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Conserved domains on  [gi|983479824|ref|WP_060635363|]
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glycosyltransferase family 2 protein [Pyrinomonas methylaliphatogenes]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10157685)

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

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|9445404|10521532|12200473|10508766
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 39-238 6.75e-104

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: 303.31  E-value: 6.75e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  39 SIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAYWVSEPDQGQSNAINKGWRRATGEICA 118
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 119 WLNSDDVYLPGALKNVARSFIEYPEKELLYGDLLYIDQKSTISGYLRAPDFSLERLVYENYIPQPTTFLKRAALERVGYL 198
Cdd:cd06433   81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPICHQATFFRRSLFEKYGGF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 983479824 199 NEDLHFCMDYDLWLR-IAANRRSFYLPRTLAAFRFHPQSKT 238
Cdd:cd06433  161 DESYRIAADYDLLLRlLLAGKIFKYLPEVLAAFRLGGVSST 201
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 39-238 6.75e-104

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: 303.31  E-value: 6.75e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  39 SIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAYWVSEPDQGQSNAINKGWRRATGEICA 118
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 119 WLNSDDVYLPGALKNVARSFIEYPEKELLYGDLLYIDQKSTISGYLRAPDFSLERLVYENYIPQPTTFLKRAALERVGYL 198
Cdd:cd06433   81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPICHQATFFRRSLFEKYGGF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 983479824 199 NEDLHFCMDYDLWLR-IAANRRSFYLPRTLAAFRFHPQSKT 238
Cdd:cd06433  161 DESYRIAADYDLLLRlLLAGKIFKYLPEVLAAFRLGGVSST 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 36-245 1.08e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.46  E-value: 1.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEK---WLAYWVSEPDQGQSNAINKGWRRA 112
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAkdpRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 113 TGEICAWLNSDDVYLPGALKNVARSFIEYPEkELLYGDlLYIDQKSTISGYLRAPDFSLERLVYEnyIPQPTT---FLKR 189
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPA-DLVYGS-RLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSgfrLFRR 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983479824 190 AALERVGYlneDLHFCMDYDLWLRIAANRRSFYLPRTlaaFRFHPQSKTTTQFVRM 245
Cdd:COG0463  158 EVLEELGF---DEGFLEDTELLRALRHGFRIAEVPVR---YRAGESKLNLRDLLRL 207
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 39-159 8.28e-29

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: 109.41  E-value: 8.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824   39 SIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKW---LAYWVSEPDQGQSNAINKGWRRATGE 115
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKdprVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 983479824  116 ICAWLNSDDVYLPGALKNVARsFIEYPEKELLYGDLLYIDQKST 159
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVE-ALEEDGADVVVGSRYVIFGETG 123
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 36-129 4.93e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 77.78  E-value: 4.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAYW--VSEPDQGQSNAINKGWRRAT 113
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVrlLHQANAGVSVARNTGLAVAT 85

                         90
                 ....*....|....*.
gi 983479824 114 GEICAWLNSDDVYLPG 129
Cdd:PRK10073  86 GKYVAFPDADDVVYPT 101
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 38-227 8.24e-11

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 60.99  E-value: 8.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824   38 ISIVTPSYNQAPFLEETIRSvLLQGYPNLEYIIIDGGSTDGSVEIIRkyeKWLAYWVSEPdQGQSNAINKGWRRATGEIC 117
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRGDAEVIVVDGGSTDGTVEIAR---SLGAKVIHSP-KGRARQMNAGAALAKGDIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  118 AWLNSDDVyLPGALKNVARSFIEYPEKELLYGDlLYIDQKSTIsgyLRapdfSLERLVYEN-YIPQPTT-----FLKRAA 191
Cdd:TIGR04283  76 LFLHADTR-LPKDFLEAIRRALAKPGYVAGAFD-LRFDGPGLL---LR----LIEWGVNLRsRLTGIPYgdqglFVRRSL 146

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 983479824  192 LERV-GYlnEDLHFCMDYDLWLRIAANRRSFYLPRTL 227
Cdd:TIGR04283 147 FEQIgGF--PDIPLMEDIELSRRLRRLGRLAILPAPV 181
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 39-238 6.75e-104

