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Conserved domains on  [gi|1898810296|ref|WP_187470416|]
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glycosyltransferase family 2 protein [Dictyoglomus thermophilum]

Protein Classification

glycosyltransferase( domain architecture ID 11440269)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
45-330 4.29e-60

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: 197.66  E-value: 4.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDLPSVSVLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYPHlIKPLFRDssQKRGKPS 124
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPR-VRVIERP--ENGGKAA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 125 ALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVmgrviplnisknlltrlfdleriggyqvdqqarynlk 204
Cdd:COG1215   102 ALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS------------------------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 205 lipqygGTVGGFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRGHNQVMF 284
Cdd:COG1215   145 ------GANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLL 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1898810296 285 RYLIPLIKSPYLslrekidgvFLLCVYLVPPLFLLGLIDSIILFFL 330
Cdd:COG1215   219 KHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLL 255
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
45-330 4.29e-60

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: 197.66  E-value: 4.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDLPSVSVLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYPHlIKPLFRDssQKRGKPS 124
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPR-VRVIERP--ENGGKAA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 125 ALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVmgrviplnisknlltrlfdleriggyqvdqqarynlk 204
Cdd:COG1215   102 ALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS------------------------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 205 lipqygGTVGGFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRGHNQVMF 284
Cdd:COG1215   145 ------GANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLL 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1898810296 285 RYLIPLIKSPYLslrekidgvFLLCVYLVPPLFLLGLIDSIILFFL 330
Cdd:COG1215   219 KHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLL 255
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-235 1.18e-58

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: 189.75  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHLIkpLFRDSSQKRGKPSALNDALKI 132
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRV--LVVRDKENGGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 133 AKGEIIIVFDADSIPPRGIIRDLTTS-FLDPEVGIVMGRVIPLNISKNLLTRLFDLERIGGYQVDQQARYNLKLIPQYGG 211
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPfFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156
                         170       180
                  ....*....|....*....|....
gi 1898810296 212 TVGGFRKDLVLSLGGFNPKILAED 235
Cdd:cd06423   157 AFGAFRREALREVGGWDEDTLTED 180
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
49-278 5.90e-29

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 112.85  E-value: 5.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPH-LIKPLFR-DSSQKRGKPSAL 126
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARFPDvRLRVIRNaRLLGPTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 127 NDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISkNLLTRLFDLERIGGYQVDQQARYNLKLI 206
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRS-TMLSALGALEFALRHLRMMSLRLALGVL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1898810296 207 PqYGGTVGGFRKDLVLSLGGFNPK-ILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRG 278
Cdd:pfam13641 159 P-LSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
45-167 9.23e-11

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 63.89  E-value: 9.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDL-PSVSVLIPMHNEE-KVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYphlikplFRDSSQKRGK 122
Cdd:PRK11498  255 DMSLwPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKY-------IARPTHEHAK 327
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1898810296 123 PSALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFL-DPEVGIV 167
Cdd:PRK11498  328 AGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLkDKKLAMM 373
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
45-330 4.29e-60

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: 197.66  E-value: 4.29e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDLPSVSVLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYPHlIKPLFRDssQKRGKPS 124
Cdd:COG1215    25 PADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEIARELAAEYPR-VRVIERP--ENGGKAA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 125 ALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVmgrviplnisknlltrlfdleriggyqvdqqarynlk 204
Cdd:COG1215   102 ALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS------------------------------------- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 205 lipqygGTVGGFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRGHNQVMF 284
Cdd:COG1215   145 ------GANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLL 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1898810296 285 RYLIPLIKSPYLslrekidgvFLLCVYLVPPLFLLGLIDSIILFFL 330
Cdd:COG1215   219 KHRPLLRPRRLL---------LFLLLLLLPLLLLLLLLALLALLLL 255
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
53-235 1.18e-58

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: 189.75  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHLIkpLFRDSSQKRGKPSALNDALKI 132
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYP--KLEVIVVDDGSTDDTLEILEELAALYIRRV--LVVRDKENGGKAGALNAGLRH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 133 AKGEIIIVFDADSIPPRGIIRDLTTS-FLDPEVGIVMGRVIPLNISKNLLTRLFDLERIGGYQVDQQARYNLKLIPQYGG 211
Cdd:cd06423    77 AKGDIVVVLDADTILEPDALKRLVVPfFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSG 156
                         170       180
                  ....*....|....*....|....
gi 1898810296 212 TVGGFRKDLVLSLGGFNPKILAED 235
Cdd:cd06423   157 AFGAFRREALREVGGWDEDTLTED 180
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
49-278 1.39e-40

