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Conserved domains on  [gi|516336125|ref|WP_017726158|]
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glycosyltransferase family 2 protein [Halalkalibacterium ligniniphilum]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 11421525)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757
PubMed:  16037492|18518825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-223 2.77e-50

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


:

Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 163.72  E-value: 2.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAK 84
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  85 GKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTYTNYDIidEHGNATGRIVRPPASMNYNDLLKNTSIGCLTVMLNKDIL 164
Cdd:COG0463   83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI--REGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516336125 165 GEIEMPNiRAGQDTAcWLSILKKGytaYRLDEVLASYRTVRGSISsnkvkaLKRTWRIY 223
Cdd:COG0463  161 EELGFDE-GFLEDTE-LLRALRHG---FRIAEVPVRYRAGESKLN------LRDLLRLL 208
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-223 2.77e-50

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 163.72  E-value: 2.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAK 84
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  85 GKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTYTNYDIidEHGNATGRIVRPPASMNYNDLLKNTSIGCLTVMLNKDIL 164
Cdd:COG0463   83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI--REGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516336125 165 GEIEMPNiRAGQDTAcWLSILKKGytaYRLDEVLASYRTVRGSISsnkvkaLKRTWRIY 223
Cdd:COG0463  161 EELGFDE-GFLEDTE-LLRALRHG---FRIAEVPVRYRAGESKLN------LRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-150 1.43e-44

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: 147.54  E-value: 1.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125    7 SIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAKGK 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516336125   87 YIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTYTNYDIIDEHGNATGRIVRPPASMNYNDLLKNT 150
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRL 144
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-113 3.98e-37

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: 128.01  E-value: 3.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAKGKY 87
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100
                 ....*....|....*....|....*.
gi 516336125  88 IAFLDSDDLWHPEKLKKQVEFMEKNN 113
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADP 106
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-113 2.38e-23

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 96.27  E-value: 2.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   1 MNSK-KISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIkHILLNKNSGAAVARNTA 79
Cdd:PRK10073   2 MNSTpKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHV-RLLHQANAGVSVARNTG 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 516336125  80 LKHAKGKYIAFLDSDDLWHPEKLKKQVEFMEKNN 113
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDD 114
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
11-96 3.47e-11

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 61.73  E-value: 3.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  11 PTYNSSQFIHITIKSIKKQT----LdNWELIIVDDNSIDETYSILKSITQI---DSRIKHILlNKNSGAAVARNTALKHA 83
Cdd:NF038302   8 PTYNGANRLPEVLERLRSQIgtesL-SWEIIVVDNNSTDNTAQVVQEYQKNwpsPYPLRYCF-EPQQGAAFARQRAIQEA 85

                         90
                 ....*....|...
gi 516336125  84 KGKYIAFLDSDDL 96
Cdd:NF038302  86 KGELIGFLDDDNL 98
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 32-99 1.88e-07

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 51.30  E-value: 1.88e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516336125   32 DNWELIIVDDNSIDETYSILKSITQIDSRIkhILLNKNSGAAVARNTALKHAKGKYIAFLDSDDLWHP 99
Cdd:TIGR03965 104 DRLEVIVVDDGSEDPVPTRAARGARLPVRV--IRHPRRQGPAAARNAGARAARTEFVAFTDSDVVPRP 169
 
Name Accession Description Interval E-value
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 5-223 2.77e-50

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 163.72  E-value: 2.77e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAK 84
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRVIRLERNRGKGAARNAGLAAAR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  85 GKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTYTNYDIidEHGNATGRIVRPPASMNYNDLLKNTSIGCLTVMLNKDIL 164
Cdd:COG0463   83 GDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLI--REGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLFRREVL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516336125 165 GEIEMPNiRAGQDTAcWLSILKKGytaYRLDEVLASYRTVRGSISsnkvkaLKRTWRIY 223
Cdd:COG0463  161 EELGFDE-GFLEDTE-LLRALRHG---FRIAEVPVRYRAGESKLN------LRDLLRLL 208
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 7-150 1.43e-44

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: 147.54  E-value: 1.43e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125    7 SIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAKGK 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516336125   87 YIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTYTNYDIIDEHGNATGRIVRPPASMNYNDLLKNT 150
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRL 144
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 8-113 3.98e-37

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: 128.01  E-value: 3.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAKGKY 87
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEY 80