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: 303.31  E-value: 6.75e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  39 SIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAYWVSEPDQGQSNAINKGWRRATGEICA 118
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 119 WLNSDDVYLPGALKNVARSFIEYPEKELLYGDLLYIDQKSTISGYLRAPDFSLERLVYENYIPQPTTFLKRAALERVGYL 198
Cdd:cd06433   81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPICHQATFFRRSLFEKYGGF 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 983479824 199 NEDLHFCMDYDLWLR-IAANRRSFYLPRTLAAFRFHPQSKT 238
Cdd:cd06433  161 DESYRIAADYDLLLRlLLAGKIFKYLPEVLAAFRLGGVSST 201
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 36-245 1.08e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 144.46  E-value: 1.08e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEK---WLAYWVSEPDQGQSNAINKGWRRA 112
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAkdpRIRVIRLERNRGKGAARNAGLAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 113 TGEICAWLNSDDVYLPGALKNVARSFIEYPEkELLYGDlLYIDQKSTISGYLRAPDFSLERLVYEnyIPQPTT---FLKR 189
Cdd:COG0463   82 RGDYIAFLDADDQLDPEKLEELVAALEEGPA-DLVYGS-RLIREGESDLRRLGSRLFNLVRLLTN--LPDSTSgfrLFRR 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 983479824 190 AALERVGYlneDLHFCMDYDLWLRIAANRRSFYLPRTlaaFRFHPQSKTTTQFVRM 245
Cdd:COG0463  158 EVLEELGF---DEGFLEDTELLRALRHGFRIAEVPVR---YRAGESKLNLRDLLRL 207
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 40-223 5.50e-35

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: 125.31  E-value: 5.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLA---YWVSEPDQGQSNAINKGWRRATGEI 116
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKDPrviRVINEENQGLAAARNAGLKAARGEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 117 CAWLNSDDVYLPGALKNVARSFIEYPEKELLYGDLLYidqkstisgylrapdfslerlvyenyipqpttFLKRAALERVG 196
Cdd:cd00761   81 ILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL--------------------------------LFRRELLEEIG 128

                        170       180
                 ....*....|....*....|....*...
gi 983479824 197 YLNEDL-HFCMDYDLWLRIAANRRSFYL 223
Cdd:cd00761  129 GFDEALlSGEEDDDFLLRLLRGGKVAFR 156
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 36-227 5.68e-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: 118.84  E-value: 5.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAP-FLEETIRSVLLQGYPNLEYIIIDGGSTDGSV-EIIRKY---EKWLAYWVSEPDQGQSNAINKGWR 110
Cdd:cd04184    1 PLISIVMPVYNTPEkYLREAIESVRAQTYPNWELCIADDASTDPEVkRVLKKYaaqDPRIKVVFREENGGISAATNSALE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 111 RATGEICAWLNSDDVYLPGALKNVARSFIEYPEKELLYGDLLYIDQKSTISGYLRAPDFSLERLVYENYIPQPTTFlKRA 190
Cdd:cd04184   81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFKPDWSPDLLLSQNYIGHLLVY-RRS 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 983479824 191 ALERVGYLNEDLHFCMDYDLWLRIAAN-RRSFYLPRTL 227
Cdd:cd04184  160 LVRQVGGFREGFEGAQDYDLVLRVSEHtDRIAHIPRVL 197
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
36-244 1.95e-29

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 112.01  E-value: 1.95e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAYWV-SEPDQGQSNAINKGWRRATG 114
Cdd:COG1216    3 PKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIrNPENLGFAAARNLGLRAAGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 115 EICAWLNSDDVYLPGALKN-VARSFIeypekellygdllyidqkstisgylrapdfslerlvyenyipqpttFLKRAALE 193
Cdd:COG1216   83 DYLLFLDDDTVVEPDWLERlLAAACL----------------------------------------------LIRREVFE 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 983479824 194 RVGYLNEDL-HFCMDYDLWLRI-AANRRSFYLPRTLAafrFHPQSKTTTQFVR 244
Cdd:COG1216  117 EVGGFDERFfLYGEDVDLCLRLrKAGYRIVYVPDAVV---YHLGGASSGPLLR 166
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 39-159 8.28e-29

