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Conserved domains on  [gi|1425876613|ref|WP_112904646|]
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glycosyltransferase [Salinibacter ruber]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
60-291 4.07e-126

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


The actual alignment was detected with superfamily member cd06437:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 232  Bit Score: 367.41  E-value: 4.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  60 VVTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDDSTDATTERVARRVAHWQAEGVNITHVRRDDRTGYKAGALAN 139
Cdd:cd06437     2 MVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQGVNIKHVRRADRTGYKAGALAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDaPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVRELAGCFL 219
Cdd:cd06437    82 GMKVAKGEYVAIFDADFVPPPDFLQKTPPYFAD-PKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSSTGLFF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1425876613 220 NFNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGG 291
Cdd:cd06437   161 NFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 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 ...
60-291 4.07e-126

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: 367.41  E-value: 4.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  60 VVTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDDSTDATTERVARRVAHWQAEGVNITHVRRDDRTGYKAGALAN 139
Cdd:cd06437     2 MVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQGVNIKHVRRADRTGYKAGALAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDaPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVRELAGCFL 219
Cdd:cd06437    82 GMKVAKGEYVAIFDADFVPPPDFLQKTPPYFAD-PKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSSTGLFF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1425876613 220 NFNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGG 291
Cdd:cd06437   161 NFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
61-386 2.21e-50

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: 174.54  E-value: 2.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDD-STDATTERVARrvahWQAEGVNITHVRRDDRTGyKAGALAN 139
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgSTDETAEIARE----LAAEYPRVRVIERPENGG-KAAALNA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVpRFFDAPDLGMvqarwghlnrddslltkvqafgldahfaieqrvrelagcfl 219
Cdd:COG1215   106 GLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA----------------------------------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 220 nfNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGGAETALKLt 299
Cdd:COG1215   144 --SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKH- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 300 GRLWRSAQPWRVklegTFHLTAHFAFPFILLAALTHAPLLLLKGIGHGPGEVYFAVMGFGLFGFAGFFLAQLFAQRALHP 379
Cdd:COG1215   221 RPLLRPRRLLLF----LLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKV 296

                  ....*..
gi 1425876613 380 DWRRRLR 386
Cdd:COG1215   297 VWKKTPR 303
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
61-290 1.45e-24

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: 102.06  E-value: 1.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRldIQVLDDSTDATTERVAR-RVAHWQAEGVNITHVRRDDRTGYKAGALAN 139
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVE--VVVVVNPSDAETLDVAEeIAARFPDVRLRVIRNARLLGPTGKSRGLNH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVPrFFDAPDLGMVQARwGHLNRDDSLLTKVQAFGLDAHFAIEQRVReLAGCFL 219
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQ-YFDSPKVGAVGTP-VFSLNRSTMLSALGALEFALRHLRMMSLR-LALGVL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1425876613 220 NFNGTAGVWRRACIEDAGGW-AHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKG 290
Cdd:pfam13641 159 PLSGAGSAIRREVLKELGLFdPFFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
61-293 2.07e-18

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 88.54  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEA-EVAHRLIDACVQLDYPRSRLDIQVLDDstdattervARRVAHWQ-AEGVNITHVRRDDRTGYKAGALA 138
Cdd:PRK11498  262 VDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDD---------GGREEFRQfAQEVGVKYIARPTHEHAKAGNIN 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 139 NGLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDAPDLGMVQ---------------ARWGHLNRDDSLLtkvqaFGL-- 201
Cdd:PRK11498  333 NALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQtphhffspdpfernlGRFRKTPNEGTLF-----YGLvq 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 202 ------DAHFaieqrvrelagcflnFNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPP 275
Cdd:PRK11498  408 dgndmwDATF---------------FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATE 472
                         250
                  ....*....|....*...
gi 1425876613 276 DMNALRAQQFRWAKGGAE 293
Cdd:PRK11498  473 SLSAHIGQRIRWARGMVQ 490
 
Name Accession Description Interval E-value
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
60-291 4.07e-126