                         90       100
                 ....*....|....*....|....*.
gi 516336125  88 IAFLDSDDLWHPEKLKKQVEFMEKNN 113
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADP 106
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-202 9.90e-36

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: 126.21  E-value: 9.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   7 SIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLN-KNSGaaVARN--TALKHA 83
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIILIRNgKNLG--VARNfeSLLQAA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  84 KGKYIAFLDSDDLWHPEKLKKQVEFMEKN-NYAFTYTNYDIIDEHGNATGriVRPPASMNY-------NDLLKNTSIGCl 155
Cdd:cd04196   79 DGDYVFFCDQDDIWLPDKLERLLKAFLKDdKPLLVYSDLELVDENGNPIG--ESFFEYQKIkpgtsfnNLLFQNVVTGC- 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 516336125 156 TVMLNKDILGEIE--MPNIRAGQDTACWLSILKKGYTAYrLDEVLASYR 202
Cdd:cd04196  156 TMAFNRELLELALpfPDADVIMHDWWLALLASAFGKVVF-LDEPLILYR 203
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 5-167 2.82e-32

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: 116.92  E-value: 2.82e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQ-FIHITIKSIKKQTLDNWELIIVDDNSID-ETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKH 82
Cdd:cd04184    2 LISIVMPVYNTPEkYLREAIESVRAQTYPNWELCIADDASTDpEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  83 AKGKYIAFLDSDDLWHPEKLKKQV-EFMEKNNYAFTYTNYDIIDEHGNATGRIVRPpaSMNYNDLLKNTSIGCLTVmLNK 161
Cdd:cd04184   82 ATGEFVALLDHDDELAPHALYEVVkALNEHPDADLIYSDEDKIDEGGKRSEPFFKP--DWSPDLLLSQNYIGHLLV-YRR 158


                 ....*.
gi 516336125 162 DILGEI 167
Cdd:cd04184  159 SLVRQV 164
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
5-108 1.64e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 109.70  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITqiDSRIKHILLNKNSGAAVARNTALKHAK 84
Cdd:COG1216    4 KVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALA--FPRVRVIRNPENLGFAAARNLGLRAAG 81

                         90       100
                 ....*....|....*....|....
gi 516336125  85 GKYIAFLDSDDLWHPEKLKKQVEF 108
Cdd:COG1216   82 GDYLLFLDDDTVVEPDWLERLLAA 105
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 5-117 1.50e-28

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: 109.83  E-value: 1.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQT--LDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKH 82
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQDypKEKLEVIVVDDGSTDETAEIARELAAEYPRVRVIERPENGGKAAALNAGLKA 109

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 516336125  83 AKGKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAFT 117
Cdd:COG1215  110 ARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGAS 144
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 7-211 1.29e-27

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: 104.93  E-value: 1.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   7 SIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSitqIDSRIKHILLNKNSGAAVARNTALKHAKGK 86
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKK---YEDKITYWISEPDKGIYDAMNKGIALATGD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  87 YIAFLDSDDLWHPEKLKKQVE-FMEKNNYAFTYTNYDIIDEHGNATGRivRPPASMNYNDLLKNTSIGCLTVMLNKDILG 165
Cdd:cd06433   78 IIGFLNSDDTLLPGALLAVVAaFAEHPEVDVVYGDVLLVDENGRVIGR--RRPPPFLDKFLLYGMPICHQATFFRRSLFE 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 516336125 166 EIEM--PNIRAGQDTACWLSILKKGYTAYRLDEVLASYRTvrGSISSN 211
Cdd:cd06433  156 KYGGfdESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRL--GGVSST 201
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 1-113 2.38e-23

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 96.27  E-value: 2.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   1 MNSK-KISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIkHILLNKNSGAAVARNTA 79
Cdd:PRK10073   2 MNSTpKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHV-RLLHQANAGVSVARNTG 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 516336125  80 LKHAKGKYIAFLDSDDLWHPEKLKKQVEFMEKNN 113
Cdd:PRK10073  81 LAVATGKYVAFPDADDVVYPTMYETLMTMALEDD 114
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 8-118 9.08e-22

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: 88.78  E-value: 9.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKK--QTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAKG 85
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRVRVIRLSRNFGKGAAVRAGFKAARG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 516336125  86 KYIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTY 118
Cdd:cd04179   81 DIVVTMDADLQHPPEDIPKLLEKLLEGGADVVI 113
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-112 1.23e-21

