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Conserved domains on  [gi|75273615|sp|Q9LJP4|]
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RecName: Full=Xyloglucan glycosyltransferase 4; AltName: Full=Cellulose synthase-like protein C4; Short=AtCslC4; AltName: Full=Xyloglucan synthase 4

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
199-435 3.02e-119

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.


The actual alignment was detected with superfamily member cd06437:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 232  Bit Score: 355.08  E-value: 3.02e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 199 PMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIQVLDDSDDPNLQLLIKEEVSVWAeKGVNIIYRHRLIRTGYKAGNL 278
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 279 KSAMTcdyVKDYEFVTIFDADFTPNPDFLKKTVPHFKgNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQQV-NG 357
Cdd:cd06437  80 AEGMK---VAKGEYVAIFDADFVPPPDFLQKTPPYFA-DPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVArSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75273615 358 VFLnFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGP 435
Cdd:cd06437 156 TGL-FFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
199-435 3.02e-119

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: 355.08  E-value: 3.02e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 199 PMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIQVLDDSDDPNLQLLIKEEVSVWAeKGVNIIYRHRLIRTGYKAGNL 278
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 279 KSAMTcdyVKDYEFVTIFDADFTPNPDFLKKTVPHFKgNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQQV-NG 357
Cdd:cd06437  80 AEGMK---VAKGEYVAIFDADFVPPPDFLQKTPPYFA-DPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVArSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75273615 358 VFLnFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGP 435
Cdd:cd06437 156 TGL-FFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
194-511 2.56e-41

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: 152.59  E-value: 2.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 194 DPSSFPMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIQVLDDSDDPNLQLLIKEevsvWAEKGVNIIYRHRLIRTGy 273
Cdd:COG1215  24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARE----LAAEYPRVRVIERPENGG- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 274 KAGNLKSAMTcdyVKDYEFVTIFDADFTPNPDFLKKTVPHFKgNPELGlvqarwsfvnkdenlltrlqninlcfhfeveq 353
Cdd:COG1215  99 KAAALNAGLK---AARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 354 qvngvflnffgFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHS 433
Cdd:COG1215 143 -----------ASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 434 GPMQLFRlclpsiiKSKISVWKKANLIFLFFLLRKLILPFYSFTLFCIILPLTMFI------PEAELPLWIICYVPIFIS 507
Cdd:COG1215 212 GGLQLLL-------KHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALllalllALRRRRLLLPLLHLLYGL 284

                ....
gi 75273615 508 LLNI 511
Cdd:COG1215 285 LLLL 288
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
151-441 9.48e-24

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 106.65  E-value: 9.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615  151 LSRFCTVLFLI-QSLDRLVLCLGcfwiKFKKIEPkLTEESIDL-EDPSSFPMVLIQIPMCNER-EVYEQSIGAASQLDWP 227
Cdd:PRK11498 215 VSLVCGLILLFaETYAWIVLVLG----YFQVVWP-LNRQPVPLpKDMSLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWP 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615  228 KDRILIQVLDDSDdpnlqlliKEEVSVWAEK-GVNIIYR----HRlirtgyKAGNLKSAMTcdyVKDYEFVTIFDADFTP 302
Cdd:PRK11498 290 KDKLNIWILDDGG--------REEFRQFAQEvGVKYIARptheHA------KAGNINNALK---YAKGEFVAIFDCDHVP 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615  303 NPDFLKKTVPHFKGNPELGLVQARWSFVNKD---ENL--LTRLQNINLCFHFEVeQQVNGVFLNFFgFNGTAGVWRIKAL 377
Cdd:PRK11498 353 TRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDpfeRNLgrFRKTPNEGTLFYGLV-QDGNDMWDATF-FCGSCAVIRRKPL 430
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75273615  378 EESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGPMQLFRL 441
Cdd:PRK11498 431 DEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRL 494
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
292-489 3.30e-15