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: 367.41  E-value: 4.07e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  60 VVTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDDSTDATTERVARRVAHWQAEGVNITHVRRDDRTGYKAGALAN 139
Cdd:cd06437     2 MVTVQLPVFNEKYVVERLIEAACALDYPKDRLEIQVLDDSTDETVRLAREIVEEYAAQGVNIKHVRRADRTGYKAGALAE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDaPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVRELAGCFL 219
Cdd:cd06437    82 GMKVAKGEYVAIFDADFVPPPDFLQKTPPYFAD-PKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSSTGLFF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1425876613 220 NFNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGG 291
Cdd:cd06437   161 NFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKGP 232
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
60-295 2.36e-55

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 185.08  E-value: 2.36e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  60 VVTVQLPLYNE-AEVAHRLIDACVQLDYPRSRLDIQVLDDSTDattERVARRVAHWQAEgVNITHVRRDDRTGYKAGALA 138
Cdd:cd06421     2 TVDVFIPTYNEpLEIVRKTLRAALAIDYPHDKLRVYVLDDGRR---PELRALAAELGVE-YGYRYLTRPDNRHAKAGNLN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 139 NGLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDAPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFaieQRVRELAGCF 218
Cdd:cd06421    78 NALAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELF---YGVIQPGRDR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 219 LN---FNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGGAETA 295
Cdd:cd06421   155 WGaafCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQIL 234
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
61-386 2.21e-50

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: 174.54  E-value: 2.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDD-STDATTERVARrvahWQAEGVNITHVRRDDRTGyKAGALAN 139
Cdd:COG1215    31 VSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVDDgSTDETAEIARE----LAAEYPRVRVIERPENGG-KAAALNA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVpRFFDAPDLGMvqarwghlnrddslltkvqafgldahfaieqrvrelagcfl 219
Cdd:COG1215   106 GLKAARGDIVVFLDADTVLDPDWLRRLV-AAFADPGVGA----------------------------------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 220 nfNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGGAETALKLt 299
Cdd:COG1215   144 --SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGLQLLLKH- 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 300 GRLWRSAQPWRVklegTFHLTAHFAFPFILLAALTHAPLLLLKGIGHGPGEVYFAVMGFGLFGFAGFFLAQLFAQRALHP 379
Cdd:COG1215   221 RPLLRPRRLLLF----LLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAALRGKKV 296

                  ....*..
gi 1425876613 380 DWRRRLR 386
Cdd:COG1215   297 VWKKTPR 303
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
63-247 5.85e-50

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: 169.33  E-value: 5.85e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  63 VQLPLYNEAEVAHRLIDACVQLDYPRsrLDIQVLDD-STDATtervARRVAHWQAEGVNITHVRRDDRTGYKAGALANGL 141
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPK--LEVIVVDDgSTDDT----LEILEELAALYIRRVLVVRDKENGGKAGALNAGL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 142 QRARGDLIAIFDADFVPRPSFLRRLVPRFFDAPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVRELAGCFLNF 221
Cdd:cd06423    75 RHAKGDIVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVL 154
                         170       180
                  ....*....|....*....|....*.
gi 1425876613 222 NGTAGVWRRACIEDAGGWAHDTLTED 247
Cdd:cd06423   155 SGAFGAFRREALREVGGWDEDTLTED 180
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
62-291 3.79e-35

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: 131.37  E-value: 3.79e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  62 TVQLPLYNEA-EVAHRLIDACVQLDYPRsrLDIQVLDDSTdaTTERVARRV-AHWQAEGVNITHVRRDDRTGYKAGALAN 139
Cdd:cd06435     1 SIHVPCYEEPpEMVKETLDSLAALDYPN--FEVIVIDNNT--KDEALWKPVeAHCAQLGERFRFFHVEPLPGAKAGALNY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGD--LIAIFDADFVPRPSFLRRLVPrFFDAPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVR-ELAG 216
Cdd:cd06435    77 ALERTAPDaeIIAVIDADYQVEPDWLKRLVP-IFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRnERNA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1425876613 217 CFlnFNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGG 291
Cdd:cd06435   156 II--QHGTMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGA 228
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
60-296 7.67e-34

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: 128.14  E-value: 7.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  60 VVTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDDSTDATTERVARrvahwQAEGVNITHVRR----DDRTgyKAG 135
Cdd:cd06427     2 VYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAAR-----ALRLPSIFRVVVvppsQPRT--KPK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 136 ALANGLQRARGDLIAIFDADFVPRPSFLRRLVPRF-FDAPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVREL 214
Cdd:cd06427    75 ACNYALAFARGEYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLAR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 215 AGCFLNFNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAA---EAPAELPpdmNALRaQQFRWAKGG 291
Cdd:cd06427   155 LGLPIPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTtleEANNALG---NWIR-QRSRWIKGY 230

