NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1063705852|ref|NP_001325222|]
View 

cellulose synthase like [Arabidopsis thaliana]

Protein Classification

cellulose synthase family protein( domain architecture ID 10157716)

cellulose synthase family protein similar to plant glucomannan 4-beta-mannosyltransferases that is involved in the synthesis of beta-1,4-mannan, the backbone for the synthesis of the storage polysaccharide galactomannan

CAZY:  GT2
EC:  2.4.1.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
47-283 1.18e-150

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: 428.65  E-value: 1.18e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKECDRWSKeGVNITFEIRDNRNGYKAGAL 126
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 127 REGMRHSyvkQCDYVAIFDADFQPDPDFLHRTvPFLIHNPKLALVQGRWEFVNAGQCMMTRLQEMSLSYHFTIEQQVGSS 206
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFLQKT-PPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705852 207 TFAFFGFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWTCGP 283
Cdd:cd06437   156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 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 ...
47-283 1.18e-150

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: 428.65  E-value: 1.18e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKECDRWSKeGVNITFEIRDNRNGYKAGAL 126
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 127 REGMRHSyvkQCDYVAIFDADFQPDPDFLHRTvPFLIHNPKLALVQGRWEFVNAGQCMMTRLQEMSLSYHFTIEQQVGSS 206
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFLQKT-PPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705852 207 TFAFFGFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWTCGP 283
Cdd:cd06437   156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-406 1.03e-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: 150.66  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852   4 MFFVEVMYMGIVVLYVKLFKRKPEkfykweameddvecgSASYPMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQV 83
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRRA---------------PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  84 LDDSTDPASKELVKKECDRWSkegvNITFEIRDNRNGyKAGALREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLi 163
Cdd:COG1215    66 VDDGSTDETAEIARELAAEYP----RVRVIERPENGG-KAAALNAGLKAA---RGDIVVFLDADTVLDPDWLRRLVAAF- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 164 HNPKLalvqgrwefvnagqcmmtrlqemslsyhftieqqvgsstfaffGFNGTAGVWRISALNESGGWNDQTTVEDMDLA 243
Cdd:COG1215   137 ADPGV-------------------------------------------GASGANLAFRREALEEVGGFDEDTLGEDLDLS 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 244 VRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWTCGpanllrkmAGQIIRSENVSLWKKWYMLYSFFFmrkivahIL 323
Cdd:COG1215   174 LRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARG--------GLQLLLKHRPLLRPRRLLLFLLLL-------LL 238
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 324 TFCFYCVILPATVLfpevtvpkwAAFYLPSLITLLIAIGRLRSIHLLAFWVLFENAMSLLRAKalvmglfetGRVQEWVV 403
Cdd:COG1215   239 PLLLLLLLLALLAL---------LLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALR---------GKKVVWKK 300

                  ...
gi 1063705852 404 TEK 406
Cdd:COG1215   301 TPR 303
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
53-214 7.89e-19

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: 83.60  E-value: 7.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKEVCEQSIAAACKISWPSNRIIIqVLDDSTDpASKELVKKecdrWSKEGVNITFEIRDNRNGyKAGALREGMRH 132
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTD-GTVEIAEE----YAKKDPRVRVIRLPENRG-KAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 133 SyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWE-FVNAGQCMMTRLQEMSLSYHFTIEQQVGSSTFAFF 211
Cdd:pfam00535  77 A---TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYViFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153

                  ...
gi 1063705852 212 GFN 214
Cdd:pfam00535 154 GGF 156
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
43-299 1.82e-13

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 72.75  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  43 SASYPMVLVQIPMYNEK-EVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKecdrwskegVNITFEIRDNRNGY 121
Cdd:PRK11498  256 MSLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQE---------VGVKYIARPTHEHA 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 122 KAGALREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWEFV-------NAGQCMMTRlQEMSLS 194
Cdd:PRK11498  327 KAGNINNALKYA---KGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFspdpferNLGRFRKTP-NEGTLF 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 195 YHFTieqQVGS----STFaffgFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFK 270
Cdd:PRK11498  403 YGLV---QDGNdmwdATF----FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLS 475
                         250       260
                  ....*....|....*....|....*....
gi 1063705852 271 ALRSQQHRWTcgpanllRKMAgQIIRSEN 299
Cdd:PRK11498  476 AHIGQRIRWA-------RGMV-QIFRLDN 496
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
47-283 1.18e-150