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: 144.38  E-value: 1.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDnSSDGT----REILESYHSRYPHlIKPLFRDSsqKRG-KP 123
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDD-STDETvrlaREIVEEYAAQGVN-IKHVRRAD--RTGyKA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 124 SALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISKNLLTRLFDLERIGGYQVDQQARYNL 203
Cdd:cd06437    77 GALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSST 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1898810296 204 KLIPQYGGTVGGFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRG 278
Cdd:cd06437   157 GLFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
45-268 9.31e-35

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: 129.24  E-value: 9.31e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDLPSVSVLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYPHLIkplfrDSSQKRGKPS 124
Cdd:cd06439    25 PAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDGSTDGTAEIAREYADKGVKLL-----RFPERRGKAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 125 ALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNisknlltrlfdleriGGYQVDQQARY--- 201
Cdd:cd06439   100 ALNRALALATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSGELVIVD---------------GGGSGSGEGLYwky 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 202 --NLKLI-PQYGGTVGG------FRKDLVlslGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPET------WH 266
Cdd:cd06439   165 enWLKRAeSRLGSTVGAngaiyaIRRELF---RPLPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDgseefrRR 241

                  ..
gi 1898810296 267 VR 268
Cdd:cd06439   242 VR 243
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
49-284 1.98e-32

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: 122.75  E-value: 1.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYhsRYPHLIKPLFRDSSQKRGKPSALND 128
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARAL--RLPSIFRVVVVPPSQPRTKPKACNY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 129 ALKIAKGEIIIVFDADSIPPRGIIRDLTTSF--LDPEVGIVMGRVIPLNISKNLLTRLFDLEriggYqvDQQARYNLK-- 204
Cdd:cd06427    79 ALAFARGEYVVIYDAEDAPDPDQLKKAVAAFarLDDKLACVQAPLNYYNARENWLTRMFALE----Y--AAWFDYLLPgl 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 205 -----LIPqYGGTVGGFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRaECYEEAPET---WHvraKQIRRWS 276
Cdd:cd06427   153 arlglPIP-LGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNS-TTLEEANNAlgnWI---RQRSRWI 227

                  ....*...
gi 1898810296 277 RGHNQVMF 284
Cdd:cd06427   228 KGYMQTWL 235
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
50-291 3.47e-30

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 116.95  E-value: 3.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  50 SVSVLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYPH--LIKplfrdsSQKRGKPSALN 127
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGGSTDGTREIVQEYAAKDPRirLID------NPKRIQSAGLN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 128 DALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMG--RVIPLN-----ISKNLLTRLfdleRIGGyqvdqqAR 200
Cdd:cd02525    75 IGIRNSRGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGpmETIGESkfqkaIAVAQSSPL----GSGG------SA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 201 Y-NLKLIPQYGGTV--GGFRKDLVLSLGGFNPK-ILAEDTELTIKAYISGVKVCYMNRAECYeeapetWHVR------AK 270
Cdd:cd02525   145 YrGGAVKIGYVDTVhhGAYRREVFEKVGGFDESlVRNEDAELNYRLRKAGYKIWLSPDIRVY------YYPRstlkklAR 218
                         250       260
                  ....*....|....*....|....*....
gi 1898810296 271 Q--------IRRWSRGHNQVMFRYLIPLI 291
Cdd:cd02525   219 QyfrygkwrARTLRKHRKSLSLRHLLPLA 247
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
49-278 5.90e-29

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 112.85  E-value: 5.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPH-LIKPLFR-DSSQKRGKPSAL 126
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYP--PVEVVVVVNPSDAETLDVAEEIAARFPDvRLRVIRNaRLLGPTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 127 NDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISkNLLTRLFDLERIGGYQVDQQARYNLKLI 206
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSLNRS-TMLSALGALEFALRHLRMMSLRLALGVL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1898810296 207 PqYGGTVGGFRKDLVLSLGGFNPK-ILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRG 278
Cdd:pfam13641 159 P-LSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
52-220 5.91e-28

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: 108.25  E-value: 5.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  52 SVLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHLIkplFRDSSQKRGKPSALNDALK 131
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYP--NFEIIVVDDGSTDGTVEIAEEYAKKDPRVR---VIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 132 IAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISKNLLTRLFDLERIGGYQVDQQARYNLKLIPQYGG 211
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155