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: 74.29  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   292 FVTIFDADFTPNPDFLKKTVPHFKgNPELGLVQArWSFVNKDENLLTRLQninlCFHFEVEQQVNGVFLNFFG----FNG 367
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMA-SPEVAIIQG-PILPMNVGNYLEELA----ALFFADDHGKSIPVRMALGrvlpFVG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   368 TAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWhsgpmqlFRLCLPSII 447
Cdd:pfam13632  75 SGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRW-------AYGCLLILL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 75273615   448 KSKISVWKKANLIFLFFLLRKLILPFYS---FTLFCIILPLTMFI 489
Cdd:pfam13632 148 IRLLGYLGTLLWSGLPLALLLLLLFSISslaLVLLLLALLAGLLL 192
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
199-435 3.02e-119

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: 355.08  E-value: 3.02e-119
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 199 PMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIQVLDDSDDPNLQLLIKEEVSVWAeKGVNIIYRHRLIRTGYKAGNL 278
Cdd:cd06437   1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 279 KSAMTcdyVKDYEFVTIFDADFTPNPDFLKKTVPHFKgNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQQV-NG 357
Cdd:cd06437  80 AEGMK---VAKGEYVAIFDADFVPPPDFLQKTPPYFA-DPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVArSS 155
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75273615 358 VFLnFFGFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGP 435
Cdd:cd06437 156 TGL-FFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
199-439 3.75e-54

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: 185.47  E-value: 3.75e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 199 PMVLIQIPMCNE-REVYEQSIGAASQLDWPKDRILIQVLDDSDDPNLQLLIKEEVSVWaekgvNIIYRHRLIRTGYKAGN 277
Cdd:cd06421   1 PTVDVFIPTYNEpLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEY-----GYRYLTRPDNRHAKAGN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 278 LKSAMtcDYVkDYEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQARWSFVNKDENLLT--RLQNINLCFHFEVEQQV 355
Cdd:cd06421  76 LNNAL--AHT-TGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLadGAPNEQELFYGVIQPGR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 356 NGVFLNFFGfnGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGP 435
Cdd:cd06421 153 DRWGAAFCC--GSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGM 230

                ....
gi 75273615 436 MQLF 439
Cdd:cd06421 231 LQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
194-511 2.56e-41

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: 152.59  E-value: 2.56e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 194 DPSSFPMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIQVLDDSDDPNLQLLIKEevsvWAEKGVNIIYRHRLIRTGy 273
Cdd:COG1215  24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARE----LAAEYPRVRVIERPENGG- 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 274 KAGNLKSAMTcdyVKDYEFVTIFDADFTPNPDFLKKTVPHFKgNPELGlvqarwsfvnkdenlltrlqninlcfhfeveq 353
Cdd:COG1215  99 KAAALNAGLK---AARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVG-------------------------------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 354 qvngvflnffgFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHS 433
Cdd:COG1215 143 -----------ASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWAR 211
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 434 GPMQLFRlclpsiiKSKISVWKKANLIFLFFLLRKLILPFYSFTLFCIILPLTMFI------PEAELPLWIICYVPIFIS 507
Cdd:COG1215 212 GGLQLLL-------KHRPLLRPRRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALllalllALRRRRLLLPLLHLLYGL 284

                ....
gi 75273615 508 LLNI 511
Cdd:COG1215 285 LLLL 288
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
203-440 7.44e-34

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: 129.44  E-value: 7.44e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 203 IQIPMCNER-EVYEQSIGAASQLDWPKDRILIqVLDDSDDPNLQLLIKEEVsvwAEKGVNIIYRHRLIRTGYKAGNLKSA 281
Cdd:cd06435   2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVIV-IDNNTKDEALWKPVEAHC---AQLGERFRFFHVEPLPGAKAGALNYA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 282 M--TCDyvkDYEFVTIFDADFTPNPDFLKKTVPHFKgNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQ----QV 355
Cdd:cd06435  78 LerTAP---DAEIIAVIDADYQVEPDWLKRLVPIFD-DPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMvsrnER 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 356 NGVFlnffgFNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGP 435
Cdd:cd06435 154 NAII-----QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGA 228

