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Conserved domains on  [gi|1149725268|ref|XP_020188534|]
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probable glucomannan 4-beta-mannosyltransferase 9 isoform X2 [Aegilops tauschii subsp. strangulata]

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

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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 ...
80-316 2.50e-145

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: 416.33  E-value: 2.50e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVQVECQRWAnKGVNIKYEIRDNRRGYKAGAL 159
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 160 KEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAmPFLIHNPEIALIQARWVFVNANECLMTRMQEMSLDYHFKVEQEVGSS 239
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFLQKT-PPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149725268 240 AYAFFGFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCGP 316
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 ...
80-316 2.50e-145

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: 416.33  E-value: 2.50e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVQVECQRWAnKGVNIKYEIRDNRRGYKAGAL 159
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 160 KEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAmPFLIHNPEIALIQARWVFVNANECLMTRMQEMSLDYHFKVEQEVGSS 239
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFLQKT-PPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149725268 240 AYAFFGFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCGP 316
Cdd:cd06437   156 TGLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
77-393 8.73e-38

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: 140.65  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  77 AAYPMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVqvecQRWANKGVNIKYEIRDNRRGyKA 156
Cdd:COG1215    26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIA----RELAAEYPRVRVIERPENGG-KA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 157 GALKEGMKHgyvKDCDFVVIFDADFQPEPDYLSRAMPFLiHNPEIaliqarwvfvnaneclmtrmqemsldyhfkveqev 236
Cdd:COG1215   101 AALNAGLKA---ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGV----------------------------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 237 gssayaffGFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCGP 316
Cdd:COG1215   142 --------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149725268 317 ANLFRKMLMEIVKNQKVTLWkkIYVIYNFFFVRKIIGHILTSVFYCLVIPATVFVPEIEIPRWGYFYIPTIITLLNA 393
Cdd:COG1215   214 LQLLLKHRPLLRPRRLLLFL--LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLL 288
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
173-315 1.52e-16

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: 77.76  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 173 FVVIFDADFQPEPDYLSRAMPFLiHNPEIALIQArWVFVNANECLMTRMQEMSLDYHFKVEQEVGSSAYAFFGFNGTAGV 252
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEM-ASPEVAIIQG-PILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149725268 253 WRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCG 315
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYG 141
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
77-321 1.76e-14

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 76.22  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  77 AAYPMVLVQIPMYNER-EVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVQvecqrwankGVNIKYEIRDNRRGYK 155
Cdd:PRK11498  257 SLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQ---------EVGVKYIARPTHEHAK 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 156 AGALKEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWVFVNANEClmtrmqEMSLDYHFKVEQE 235
Cdd:PRK11498  328 AGNINNALKYA---KGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPF------ERNLGRFRKTPNE 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 236 vGSSAY-----------AFFgFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKA 304
Cdd:PRK11498  399 -GTLFYglvqdgndmwdATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSA 476
                         250
                  ....*....|....*..
gi 1149725268 305 FRYQQHRWSCGPANLFR 321
Cdd:PRK11498  477 HIGQRIRWARGMVQIFR 493
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
80-316 2.50e-145

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: 416.33  E-value: 2.50e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVQVECQRWAnKGVNIKYEIRDNRRGYKAGAL 159
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAA-QGVNIKHVRRADRTGYKAGAL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 160 KEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAmPFLIHNPEIALIQARWVFVNANECLMTRMQEMSLDYHFKVEQEVGSS 239
Cdd:cd06437    80 AEGMKVA---KGEYVAIFDADFVPPPDFLQKT-PPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSS 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149725268 240 AYAFFGFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCGP 316
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 ...
80-320 7.95e-41

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: 146.95  E-value: 7.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNE-REVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVQVECQRWankgvNIKYEIRDNRRGYKAGA 158
Cdd:cd06421     1 PTVDVFIPTYNEpLEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEY-----GYRYLTRPDNRHAKAGN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 159 LKEGMKHgyvKDCDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWVFVNANEC-LMTRMQEMSLDYHFKVEQEVG 237
Cdd:cd06421    76 LNNALAH---TTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFdWLADGAPNEQELFYGVIQPGR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 238 SSAYAFFgFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCGPA 317
Cdd:cd06421   153 DRWGAAF-CCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGML 231