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: 428.65  E-value: 1.18e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKECDRWSKeGVNITFEIRDNRNGYKAGAL 126
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQ-GVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 127 REGMRHSyvkQCDYVAIFDADFQPDPDFLHRTvPFLIHNPKLALVQGRWEFVNAGQCMMTRLQEMSLSYHFTIEQQVGSS 206
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFLQKT-PPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063705852 207 TFAFFGFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWTCGP 283
Cdd:cd06437   156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
47-287 3.75e-43

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: 152.34  E-value: 3.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEK-EVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKECDRWSKEGVnitfeIRDNRNGYKAGA 125
Cdd:cd06421     1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGYRYL-----TRPDNRHAKAGN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 126 LREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWEFVN-----AGQCMMTRLQEMslsYHFTIE 200
Cdd:cd06421    76 LNNALAHT---TGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNpdpfdWLADGAPNEQEL---FYGVIQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 201 QQVGSSTFAFFGfnGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWT 280
Cdd:cd06421   150 PGRDRWGAAFCC--GSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWA 227

                  ....*..
gi 1063705852 281 CGPANLL 287
Cdd:cd06421   228 RGMLQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-406 1.03e-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: 150.66  E-value: 1.03e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852   4 MFFVEVMYMGIVVLYVKLFKRKPEkfykweameddvecgSASYPMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQV 83
Cdd:COG1215     1 LLLLLALLALLYLLLLALARRRRA---------------PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIV 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  84 LDDSTDPASKELVKKECDRWSkegvNITFEIRDNRNGyKAGALREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLi 163
Cdd:COG1215    66 VDDGSTDETAEIARELAAEYP----RVRVIERPENGG-KAAALNAGLKAA---RGDIVVFLDADTVLDPDWLRRLVAAF- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 164 HNPKLalvqgrwefvnagqcmmtrlqemslsyhftieqqvgsstfaffGFNGTAGVWRISALNESGGWNDQTTVEDMDLA 243
Cdd:COG1215   137 ADPGV-------------------------------------------GASGANLAFRREALEEVGGFDEDTLGEDLDLS 173
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 244 VRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWTCGpanllrkmAGQIIRSENVSLWKKWYMLYSFFFmrkivahIL 323
Cdd:COG1215   174 LRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARG--------GLQLLLKHRPLLRPRRLLLFLLLL-------LL 238
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 324 TFCFYCVILPATVLfpevtvpkwAAFYLPSLITLLIAIGRLRSIHLLAFWVLFENAMSLLRAKalvmglfetGRVQEWVV 403
Cdd:COG1215   239 PLLLLLLLLALLAL---------LLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALR---------GKKVVWKK 300

                  ...
gi 1063705852 404 TEK 406
Cdd:COG1215   301 TPR 303
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
51-239 2.08e-36

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: 132.74  E-value: 2.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  51 VQIPMYNEKEVCEQSIAAACKISWPSNRIIiqVLDDSTDPASKELVKKEcdrWSKEGVNITFeIRDNRNGYKAGALREGM 130
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVI--VVDDGSTDDTLEILEEL---AALYIRRVLV-VRDKENGGKAGALNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 131 RHSYVkqcDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWEFVNAGQCMMTRLQEMSLSYHFTIEQQVGSSTFAF 210
Cdd:cd06423    75 RHAKG---DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGV 151
                         170       180
                  ....*....|....*....|....*....
gi 1063705852 211 FGFNGTAGVWRISALNESGGWNDQTTVED 239
Cdd:cd06423   152 LVLSGAFGAFRREALREVGGWDEDTLTED 180
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
51-289 6.95e-31

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: 119.43  E-value: 6.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  51 VQIPMYNEK-EVCEQSIAAACKISWPSNRIIiqVLDDST-DPASKELVKKECdrwSKEGVNITFEIRDNRNGYKAGALRE 128
Cdd:cd06435     2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVI--VIDNNTkDEALWKPVEAHC---AQLGERFRFFHVEPLPGAKAGALNY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 129 GMRHSYVkQCDYVAIFDADFQPDPDFLHRTVPfLIHNPKLALVQGRWEFVNAGQCMMTRLQEMSLSYHFTIEQQVGSSTF 208
Cdd:cd06435    77 ALERTAP-DAEIIAVIDADYQVEPDWLKRLVP-IFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 209 AFFgFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWTCGPANLLR 288
Cdd:cd06435   155 AII-QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILK 233