                ....*
gi 75273615 436 MQLFR 440
Cdd:cd06435 229 VQILK 233
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
203-391 5.70e-33

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: 125.03  E-value: 5.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 203 IQIPMCNEREVYEQSIGAASQLDWPKDRILIqVLDDSDDPNLQLLIKEevsvwAEKGVNIIYRHRLIRTGYKAGNLKSAm 282
Cdd:cd06423   1 IIVPAYNEEAVIERTIESLLALDYPKLEVIV-VDDGSTDDTLEILEEL-----AALYIRRVLVVRDKENGGKAGALNAG- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 283 tCDYVKdYEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQQVNGVFLNF 362
Cdd:cd06423  74 -LRHAK-GDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGV 151
                       170       180
                ....*....|....*....|....*....
gi 75273615 363 FGFNGTAGVWRIKALEESGGWLERTTVED 391
Cdd:cd06423 152 LVLSGAFGAFRREALREVGGWDEDTLTED 180
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
199-437 2.21e-28

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: 113.89  E-value: 2.21e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 199 PMVLIQIPMCNEREVYEQSIGAASQLDWPKDRI-LIQVLDDSDDPNLQLLIKEEVSVWAEKgvnIIYRHRLIRTGYKAgn 277
Cdd:cd06427   1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLdVKLLLEEDDEETIAAARALRLPSIFRV---VVVPPSQPRTKPKA-- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 278 lksamtCDYVKDY---EFVTIFDADFTPNPDFLKKTVPHF-KGNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEveq 353
Cdd:cd06427  76 ------CNYALAFargEYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFD--- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 354 qvngVFLNFFG-------FNGTAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTcELPESYEAYKK 426
Cdd:cd06427 147 ----YLLPGLArlglpipLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLE-EANNALGNWIR 221
                       250
                ....*....|.
gi 75273615 427 QQHRWHSGPMQ 437
Cdd:cd06427 222 QRSRWIKGYMQ 232
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
151-441 9.48e-24

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 106.65  E-value: 9.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615  151 LSRFCTVLFLI-QSLDRLVLCLGcfwiKFKKIEPkLTEESIDL-EDPSSFPMVLIQIPMCNER-EVYEQSIGAASQLDWP 227
Cdd:PRK11498 215 VSLVCGLILLFaETYAWIVLVLG----YFQVVWP-LNRQPVPLpKDMSLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWP 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615  228 KDRILIQVLDDSDdpnlqlliKEEVSVWAEK-GVNIIYR----HRlirtgyKAGNLKSAMTcdyVKDYEFVTIFDADFTP 302
Cdd:PRK11498 290 KDKLNIWILDDGG--------REEFRQFAQEvGVKYIARptheHA------KAGNINNALK---YAKGEFVAIFDCDHVP 352
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615  303 NPDFLKKTVPHFKGNPELGLVQARWSFVNKD---ENL--LTRLQNINLCFHFEVeQQVNGVFLNFFgFNGTAGVWRIKAL 377
Cdd:PRK11498 353 TRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDpfeRNLgrFRKTPNEGTLFYGLV-QDGNDMWDATF-FCGSCAVIRRKPL 430
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75273615  378 EESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWHSGPMQLFRL 441
Cdd:PRK11498 431 DEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFRL 494
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
292-489 3.30e-15

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: 74.29  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   292 FVTIFDADFTPNPDFLKKTVPHFKgNPELGLVQArWSFVNKDENLLTRLQninlCFHFEVEQQVNGVFLNFFG----FNG 367
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMA-SPEVAIIQG-PILPMNVGNYLEELA----ALFFADDHGKSIPVRMALGrvlpFVG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   368 TAGVWRIKALEESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRWhsgpmqlFRLCLPSII 447
Cdd:pfam13632  75 SGAFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRW-------AYGCLLILL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 75273615   448 KSKISVWKKANLIFLFFLLRKLILPFYS---FTLFCIILPLTMFI 489
Cdd:pfam13632 148 IRLLGYLGTLLWSGLPLALLLLLLFSISslaLVLLLLALLAGLLL 192
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
199-431 3.85e-12