                  ....*
gi 1425876613 292 AETAL 296
Cdd:cd06427   231 MQTWL 235
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
61-290 1.45e-24

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: 102.06  E-value: 1.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRldIQVLDDSTDATTERVAR-RVAHWQAEGVNITHVRRDDRTGYKAGALAN 139
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVE--VVVVVNPSDAETLDVAEeIAARFPDVRLRVIRNARLLGPTGKSRGLNH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVPrFFDAPDLGMVQARwGHLNRDDSLLTKVQAFGLDAHFAIEQRVReLAGCFL 219
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQ-YFDSPKVGAVGTP-VFSLNRSTMLSALGALEFALRHLRMMSLR-LALGVL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1425876613 220 NFNGTAGVWRRACIEDAGGW-AHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKG 290
Cdd:pfam13641 159 PLSGAGSAIRREVLKELGLFdPFFLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
61-291 1.75e-19

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: 88.02  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQV-LDDSTDATTErVARRVAHwQAEGVNITHVRRddrtGyKAGALAN 139
Cdd:cd06439    31 VTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVvSDGSTDGTAE-IAREYAD-KGVKLLRFPERR----G-KAAALNR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDaPDLGMVQARWGHLNRDDSlltkvqAFGLDAHFAIEQRVRE---LAG 216
Cdd:cd06439   104 ALALATGEIVVFTDANALLDPDALRLLVRHFAD-PSVGAVSGELVIVDGGGS------GSGEGLYWKYENWLKRaesRLG 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1425876613 217 CFLNFNGTAGVWRRaciEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGG 291
Cdd:cd06439   177 STVGANGAIYAIRR---ELFRPLPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEVAEDGSEEFRRRVRIAAGN 248
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
65-234 4.69e-19

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 84.37  E-value: 4.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  65 LPLYNEAEVAHRLIDACVQLDYPRsrLDIQVLDD-STDATTErVARRvahWQAEGVNITHVRRDDRTGyKAGALANGLQR 143
Cdd:pfam00535   4 IPTYNEEKYLLETLESLLNQTYPN--FEIIVVDDgSTDGTVE-IAEE---YAKKDPRVRVIRLPENRG-KAGARNAGLRA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 144 ARGDLIAIFDADFVPRPSFLRRLVpRFFDAPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVRELAGCFLNFNG 223
Cdd:pfam00535  77 ATGDYIAFLDADDEVPPDWLEKLV-EALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155
                         170
                  ....*....|.
gi 1425876613 224 TAGVWRRACIE 234
Cdd:pfam00535 156 FALYRREALEE 166
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
61-265 9.40e-19

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 84.75  E-value: 9.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRLdIQVLDDSTDATTERVARrvahWQAEGVNITHVRRDDRTGyKAGALANG 140
Cdd:COG0463     4 VSVVIPTYNEEEYLEEALESLLAQTYPDFEI-IVVDDGSTDGTAEILRE----LAAKDPRIRVIRLERNRG-KGAARNAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 141 LQRARGDLIAIFDADFVPRPSFLRRLVpRFFDAPDLGMVQARWghLNRDDSLLTKVQAFGLDAHFAIEQRVRELAGCFLn 220
Cdd:COG0463    78 LAAARGDYIAFLDADDQLDPEKLEELV-AALEEGPADLVYGSR--LIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFR- 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1425876613 221 fngtagVWRRACIEDAGgwAHDTLTEDLDLsYRAQLQGWRLTYVP 265
Cdd:COG0463   154 ------LFRREVLEELG--FDEGFLEDTEL-LRALRHGFRIAEVP 189
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
148-333 1.81e-18

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


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 83.54  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 148 LIAIFDADFVPRPSFLRRLVpRFFDAPDLGMVQARWGHLNRDdSLLTKVQAFGLDAHFAIEQRVRELAGCFLNFNGTAGV 227
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIA-NEMASPEVAIIQGPILPMNVG-NYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGAF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 228 WRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALRAQQFRWAKGGAETA----LKLTGRLW 303
Cdd:pfam13632  79 LRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGCLLILlirlLGYLGTLL 158
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1425876613 304 RSAQPWRVKLEGTF--HLTAHFAFPFILLAAL 333
Cdd:pfam13632 159 WSGLPLALLLLLLFsiSSLALVLLLLALLAGL 190
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
61-293 2.07e-18