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: 109.41  E-value: 8.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824   39 SIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKW---LAYWVSEPDQGQSNAINKGWRRATGE 115
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAKKdprVRVIRLPENRGKAGARNAGLRAATGD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 983479824  116 ICAWLNSDDVYLPGALKNVARsFIEYPEKELLYGDLLYIDQKST 159
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVE-ALEEDGADVVVGSRYVIFGETG 123
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 31-245 4.56e-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: 110.99  E-value: 4.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  31 EDVRWPKISIVTPSYNQAPFLEETIRSVLLQGYP--NLEYIIIDGGSTDGSVEIIRKY---EKWLAYWVSEPDQGQSNAI 105
Cdd:COG1215   24 APADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELaaeYPRVRVIERPENGGKAAAL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 106 NKGWRRATGEICAWLNSDDVYLPGALKNVARSFieypekellygdllyIDQKSTISGylrapdfslerlvyenyipqPTT 185
Cdd:COG1215  104 NAGLKAARGDIVVFLDADTVLDPDWLRRLVAAF---------------ADPGVGASG--------------------ANL 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 983479824 186 FLKRAALERVGYLNEDlHFCMDYDLWLRI-AANRRSFYLPRTLAafrFHPQSKTTTQFVRM 245
Cdd:COG1215  149 AFRREALEEVGGFDED-TLGEDLDLSLRLlRAGYRIVYVPDAVV---YEEAPETLRALFRQ 205
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 39-233 4.85e-23

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: 95.00  E-value: 4.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  39 SIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKY-EKWLAYWVSepdqgQSNAINKGWRR------ 111
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYiDKDPFIIIL-----IRNGKNLGVARnfesll 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 112 --ATGEICAWLNSDDVYLPGALKNVARSFIEYPEKELLYGDLLYIDQKSTISGYL------RAPDFSLERLVYENYIPQP 183
Cdd:cd04196   76 qaADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPIGESffeyqkIKPGTSFNNLLFQNVVTGC 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 983479824 184 TTFLKRAALERVgyLNEDLHFCMDYDLWLRIAANRRS--FYLPRTLAAFRFH 233
Cdd:cd04196  156 TMAFNRELLELA--LPFPDADVIMHDWWLALLASAFGkvVFLDEPLILYRQH 205
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 37-230 1.10e-21

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: 92.29  E-value: 1.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  37 KISIVTPSYNQAPFLEETIRSVLLQGYP--NLEYIIIDGGSTDGSVEIIRKY-EKWLAY-WVSEPDQGQSNAINKGWRRA 112
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYaAKDPRIrLIDNPKRIQSAGLNIGIRNS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 113 TGEICAWLNSDDVYLPGALKNVARSFIEyPEKELLYGDLLYIDQKSTISGYLRAPDF------SLERLVYENYIPQPTTF 186
Cdd:cd02525   81 RGDIIIRVDAHAVYPKDYILELVEALKR-TGADNVGGPMETIGESKFQKAIAVAQSSplgsggSAYRGGAVKIGYVDTVH 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 983479824 187 L---KRAALERVGYLNEDLHFCMDYDLWLRI---------AANRRSFYLPR-TLAAF 230
Cdd:cd02525  160 HgayRREVFEKVGGFDESLVRNEDAELNYRLrkagykiwlSPDIRVYYYPRsTLKKL 216
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 25-138 1.00e-18

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: 84.17  E-value: 1.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  25 GRIPSNEDVR-WPKISIVTPSYNQAPFLEETIRSVLLQGYPN--LEYIIIDGGSTDGSVEIIRKY-EKWLAYWVSEPDQG 100
Cdd:cd06439   17 PKPPSLPDPAyLPTVTIIIPAYNEEAVIEAKLENLLALDYPRdrLEIIVVSDGSTDGTAEIAREYaDKGVKLLRFPERRG 96