                  ...
gi 1149725268 318 NLF 320
Cdd:cd06421   232 QIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
77-393 8.73e-38

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: 140.65  E-value: 8.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  77 AAYPMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVqvecQRWANKGVNIKYEIRDNRRGyKA 156
Cdd:COG1215    26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIA----RELAAEYPRVRVIERPENGG-KA 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 157 GALKEGMKHgyvKDCDFVVIFDADFQPEPDYLSRAMPFLiHNPEIaliqarwvfvnaneclmtrmqemsldyhfkveqev 236
Cdd:COG1215   101 AALNAGLKA---ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGV----------------------------------- 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 237 gssayaffGFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCGP 316
Cdd:COG1215   142 --------GASGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGG 213
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149725268 317 ANLFRKMLMEIVKNQKVTLWkkIYVIYNFFFVRKIIGHILTSVFYCLVIPATVFVPEIEIPRWGYFYIPTIITLLNA 393
Cdd:COG1215   214 LQLLLKHRPLLRPRRLLLFL--LLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLL 288
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
84-322 2.22e-33

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: 126.75  E-value: 2.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  84 VQIPMYNER-EVYKKSIGAACGLSWPSDRIViqVLDDST-DPAIKELVQVECQRWankGVNIKYEIRDNRRGYKAGALKE 161
Cdd:cd06435     2 IHVPCYEEPpEMVKETLDSLAALDYPNFEVI--VIDNNTkDEALWKPVEAHCAQL---GERFRFFHVEPLPGAKAGALNY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 162 GMKHGYVkDCDFVVIFDADFQPEPDYLSRAMPfLIHNPEIALIQARWVFVNANECLMTRMQEMSLDYHFKVEQEVGSSAY 241
Cdd:cd06435    77 ALERTAP-DAEIIAVIDADYQVEPDWLKRLVP-IFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 242 AFFgFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCGPANLFR 321
Cdd:cd06435   155 AII-QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILK 233

                  .
gi 1149725268 322 K 322
Cdd:cd06435   234 K 234
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
84-272 2.54e-32

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: 121.95  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  84 VQIPMYNEREVYKKSIGAACGLSWPSDRIVIqVLDDSTDPAIKELvqvecQRWANKGVNIKYEIRDNRRGYKAGALKEGM 163
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIV-VDDGSTDDTLEIL-----EELAALYIRRVLVVRDKENGGKAGALNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 164 KH--GyvkdcDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWVFVNANECLMTRMQEMSLDYHFKVEQEVGSSAY 241
Cdd:cd06423    75 RHakG-----DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALG 149
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1149725268 242 AFFGFNGTAGVWRISALNEAGGWKDRTTVED 272
Cdd:cd06423   150 GVLVLSGAFGAFRREALREVGGWDEDTLTED 180
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
173-315 1.52e-16

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: 77.76  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 173 FVVIFDADFQPEPDYLSRAMPFLiHNPEIALIQArWVFVNANECLMTRMQEMSLDYHFKVEQEVGSSAYAFFGFNGTAGV 252
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEM-ASPEVAIIQG-PILPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149725268 253 WRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSCG 315
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYG 141
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
86-247 7.85e-15

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: 72.43  E-value: 7.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  86 IPMYNEREVYKKSIGAACGLSWPSDRIVIqVLDDSTDpaikELVQVeCQRWANKGVNIKYEIRDNRRGyKAGALKEGMKH 165
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPNFEIIV-VDDGSTD----GTVEI-AEEYAKKDPRVRVIRLPENRG-KAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 166 GyvkDCDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWV-FVNANECLMTRMQEMSLDYHFKVEQEVGSSAYAFF 244
Cdd:pfam00535  77 A---TGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYViFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLI 153

                  ...
gi 1149725268 245 GFN 247
Cdd:pfam00535 154 GGF 156
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
80-312 1.55e-14