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: 88.00  E-value: 1.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKsitQIDSRIKHILLNKNSGAAVARNTALKHAKGKY 87
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLR---ELFPEVRLIRNGENLGFGAGNNQGIREAKGDY 77

                         90       100
                 ....*....|....*....|....*
gi 516336125  88 IAFLDSDDLWHPEKLKKQVEFMEKN 112
Cdd:cd04186   78 VLLLNPDTVVEPGALLELLDAAEQD 102
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 8-129 4.16e-21

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: 86.90  E-value: 4.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNK-NSGAAVARNTALKHAKGK 86
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKeNGGKAGALNAGLRHAKGD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 516336125  87 YIAFLDSDDLWHPEKLKK-QVEFMEKNNYAFTYTNYDIIDEHGN 129
Cdd:cd06423   81 IVVVLDADTILEPDALKRlVVPFFADPKVGAVQGRVRVRNGSEN 124
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
6-141 3.11e-20

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 86.97  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   6 ISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSidETYSILKSITQI--DSRIKHILLNKNSGAAVARNTALKHA 83
Cdd:PRK10018   7 ISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCS--TSWEQLQQYVTAlnDPRITYIHNDINSGACAVRNQAIMLA 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 516336125  84 KGKYIAFLDSDDLWHPEKLKKQVEFMEK-NNYAFTYTNyDIIDEhgnatGRIVRPPASM 141
Cdd:PRK10018  85 QGEYITGIDDDDEWTPNRLSVFLAHKQQlVTHAFLYAN-DYVCQ-----GEVYSQPASL 137
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 7-202 4.87e-19

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: 81.98  E-value: 4.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   7 SIITPTYN--SSQFIHITIKSIKKQTLDNWELIIVDDNSI-DETYSILKSiTQIDSRIKHILLNKNSGAAVARNTALKHA 83
Cdd:cd04195    1 SVLMSVYIkeKPEFLREALESILKQTLPPDEVVLVKDGPVtQSLNEVLEE-FKRKLPLKVVPLEKNRGLGKALNEGLKHC 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  84 KGKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAftytnyDI-------IDEHGNATGRIVRPPASmnyNDLLKNTSIGC-- 154
Cdd:cd04195   80 TYDWVARMDTDDISLPDRFEKQLDFIEKNPEI------DIvgggvleFDSDGNDIGKRRLPTSH---DDILKFARRRSpf 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 516336125 155 --LTVMLNKD-ILGEIEMPNIRAGQDTACWLSILKKGYTAYRLDEVLASYR 202
Cdd:cd04195  151 nhPTVMFRKSkVLAVGGYQDLPLVEDYALWARMLANGARFANLPEILVKAR 201
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 8-111 5.85e-19

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: 81.37  E-value: 5.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKK---QTLDNWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSG--AAVArnTALKH 82
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAvleSLGYDYEIIFVDDGSTDRTLEILRELAARDPRVKVIRLSRNFGqqAALL--AGLDH 78

                         90       100       110
                 ....*....|....*....|....*....|
gi 516336125  83 AKGKYIAFLDSdDLWH-PEKLKKQVEFMEK 111
Cdd:cd04187   79 ARGDAVITMDA-DLQDpPELIPEMLAKWEE 107
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 5-111 7.23e-17

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: 77.27  E-value: 7.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQT--LDNWELIIVDDNSIDETYSILKSITQIDSRIKhILLNKNSGAAVARNTALKH 82
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSypKDLIEIIVVDGGSTDGTREIVQEYAAKDPRIR-LIDNPKRIQSAGLNIGIRN 79

                         90       100
                 ....*....|....*....|....*....
gi 516336125  83 AKGKYIAFLDSDDLWHPEKLKKQVEFMEK 111
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDYILELVEALKR 108
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 8-202 8.91e-15

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: 70.95  E-value: 8.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTLDN-WELIIVDDNSIDETYSILKSITQI--DSRIKHILLNKNS----GAAVARNTAL 80
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKleDSGVIVLVGSHNSpspkGVGYAKNQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  81 KHAKGKYIAFLDSDDLWHPEKLKKQVEfmEKNNYAFTYTNYDIIDEHGNATGRIVRPPASMNYNDLLKN--TSIGCLTVM 158
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYE--AALQHPNSIIGCQVRRIPEDSTERYTRWINTLTREQLLTQvyTSHGPTVIM 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 516336125 159 ----LNKDILGEIEmPNIRAGQ----DTACWLSILKKGYTAYRLDEVLASYR 202
Cdd:cd06913  159 ptwfCSREWFSHVG-PFDEGGKgvpeDLLFFYEHLRKGGGVYRVDRCLLLYR 209
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 8-116 2.98e-14