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 983479824 101 QSNAINKGWRRATGEICAWLNSDDVYLPGALKNVARSF 138
Cdd:cd06439   97 KAAALNRALALATGEIVVFTDANALLDPDALRLLVRHF 134
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 40-224 7.33e-18

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: 79.53  E-value: 7.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAYWVSEPDQGQSNAINKGWRRATGEICAW 119
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 120 LNSDDVYLPGALKNVARSFIEYPEkellYGdllyidqkstISGYlRAPDFSLerlvyenyipqpttFLKRAALERVGYLN 199
Cdd:cd04186   81 LNPDTVVEPGALLELLDAAEQDPD----VG----------IVGP-KVSGAFL--------------LVRREVFEEVGGFD 131

                        170       180
                 ....*....|....*....|....*..
gi 983479824 200 EDLHFCM-DYDLWLRI-AANRRSFYLP 224
Cdd:cd04186  132 EDFFLYYeDVDLCLRArLAGYRVLYVP 158
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 40-201 1.36e-17

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: 79.19  E-value: 1.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIR----KYEKWLAYWVSEPDQGQSNAINKGWRRATGE 115
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEelaaLYIRRVLVVRDKENGGKAGALNAGLRHAKGD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 116 ICAWLNSDDVYLPGALKNVARSFIEYPEKELLYGDLLYIDQKSTISG------YLRAPDFSLERLVYENYIPQ---PTTF 186
Cdd:cd06423   81 IVVVLDADTILEPDALKRLVVPFFADPKVGAVQGRVRVRNGSENLLTrlqaieYLSIFRLGRRAQSALGGVLVlsgAFGA 160

                        170
                 ....*....|....*
gi 983479824 187 LKRAALERVGYLNED 201
Cdd:cd06423  161 FRREALREVGGWDED 175
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 36-129 4.93e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 77.78  E-value: 4.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAYW--VSEPDQGQSNAINKGWRRAT 113
Cdd:PRK10073   6 PKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVrlLHQANAGVSVARNTGLAVAT 85

                         90
                 ....*....|....*.
gi 983479824 114 GEICAWLNSDDVYLPG 129
Cdd:PRK10073  86 GKYVAFPDADDVVYPT 101
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 38-205 4.62e-14

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: 70.29  E-value: 4.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  38 ISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEkwlAYWVSEPdQGQSNAINKGWRRATGEIC 117
Cdd:cd02522    1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAG---VVVISSP-KGRARQMNAGAAAARGDWL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 118 AWLNSDDVYLPGALKNVARSFIEYPEKelLYGDLLYIDQKSTI-SGYLRAPD--FSLERLVYENyipQpTTFLKRAALER 194
Cdd:cd02522   77 LFLHADTRLPPDWDAAIIETLRADGAV--AGAFRLRFDDPGPRlRLLELGANlrSRLFGLPYGD---Q-GLFIRRELFEE 150

                        170
                 ....*....|....*.
gi 983479824 195 VG-----YLNEDLHFC 205
Cdd:cd02522  151 LGgfpelPLMEDVELV 166
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 45-231 7.81e-14

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: 69.27  E-value: 7.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  45 YNQAP-FLEETIRSVLLQGYPNLEYIII-DGGSTDGSVEIIRKYEKWLAYWV--SEPDQGQSNAINKGWRRATGEICAWL 120
Cdd:cd04195    8 IKEKPeFLREALESILKQTLPPDEVVLVkDGPVTQSLNEVLEEFKRKLPLKVvpLEKNRGLGKALNEGLKHCTYDWVARM 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 121 NSDDVYLPGALKNVARSFIEYPEKELLYGDLLYIDQKSTISGYLRAPDFSLERLVY---ENYIPQPTTFLKRAALERVG- 196
Cdd:cd04195   88 DTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRRLPTSHDDILKFarrRSPFNHPTVMFRKSKVLAVGg 167

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 983479824 197 YlnEDLHFCMDYDLWLRIAANRRSFY-LPRTLAAFR 231
Cdd:cd04195  168 Y--QDLPLVEDYALWARMLANGARFAnLPEILVKAR 201
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 40-123 2.86e-13