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: 66.24  E-value: 3.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   199 PMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIqVLDDSDDPNLQLLIKEEVSVWAEKGVNIIYRHRLIRTGyKAGNL 278
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVV-VVNPSDAETLDVAEEIAARFPDVRLRVIRNARLLGPTG-KSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   279 KSAmtCDYVKDyEFVTIFDADFTPNPDFLKKTVPHFKGnPELGLVQARwSFVNKDENLLTRLQninlCFHFEVEQQVNGV 358
Cdd:pfam13641  80 NHG--FRAVKS-DLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTP-VFSLNRSTMLSALG----ALEFALRHLRMMS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75273615   359 FLNFFGF---NGTAGVWRIKALEESGGWLERTTV-EDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQHRW 431
Cdd:pfam13641 151 LRLALGVlplSGAGSAIRREVLKELGLFDPFFLLgDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARW 227
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
205-379 5.51e-12

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: 64.34  E-value: 5.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   205 IPMCNEREVYEQSIGAASQLDWPKDRILIqvLDDSDDPNLQLLIKEevsvWAEKGVNIIYRHRLIRTGyKAGNLKSAMtc 284
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV--VDDGSTDGTVEIAEE----YAKKDPRVRVIRLPENRG-KAGARNAGL-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   285 DYVKDyEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQARWSFvNKDENLLTRLQNINLCFHFEVEQQVNGVFLNFFG 364
Cdd:pfam00535  75 RAATG-DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI-FGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL 152
                         170
                  ....*....|....*
gi 75273615   365 FNGTAGVWRiKALEE 379
Cdd:pfam00535 153 IGGFALYRR-EALEE 166
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
191-430 9.26e-10

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: 59.52  E-value: 9.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 191 DLEDPSSFPMVLIQIPMCNEREVYEQSIGAASQLDWPKDR--ILIqVLDDSDDPNLqllikEEVSVWAEKGVNIIYRHRl 268
Cdd:cd06439  21 SLPDPAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRleIIV-VSDGSTDGTA-----EIAREYADKGVKLLRFPE- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 269 iRTGyKAGNLKSAM---TCDYVkdyefvtIF-DADFTPNPDFLKKTVPHFKgNPELGLVQARWSFVNKD-----ENLLTR 339
Cdd:cd06439  94 -RRG-KAAALNRALalaTGEIV-------VFtDANALLDPDALRLLVRHFA-DPSVGAVSGELVIVDGGgsgsgEGLYWK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 340 LQNiNLCFHfevEQQVNGVflnfFGFNGTagvwrIKAL--EESGGWLERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCEL 417
Cdd:cd06439 164 YEN-WLKRA---ESRLGST----VGANGA-----IYAIrrELFRPLPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEV 230
                       250
                ....*....|...
gi 75273615 418 PESYEAYKKQQHR 430
Cdd:cd06439 231 AEDGSEEFRRRVR 243
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
203-341 2.49e-09

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: 58.44  E-value: 2.49e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 203 IQIPMCNE--REVYE--QSIGAASQLDWPKDRILIQVLDDSDDPnlQLLIKEEvSVWAE------KGVNIIYRHRLIRTG 272
Cdd:cd04191   3 IVMPVYNEdpARVFAglRAMYESLAKTGLADHFDFFILSDTRDP--DIWLAEE-AAWLDlceelgAQGRIYYRRRRENTG 79
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 273 YKAGNLksAMTCD-YVKDYEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQARWSFVNKdENLLTRLQ 341
Cdd:cd04191  80 RKAGNI--ADFCRrWGSRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGA-ETLFARLQ 146
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
205-330 8.48e-09