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: 69.48  E-value: 2.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTLD-NWELIIVDDNSIDETYSILKSITQIDSRIKHILLNKNSGAAVARNTALKHAKGK 86
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAARGD 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 516336125  87 YIAFLDSDDLWHPEKLKKQVEFMEKNNYAF 116
Cdd:cd06442   81 VIVVMDADLSHPPEYIPELLEAQLEGGADL 110
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 8-112 3.05e-14

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: 68.76  E-value: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSI-TQIDSRIKHIlLNKNSG--AAVARNTALKHAK 84
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFkSQFPIPIKHV-WQEDEGfrKAKIRNKAIAAAK 79

                         90       100
                 ....*....|....*....|....*...
gi 516336125  85 GKYIAFLDSDDLWHPEKLKKQVEFMEKN 112
Cdd:cd06420   80 GDYLIFIDGDCIPHPDFIADHIELAEPG 107
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 5-107 7.68e-13

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 65.87  E-value: 7.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKK--QTLDNWELIIVDDNSIDETYSILKSITQI--DSRIKHILLNKNSGAAVARNTAL 80
Cdd:PLN02726  10 KYSIIVPTYNERLNIALIVYLIFKalQDVKDFEIIVVDDGSPDGTQDVVKQLQKVygEDRILLRPRPGKLGLGTAYIHGL 89

                         90       100       110
                 ....*....|....*....|....*....|..
gi 516336125  81 KHAKGKYIAFLDSdDLWH-----PEKLKKQVE 107
Cdd:PLN02726  90 KHASGDFVVIMDA-DLSHhpkylPSFIKKQRE 120
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 7-129 1.40e-12

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 65.76  E-value: 1.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125    7 SIITPTYNSSQ--FIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRI--KHiLLNKNSGAAVARNTALKH 82
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVyyPN-APDTTYSLAASRNRGTSH 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 516336125   83 AKGKYIAFLDSDDLWHPEKLKKQVEF-----MEKN-NYAFTYTNYDIIDEHGN 129
Cdd:pfam10111  80 AIGEYISFIDGDCLWSPDKFEKQLKIatslaLQENiQAAVVLPVTDLNDESSN 132
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 8-116 2.25e-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: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSI----KKQTLDNWELIIVDDNSIDETYSILKSIT-QIDSRIKHILLNKNSGAAVARNTALKH 82
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAveylEERPSFSYEIIVVDDGSKDGTAEVARKLArKNPALIRVLTLPKNRGKGGAVRAGMLA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 516336125  83 AKGKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAF 116
Cdd:cd04188   81 ARGDYILFADADLATPFEELEKLEEALKTSGYDI 114
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
11-96 3.47e-11

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 61.73  E-value: 3.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  11 PTYNSSQFIHITIKSIKKQT----LdNWELIIVDDNSIDETYSILKSITQI---DSRIKHILlNKNSGAAVARNTALKHA 83
Cdd:NF038302   8 PTYNGANRLPEVLERLRSQIgtesL-SWEIIVVDNNSTDNTAQVVQEYQKNwpsPYPLRYCF-EPQQGAAFARQRAIQEA 85

                         90
                 ....*....|...
gi 516336125  84 KGKYIAFLDSDDL 96
Cdd:NF038302  86 KGELIGFLDDDNL 98
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-136 5.94e-11

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: 60.38  E-value: 5.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQTlDnwELIIVDDNSIDETYSILKSITQidsrikHILLNKNSGAAVARNTALKHAK 84
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAV-D--EIIVVDSGSTDRTVEIAKEYGA------KVYQRWWDGFGAQRNFALELAT 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  85 GKYIAFLDSD-----DLWhpEKLKKQVEFMEKNNYAFTYTNY---DIIDEHGNATGRIVR 136
Cdd:cd02511   72 NDWVLSLDADerltpELA--DEILALLATDDYDGYYVPRRNFflgRWIRHGGWYPDRQLR 129
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 8-116 6.74e-11