                  ....*....
gi 1898810296 212 TVGGFRKDL 220
Cdd:pfam00535 156 FALYRREAL 164
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-275 4.56e-27

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: 107.76  E-value: 4.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHS-RYPHLiKPLFRDSSQKRGKPSALNDALK 131
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDHSTDGTVQILEFAAAkPNFQL-KILNNSRVSISGKKNALTTAIK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 132 IAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNiSKNLLTRLFDLERIggyqvDQQARYNLKLIPQYGG 211
Cdd:cd04192    80 AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFK-GKSLLAKFQRLDWL-----SLLGLIAGSFGLGKPF 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1898810296 212 TVGG----FRKDLVLSLGGF--NPKILAEDTELTIKAYISG-VKVCYMNRAEC--YEEAPETWHVRAKQIRRW 275
Cdd:cd04192   154 MCNGanmaYRKEAFFEVGGFegNDHIASGDDELLLAKVASKyPKVAYLKNPEAlvTTQPVTSWKELLNQRKRW 226
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
49-268 7.94e-27

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 106.71  E-value: 7.94e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHlIKPLFRdsSQKRGKPSALND 128
Cdd:COG0463     2 PLVSVVIPTYNEEEYLEEALESLLAQTYP--DFEIIVVDDGSTDGTAEILRELAAKDPR-IRVIRL--ERNRGKGAARNA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 129 ALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMG-RVIPLN--ISKNLLTRLFDLERIggyqvdqqarynLKL 205
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGsRLIREGesDLRRLGSRLFNLVRL------------LTN 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1898810296 206 IPQYGGTVGGFRKDLVLSLgGFNPKiLAEDTELtIKAYISGVKVCYMNraECYEEAPETWHVR 268
Cdd:COG0463   145 LPDSTSGFRLFRREVLEEL-GFDEG-FLEDTEL-LRALRHGFRIAEVP--VRYRAGESKLNLR 202
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
49-283 3.12e-26

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: 105.73  E-value: 3.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEE-KVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYP-HLIKPLFRdssqKRGKPSAL 126
Cdd:cd06421     1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYPHDKLRVYVLDDGRRPELRALAAELGVEYGyRYLTRPDN----RHAKAGNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 127 NDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLD-PEVGIVMGRVIPLNISKN-LLTRLFDLERIGGYQVDQQARyNLK 204
Cdd:cd06421    77 NNALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDdPKVALVQTPQFFYNPDPFdWLADGAPNEQELFYGVIQPGR-DRW 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1898810296 205 LIPQYGGTVGGFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRGHNQVM 283
Cdd:cd06421   156 GAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
53-193 3.05e-25

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 100.66  E-value: 3.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHLIKplfRDSSQKRGKPSALNDALKI 132
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYP--NFEVIVVDDGSTDGTLEILEEYAKKDPRVIR---VINEENQGLAAARNAGLKA 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1898810296 133 AKGEIIIVFDADSIPPRGIIRDLTTSFL-DPEVGIVMGRviplnisKNLLTRLFDLERIGGY 193
Cdd:cd00761    76 ARGEYILFLDADDLLLPDWLERLVAELLaDPEADAVGGP-------GNLLFRRELLEEIGGF 130
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
53-169 4.55e-18

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: 81.47  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYPHlIKPLFRdsSQKRGKPSALNDALKI 132
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDGSTDGTAEIARELAARVPR-VRVIRL--SRNFGKGAAVRAGFKA 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1898810296 133 AKGEIIIVFDAD-SIPPRgIIRDLTTSFLDPEVGIVMG 169
Cdd:cd04179    78 ARGDIVVTMDADlQHPPE-DIPKLLEKLLEGGADVVIG 114
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
137-322 4.14e-17

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: 78.92  E-value: 4.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 137 IIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNiSKNLLTRLFDLERIGGYQVDQQARYNLKLIPQYGGTVGGF 216
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPEVAIIQGPILPMN-VGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 217 RKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRGHN----QVMFRYLIPLIK 292
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLlillIRLLGYLGTLLW 159
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1898810296 293 S--PYLSLREKIDGVFLLCVYLVPPLFLLGLI 322
Cdd:pfam13632 160 SglPLALLLLLLFSISSLALVLLLLALLAGLL 191
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
52-287 5.65e-16