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 88.54  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEA-EVAHRLIDACVQLDYPRSRLDIQVLDDstdattervARRVAHWQ-AEGVNITHVRRDDRTGYKAGALA 138
Cdd:PRK11498  262 VDIFVPTYNEDlNVVKNTIYASLGIDWPKDKLNIWILDD---------GGREEFRQfAQEVGVKYIARPTHEHAKAGNIN 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 139 NGLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDAPDLGMVQ---------------ARWGHLNRDDSLLtkvqaFGL-- 201
Cdd:PRK11498  333 NALKYAKGEFVAIFDCDHVPTRSFLQMTMGWFLKDKKLAMMQtphhffspdpfernlGRFRKTPNEGTLF-----YGLvq 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 202 ------DAHFaieqrvrelagcflnFNGTAGVWRRACIEDAGGWAHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPP 275
Cdd:PRK11498  408 dgndmwDATF---------------FCGSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHRRGYTSAYMRIPQAAGLATE 472
                         250
                  ....*....|....*...
gi 1425876613 276 DMNALRAQQFRWAKGGAE 293
Cdd:PRK11498  473 SLSAHIGQRIRWARGMVQ 490
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
66-186 2.58e-18

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: 81.78  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  66 PLYNEAEVAHRLIDACVQLDYPRsrLDIQVLDD-STDATTERVARrvahWQAEGVNITHVRRDDRTGyKAGALANGLQRA 144
Cdd:cd00761     4 PAYNEEPYLERCLESLLAQTYPN--FEVIVVDDgSTDGTLEILEE----YAKKDPRVIRVINEENQG-LAAARNAGLKAA 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1425876613 145 RGDLIAIFDADFVPRPSFLRRLVPRFFDAPDLGMVQARWGHL 186
Cdd:cd00761    77 RGEYILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNLL 118
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
69-290 4.21e-16

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: 77.33  E-value: 4.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  69 NEAEVAHRLIDACVQLDYPRSRLDIQVLDD-STDATTERVARRVAHwqaEGVNITHVRRDDRTG-YKAGALANGLQRARG 146
Cdd:cd04192     7 NEAENLPRLLQSLSALDYPKEKFEVILVDDhSTDGTVQILEFAAAK---PNFQLKILNNSRVSIsGKKNALTTAIKAAKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 147 DLIAIFDADFVPRPSFLRRLVPRFFDAPDlGMV---------QARWGHLNRDDSL----LTKVqAFGLDAHFaieqrvre 213
Cdd:cd04192    84 DWIVTTDADCVVPSNWLLTFVAFIQKEQI-GLVagpviyfkgKSLLAKFQRLDWLsllgLIAG-SFGLGKPF-------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 214 laGCflnfNGTAGVWRRACIEDAGGWA-HDTL-TEDLDLSYRAQLQGWRLT-YVPAAEA-----PAElppDMNALRAQQF 285
Cdd:cd04192   154 --MC----NGANMAYRKEAFFEVGGFEgNDHIaSGDDELLLAKVASKYPKVaYLKNPEAlvttqPVT---SWKELLNQRK 224

                  ....*
gi 1425876613 286 RWAKG 290
Cdd:cd04192   225 RWASK 229
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
65-269 2.95e-15

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: 73.36  E-value: 2.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  65 LPLYNEAEVAHRLIDACVQLDYPRSRLdIQVLDDSTDATTERVARrvaHWQaegvNITHVRRDDRTGYkaGALAN-GLQR 143
Cdd:cd04186     3 IVNYNSLEYLKACLDSLLAQTYPDFEV-IVVDNASTDGSVELLRE---LFP----EVRLIRNGENLGF--GAGNNqGIRE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 144 ARGDLIAIFDADFVPRPSFLRRLVPRFFDAPDLGMVQARwghlnrddslltkvqafgldahfaieqrvreLAGCFLnfng 223
Cdd:cd04186    73 AKGDYVLLLNPDTVVEPGALLELLDAAEQDPDVGIVGPK-------------------------------VSGAFL---- 117
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1425876613 224 tagVWRRACIEDAGGWAHDTLT--EDLDLSYRAQLQGWRLTYVPAAEA 269
Cdd:cd04186   118 ---LVRREVFEEVGGFDEDFFLyyEDVDLCLRARLAGYRVLYVPQAVI 162
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
66-250 2.51e-14