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: 60.38  E-value: 6.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   8 IITPTYNSSQFIHITIKSIKKQTL--DNWELIIVDDNSIDETYSILKSITQIDS-RIKHILLN--KNSGAAVARNTALKH 82
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAKPNfQLKILNNSrvSISGKKNALTTAIKA 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 516336125  83 AKGKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAF 116
Cdd:cd04192   81 AKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGL 114
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-120 9.16e-11

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: 60.08  E-value: 9.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125    6 ISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDSRIK-HILLNKN----SGAAVARNTAL 80
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFPDVRlRVIRNARllgpTGKSRGLNHGF 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 516336125   81 KHAKGKYIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTYTN 120
Cdd:pfam13641  84 RAVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTP 123
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 12-117 9.39e-11

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: 59.57  E-value: 9.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  12 TYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETYSILKSITQIDsRIKHILLNKNSGAAVARNTALKHA---KGKYI 88
Cdd:cd04185    5 TYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLD-NIVYLRLPENLGGAGGFYEGVRRAyelGYDWI 83

                         90       100
                 ....*....|....*....|....*....
gi 516336125  89 AFLDSDDLWHPEKLKKQVEFMEKNNYAFT 117
Cdd:cd04185   84 WLMDDDAIPDPDALEKLLAYADKDNPQFL 112
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 5-104 2.88e-10

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 58.75  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   5 KISIITPTYNSSQFIHITIKSIKKQT--LDNWELIIVDDNSIDETYSILKSItqIDSRIKHILLNKNSGAAVARNTALKH 82
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKLENLLALDypRDRLEIIVVSDGSTDGTAEIAREY--ADKGVKLLRFPERRGKAAALNRALAL 107

                         90       100
                 ....*....|....*....|..
gi 516336125  83 AKGKYIAFLDSDDLWHPEKLKK 104
Cdd:cd06439  108 ATGEIVVFTDANALLDPDALRL 129
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 6-119 4.39e-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: 57.97  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   6 ISIITPTYNSSQFIHITIKSIKKQTLDNWELIIVDDNSIDETysilksiTQIDSRIKHILLNKNSGAAVARNTALKHAKG 85
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGT-------VAIARSAGVVVISSPKGRARQMNAGAAAARG 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 516336125  86 KYIAFLDSDDLWHPEKLKKQVEFMEKNNY---AFTYT 119
Cdd:cd02522   74 DWLLFLHADTRLPPDWDAAIIETLRADGAvagAFRLR 110
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 4-111 6.26e-10

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 58.21  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   4 KKISIITPTYNSS----QFIHITIKSIKKQTLDnWELIIVDDNSIDETYSILKSITQI-DSRIKHILLNKNSGAAVARNT 78
Cdd:PRK10714   6 KKVSVVIPVYNEQeslpELIRRTTAACESLGKE-YEILLIDDGSSDNSAEMLVEAAQApDSHIVAILLNRNYGQHSAIMA 84

                         90       100       110
                 ....*....|....*....|....*....|...
gi 516336125  79 ALKHAKGKYIAFLDSDDLWHPEKLKKQVEFMEK 111
Cdd:PRK10714  85 GFSHVTGDLIITLDADLQNPPEEIPRLVAKADE 117
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 6-126 5.77e-08

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 52.46  E-value: 5.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   6 ISIITPTYNSSQFIHITIKS--------IKKQTLDNWELIIVDDNSIDETYSILKSITQ------IDSRIKHILLNKNSG 71
Cdd:PTZ00260  72 LSIVIPAYNEEDRLPKMLKEtikylesrSRKDPKFKYEIIIVNDGSKDKTLKVAKDFWRqninpnIDIRLLSLLRNKGKG 151

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 516336125  72 AAVARNTALkhAKGKYIAFLDSD---DLWHPEKLKKQVEFMEKNNYAFTYTNYDIIDE 126
Cdd:PTZ00260 152 GAVRIGMLA--SRGKYILMVDADgatDIDDFDKLEDIMLKIEQNGLGIVFGSRNHLVD 207
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
 32-99 1.88e-07

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 51.30  E-value: 1.88e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 516336125   32 DNWELIIVDDNSIDETYSILKSITQIDSRIkhILLNKNSGAAVARNTALKHAKGKYIAFLDSDDLWHP 99
Cdd:TIGR03965 104 DRLEVIVVDDGSEDPVPTRAARGARLPVRV--IRHPRRQGPAAARNAGARAARTEFVAFTDSDVVPRP 169
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 7-93 1.44e-05