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: 54.82  E-value: 8.48e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 205 IPMCNEREVYEQSIGAASQLDWPKDRILIqVLDDSDDPNLQLLIKeevsvWAEKGVNIIYRHRLIRTGyKAGNLKSAmtC 284
Cdd:cd00761   3 IPAYNEEPYLERCLESLLAQTYPNFEVIV-VDDGSTDGTLEILEE-----YAKKDPRVIRVINEENQG-LAAARNAG--L 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 75273615 285 DYVKdYEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQARWSFV 330
Cdd:cd00761  74 KAAR-GEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
272-431 9.54e-09

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: 55.37  E-value: 9.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   272 GYKAGNLKSAMtcDYVKdYEFVTIFDADFTPNPDFLKKTVPHFKGnPELGLVQArWSFVNKDENLLTRLQNINLCFHfev 351
Cdd:pfam13506  16 NPKVNNLLQGL--EAAK-YDLLVISDSDIRVPPDYLRDLLAPLAD-PKVGLVTS-PPVGSDPKGLAAALEAAFFNTL--- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615   352 eqqvNGVFLNFFGFNGTA-G---VWRIKALEESGGW--LERTTVEDMDIAVRAHLNGWKFIYLNDVEVTCELPE--SYEA 423
Cdd:pfam13506  88 ----AGVLQAALSGIGFAvGmsmAFRRADLERIGGFeaLADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRrtSFRA 163

                  ....*...
gi 75273615   424 YKKQQHRW 431
Cdd:pfam13506 164 FMARQLRW 171
MdoH COG2943
Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport ...
206-324 2.57e-07

Membrane glycosyltransferase [Cell wall/membrane/envelope biogenesis, Carbohydrate transport and metabolism];


Pssm-ID: 442186 [Multi-domain]  Cd Length: 661  Bit Score: 53.73  E-value: 2.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 206 PMCNE---------REVYEqSIGAASQLDwpkdRILIQVLDDSDDPNLQLlikEEVSVWAE------KGVNIIYRHRLIR 270
Cdd:COG2943 103 PVYNEdparvfaglRAMYE-SLAATGQLD----HFDFFILSDTTDPDIWA---AEEAAWAAlrarlgGGGRIFYRRRRRN 174
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75273615 271 TGYKAGNLKsamtcDYV----KDYEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQ 324
Cdd:COG2943 175 TGRKAGNIA-----DFCrrwgGAYDYMLVLDADSLMSGETIVRLVRRMEANPRAGLIQ 227
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
199-409 3.19e-07

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 51.63  E-value: 3.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 199 PMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIqVLDDSDDPNLQLLikEEvsvWAEKGVNIIYRHRLIRTGyKAGNL 278
Cdd:COG0463   2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV-VDDGSTDGTAEIL--RE---LAAKDPRIRVIRLERNRG-KGAAR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 279 KSAMtcDYVKdYEFVTIFDADFTPNPDFLKKTVPHFKGNPElGLVQARWsFVNKDENLLTRLQNINLCFHfeveqqvnGV 358
Cdd:COG0463  75 NAGL--AAAR-GDYIAFLDADDQLDPEKLEELVAALEEGPA-DLVYGSR-LIREGESDLRRLGSRLFNLV--------RL 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 75273615 359 FLNFFGFNGTAGVWRIKALEESGgwLERTTVEDMDIaVRAHLNGWKFIYLN 409
Cdd:COG0463 142 LTNLPDSTSGFRLFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
PRK05454 PRK05454
glucans biosynthesis glucosyltransferase MdoH;
206-324 1.46e-06

glucans biosynthesis glucosyltransferase MdoH;