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: 71.09  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  66 PLYNEAEVAHRLIDACVQLDYPRSRLDIQVL-DDSTDATTErVARrvahwqAEGVNItHVRRD-DRTGyKAGALANGLQR 143
Cdd:cd06438     4 PAHNEEAVIGNTVRSLKAQDYPRELYRIFVVaDNCTDDTAQ-VAR------AAGATV-LERHDpERRG-KGYALDFGFRH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 144 ARG-----DLIAIFDADFVPRPSFLRRLVPRFfdAPDLGMVQARWGHLNRDDSLLTKVQAFgldaHFAIEQRVRELAGCF 218
Cdd:cd06438    75 LLNladdpDAVVVFDADNLVDPNALEELNARF--AAGARVVQAYYNSKNPDDSWITRLYAF----AFLVFNRLRPLGRSN 148
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1425876613 219 LN----FNGTAGVWRRACIEDAgGWAHDTLTEDLDL 250
Cdd:cd06438   149 LGlscqLGGTGMCFPWAVLRQA-PWAAHSLTEDLEF 183
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
61-269 6.03e-13

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 67.71  E-value: 6.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRLdIQVLDDSTDATTERVArrvahwQAEGVNITHVRRDDRTGYkAGALANG 140
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPPFEV-IVVDNGSTDGTAELLA------ALAFPRVRVIRNPENLGF-AAARNLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 141 LQRARGDLIAIFDADFVPRPSFLRRLVprffdapdlgmvqarwghlnrddslltkvqafgldahfaieqrvrELAGCFLn 220
Cdd:COG1216    77 LRAAGGDYLLFLDDDTVVEPDWLERLL---------------------------------------------AAACLLI- 110
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1425876613 221 fngtagvwRRACIEDAGGWAHDTLT--EDLDLSYRAQLQGWRLTYVPAAEA 269
Cdd:COG1216   111 --------RREVFEEVGGFDERFFLygEDVDLCLRLRKAGYRIVYVPDAVV 153
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
61-308 2.20e-11

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: 64.18  E-value: 2.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDD-STDATTERVARrvahWQAEGVNITHVRRDDRTgyKAGALAN 139
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVDGgSTDGTREIVQE----YAAKDPRIRLIDNPKRI--QSAGLNI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLVPRF--FDAPDLGMVQarwghLNRDDSLLTKVQA------FGL-DAHFAIEQR 210
Cdd:cd02525    76 GIRNSRGDIIIRVDAHAVYPKDYILELVEALkrTGADNVGGPM-----ETIGESKFQKAIAvaqsspLGSgGSAYRGGAV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 211 VRELA--GCFlnfngtaGVWRRACIEDAGGWAHD-TLTEDLDLSYRAQLQGWRLTYVPAAEA---PAELPPDMnaLRaQQ 284
Cdd:cd02525   151 KIGYVdtVHH-------GAYRREVFEKVGGFDESlVRNEDAELNYRLRKAGYKIWLSPDIRVyyyPRSTLKKL--AR-QY 220
                         250       260
                  ....*....|....*....|....*
gi 1425876613 285 FRWAKGGAETALKLTGRL-WRSAQP 308
Cdd:cd02525   221 FRYGKWRARTLRKHRKSLsLRHLLP 245
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
63-167 2.36e-11

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: 62.59  E-value: 2.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  63 VQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLDD-STDATTERVARrvahWQAEGVNITHVRRDDRTGyKAGALANGL 141
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAVLEEGYDYEIIVVDDgSTDGTAEIARE----LAARVPRVRVIRLSRNFG-KGAAVRAGF 75
                          90       100
                  ....*....|....*....|....*.
gi 1425876613 142 QRARGDLIAIFDADFVPRPSFLRRLV 167
Cdd:cd04179    76 KAARGDIVVTMDADLQHPPEDIPKLL 101
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
131-289 4.94e-11