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: 67.21  E-value: 2.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSVL--LQGYPNLEYIIIDGGSTDGSVEIIRKYEK---WLAYWVSEPDQGQSNAINKGWRRATG 114
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLavLEEGYDYEIIVVDDGSTDGTAEIARELAArvpRVRVIRLSRNFGKGAAVRAGFKAARG 80


                 ....*....
gi 983479824 115 EICAWLNSD 123
Cdd:cd04179   81 DIVVTMDAD 89
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 40-224 2.87e-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: 61.88  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTpsYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIR--KYEKWLAYWVSEPDQGQSNAINKGWRRATGEIC 117
Cdd:cd04185    3 VVT--YNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTslGDLDNIVYLRLPENLGGAGGFYEGVRRAYELGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 118 --AWLNSDDVY-LPGALknvarsfieypEKELLYGDLlyiDQKSTISGYLRAPDFSLErlvyenyipqpTTFLKRAALER 194
Cdd:cd04185   81 dwIWLMDDDAIpDPDAL-----------EKLLAYADK---DNPQFLAPLVLDPDGSFV-----------GVLISRRVVEK 135

                        170       180       190
                 ....*....|....*....|....*....|..
gi 983479824 195 VGYLNEDL--HFCmDYDLWLRIAANRRSFYLP 224
Cdd:cd04185  136 IGLPDKEFfiWGD-DTEYTLRASKAGPGIYVP 166
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 38-227 8.24e-11

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 60.99  E-value: 8.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824   38 ISIVTPSYNQAPFLEETIRSvLLQGYPNLEYIIIDGGSTDGSVEIIRkyeKWLAYWVSEPdQGQSNAINKGWRRATGEIC 117
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLAD-LQALRGDAEVIVVDGGSTDGTVEIAR---SLGAKVIHSP-KGRARQMNAGAALAKGDIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  118 AWLNSDDVyLPGALKNVARSFIEYPEKELLYGDlLYIDQKSTIsgyLRapdfSLERLVYEN-YIPQPTT-----FLKRAA 191
Cdd:TIGR04283  76 LFLHADTR-LPKDFLEAIRRALAKPGYVAGAFD-LRFDGPGLL---LR----LIEWGVNLRsRLTGIPYgdqglFVRRSL 146

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 983479824  192 LERV-GYlnEDLHFCMDYDLWLRIAANRRSFYLPRTL 227
Cdd:TIGR04283 147 FEQIgGF--PDIPLMEDIELSRRLRRLGRLAILPAPV 181
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 39-233 6.86e-10

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: 59.21  E-value: 6.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824   39 SIVTPSYN--QAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIR--KYEKWLAYWVSEPDQ--GQSNAINKGWRRA 112
Cdd:pfam10111   1 SVVIPVYNgeKTHWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSsiKDHNLQVYYPNAPDTtySLAASRNRGTSHA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  113 TGEICAWLNSDDVYLPGALKNVAR-----SFIEYPEKELLYGDLLYIDQKSTI---SGYLRAPDFSLERLV------YEN 178
Cdd:pfam10111  81 IGEYISFIDGDCLWSPDKFEKQLKiatslALQENIQAAVVLPVTDLNDESSNFlrrGGDLTASGDVLRDLLvfysplAIF 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 983479824  179 YIPQPTTFL-KRAALERVGYLNEDL--HFCMDYDLWLRIAANRRSFYLPRTLAAFRFH 233
Cdd:pfam10111 161 FAPNSSNALiNRQAFIEVGGFDESFrgHGAEDFDIFLRLAARYPFVAVMPPQLLYRLS 218
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 40-238 3.86e-09