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 76.67  E-value: 5.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  52 SVLIPMHNEE-KVAKNILNALLNADYPQerLEIIPIDDNSSD-GTREILESYHSRYPHLIKpLFRDSSQKRGKPSALNDA 129
Cdd:cd06435     1 SIHVPCYEEPpEMVKETLDSLAALDYPN--FEVIVIDNNTKDeALWKPVEAHCAQLGERFR-FFHVEPLPGAKAGALNYA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 130 LKIAKG--EIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISKNLLTRLFDLERIGGYQVDQQARYNLKLIP 207
Cdd:cd06435    78 LERTAPdaEIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERNAII 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 208 QYGgTVGGFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQIRRWSRGHNQVMFRYL 287
Cdd:cd06435   158 QHG-TMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKKHW 236
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
49-285 9.12e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 75.41  E-value: 9.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHLIKplfrdSSQKRGKPSALND 128
Cdd:COG1216     3 PKVSVVIPTYNRPELLRRCLESLLAQTYP--PFEVIVVDNGSTDGTAELLAALAFPRVRVIR-----NPENLGFAAARNL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 129 ALKIAKGEIIIVFDADSIPPRGIIRDLTTSFldpevgivmgrviplniskNLLtrlfdleriggyqvdqqarynlklipq 208
Cdd:COG1216    76 GLRAAGGDYLLFLDDDTVVEPDWLERLLAAA-------------------CLL--------------------------- 109
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1898810296 209 yggtvggFRKDLVLSLGGFNPK--ILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHvraKQIRRWSRGHNQVMFR 285
Cdd:COG1216   110 -------IRREVFEEVGGFDERffLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSG---PLLRAYYLGRNRLLFL 178
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
52-254 1.99e-14

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 71.42  E-value: 1.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  52 SVLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHLIkplfrdsSQK-RGKPSALNDAL 130
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYP--NIEYIVIDGGSTDGTVDIIKKYEDKITYWI-------SEPdKGIYDAMNKGI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 131 KIAKGEIIIVFDA-DSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISKNLLTR-----LFDLERIGGYQVDQQARYnlk 204
Cdd:cd06433    72 ALATGDIIGFLNSdDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRrrpppFLDKFLLYGMPICHQATF--- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1898810296 205 lipqyggtvggFRKDLVLSLGGFNPKI-LAEDTELTIKAYISGVKVCYMNR 254
Cdd:cd06433   149 -----------FRRSLFEKYGGFDESYrIAADYDLLLRLLLAGKIFKYLPE 188
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
50-278 6.24e-14

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 70.75  E-value: 6.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  50 SVSVLIPMHNE-----EKVAKNILNallnadypQERLEIIPIDDNSSDGTREILESyhsRYPHliKPLFRDSSQKRGKPS 124
Cdd:cd06434     1 DVTVIIPVYDEdpdvfRECLRSILR--------QKPLEIIVVTDGDDEPYLSILSQ---TVKY--GGIFVITVPHPGKRR 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 125 ALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISKNLLTRLFD--LERIggYQVDQQARYN 202
Cdd:cd06434    68 ALAEGIRHVTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTNQRILRPRDSKWSFLAAeyLERR--NEEIRAAMSY 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 203 LKLIPQYGGTVGGFRKDLVLSL----------GGFNPKILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRAKQI 272
Cdd:cd06434   146 DGGVPCLSGRTAAYRTEILKDFlfleeftnetFMGRRLNAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFLKQQ 225

                  ....*.
gi 1898810296 273 RRWSRG 278
Cdd:cd06434   226 LRWSRS 231
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
53-238 1.21e-13

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: 68.78  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYphlikpLFRDSSQKRGKPSALNDALKI 132
Cdd:cd06438     1 ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADNCTDDTAQVARAAGATV------LERHDPERRGKGYALDFGFRH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 133 AKG-----EIIIVFDADSIPPRGIIRDLTTSF-LDPEVgiVMGRVIPLNISKNLLTRLFDLERIGGYQVDQQARYNLKLI 206
Cdd:cd06438    75 LLNladdpDAVVVFDADNLVDPNALEELNARFaAGARV--VQAYYNSKNPDDSWITRLYAFAFLVFNRLRPLGRSNLGLS 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1898810296 207 PQYGGTVGGFRKDlVLSLGGFNPKILAEDTEL 238
Cdd:cd06438   153 CQLGGTGMCFPWA-VLRQAPWAAHSLTEDLEF 183
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
53-258 9.83e-13