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: 73.06  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVQVECQRWANKGVNIKY-EIRDnrrgyKAGA 158
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVPPsQPRT-----KPKA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 159 LKEGMK--HGyvkdcDFVVIFDADFQPEPDYLSRAM-PFLIHNPEIALIQARWVFVNANECLMTRMQEMSLDYHFKVEQE 235
Cdd:cd06427    76 CNYALAfaRG-----EYVVIYDAEDAPDPDQLKKAVaAFARLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLP 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 236 VGSSAYAFFGFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKfvylgdLRVKS-----ELPSTFKAFRYQQH 310
Cdd:cd06427   151 GLARLGLPIPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYR------TGVLNsttleEANNALGNWIRQRS 224

                  ..
gi 1149725268 311 RW 312
Cdd:cd06427   225 RW 226
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
77-321 1.76e-14

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 76.22  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  77 AAYPMVLVQIPMYNER-EVYKKSIGAACGLSWPSDRIVIQVLDDSTDPAIKELVQvecqrwankGVNIKYEIRDNRRGYK 155
Cdd:PRK11498  257 SLWPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQ---------EVGVKYIARPTHEHAK 327
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 156 AGALKEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWVFVNANEClmtrmqEMSLDYHFKVEQE 235
Cdd:PRK11498  328 AGNINNALKYA---KGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQTPHHFFSPDPF------ERNLGRFRKTPNE 398
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 236 vGSSAY-----------AFFgFNGTAGVWRISALNEAGGWKDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKA 304
Cdd:PRK11498  399 -GTLFYglvqdgndmwdATF-FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATESLSA 476
                         250
                  ....*....|....*..
gi 1149725268 305 FRYQQHRWSCGPANLFR 321
Cdd:PRK11498  477 HIGQRIRWARGMVQIFR 493
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
80-315 4.66e-14

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: 71.63  E-value: 4.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVL--DDSTDPAIKELVQVEcqrwanKGVNIKYEIRDNRRGY--K 155
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNpsDAETLDVAEEIAARF------PDVRLRVIRNARLLGPtgK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 156 AGALKEGMKHgyVKDcDFVVIFDADFQPEPDYLSRAMPFLIHnPEIALIQARwVFVNANECLMTRMQEMSLDYHFK---V 232
Cdd:pfam13641  76 SRGLNHGFRA--VKS-DLVVLHDDDSVLHPGTLKKYVQYFDS-PKVGAVGTP-VFSLNRSTMLSALGALEFALRHLrmmS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 233 EQEVGSSAYaffgFNGTAGVWRISALNEAGGW-KDRTTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHR 311
Cdd:pfam13641 151 LRLALGVLP----LSGAGSAIRREVLKELGLFdPFFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRAR 226

                  ....
gi 1149725268 312 WSCG 315
Cdd:pfam13641 227 WVYG 230
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
80-289 5.76e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 65.11  E-value: 5.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIqVLDDSTD--PAIkelvqveCQRWANKGVNIKYeIRDNRRGYKAG 157
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIV-VDDGSTDgtAEI-------LRELAAKDPRIRV-IRLERNRGKGA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 158 ALKEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWVfvnANECLMTRMQEMSLDYHFKVEQEVG 237
Cdd:COG0463    73 ARNAGLAAA---RGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI---REGESDLRRLGSRLFNLVRLLTNLP 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1149725268 238 SSAYAFFGFngtagvwRISALNEAGgwKDRTTVEDMDLaVRASLKGWKFVYL 289
Cdd:COG0463   147 DSTSGFRLF-------RREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEV 188
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
86-211 2.08e-11

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: 62.14  E-value: 2.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  86 IPMYNEREVYKKSIGAACGLSWPSDRIVIqVLDDSTDPAIKELvqvecQRWANKGVNIKYEIRDNRRGyKAGALKEGMKH 165
Cdd:cd00761     3 IPAYNEEPYLERCLESLLAQTYPNFEVIV-VDDGSTDGTLEIL-----EEYAKKDPRVIRVINEENQG-LAAARNAGLKA 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1149725268 166 GyvkDCDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWVFV 211
Cdd:cd00761    76 A---RGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
80-294 2.48e-10