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: 55.93  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSVLLQGYPN-LEYIIIDGGSTDGSVEIIRKYEKWLAYWVSEPDQGQSN---------AINKGW 109
Cdd:cd06913    1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRKKLEDSGVIVLVGSHNspspkgvgyAKNQAI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 110 RRATGEICAWLNSDDVYLPGALKNVARSFIEYPekellygdllyidqkSTISG--YLRAPDFSLERL------------- 174
Cdd:cd06913   81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHP---------------NSIIGcqVRRIPEDSTERYtrwintltreqll 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 983479824 175 --VYENYIP---QPTTFLKRAALERVGYLN-------EDLHFCMDYdlwLRIAAnrRSFYLPRTLAAFRFHPQSKT 238
Cdd:cd06913  146 tqVYTSHGPtviMPTWFCSREWFSHVGPFDeggkgvpEDLLFFYEH---LRKGG--GVYRVDRCLLLYRYHPGATT 216
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 40-123 8.08e-08

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: 51.71  E-value: 8.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEET---IRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKyekwLAywvsEPDQ-----------GQSNAI 105
Cdd:cd04187    1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRE----LA----ARDPrvkvirlsrnfGQQAAL 72

                         90
                 ....*....|....*...
gi 983479824 106 NKGWRRATGEICAWLNSD 123
Cdd:cd04187   73 LAGLDHARGDAVITMDAD 90
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 36-242 1.45e-07

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: 51.60  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824   36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSV----EIIRKYEKWLAYWVSEPDQGQSN----AINK 107
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLdvaeEIAARFPDVRLRVIRNARLLGPTgksrGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  108 GWRRATGEICAWLNSDDVYLPGALKNVARSFiEYPEKELLYGDlLYIDQKSTISGYLRAPDFS---LERLVYENYIPQPT 184
Cdd:pfam13641  82 GFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTP-VFSLNRSTMLSALGALEFAlrhLRMMSLRLALGVLP 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 983479824  185 -----TFLKRAALERVGYLNEDLHFCMDYDLWLRIAANRRSFYlprtlaafrFHPQSKTTTQF 242
Cdd:pfam13641 160 lsgagSAIRREVLKELGLFDPFFLLGDDKSLGRRLRRHGWRVA---------YAPDAAVRTVF 213
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 40-115 6.34e-07

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: 49.11  E-value: 6.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYEKWLAY-----WvsEPDQG-QSNAI-NKGWRRA 112
Cdd:cd06420    1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPIpikhvW--QEDEGfRKAKIrNKAIAAA 78


                 ...
gi 983479824 113 TGE 115
Cdd:cd06420   79 KGD 81
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
36-214 1.74e-06

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 48.84  E-value: 1.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTdgSVEIIRKYEKWL-----AYWVSEPDQGQSNAINKGWR 110
Cdd:PRK10018   5 PLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCST--SWEQLQQYVTALndpriTYIHNDINSGACAVRNQAIM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 111 RATGEICAWLNSDDVYLPGAL--------KNVARSFIeYPEKELLYGDLLyiDQKSTISGYLRAPdFSLERLVYENYI-P 181
Cdd:PRK10018  83 LAQGEYITGIDDDDEWTPNRLsvflahkqQLVTHAFL-YANDYVCQGEVY--SQPASLPLYPKSP-YSRRLFYKRNIIgN 158

                        170       180       190
                 ....*....|....*....|....*....|...
gi 983479824 182 QPTTFLKRAaleRVGYLNEDLHFCMDYDLWLRI 214
Cdd:PRK10018 159 QVFTWAWRF---KECLFDTELKAAQDYDIFLRM 188
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 37-86 8.47e-06

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: 46.13  E-value: 8.47e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 983479824  37 KISIVTPSYNQAPFLEETIRSVLLQGYpnlEYIIIDGGSTDGSVEIIRKY 86
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVD---EIIVVDSGSTDRTVEIAKEY 47
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 40-132 4.83e-05

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 44.20  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSVLLQGYP--NLEYIIIDGGSTDGSVEII--RKYEKWLAYWVSEPDQ----GQSNAINKGWRR 111
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPkeKFEVILVDDHSTDGTVQILefAAAKPNFQLKILNNSRvsisGKKNALTTAIKA 80

                         90       100
                 ....*....|....*....|.
gi 983479824 112 ATGEICAWLNSDDVYLPGALK 132
Cdd:cd04192   81 AKGDWIVTTDADCVVPSNWLL 101
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 40-123 1.67e-04