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: 65.66  E-value: 9.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYhsrYPH--LIKplfrdSSQKRGKPSALNDAL 130
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYP--DFEVIVVDNASTDGSVELLREL---FPEvrLIR-----NGENLGFGAGNNQGI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 131 KIAKGEIIIVFDADSIPPRGIIRDLTTSF-LDPEVGIVMGRVIplnisknlltrlfdleriggyqvdqqarynlklipqy 209
Cdd:cd04186    71 REAKGDYVLLLNPDTVVEPGALLELLDAAeQDPDVGIVGPKVS------------------------------------- 113
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1898810296 210 ggtvGGF---RKDLVLSLGGFNPKILA--EDTELTIKAYISGVKVCYMNRAECY 258
Cdd:cd04186   114 ----GAFllvRREVFEEVGGFDEDFFLyyEDVDLCLRARLAGYRVLYVPQAVIY 163
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
53-169 4.79e-12

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: 65.25  E-value: 4.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEekvAKNI--LNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYPhliKPLFRDSSQKRGKPSALNDAL 130
Cdd:cd06442     1 IIIPTYNE---RENIpeLIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKEYP---RVRLIVRPGKRGLGSAYIEGF 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1898810296 131 KIAKGEIIIVFDAD-SIPPRgIIRDLTTSFLDPEVGIVMG 169
Cdd:cd06442    75 KAARGDVIVVMDADlSHPPE-YIPELLEAQLEGGADLVIG 113
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
53-185 9.22e-12

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: 64.13  E-value: 9.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLN--ADYPQERLEIIPIDDNSSDGTREILESYHSRYPHLIKPLfrDSSQKRGKPSALNDAL 130
Cdd:cd04188     1 VVIPAYNEEKRLPPTLEEAVEylEERPSFSYEIIVVDDGSKDGTAEVARKLARKNPALIRVL--TLPKNRGKGGAVRAGM 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1898810296 131 KIAKGEIIIVFDAD-SIPPRGIIRdLTTSFLDPEVGIVMG-RVIPLNISK-------NLLTRLF 185
Cdd:cd04188    79 LAARGDYILFADADlATPFEELEK-LEEALKTSGYDIAIGsRAHLASAAVvkrswlrNLLGRGF 141
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
49-194 2.27e-11

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 62.61  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNEEKVAKNILNALLNADYPqeRLEIIPIDDNSSDGTREILESYHSRYPHLIKPLFRDSSQK--RGKPSAL 126
Cdd:cd02520     1 PGVSILKPLCGVDPNLYENLESFFQQDYP--KYEILFCVQDEDDPAIPVVRKLIAKYPNVDARLLIGGEKVgiNPKVNNL 78
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1898810296 127 NDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGrvIPLNISKNLLTRLfDLERIGGYQ 194
Cdd:cd02520    79 IKGYEEARYDILVISDSDISVPPDYLRRMVAPLMDPGVGLVTC--LCAFGKSMALRRE-VLDAIGGFE 143
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
53-214 4.53e-11

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: 61.63  E-value: 4.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLnADYPQERleIIPIDDNSSDGTREI--LESYHSRYPHLIKPLfrdSSQKRGKPSALN--- 127
Cdd:cd06436     1 VLVPCLNEEAVIQRTLASLL-RNKPNFL--VLVIDDASDDDTAGIvrLAITDSRVHLLRRHL---PNARTGKGDALNaay 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 128 DALK---IAKG-----EIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGRVIPLNISKNLLTRLFDLERIGGYQVDQQA 199
Cdd:cd06436    75 DQIRqilIEEGadperVIIAVIDADGRLDPNALEAVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQSL 154
                         170
                  ....*....|....*
gi 1898810296 200 RynlklipQYGGTVG 214
Cdd:cd06436   155 R-------ALTGTVG 162
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
45-167 9.23e-11

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 63.89  E-value: 9.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDL-PSVSVLIPMHNEE-KVAKNILNALLNADYPQERLEIIPIDDNSSDGTREILESYHSRYphlikplFRDSSQKRGK 122
Cdd:PRK11498  255 DMSLwPTVDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDDGGREEFRQFAQEVGVKY-------IARPTHEHAK 327
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1898810296 123 PSALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFL-DPEVGIV 167
Cdd:PRK11498  328 AGNINNALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLkDKKLAMM 373
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
53-144 1.21e-10