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 60.01  E-value: 2.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  80 PMVLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIqVLDDSTDPAIKELVQVECQRwankgvnIKYEIRDNRRGYkAGAL 159
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIV-VDNGSTDGTAELLAALAFPR-------VRVIRNPENLGF-AAAR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 160 KEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAMpflihnpeialiqarwvfvnaneclmtrmqemsldyhfkveqevgss 239
Cdd:COG1216    74 NLGLRAA---GGDYLLFLDDDTVVEPDWLERLL----------------------------------------------- 103
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149725268 240 AYAFFGFngtagvwRISALNEAGGWKDRTTV--EDMDLAVRASLKGWKFVYLGDLRV 294
Cdd:COG1216   104 AAACLLI-------RREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVV 153
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
49-303 2.33e-09

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: 57.98  E-value: 2.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  49 VAMRLIGRrperqWRWEPLRDDDPelgnAAYPMVLVQIPMYNEREVYKKSIGAACGLSWPSDRI-VIQVLDDSTDpAIKE 127
Cdd:cd06439     7 LLLKLLAR-----LRPKPPSLPDP----AYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLeIIVVSDGSTD-GTAE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 128 LVqvecQRWANKGVniKYEIRDNRRGyKAGALKEGMKHgyVKDcDFVVIFDADFQPEPDYLSRAM-PFLihNPEIALIQA 206
Cdd:cd06439    77 IA----REYADKGV--KLLRFPERRG-KAAALNRALAL--ATG-EIVVFTDANALLDPDALRLLVrHFA--DPSVGAVSG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 207 RWVFVNANEclMTRMQEMSLDYHFKV-EQEvgSSAYAFFGFNGTagvwrISAL-NEA-GGWKDRTTVEDMDLAVRASLKG 283
Cdd:cd06439   145 ELVIVDGGG--SGSGEGLYWKYENWLkRAE--SRLGSTVGANGA-----IYAIrRELfRPLPADTINDDFVLPLRIARQG 215
                         250       260
                  ....*....|....*....|
gi 1149725268 284 WKFVYLGDLRVKSELPSTFK 303
Cdd:cd06439   216 YRVVYEPDAVAYEEVAEDGS 235
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
82-322 1.35e-06

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: 49.54  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  82 VLVQIPMYNEREVYKKSIGAACGLSWPSDRIVIQVLDD-STDpAIKELVQvecqRWANKgvNIKYEIRDNRRGYKAGALK 160
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGgSTD-GTREIVQ----EYAAK--DPRIRLIDNPKRIQSAGLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 161 EGMKHGyvkDCDFVVIFDADFQPEPDYLSRAMPFLIHNPE-----IALIQARWVFVNANECLMTRMQEMSLDYHFKVEQE 235
Cdd:cd02525    75 IGIRNS---RGDIIIRVDAHAVYPKDYILELVEALKRTGAdnvggPMETIGESKFQKAIAVAQSSPLGSGGSAYRGGAVK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 236 VGSSAYAFFgfngtaGVWRISALNEAGGWKDR-TTVEDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAFRYQQHRWSC 314
Cdd:cd02525   152 IGYVDTVHH------GAYRREVFEKVGGFDESlVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGK 225

                  ....*...
gi 1149725268 315 GPANLFRK 322
Cdd:cd02525   226 WRARTLRK 233
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
84-190 1.45e-06

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: 48.72  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  84 VQIPMYNEREVYKKSIGA--ACGLSWPSDRIVIqVLDDSTDPAIKELvqvecQRWANKGVNIKYEIRDNRRGyKAGALKE 161
Cdd:cd04179     1 VVIPAYNEEENIPELVERllAVLEEGYDYEIIV-VDDGSTDGTAEIA-----RELAARVPRVRVIRLSRNFG-KGAAVRA 73
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1149725268 162 GMKH--GyvkdcDFVVIFDADFQPEPDYLSR 190
Cdd:cd04179    74 GFKAarG-----DIVVTMDADLQHPPEDIPK 99
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
84-224 1.05e-05

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: 46.22  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  84 VQIPMYNEREVYKKSIGAACGLSwpsDRIVIQVLDDSTDPAikELVQVECQRwANKGVNIKYEIRDNRRGYKAGALKEGM 163
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLLRNK---PNFLVLVIDDASDDD--TAGIVRLAI-TDSRVHLLRRHLPNARTGKGDALNAAY 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149725268 164 KH----GYVKDCDF----VVIFDADFQPEPDYLSRAMPFLiHNPEIALIQARWVFVNANECLMTRMQEM 224
Cdd:cd06436    75 DQirqiLIEEGADPerviIAVIDADGRLDPNALEAVAPYF-SDPRVAGTQSRVRMYNRHKNLLTILQDL 142
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
87-225 5.82e-05