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: 45.27  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   7 SIITPTYNSS-QFIHITIKSIKKQT----LDnwELIIVDDNSIDETYSILKS--ITQIDSRIKHILLNKNSGAAVARNTA 79
Cdd:cd02510    1 SVIIIFHNEAlSTLLRTVHSVINRTppelLK--EIILVDDFSDKPELKLLLEeyYKKYLPKVKVLRLKKREGLIRARIAG 78

                         90
                 ....*....|....
gi 516336125  80 LKHAKGKYIAFLDS 93
Cdd:cd02510   79 ARAATGDVLVFLDS 92
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 7-134 2.88e-05

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: 43.93  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   7 SIITPTYNSSQFIHI-TIKSIKKQTLDNWELIIVDDNSIDETY--SILKSITQIDSRIKHILLNKNSGA-AVARNTALKH 82
Cdd:cd06435    1 SIHVPCYEEPPEMVKeTLDSLAALDYPNFEVIVIDNNTKDEALwkPVEAHCAQLGERFRFFHVEPLPGAkAGALNYALER 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 516336125  83 AKG--KYIAFLDSDDLWHPEKLKKQVEFMEKNNYAFTYTNYDIIDEHGNATGRI 134
Cdd:cd06435   81 TAPdaEIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLFKRM 134
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 6-110 2.16e-04

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 41.47  E-value: 2.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   6 ISIITPTY--NSSQFIHiTIKSIKKQTLDnwELIIVDDNSIDETYSILKSITQiDSRIKhILLNKNSGAAVARNTALKHA 83
Cdd:cd06434    2 VTVIIPVYdeDPDVFRE-CLRSILRQKPL--EIIVVTDGDDEPYLSILSQTVK-YGGIF-VITVPHPGKRRALAEGIRHV 76

                         90       100
                 ....*....|....*....|....*..
gi 516336125  84 KGKYIAFLDSDDLWHPEKLKKQVEFME 110
Cdd:cd06434   77 TTDIVVLLDSDTVWPPNALPEMLKPFE 103
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 7-108 9.09e-04

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


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 39.57  E-value: 9.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125   7 SIITpTYNSSqfIHITIKSIKKQTLDNWELIIVDDNSidETYSILKSITQIDsRIKHILLNKNSGAAVARNTALKHAKGK 86
Cdd:cd02526    1 AVVV-TYNPD--LSKLKELLAALAEQVDKVVVVDNSS--GNDIELRLRLNSE-KIELIHLGENLGIAKALNIGIKAALEN 74

                         90       100
                 ....*....|....*....|....*
gi 516336125  87 ---YIAFLDSDDLWHPEKLKKQVEF 108
Cdd:cd02526   75 gadYVLLFDQDSVPPPDMVEKLLAY 99
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 5-113 2.54e-03

glycosyltransferase domain; This model describes a putative glycotransferase domain, related to the group 2 family glycosyltransferases of pfam00535.


Pssm-ID: 275233  Cd Length: 215  Bit Score: 38.05  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125    5 KISIITPTYNSSQFIHITIKSIKKQTLDnWELIIVDDNSIDETYSILKSI-TQIDSRIKHILLNKNSGAAVARNT-ALKH 82
Cdd:TIGR04440   1 KLTIIIPTYNRPEYLKRWLRYYSDFGCD-YRIIIADSSDEKFNENNLKVFkNYSNPNITYLHYPDLGVPFYEKLLdALEQ 79

                          90       100       110
                  ....*....|....*....|....*....|.
gi 516336125   83 AKGKYIAFLDSDDLWHPEKLKKQVEFMEKNN 113
Cdd:TIGR04440  80 VETPYVVICADDDFIIPSGLTECLSFLEANP 110
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 36-122 7.56e-03

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: 36.52  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516336125  36 LIIVDDNSIDETYSILKS-ITQIDSR---IKHILLNKNSG-AAVARNTALKHAKGKYIAFLDSDDLWHPEKLKKQVEFME 110
Cdd:cd06437   34 EIQVLDDSTDETVRLAREiVEEYAAQgvnIKHVRRADRTGyKAGALAEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFA 113

                         90
                 ....*....|....*..
gi 516336125 111 KNNYAF-----TYTNYD 122
Cdd:cd06437  114 DPKLGFvqtrwGHINAN 130
 
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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