAWREADVIGRMLEHnLATLDYENYRIFV---GTYPNDPATLREvdrLAARYPRVhLVIVP--HDGptsKADC 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 122 LNTAAQ-----------------LSDAEFLLcidgdslpHPDSITYMlTHFLHAGHVGAVTGNPRIRNRSTVLGRMQVGE 184
Cdd:PRK14716  141 LNWIYQaifaferergirfaiivLHDAEDVI--------HPLELRLY-NYLLPRHDFVQLPVFSLPRDWGEWVAGTYMDE 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 185 FSsivglikrtqQLYGKLMTV----------SGVMTMFRKQALHQV------GYWSPDMQTEDIDISWKLQLAGWTLRYE 248
Cdd:PRK14716  212 FA----------ESHLKDLPVrealgglipsAGVGTAFSRRALERLaaerggQPFDSDSLTEDYDIGLRLKRAGFRQIFV 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 249 PRALTWI---------------LMPETFRGLFKQRYRWARGgieTALKYAPRMLNPRQILMWPIFLE------FSLSVLW 307
Cdd:PRK14716  282 RVRADDTtdrpdrrgepiatreFFPDTFKAAVRQKARWIYG---IAFQGWERLGWKGPAATKYMLWRdrkgllTNLLLFL 358

                         330       340
                  ....*....|....*....|....*....
gi 1320716433 308 AYAMLFLICMAVLGQFVALPPAWQFEIFP 336
Cdd:PRK14716  359 AYLLLLLVALVLFGSWLGGWAWSYGSPLP 387
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 50-274 1.49e-03

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 40.78  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  50 PRVAIVVPCYNEGENV--AEVIAHLDrMHYP--NYRIIAVNDGSRDNTGALLNELAEQYprllVVHQSRNEGKAIGLNTA 125
Cdd:PRK11498  260 PTVDIFVPTYNEDLNVvkNTIYASLG-IDWPkdKLNIWILDDGGREEFRQFAQEVGVKY----IARPTHEHAKAGNINNA 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 126 AQLSDAEFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAV-------TGNPRIRNrstvLGRMQV--GEFSSIVGLIKRTQ 196
Cdd:PRK11498  335 LKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMqtphhffSPDPFERN----LGRFRKtpNEGTLFYGLVQDGN 410

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1320716433 197 QLYGKLMtVSGVMTMFRKQALHQVGYWSPDMQTEDIDISWKLQLAGWTLRYEPRALTWILMPETFRGLFKQRYRWARG 274
Cdd:PRK11498  411 DMWDATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARG 487
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
 54-232 4.15e-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: 37.97  E-value: 4.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  54 IVVPCYNEGENVAEVIAHLDRMHYP--NYRIIAVNDGSRDNTGALLNEL-AEQYPRllvvHQSRNEGKAIGLN-----TA 125
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPreLYRIFVVADNCTDDTAQVARAAgATVLER----HDPERRGKGYALDfgfrhLL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 126 AQLSDAEFLLCIDGDSLPHPDSITYMLTHFlhAGHVGAVTG-----NP-------------RIRNRSTVLGRMQVGEfss 187
Cdd:cd06438    77 NLADDPDAVVVFDADNLVDPNALEELNARF--AAGARVVQAyynskNPddswitrlyafafLVFNRLRPLGRSNLGL--- 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1320716433 188 ivglikrTQQLYGKLMtvsgvmtMFRKQALHQVGYWSPDMqTEDI 232
Cdd:cd06438   152 -------SCQLGGTGM-------CFPWAVLRQAPWAAHSL-TEDL 181
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
 52-204 4.85e-03

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


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 38.41  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433  52 VAIVVPCYNegENVAEVIAHLDRM--------HYPNYRIIAVNDgSRDNTGALLNELA--------EQYPRLLVVHQSRN 115
Cdd:cd04191     1 TAIVMPVYN--EDPARVFAGLRAMyeslaktgLADHFDFFILSD-TRDPDIWLAEEAAwldlceelGAQGRIYYRRRREN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1320716433 116 EGKAIGlNTAAQL----SDAEFLLCIDGDSLPHPDSITYMLTHFLHAGHVGAVTGNPRIRNRSTVLGRMQvgEFSSivgl 191
Cdd:cd04191    78 TGRKAG-NIADFCrrwgSRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGAETLFARLQ--QFAN---- 150

                         170
                  ....*....|...
gi 1320716433 192 ikrtqQLYGKLMT 204
Cdd:cd04191   151 -----RLYGPVFG 158
 
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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