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: 60.18  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNA-DYPQERLEIIPIDDNSSDGTREILESYHSRYPHlIKPLfrDSSQKRGKPSALNDALK 131
Cdd:cd04187     1 IVVPVYNEEENLPELYERLKAVlESLGYDYEIIFVDDGSTDRTLEILRELAARDPR-VKVI--RLSRNFGQQAALLAGLD 77
                          90
                  ....*....|...
gi 1898810296 132 IAKGEIIIVFDAD 144
Cdd:cd04187    78 HARGDAVITMDAD 90
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
51-238 1.91e-10

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


Pssm-ID: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 60.28  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  51 VSVLIPMHNEEKVAKNILNALLNAdyPQERLEIIPIDDNSSDGTREILESYHSRyphLIKPlfrdssqKRGKPSALNDAL 130
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRL--NPLPLEIIVVDGGSTDGTVAIARSAGVV---VISS-------PKGRARQMNAGA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 131 KIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPevGIVMGRVIPLNISKNLLTRLfdLERiggyqvdqqaRYNLKLipQYG 210
Cdd:cd02522    69 AAARGDWLLFLHADTRLPPDWDAAIIETLRAD--GAVAGAFRLRFDDPGPRLRL--LEL----------GANLRS--RLF 132
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1898810296 211 GTVGG-----FRKDLVLSLGGFNPKILAEDTEL 238
Cdd:cd02522   133 GLPYGdqglfIRRELFEELGGFPELPLMEDVEL 165
PRK10073 PRK10073
putative glycosyl transferase; Provisional
45-144 6.57e-10

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 60.06  E-value: 6.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDLPSVSVLIPMHNEEKVAKNILNALLNADYpqERLEIIPIDDNSSDGTREILESYHSRYPHlikplFRDSSQKRGKPS 124
Cdd:PRK10073    2 MNSTPKLSIIIPLYNAGKDFRAFMESLIAQTW--TALEIIIVNDGSTDNSVEIAKHYAENYPH-----VRLLHQANAGVS 74
                          90       100
                  ....*....|....*....|.
gi 1898810296 125 -ALNDALKIAKGEIIIVFDAD 144
Cdd:PRK10073   75 vARNTGLAVATGKYVAFPDAD 95
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
53-248 1.42e-09

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


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 57.20  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNadypQERL--EIIPIDDNSSDGTREILESYHSRYPHLIKPL------FRdssqkrgKPS 124
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLN----QSILpfEVIIADDGSTEETKELIEEFKSQFPIPIKHVwqedegFR-------KAK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 125 ALNDALKIAKGEIIIVFDADSIPPRGIIRDlTTSFLDPEVGIVMGRViplNISKNLLTRLFDleriggyqvdqqarynlk 204
Cdd:cd06420    70 IRNKAIAAAKGDYLIFIDGDCIPHPDFIAD-HIELAEPGVFLSGSRV---LLNEKLTERGIR------------------ 127
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1898810296 205 lipqyGGTVGGFRKDLvLSLGGFNPKIL---AEDTELTIKAYISGVK 248
Cdd:cd06420   128 -----GCNMSFWKKDL-LAVNGFDEEFTgwgGEDSELVARLLNSGIK 168
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
122-277 2.17e-08

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 53.44  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 122 KPSALNDALKIAKGEIIIVFDADSIPPRGIIRDLTTSFLDPEVGIVMGrvIPLNIS-KNLLTRlfdLERIGGYQVDQQAR 200
Cdd:pfam13506  18 KVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTS--PPVGSDpKGLAAA---LEAAFFNTLAGVLQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 201 YNLKLIPQYGGTVGGFRKDLVLSLGGFNP--KILAEDTELTIKAYISGVKVCYMNRAECYEEAPETWHVRA--KQIRRWS 276
Cdd:pfam13506  93 AALSGIGFAVGMSMAFRRADLERIGGFEAlaDYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRRTSFRAfmARQLRWA 172

                  .
gi 1898810296 277 R 277
Cdd:pfam13506 173 R 173
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
49-144 9.03e-08