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: 61.53  E-value: 4.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 131 GYKAGALANGLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDaPDLGMVQARWGHLNRdDSLLTKVQAFGLDAHFAIEQR 210
Cdd:pfam13506  16 NPKVNNLLQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPLAD-PKVGLVTSPPVGSDP-KGLAAALEAAFFNTLAGVLQA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 211 VRELAGCflnFNGTAGVWRRACIEDAGGWA--HDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPD--MNALRAQQFR 286
Cdd:pfam13506  94 ALSGIGF---AVGMSMAFRRADLERIGGFEalADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRRtsFRAFMARQLR 170

                  ...
gi 1425876613 287 WAK 289
Cdd:pfam13506 171 WAR 173
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
65-168 1.01e-07

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: 52.57  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  65 LPLYNEAEVAHRLIDACVQL--DYPRSRLDIQVLDD-STDATTERVArrvAHWQAEGVNITHVRRDDRTGyKAGALANGL 141
Cdd:cd04188     3 IPAYNEEKRLPPTLEEAVEYleERPSFSYEIIVVDDgSKDGTAEVAR---KLARKNPALIRVLTLPKNRG-KGGAVRAGM 78
                          90       100
                  ....*....|....*....|....*..
gi 1425876613 142 QRARGDLIAIFDADFVPRPSFLRRLVP 168
Cdd:cd04188    79 LAARGDYILFADADLATPFEELEKLEE 105
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
65-167 1.97e-07

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: 51.77  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  65 LPLYNEAE----VAHRLIDACVQLDYprsrlDIQVLDD-STDATTERVARrvahWQAEGVNITHVRRDDRTGYkAGALAN 139
Cdd:cd06442     3 IPTYNEREnipeLIERLDAALKGIDY-----EIIVVDDnSPDGTAEIVRE----LAKEYPRVRLIVRPGKRGL-GSAYIE 72
                          90       100
                  ....*....|....*....|....*...
gi 1425876613 140 GLQRARGDLIAIFDADFVPRPSFLRRLV 167
Cdd:cd06442    73 GFKAARGDVIVVMDADLSHPPEYIPELL 100
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
66-196 2.22e-07

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: 50.94  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  66 PLYNEAEVAHRLIDACVQ-LDYPRSRLDIQVLDD-STDATTERVARRVAHWQaegvNITHVRRDDRTGYKAgALANGLQR 143
Cdd:cd04187     4 PVYNEEENLPELYERLKAvLESLGYDYEIIFVDDgSTDRTLEILRELAARDP----RVKVIRLSRNFGQQA-ALLAGLDH 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1425876613 144 ARGDLIAIFDADFVPRPSflrrLVPRFFDAPDLG--MVQARwgHLNRDDSLLTKV 196
Cdd:cd04187    79 ARGDAVITMDADLQDPPE----LIPEMLAKWEEGydVVYGV--RKNRKESWLKRL 127
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
63-247 3.61e-07

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 50.46  E-value: 3.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  63 VQLPLYNEAEVAHRLIdACVQLDYPRSRldIQVLDDSTDATTERVARrvahWQAEGVNITHVRR---DDRTG------YK 133
Cdd:cd06436     1 VLVPCLNEEAVIQRTL-ASLLRNKPNFL--VLVIDDASDDDTAGIVR----LAITDSRVHLLRRhlpNARTGkgdalnAA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 134 AGALANGLQRARGD----LIAIFDADFVPRPSFLRRLVPrFFDAPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQ 209
Cdd:cd06436    74 YDQIRQILIEEGADpervIIAVIDADGRLDPNALEAVAP-YFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQ 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1425876613 210 RVRELAGCfLNFNGTAGVWRRACIEDAGG---WaHDTLTED 247
Cdd:cd06436   153 SLRALTGT-VGLGGNGQFMRLSALDGLIGeepW-SDSLLED 191
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
61-200 1.87e-06

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: 49.20  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNE--AEVAHRL--IDACVQLDYPRSRLDIQVLDDSTDATT----ERVARRVAHWQAEGVNITHVRRDDRTGY 132
Cdd:cd04191     1 TAIVMPVYNEdpARVFAGLraMYESLAKTGLADHFDFFILSDTRDPDIwlaeEAAWLDLCEELGAQGRIYYRRRRENTGR 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 133 KAGALANGLQR--ARGDLIAIFDADFVPRPSFLRRLVPRFFDAPDLGMVQARWGHLNRdDSLLTKVQAFG 200
Cdd:cd04191    81 KAGNIADFCRRwgSRYDYMVVLDADSLMSGDTIVRLVRRMEANPRAGIIQTAPKLIGA-ETLFARLQQFA 149
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
61-181 1.17e-05