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: 44.58  E-value: 5.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  87 PMYNE--REVYK--KSIGAACGLSWPSDRIVIQVLDDSTDPAIkelVQVECQRWAN------KGVNIKYEIRDNRRGYKA 156
Cdd:cd04191     6 PVYNEdpARVFAglRAMYESLAKTGLADHFDFFILSDTRDPDI---WLAEEAAWLDlceelgAQGRIYYRRRRENTGRKA 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 157 GALKEGMK-HGyvKDCDFVVIFDADFQPEPDYLSRAMPFLIHNPEIALIQARWVFVNAnECLMTRMQEMS 225
Cdd:cd04191    83 GNIADFCRrWG--SRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGA-ETLFARLQQFA 149
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
86-190 7.72e-05

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: 43.36  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  86 IPMYNEREVYKKSIGAACGLSWPSDRI-VIQVLDDSTDPAikelvqveCQRWANKGVNIkYEIRDN-RRGyKAGALKEGM 163
Cdd:cd06438     3 IPAHNEEAVIGNTVRSLKAQDYPRELYrIFVVADNCTDDT--------AQVARAAGATV-LERHDPeRRG-KGYALDFGF 72
                          90       100
                  ....*....|....*....|....*....
gi 1149725268 164 KH--GYVKDCDFVVIFDADFQPEPDYLSR 190
Cdd:cd06438    73 RHllNLADDPDAVVVFDADNLVDPNALEE 101
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
86-188 1.68e-04

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: 42.91  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  86 IPMYNERE-----VYKksIGAAcgLSWPSDRIVIqVLDDSTDPAIKElvqveCQRWANKGVNIKYEIRDNRRGYkAGALK 160
Cdd:cd06442     3 IPTYNEREnipelIER--LDAA--LKGIDYEIIV-VDDNSPDGTAEI-----VRELAKEYPRVRLIVRPGKRGL-GSAYI 71
                          90       100
                  ....*....|....*....|....*...
gi 1149725268 161 EGMKHGYvkdCDFVVIFDADFQPEPDYL 188
Cdd:cd06442    72 EGFKAAR---GDVIVVMDADLSHPPEYI 96
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
156-194 2.45e-04

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


Pssm-ID: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 42.24  E-value: 2.45e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1149725268 156 AGALKEGMKHGYVKDCDFVVIFDADFQPEPDYLSRAMPF 194
Cdd:cd04185    65 AGGFYEGVRRAYELGYDWIWLMDDDAIPDPDALEKLLAY 103
PRK05454 PRK05454
glucans biosynthesis glucosyltransferase MdoH;
28-222 4.67e-04

glucans biosynthesis glucosyltransferase MdoH;


Pssm-ID: 235476 [Multi-domain]  Cd Length: 605  Bit Score: 42.95  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  28 MVCLAMCVILFVEKVY---MAVVIVAMRLIGRRPERQWRWEPLRDDDPELGNAAypmVLVqiPMYNE---------REVY 95
Cdd:PRK05454   74 PALLVLFALLFAWISLgfwTALMGFLQLLRGRDKYSISASAAGDPPPPPEARTA---ILM--PIYNEdparvfaglRAMY 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  96 KkSIGAACGLswpsDRIVIQVLDDSTDPAI---KELVQVECQRWANKGVNIKYEIRDNRRGYKAGALKE-----GmkHGY 167
Cdd:PRK05454  149 E-SLAATGHG----AHFDFFILSDTRDPDIaaaEEAAWLELRAELGGEGRIFYRRRRRNVGRKAGNIADfcrrwG--GAY 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149725268 168 vkdcDFVVIFDADFQPEPD---YLSRAMpflIHNPEIALIQARWVFVNAnECLMTRMQ 222
Cdd:PRK05454  222 ----DYMVVLDADSLMSGDtlvRLVRLM---EANPRAGLIQTLPVAVGA-DTLFARLQ 271
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
82-313 6.68e-04