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


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 52.21  E-value: 9.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHN-EEKVAKNILNALLNADYPqeRLEIIPIDDNSSD-GTREILESYHSRYPHlIKPLFRDSSQkrGKPSAL 126
Cdd:cd04184     1 PLISIVMPVYNtPEKYLREAIESVRAQTYP--NWELCIADDASTDpEVKRVLKKYAAQDPR-IKVVFREENG--GISAAT 75
                          90
                  ....*....|....*...
gi 1898810296 127 NDALKIAKGEIIIVFDAD 144
Cdd:cd04184    76 NSALELATGEFVALLDHD 93
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
49-144 1.54e-07

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 52.01  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  49 PSVSVLIPMHNE-EKVAknILNALLNADYPQ-ERLEIIPIDDNSSDGTREILESYHSRY-PHLIkpLFRDSSQKRGKPSA 125
Cdd:PLN02726    9 MKYSIIVPTYNErLNIA--LIVYLIFKALQDvKDFEIIVVDDGSPDGTQDVVKQLQKVYgEDRI--LLRPRPGKLGLGTA 84
                          90
                  ....*....|....*....
gi 1898810296 126 LNDALKIAKGEIIIVFDAD 144
Cdd:PLN02726   85 YIHGLKHASGDFVVIMDAD 103
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
52-249 1.67e-06

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 48.47  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  52 SVLIPMHNEEKVA------KNILNALLNADypqerlEIIPIDDNS-SDGTREILESYHSRYPHLIKPLfrdsSQKRGKPS 124
Cdd:cd04195     1 SVLMSVYIKEKPEflrealESILKQTLPPD------EVVLVKDGPvTQSLNEVLEEFKRKLPLKVVPL----EKNRGLGK 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 125 ALNDALKIAKGEIIIVFDAD--SIPPRgIIRDLTTSFLDPEVGIVMGRVipLNISknlltrlFDLERIGGYQVDQQA--- 199
Cdd:cd04195    71 ALNEGLKHCTYDWVARMDTDdiSLPDR-FEKQLDFIEKNPEIDIVGGGV--LEFD-------SDGNDIGKRRLPTSHddi 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1898810296 200 -RYNLKLIPQYGGTVGgFRKDLVLSLGGFNPKILAEDTELTIKAYISGVKV 249
Cdd:cd04195   141 lKFARRRSPFNHPTVM-FRKSKVLAVGGYQDLPLVEDYALWARMLANGARF 190
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
50-169 2.33e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 46.06  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  50 SVSVLIPMHNEEK-VAKNI--LNALLNADYPqerLEIIPIDDNSSDGTREILESY----HSRyphliKPLFRDSSQKRGK 122
Cdd:PRK13915   32 TVSVVLPALNEEEtVGKVVdsIRPLLMEPLV---DELIVIDSGSTDATAERAAAAgarvVSR-----EEILPELPPRPGK 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1898810296 123 PSALNDALKIAKGEIIIVFDADSIPPR-GIIRDLTTSFL-DPEVGIVMG 169
Cdd:PRK13915  104 GEALWRSLAATTGDIVVFVDADLINFDpMFVPGLLGPLLtDPGVHLVKA 152
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
51-144 2.82e-05

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


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 44.97  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  51 VSVLIPMHNEEKVAKNILNALLNA-DypqerlEIIPIDDNSSDGTREILESYHSRyphLIKPLFRD-SSQKrgkpsalND 128
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVKWAvD------EIIVVDSGSTDRTVEIAKEYGAK---VYQRWWDGfGAQR-------NF 65
                          90
                  ....*....|....*.
gi 1898810296 129 ALKIAKGEIIIVFDAD 144
Cdd:cd02511    66 ALELATNDWVLSLDAD 81
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
51-153 6.50e-05

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 44.73  E-value: 6.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  51 VSVLIPMHNEEKVAKNILN------ALLNADYpqerlEIIPIDDNSSDGTREIL-ESYHSRYPHLIKPLFrdsSQKRGKP 123
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRrttaacESLGKEY-----EILLIDDGSSDNSAEMLvEAAQAPDSHIVAILL---NRNYGQH 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1898810296 124 SALNDALKIAKGEIIIVFDAD-SIPPRGIIR 153
Cdd:PRK10714   80 SAIMAGFSHVTGDLIITLDADlQNPPEEIPR 110
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
45-144 1.19e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 43.99  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  45 DSDLpSVSVLIPMHNEE-KVAKNI------LNALLNADyPQERLEIIPIDDNSSDGTREILESYHSRYphlIKPL--FR- 114
Cdd:PTZ00260   67 DSDV-DLSIVIPAYNEEdRLPKMLketikyLESRSRKD-PKFKYEIIIVNDGSKDKTLKVAKDFWRQN---INPNidIRl 141
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1898810296 115 -DSSQKRGKPSALNDALKIAKGEIIIVFDAD 144
Cdd:PTZ00260  142 lSLLRNKGKGGAVRIGMLASRGKYILMVDAD 172
Chitin_synth_C cd04190
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate ...
53-275 2.92e-04

C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin; Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.