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 47.22  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLIDACVQLDYPRSRLDIQVLD-DSTDATTERVAR---RVAHWQAegvnithVRRD--DRTGyKA 134
Cdd:PRK13915   33 VSVVLPALNEEETVGKVVDSIRPLLMEPLVDELIVIDsGSTDATAERAAAagaRVVSREE-------ILPElpPRPG-KG 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1425876613 135 GALANGLQRARGDLIAIFDADFV-PRPSFLRRLVPRFFDAPDLGMVQA 181
Cdd:PRK13915  105 EALWRSLAATTGDIVVFVDADLInFDPMFVPGLLGPLLTDPGVHLVKA 152
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
133-291 4.37e-05

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: 44.94  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 133 KAGALANGLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDaPDLGMVQARWGHLNRDDSLLTKVQAFGLDAHFAIEQRVR 212
Cdd:cd06434    65 KRRALAEGIRHVTTDIVVLLDSDTVWPPNALPEMLKPFED-PKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAM 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 213 ELAGCFLNFNGTAGVWR----RACIEDA-------GGWaHDTLTEDLDLSYRAQLQGWRLTYVPAAEAPAELPPDMNALR 281
Cdd:cd06434   144 SYDGGVPCLSGRTAAYRteilKDFLFLEeftnetfMGR-RLNAGDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYKKFL 222
                         170
                  ....*....|
gi 1425876613 282 AQQFRWAKGG 291
Cdd:cd06434   223 KQQLRWSRSN 232
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
83-289 6.36e-05

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: 44.13  E-value: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  83 QLDYPRsrldIQVL---DDSTDATTErVARRVahwQAE--GVNITHVRRDDRTGY--KAGALANGLQRARGDLIAIFDAD 155
Cdd:cd02520    25 QQDYPK----YEILfcvQDEDDPAIP-VVRKL---IAKypNVDARLLIGGEKVGInpKVNNLIKGYEEARYDILVISDSD 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 156 FVPRPSFLRRLVPRFFDaPDLGMVqarwghlnrddsllTKVQAFGldahfaieqrvrelAGCFlnfngtagvWRRACIED 235
Cdd:cd02520    97 ISVPPDYLRRMVAPLMD-PGVGLV--------------TCLCAFG--------------KSMA---------LRREVLDA 138
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1425876613 236 AGGWA--HDTLTEDLDLSYRAQLQGWR--LTYVPAAEAPAElpPDMNALRAQQFRWAK 289
Cdd:cd02520   139 IGGFEafADYLAEDYFLGKLIWRLGYRvvLSPYVVMQPLGS--TSLASFWRRQLRWSR 194
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
61-195 1.05e-04

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 44.34  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAEVAHRLID----ACVQLDYPrsrLDIQVLDD-STDATTERVarrVAHWQAEGVNITHVRRDDRTGYKAG 135
Cdd:PRK10714    8 VSVVIPVYNEQESLPELIRrttaACESLGKE---YEILLIDDgSSDNSAEML---VEAAQAPDSHIVAILLNRNYGQHSA 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1425876613 136 ALAnGLQRARGDLIAIFDADFVPRPSFLRRLVPRFFDAPD-LGMVQArwghlNRDDSLLTK 195
Cdd:PRK10714   82 IMA-GFSHVTGDLIITLDADLQNPPEEIPRLVAKADEGYDvVGTVRQ-----NRQDSWFRK 136
PLN02189 PLN02189
cellulose synthase
238-338 5.25e-04

cellulose synthase


Pssm-ID: 215121 [Multi-domain]  Cd Length: 1040  Bit Score: 42.69  E-value: 5.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  238 GWAHDTLTEDLDLSYRAQLQGWRLTYV----PA--AEAPAELPPDMNalraQQFRWAKGGAETALKLTGRLWRSAQPWRV 311
Cdd:PLN02189   731 GWIYGSITEDILTGFKMHCRGWRSIYCmpkrAAfkGSAPINLSDRLN----QVLRWALGSVEIFFSRHSPLLYGYKGGNL 806
                           90       100
                   ....*....|....*....|....*..
gi 1425876613  312 KLEGTFHLTAHFAFPFILLAALTHAPL 338
Cdd:PLN02189   807 KWLERFAYVNTTIYPFTSLPLLAYCTL 833
PLN02195 PLN02195
cellulose synthase A
238-343 1.61e-03