Pssm-ID: 235476 [Multi-domain]  Cd Length: 605  Bit Score: 51.42  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615  206 PMCNE---------REVYEqSIGAASQLDwpkdRILIQVLDDSDDPNLQLlikEEVSVWAE------KGVNIIYRHRLIR 270
Cdd:PRK05454 131 PIYNEdparvfaglRAMYE-SLAATGHGA----HFDFFILSDTRDPDIAA---AEEAAWLElraelgGEGRIFYRRRRRN 202
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 75273615  271 TGYKAGNLKsamtcDYV----KDYEFVTIFDADFTPNPDFLKKTVPHFKGNPELGLVQ 324
Cdd:PRK05454 203 VGRKAGNIA-----DFCrrwgGAYDYMVVLDADSLMSGDTLVRLVRLMEANPRAGLIQ 255
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
205-343 2.81e-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: 48.53  E-value: 2.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 205 IPMCNEREVYEQSIGAASQLDwpkDRILIQVLDD-SDDPNLQLlikeeVSVWAEKG-VNIIYRHRL-IRTG------YKA 275
Cdd:cd06436   3 VPCLNEEAVIQRTLASLLRNK---PNFLVLVIDDaSDDDTAGI-----VRLAITDSrVHLLRRHLPnARTGkgdalnAAY 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 276 GNLKSAMTCDYVkDYE--FVTIFDADFTPNPDFLKKTVPHFkGNPELGLVQARWSFVNKDENLLTRLQNI 343
Cdd:cd06436  75 DQIRQILIEEGA-DPErvIIAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDL 142
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
199-443 3.24e-05

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 45.37  E-value: 3.24e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 199 PMVLIQIPMCNEREVYEQSIGAASQLDWPKDRILIqVLDDSDDPNLQLLIKeevsvWAEKGVNIIYRHRliRTGYKAGN- 277
Cdd:COG1216   3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIV-VDNGSTDGTAELLAA-----LAFPRVRVIRNPE--NLGFAAARn 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 278 --LKSAmtcdyvkDYEFVTIFDADFTPNPDFLKKtvphfkgnpelgLVQArwsfvnkdENLLTRLQninlcfhfeveqqv 355
Cdd:COG1216  75 lgLRAA-------GGDYLLFLDDDTVVEPDWLER------------LLAA--------ACLLIRRE-------------- 113
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 356 ngvflnffgfngtagvwrikALEESGGWLERTTV--EDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEAYKKQQH---- 429
Cdd:COG1216 114 --------------------VFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYlgrn 173
                       250
                ....*....|....*....
gi 75273615 430 -----RWHSGPMQLFRLCL 443
Cdd:COG1216 174 rllflRKHGPRPLLRLALL 192
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
203-309 1.79e-04

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 42.97  E-value: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 203 IQIPMCNEREVYEQSIGAASQLDWPKDRILIQVLDD--SDDpnlqllikeEVSVWAEKGVNIIYRHRLIRTGyKAGNLKS 280
Cdd:cd06438   1 ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADncTDD---------TAQVARAAGATVLERHDPERRG-KGYALDF 70
                        90       100       110
                ....*....|....*....|....*....|.
gi 75273615 281 AMT--CDYVKDYEFVTIFDADFTPNPDFLKK 309
Cdd:cd06438  71 GFRhlLNLADDPDAVVVFDADNLVDPNALEE 101
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
201-431 5.40e-03

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: 39.16  E-value: 5.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 201 VLIQIPMCNE-REVYEQSIGAASQLdwpKDRILIQVLDDSDDPNLQLLIKEEVSvwaeKGVNIIY-----RHRLIRTGYK 274
Cdd:cd06434   2 VTVIIPVYDEdPDVFRECLRSILRQ---KPLEIIVVTDGDDEPYLSILSQTVKY----GGIFVITvphpgKRRALAEGIR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 275 AgnlksaMTCDYvkdyefvTIF-DADFTPNPDFLKKTVPHFKgNPELGLVQARWSFVNKDENLLTRLQNINLCFHFEVEQ 353
Cdd:cd06434  75 H------VTTDI-------VVLlDSDTVWPPNALPEMLKPFE-DPKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIR 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75273615 354 QVNGVFLNFFGFNGTAGVWRIKALEE--------SGGWLERTTV--EDMDIAVRAHLNGWKFIYLNDVEVTCELPESYEA 423
Cdd:cd06434 141 AAMSYDGGVPCLSGRTAAYRTEILKDflfleeftNETFMGRRLNagDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKK 220

                ....*...
gi 75273615 424 YKKQQHRW 431
Cdd:cd06434 221 FLKQQLRW 228
 
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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