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 42.52  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  40 IVTPSYNQAPFLEETIRSV--LLQGyPNLEYIIIDGGSTDGSVEIIRKYEKWLAYWVSEP---DQGQSNAINKGWRRATG 114
Cdd:cd06442    1 IIIPTYNERENIPELIERLdaALKG-IDYEIIVVDDNSPDGTAEIVRELAKEYPRVRLIVrpgKRGLGSAYIEGFKAARG 79


                 ....*....
gi 983479824 115 EICAWLNSD 123
Cdd:cd06442   80 DVIVVMDAD 88
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 39-226 2.18e-04

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: 42.00  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  39 SIVTPSYNQAP-FLEETIRSVLLQGYPNLEYIIIDGGSTDGSV-EIIRKY-----EKWLAYWVSEPDQGQSNAINKGWRR 111
Cdd:cd06435    1 SIHVPCYEEPPeMVKETLDSLAALDYPNFEVIVIDNNTKDEALwKPVEAHcaqlgERFRFFHVEPLPGAKAGALNYALER 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824 112 ATG--EICAWLNSDDVYLPGALKNVARSFiEYPEKELLYGDLLYIDQKST----ISGYLRAPDFSLERLVY--ENYIPQP 183
Cdd:cd06435   81 TAPdaEIIAVIDADYQVEPDWLKRLVPIF-DDPRVGFVQAPQDYRDGEESlfkrMCYAEYKGFFDIGMVSRneRNAIIQH 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 983479824 184 TT--FLKRAALERVGYLNEDLhFCMDYDLWLRI-AANRRSFYLPRT 226
Cdd:cd06435  160 GTmcLIRRSALDDVGGWDEWC-ITEDSELGLRMhEAGYIGVYVAQS 204
PRK10714 PRK10714
undecaprenyl phosphate 4-deoxy-4-formamido-L-arabinose transferase; Provisional
 37-123 1.66e-03

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


Pssm-ID: 182669 [Multi-domain]  Cd Length: 325  Bit Score: 39.72  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  37 KISIVTPSYNQAPFLEETIRSV------LLQGYpnlEYIIIDGGSTDGSVEIirkyekwLAYWVSEPDQ----------- 99
Cdd:PRK10714   7 KVSVVIPVYNEQESLPELIRRTtaacesLGKEY---EILLIDDGSSDNSAEM-------LVEAAQAPDShivaillnrny 76

                         90       100
                 ....*....|....*....|....
gi 983479824 100 GQSNAINKGWRRATGEICAWLNSD 123
Cdd:PRK10714  77 GQHSAIMAGFSHVTGDLIITLDAD 100
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
 36-138 3.53e-03

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: 37.96  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  36 PKISIVTPSYNQAPFLEETIRSVLLQGYPNLEYIIIDGGSTDGSVEIIR----KYEKWLAYW-VSEPDQGQS---NAINK 107
Cdd:cd02520    1 PGVSILKPLCGVDPNLYENLESFFQQDYPKYEILFCVQDEDDPAIPVVRkliaKYPNVDARLlIGGEKVGINpkvNNLIK 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 983479824 108 GWRRATGEICAWLNSDDVYLPGALKNVARSF 138
Cdd:cd02520   81 GYEEARYDILVISDSDISVPPDYLRRMVAPL 111
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 38-123 6.52e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 37.82  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983479824  38 ISIVTPSYNQAP----FLEETI----RSVLLQGYPNLEYIIIDGGSTDGSVEIIRKYekWLAYWVSEPD---------QG 100
Cdd:PTZ00260  72 LSIVIPAYNEEDrlpkMLKETIkyleSRSRKDPKFKYEIIIVNDGSKDKTLKVAKDF--WRQNINPNIDirllsllrnKG 149

                         90       100
                 ....*....|....*....|...
gi 983479824 101 QSNAINKGWRRATGEICAWLNSD 123
Cdd:PTZ00260 150 KGGAVRIGMLASRGKYILMVDAD 172
 
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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