cellulose synthase A


Pssm-ID: 215124 [Multi-domain]  Cd Length: 977  Bit Score: 41.11  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 238 GWAHDTLTEDLDLSYRAQLQGWRLTYV----PAAEAPAelPPDMNALRAQQFRWAKGGAETALKLTGRLWRSAQPWRVKL 313
Cdd:PLN02195  666 GWIYGSVTEDILTGFKMHCRGWRSIYCmpvrPAFKGSA--PINLSDRLHQVLRWALGSVEIFLSRHCPLWYGYGGGRLKW 743
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1425876613 314 EGTFHLTAHFAFPFI---LLAALTHAPLLLLKG 343
Cdd:PLN02195  744 LQRLAYINTIVYPFTslpLIAYCTLPAICLLTG 776
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
89-165 1.92e-03

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: 39.48  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  89 SRLDIQVL--DD-STDATTERVARRVAHWQaegVNITHVRRDDrTGYKAGALAN-GLQRARGDLIAIFDADFVPRPSFLR 164
Cdd:cd06420    23 SILPFEVIiaDDgSTEETKELIEEFKSQFP---IPIKHVWQED-EGFRKAKIRNkAIAAAKGDYLIFIDGDCIPHPDFIA 98

                  .
gi 1425876613 165 R 165
Cdd:cd06420    99 D 99
PLN02915 PLN02915
cellulose synthase A [UDP-forming], catalytic subunit
238-343 2.49e-03

cellulose synthase A [UDP-forming], catalytic subunit


Pssm-ID: 215494 [Multi-domain]  Cd Length: 1044  Bit Score: 40.69  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  238 GWAHDTLTEDLDLSYRAQLQGWRLTYV----PAAEAPAelPPDMNALRAQQFRWAKGGAETALKLTGRLWrSAQPWRVKL 313
Cdd:PLN02915   734 GWIYGSVTEDILTGFKMHCRGWKSVYCmpkrPAFKGSA--PINLSDRLHQVLRWALGSVEIFMSRHCPLW-YAYGGKLKW 810
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1425876613  314 EGTFHLTAHFAFPFI---LLAALTHAPLLLLKG 343
Cdd:PLN02915   811 LERLAYINTIVYPFTsipLLAYCTIPAVCLLTG 843
PLN02190 PLN02190
cellulose synthase-like protein
238-293 4.75e-03

cellulose synthase-like protein


Pssm-ID: 215122 [Multi-domain]  Cd Length: 756  Bit Score: 39.85  E-value: 4.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1425876613 238 GWAHDTLTEDLDLSYRAQLQGWRLTYVpAAEAPAEL---PPDMNALRAQQFRWAKGGAE 293
Cdd:PLN02190  452 GWLYDSVAEDLNTSIGIHSRGWTSSYI-SPDPPAFLgsmPPGGPEAMVQQRRWATGLIE 509
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
61-265 8.86e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 38.14  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613  61 VTVQLPLYNEAE-------VAHRLIDACvqldyprSRLDIQVLDDSTDATTERVARRVAhwQAEGVNitHVRRDDRTGyK 133
Cdd:PLN02726   11 YSIIVPTYNERLnialivyLIFKALQDV-------KDFEIIVVDDGSPDGTQDVVKQLQ--KVYGED--RILLRPRPG-K 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1425876613 134 AG---ALANGLQRARGDLIAIFDADFVPRPSFLRRLVpRFFDAPDLGMVQ----------ARWgHLNRDdslLTKVQAFG 200
Cdd:PLN02726   79 LGlgtAYIHGLKHASGDFVVIMDADLSHHPKYLPSFI-KKQRETGADIVTgtryvkgggvHGW-DLRRK---LTSRGANV 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1425876613 201 LdAHFAIEQRVRELAGCFLnfngtagVWRRACIED------AGGWAHdtlteDLDLSYRAQLQGWRLTYVP 265
Cdd:PLN02726  154 L-AQTLLWPGVSDLTGSFR-------LYKRSALEDlvssvvSKGYVF-----QMEIIVRASRKGYRIEEVP 211
 
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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