Pssm-ID: 133033 [Multi-domain]  Cd Length: 244  Bit Score: 42.29  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEK---------VAKNILNALLNADYPQERLEIIPIDDNSSDGTREilesyhSRYPHLIkpLFrdssqkrgkp 123
Cdd:cd04190     1 VCVTMYNEDEeelartldsILKNDYPFCARGGDSWKKIVVCVIFDGAIKKNRG------KRDSQLW--FF---------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 124 SALNDALKIAKGEIIIVFDADSIP-PRGIIRDLTTSFLDPEVGIVMGRVIPLNISKNLLTRlfdleriggYQVDQQA--- 199
Cdd:cd04190    63 NYFCRVLFPDDPEFILLVDADTKFdPDSIVQLYKAMDKDPEIGGVCGEIHPMGKKQGPLVM---------YQVFEYAish 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296 200 -----------------------RY-NLKLIPQYGGTVG--GFRKDLVLSLGGFNPKILAED----TELTIKAYisGVKV 249
Cdd:cd04190   134 wldkafesvfgfvtclpgcfsmyRIeALKGDNGGKGPLLdyAYLTNTVDSLHKKNNLDLGEDrilcTLLLKAGP--KRKY 211
                         250       260
                  ....*....|....*....|....*.
gi 1898810296 250 CYMNRAECYEEAPETWHVRAKQIRRW 275
Cdd:cd04190   212 LYVPGAVAETDVPETFVELLSQRRRW 237
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
52-143 7.27e-04

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 41.42  E-value: 7.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  52 SVLIPMHNEEkvakniLNALLNADY------PQERL-EIIPIDDNSSDG-TREILESYHSRYPHLIKpLFRdSSQKRGKP 123
Cdd:cd02510     1 SVIIIFHNEA------LSTLLRTVHsvinrtPPELLkEIILVDDFSDKPeLKLLLEEYYKKYLPKVK-VLR-LKKREGLI 72
                          90       100
                  ....*....|....*....|
gi 1898810296 124 SALNDALKIAKGEIIIVFDA 143
Cdd:cd02510    73 RARIAGARAATGDVLVFLDS 92
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
65-104 1.32e-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: 39.93  E-value: 1.32e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1898810296  65 KNILNALLNADYPQERleIIPIDDNSSDGTREILESYHSR 104
Cdd:cd04185    13 KECLDALLAQTRPPDH--IIVIDNASTDGTAEWLTSLGDL 50
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
82-146 1.45e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 39.92  E-value: 1.45e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1898810296  82 EIIPIDDNSSDGTREILESYHSRYPHLIkpLFRDSSQKRGkpSALN--DALKIAKGEIIIVFDADSI 146
Cdd:cd04196    29 ELIISDDGSTDGTVEIIKEYIDKDPFII--ILIRNGKNLG--VARNfeSLLQAADGDYVFFCDQDDI 91
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
66-155 3.35e-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: 38.80  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  66 NILNALLNADYPQ-ERLEIIpidDNSSDGTREILESYHSRYPHLIKPlfrdsSQKRGKPSALNDALKIAKG---EIIIVF 141
Cdd:cd02526    11 SKLKELLAALAEQvDKVVVV---DNSSGNDIELRLRLNSEKIELIHL-----GENLGIAKALNIGIKAALEngaDYVLLF 82
                          90
                  ....*....|....
gi 1898810296 142 DADSIPPRGIIRDL 155
Cdd:cd02526    83 DQDSVPPPDMVEKL 96
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
53-146 4.45e-03

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 38.21  E-value: 4.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1898810296  53 VLIPMHNEEKVAKNILNALLNADYPQErLEIIPIDDNSSDGTREILESYHSRYPHLIKPLF---RDSSQKRGKPSALNDA 129
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGT-LELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLvgsHNSPSPKGVGYAKNQA 79
                          90
                  ....*....|....*..
gi 1898810296 130 LKIAKGEIIIVFDADSI 146
Cdd:cd06913    80 IAQSSGRYLCFLDSDDV 96
 
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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