                  .
gi 1063705852 289 K 289
Cdd:cd06435   234 K 234
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
47-279 4.68e-19

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: 86.15  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKECDRWSKEGVNI-TFEIRDnrngyKAGA 125
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVpPSQPRT-----KPKA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 126 LREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTV-PFLIHNPKLALVQGRWEFVNAGQCMMTRLQEMSLSYHFTIEQQVG 204
Cdd:cd06427    76 CNYALAFA---RGEYVVIYDAEDAPDPDQLKKAVaAFARLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063705852 205 SSTFAFFGFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKsELPCSFKALRSQQHRW 279
Cdd:cd06427   153 ARLGLPIPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLE-EANNALGNWIRQRSRW 226
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
53-214 7.89e-19

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: 83.60  E-value: 7.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKEVCEQSIAAACKISWPSNRIIIqVLDDSTDpASKELVKKecdrWSKEGVNITFEIRDNRNGyKAGALREGMRH 132
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTD-GTVEIAEE----YAKKDPRVRVIRLPENRG-KAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 133 SyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWE-FVNAGQCMMTRLQEMSLSYHFTIEQQVGSSTFAFF 211
Cdd:pfam00535  77 A---TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYViFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153

                  ...
gi 1063705852 212 GFN 214
Cdd:pfam00535 154 GGF 156
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
47-282 3.47e-18

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: 83.57  E-value: 3.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQVL--DDSTDPASKELVkkecDRWSKEGVNITFEIRDNRNGYKAG 124
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNpsDAETLDVAEEIA----ARFPDVRLRVIRNARLLGPTGKSR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 125 ALREGMRHsyVKQcDYVAIFDADFQPDPDFLHRTVPFLIHnPKLALVQGRwEFVNAGQCMMTRLQEMSLSYHFTIE---Q 201
Cdd:pfam13641  78 GLNHGFRA--VKS-DLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTP-VFSLNRSTMLSALGALEFALRHLRMmslR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 202 QVGSSTFaffgFNGTAGVWRISALNESGGWNDQTTV-EDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWT 280
Cdd:pfam13641 153 LALGVLP----LSGAGSAIRREVLKELGLFDPFFLLgDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWV 228

                  ..
gi 1063705852 281 CG 282
Cdd:pfam13641 229 YG 230
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
140-338 5.51e-18

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: 82.00  E-value: 5.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 140 YVAIFDADFQPDPDFLHRTVPFLiHNPKLALVQGrWEFVNAGQCMMTRLQ--EMSLSYHFTIEQQVGSSTFAFFgfNGTA 217
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEM-ASPEVAIIQG-PILPMNVGNYLEELAalFFADDHGKSIPVRMALGRVLPF--VGSG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 218 GVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRWTCGPAN----LLRKMAGQ 293
Cdd:pfam13632  77 AFLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLilliRLLGYLGT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1063705852 294 IIRSeNVSLWKKWYMLYSFFfmrkivahILTFCFYCVILPATVLF 338
Cdd:pfam13632 157 LLWS-GLPLALLLLLLFSIS--------SLALVLLLLALLAGLLL 192
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
47-257 4.91e-17

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 79.75  E-value: 4.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIqVLDDSTDpASKELVKkecdRWSKEGVNITFeIRDNRNGYKAGAL 126
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV-VDDGSTD-GTAEILR----ELAAKDPRIRV-IRLERNRGKGAAR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 127 REGMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPkLALVQGrWEFVNAGQCMMTRLqemsLSYHFTIEQQVGSS 206
Cdd:COG0463    75 NAGLAAA---RGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYG-SRLIREGESDLRRL----GSRLFNLVRLLTNL 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063705852 207 TFAFFGFNgtagVWRISALNESGgwNDQTTVEDMDLaVRATLRGWKFLYID 257
Cdd:COG0463   146 PDSTSGFR----LFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
53-178 3.22e-15