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: 41.47  E-value: 6.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  82 VLVQIPMYNE-REVYKKSIgAACGLSWPSDRIVIqvlddsTDPAIKELVQVECQRWANKGVNIKYEIRDNRRGykagALK 160
Cdd:cd06434     2 VTVIIPVYDEdPDVFRECL-RSILRQKPLEIIVV------TDGDDEPYLSILSQTVKYGGIFVITVPHPGKRR----ALA 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 161 EGMKHgyvKDCDFVVIFDADFQPEPDYLSRA-MPFLihNPEIALIQARWVFVNANECLMTRMQEMSLDYHFkveqEVGSS 239
Cdd:cd06434    71 EGIRH---VTTDIVVLLDSDTVWPPNALPEMlKPFE--DPKVGGVGTNQRILRPRDSKWSFLAAEYLERRN----EEIRA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 240 AYAFFG----FNGTAGVWRISALNEA---------GGWKDRTTV-EDMDLAVRASLKGWKFVYLGDLRVKSELPSTFKAF 305
Cdd:cd06434   142 AMSYDGgvpcLSGRTAAYRTEILKDFlfleeftneTFMGRRLNAgDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKF 221

                  ....*...
gi 1149725268 306 RYQQHRWS 313
Cdd:cd06434   222 LKQQLRWS 229
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
105-204 3.03e-03

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 39.19  E-value: 3.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 105 LSWPSDRIVIqvLDDST--DPAIKELV---QVECQR-WANKGVnikyeirdnrrgykAGALKEGMKHGYVKDCDFVVIFD 178
Cdd:cd02526    20 LAEQVDKVVV--VDNSSgnDIELRLRLnseKIELIHlGENLGI--------------AKALNIGIKAALENGADYVLLFD 83
                          90       100
                  ....*....|....*....|....*....
gi 1149725268 179 ADFQPEPDYLSRAMPFLIH---NPEIALI 204
Cdd:cd02526    84 QDSVPPPDMVEKLLAYKILsdkNSNIGAV 112
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
172-313 4.85e-03

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: 38.03  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 172 DFVVIFDADFQPEPDYLSRAM-PFLihNPEIALIQARWVFVNANECLMTRMQEMSLDYHfkveqevGSSAYAFFGF---N 247
Cdd:pfam13506  32 DLLVISDSDIRVPPDYLRDLLaPLA--DPKVGLVTSPPVGSDPKGLAAALEAAFFNTLA-------GVLQAALSGIgfaV 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149725268 248 GTAGVWRISALNEAGG---WKDrTTVEDMDLAVRASLKGWKFVYLGDLRVKSELP--STFKAFRYQQHRWS 313
Cdd:pfam13506 103 GMSMAFRRADLERIGGfeaLAD-YLAEDYALGKLLRAAGLKVVLSPRPILQTSGPrrTSFRAFMARQLRWA 172
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
84-312 5.01e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 38.81  E-value: 5.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268  84 VQIPMYNEREVYKKSIGAACGLSWPSDRI-VIQVLDDSTDpAIKELVQVECQrwaNKGVNIKyeIRDNRRGY---KAGAL 159
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKEKFeVILVDDHSTD-GTVQILEFAAA---KPNFQLK--ILNNSRVSisgKKNAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 160 KEGMKHGyvkDCDFVVIFDADFQPEPDYLSRAMPFliHNPEIALIQARWVFVNANECLMTRMQemSLDYHFKVeqevGSS 239
Cdd:cd04192    75 TTAIKAA---KGDWIVTTDADCVVPSNWLLTFVAF--IQKEQIGLVAGPVIYFKGKSLLAKFQ--RLDWLSLL----GLI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149725268 240 AYAF-----FGFNGTAGVWRISALNEAGGWK--DRTTVEDMDLAVRASLKGW-KFVYL--GDLRVKSELPSTFKAFRYQQ 309
Cdd:cd04192   144 AGSFglgkpFMCNGANMAYRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYpKVAYLknPEALVTTQPVTSWKELLNQR 223

                  ...
gi 1149725268 310 HRW 312
Cdd:cd04192   224 KRW 226
 
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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