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: 72.92  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKEVCEQSIAAACKISWPSNRIIIqVLDDSTDpASKELVKkecdRWSKEGVNITFeIRDNRNGYKAGALREGMRH 132
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQTYPNFEVIV-VDDGSTD-GTLEILE----EYAKKDPRVIR-VINEENQGLAAARNAGLKA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1063705852 133 SyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWEFV 178
Cdd:cd00761    76 A---RGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
43-299 1.82e-13

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 72.75  E-value: 1.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  43 SASYPMVLVQIPMYNEK-EVCEQSIAAACKISWPSNRIIIQVLDDSTDPASKELVKKecdrwskegVNITFEIRDNRNGY 121
Cdd:PRK11498  256 MSLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQE---------VGVKYIARPTHEHA 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 122 KAGALREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRWEFV-------NAGQCMMTRlQEMSLS 194
Cdd:PRK11498  327 KAGNINNALKYA---KGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFspdpferNLGRFRKTP-NEGTLF 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 195 YHFTieqQVGS----STFaffgFNGTAGVWRISALNESGGWNDQTTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFK 270
Cdd:PRK11498  403 YGLV---QDGNdmwdATF----FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLS 475
                         250       260
                  ....*....|....*....|....*....
gi 1063705852 271 ALRSQQHRWTcgpanllRKMAgQIIRSEN 299
Cdd:PRK11498  476 AHIGQRIRWA-------RGMV-QIFRLDN 496
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
47-261 1.15e-11

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 63.86  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  47 PMVLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIqVLDDSTDPaSKELVKkecdRWSKEGVNItfeIRDNRN-GYkAGA 125
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIV-VDNGSTDG-TAELLA----ALAFPRVRV---IRNPENlGF-AAA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 126 LREGMRHSyvkQCDYVAIFDADFQPDPDFLHRtvpflihnpklalvqgrweFVNAGqCMMTRLqemslsyhftieqqvgs 205
Cdd:COG1216    73 RNLGLRAA---GGDYLLFLDDDTVVEPDWLER-------------------LLAAA-CLLIRR----------------- 112
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063705852 206 stfaffgfngtagvwriSALNESGGWNDQTTV--EDMDLAVRATLRGWKFLYIDDLKV 261
Cdd:COG1216   113 -----------------EVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVV 153
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
51-155 2.01e-09

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: 56.81  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  51 VQIPMYNEKEVCEQSIAAACKI--SWPSNRIIIqVLDDSTDpASKELVKKECDRWSKEGVnitfeIRDNRNGYKAGALRE 128
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVleEGYDYEIIV-VDDGSTD-GTAEIARELAARVPRVRV-----IRLSRNFGKGAAVRA 73
                          90       100
                  ....*....|....*....|....*..
gi 1063705852 129 GMRHSyvkQCDYVAIFDADFQPDPDFL 155
Cdd:cd04179    74 GFKAA---RGDIVVTMDADLQHPPEDI 97
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
49-289 3.06e-09

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: 57.63  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  49 VLVQIPMYNEKEVCEQSIAAACKISWPSNRIIIQVLDD-STDpASKELVKKECDRwskegvNITFEIRDNRNGYKAGALR 127
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGgSTD-GTREIVQEYAAK------DPRIRLIDNPKRIQSAGLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 128 EGMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLIhNPKLALVQGRWEFV--NAGQCMMTRLQEMSLS-----YHFTIE 200
Cdd:cd02525    75 IGIRNS---RGDIIIRVDAHAVYPKDYILELVEALK-RTGADNVGGPMETIgeSKFQKAIAVAQSSPLGsggsaYRGGAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 201 QQVGSSTFAFfgfngtaGVWRISALNESGGWNDQ-TTVEDMDLAVRATLRGWKFLYIDDLKVKSELPCSFKALRSQQHRW 279
Cdd:cd02525   151 KIGYVDTVHH-------GAYRREVFEKVGGFDESlVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRY 223
                         250
                  ....*....|
gi 1063705852 280 TCGPANLLRK 289
Cdd:cd02525   224 GKWRARTLRK 233
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
51-239 4.39e-07

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: 50.07  E-value: 4.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  51 VQIPMYNEKEVCEQSIAAACKISwPSNRIIiqVLDDSTDPASKELVKKECdrwSKEGVNITFEIRDN-RNG------YKA 123
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNK-PNFLVL--VIDDASDDDTAGIVRLAI---TDSRVHLLRRHLPNaRTGkgdalnAAY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 124 GALREGMRHSYVKQCD-YVAIFDADFQPDPDFLHRTVPFLiHNPKLALVQGRWEFVNAGQCMMTRLQEM---SLSYHFti 199
Cdd:cd06436    75 DQIRQILIEEGADPERvIIAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDLeffIIIAAT-- 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1063705852 200 eqQVGSSTFAFFGFNGTAGVWRISALNESGG---WNDQTTvED 239
Cdd:cd06436   152 --QSLRALTGTVGLGGNGQFMRLSALDGLIGeepWSDSLL-ED 191
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
11-181 4.84e-07

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: 51.04  E-value: 4.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  11 YMGIVVLyVKLFKRKPEKFykwEAMEDDvecgsASYPMVLVQIPMYNEKEVCE---QSIAAackISWPSNRI-IIQVLDD 86
Cdd:cd06439     2 YFGYPLL-LKLLARLRPKP---PSLPDP-----AYLPTVTIIIPAYNEEAVIEaklENLLA---LDYPRDRLeIIVVSDG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  87 STDpASKELVKkecdRWSKEGVNITFEirDNRNGyKAGALREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTV-PFLihN 165
Cdd:cd06439    70 STD-GTAEIAR----EYADKGVKLLRF--PERRG-KAAALNRALALA---TGEIVVFTDANALLDPDALRLLVrHFA--D 136
                         170
                  ....*....|....*.
gi 1063705852 166 PKLALVQGRWEFVNAG 181
Cdd:cd06439   137 PSVGAVSGELVIVDGG 152
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-255 9.04e-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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 48.71  E-value: 9.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKEV---CEQSIAAACKISWpsnRIIIqVLDDSTDPaSKELVKKECDRwskegVNItfeIRDNRN-GYkAGALRE 128
Cdd:cd04186     3 IVNYNSLEYlkaCLDSLLAQTYPDF---EVIV-VDNASTDG-SVELLRELFPE-----VRL---IRNGENlGF-GAGNNQ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 129 GMRHSyvkQCDYVAIFDADFQPDPDFLHRTVPFLIHNPKLALVQGRwefVNAGqCMMTRlqemslsyhFTIEQQVG---S 205
Cdd:cd04186    69 GIREA---KGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPK---VSGA-FLLVR---------REVFEEVGgfdE 132
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063705852 206 STFAFFgfngtagvwrisalnesggwndqttvEDMDLAVRATLRGWKFLY 255
Cdd:cd04186   133 DFFLYY--------------------------EDVDLCLRARLAGYRVLY 156
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
53-197 2.57e-06

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: 48.33  E-value: 2.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKEVCEQSIAAAC----KISWPSNRIIIqVLDDSTDpASKELVKKECDRWSKEGVNITFEirdnRNGYKAGALRE 128
Cdd:cd04188     3 IPAYNEEKRLPPTLEEAVeyleERPSFSYEIIV-VDDGSKD-GTAEVARKLARKNPALIRVLTLP----KNRGKGGAVRA 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063705852 129 GMRHSYvkqCDYVAIFDADFQPDPDFLHRTVPfLIHNPKLALVQG-RWefVNAGQCMMTR--LQE-MSLSYHF 197
Cdd:cd04188    77 GMLAAR---GDYILFADADLATPFEELEKLEE-ALKTSGYDIAIGsRA--HLASAAVVKRswLRNlLGRGFNF 143
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
53-155 3.31e-05

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: 45.22  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKE----VCEQSIAAACKISWpsnRIIIqVLDDSTDpASKELVKKecdrWSKEGVNITFEIRDNRNGYkAGALRE 128
Cdd:cd06442     3 IPTYNEREnipeLIERLDAALKGIDY---EIIV-VDDNSPD-GTAEIVRE----LAKEYPRVRLIVRPGKRGL-GSAYIE 72
                          90       100
                  ....*....|....*....|....*..
gi 1063705852 129 GMRHSYvkqCDYVAIFDADFQPDPDFL 155
Cdd:cd06442    73 GFKAAR---GDVIVVMDADLSHPPEYI 96
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
51-282 5.89e-05

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: 44.20  E-value: 5.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  51 VQIPMYNEKE---VCEQSIAaacKISWPSNRI-IIQVLDDSTDpASKELVKKECDrwsKEGVNItFEIRDNR--NGYKAG 124
Cdd:cd04192     1 VVIAARNEAEnlpRLLQSLS---ALDYPKEKFeVILVDDHSTD-GTVQILEFAAA---KPNFQL-KILNNSRvsISGKKN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 125 ALREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTV-PFLIHNPKLAL----VQGRWEFVNAGQcmmtRLQEMSLS--YHF 197
Cdd:cd04192    73 ALTTAIKAA---KGDWIVTTDADCVVPSNWLLTFVaFIQKEQIGLVAgpviYFKGKSLLAKFQ----RLDWLSLLglIAG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 198 TIEQQVGsstfafFGFNGTAGVWRISALNESGGW--NDQTTVEDMDLAVRATLRGW---KFLYIDDLKVKSELPCSFKAL 272
Cdd:cd04192   146 SFGLGKP------FMCNGANMAYRKEAFFEVGGFegNDHIASGDDELLLAKVASKYpkvAYLKNPEALVTTQPVTSWKEL 219
                         250
                  ....*....|
gi 1063705852 273 RSQQHRWTCG 282
Cdd:cd04192   220 LNQRKRWASK 229
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
53-157 7.25e-05

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: 43.62  E-value: 7.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKEVCE---QSIAAACKISWPSNRIIIqVLDDSTDpASKELVKKECDRWSkegvNITFeIRDNRNGYKAGALREG 129
Cdd:cd04187     3 VPVYNEEENLPelyERLKAVLESLGYDYEIIF-VDDGSTD-RTLEILRELAARDP----RVKV-IRLSRNFGQQAALLAG 75
                          90       100
                  ....*....|....*....|....*...
gi 1063705852 130 MRHSyvkQCDYVAIFDADFQPDPDFLHR 157
Cdd:cd04187    76 LDHA---RGDAVITMDADLQDPPELIPE 100
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
107-279 3.72e-04

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: 41.11  E-value: 3.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 107 GVNITFEIRDNRN-GYKAGALREGMRHSyvkQCDYVAIFDADFQPDPDFLHRTV-PFLihNPKLALVQGrWEFVNAGQCM 184
Cdd:pfam13506   2 SVRALVVGGPPVGvNPKVNNLLQGLEAA---KYDLLVISDSDIRVPPDYLRDLLaPLA--DPKVGLVTS-PPVGSDPKGL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852 185 MTRLqEMSLsyhFTIEQQVGSSTFAFFGF-NGTAGVWRISALNESGGWN--DQTTVEDMDLAVRATLRGWKFLYIDDLKV 261
Cdd:pfam13506  76 AAAL-EAAF---FNTLAGVLQAALSGIGFaVGMSMAFRRADLERIGGFEalADYLAEDYALGKLLRAAGLKVVLSPRPIL 151
                         170       180
                  ....*....|....*....|
gi 1063705852 262 KSELP--CSFKALRSQQHRW 279
Cdd:pfam13506 152 QTSGPrrTSFRAFMARQLRW 171
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
56-155 2.23e-03

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: 39.16  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  56 YNEKEVCEQSIAAACKISWPSNRIIIqVLDDSTDpASKELVKKECDRWSKEGVNITfeirdnRNGYKAGALREGMRHSYV 135
Cdd:cd04185     6 YNRLDLLKECLDALLAQTRPPDHIIV-IDNASTD-GTAEWLTSLGDLDNIVYLRLP------ENLGGAGGFYEGVRRAYE 77
                          90       100
                  ....*....|....*....|
gi 1063705852 136 KQCDYVAIFDADFQPDPDFL 155
Cdd:cd04185    78 LGYDWIWLMDDDAIPDPDAL 97
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
53-157 2.77e-03

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 38.74  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063705852  53 IPMYNEKEVCEQSIAAACKISWPSNRI-IIQVLDDSTDpASKELVKKEcdrwskeGVNItFEIRDNRNGYKAGALREGMR 131
Cdd:cd06438     3 IPAHNEEAVIGNTVRSLKAQDYPRELYrIFVVADNCTD-DTAQVARAA-------GATV-LERHDPERRGKGYALDFGFR 73
                          90       100
                  ....*....|....*....|....*...
gi 1063705852 132 HSYVKQCDY--VAIFDADFQPDPDFLHR 157
Cdd:cd06438    74 HLLNLADDPdaVVVFDADNLVDPNALEE 101
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH