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Conserved domains on  [gi|2205656907|ref|WP_240781836|]
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MULTISPECIES: glycosyltransferase family 2 protein [Saccharolobus]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135509)

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
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-184 3.85e-57

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: 181.60  E-value: 3.85e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG--VRLISLDKNYGPAYARNIVLKTFKSKFIAF 83
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFpeVRLIRNGENLGFGAGNNQGIREAKGDYVLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  84 LDNDVRTPPDWLDPLVETIILDDKIAAVQslytdwpygeqPRLipwfSTASALVRREEILKIGGFDEHYFFYWEDAELSW 163
Cdd:cd04186    81 LNPDTVVEPGALLELLDAAEQDPDVGIVG-----------PKV----SGAFLLVRREVFEEVGGFDEDFFLYYEDVDLCL 145
                         170       180
                  ....*....|....*....|.
gi 2205656907 164 RLYRAGYKILMVPKSKVYHEA 184
Cdd:cd04186   146 RARLAGYRVLYVPQAVIYHHG 166
 
Name Accession Description Interval E-value
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-184 3.85e-57

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: 181.60  E-value: 3.85e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG--VRLISLDKNYGPAYARNIVLKTFKSKFIAF 83
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFpeVRLIRNGENLGFGAGNNQGIREAKGDYVLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  84 LDNDVRTPPDWLDPLVETIILDDKIAAVQslytdwpygeqPRLipwfSTASALVRREEILKIGGFDEHYFFYWEDAELSW 163
Cdd:cd04186    81 LNPDTVVEPGALLELLDAAEQDPDVGIVG-----------PKV----SGAFLLVRREVFEEVGGFDEDFFLYYEDVDLCL 145
                         170       180
                  ....*....|....*....|.
gi 2205656907 164 RLYRAGYKILMVPKSKVYHEA 184
Cdd:cd04186   146 RARLAGYRVLYVPQAVIYHHG 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
6-218 9.23e-57

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 181.73  E-value: 9.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSL---GVRLISLDKNYGPAYARNIVLKTFKSKFIA 82
Cdd:COG1216     7 VVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALafpRVRVIRNPENLGFAAARNLGLRAAGGDYLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  83 FLDNDVRTPPDWLDPLVETiilddkiaavqslytdwpygeqprlipwfstASALVRREEILKIGGFDEHYFFYWEDAELS 162
Cdd:COG1216    87 FLDDDTVVEPDWLERLLAA-------------------------------ACLLIRREVFEEVGGFDERFFLYGEDVDLC 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2205656907 163 WRLYRAGYKILMVPKSKVYHEAHGTFKKLpspFTSYLTLRNQMLLLLTYYHLSQLL 218
Cdd:COG1216   136 LRLRKAGYRIVYVPDAVVYHLGGASSGPL---LRAYYLGRNRLLFLRKHGPRPLLR 188
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
6-155 6.29e-23

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: 92.84  E-value: 6.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSL-----GVRLISLDKNYGPAYARNIVLKTFKSKF 80
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGDY 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVETIILDDKIAAVQSLY---TDWPYGEQPRLIPWFSTASALVRREEILKIGGFDEHYFFY 155
Cdd:pfam00535  82 IAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYvifGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
3-183 4.19e-21

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: 92.90  E-value: 4.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   3 EIPIVVLNYNGLELLKKYLPSILETRYP--YKEVVIVDNGSNDG---SKEYVKSLGVRLISLDKNYGPAYARNIVLKTFK 77
Cdd:TIGR03965  75 SVTVVVPVRNRPAGLARLLAALLALDYPrdRLEVIVVDDGSEDPvptRAARGARLPVRVIRHPRRQGPAAARNAGARAAR 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  78 SKFIAFLDNDVRTPPDWLDPLVETI-----------IL-----DDKIAAVQSLYTDWPYGEQPRLI------PWFSTASA 135
Cdd:TIGR03965 155 TEFVAFTDSDVVPRPGWLRALLAHFddpgvalvaprVValpaaDTRLARYEAVRSSLDLGPEEAVVrprgpvSYVPSAAL 234
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2205656907 136 LVRREEILKIGGFDEHYFFyWEDAELSWRLYRAGYKILMVPKSKVYHE 183
Cdd:TIGR03965 235 LVRRRALLEVGGFDERLEV-GEDVDLCWRLCEAGGRVRYEPAAVVAHD 281
PRK10073 PRK10073
putative glycosyl transferase; Provisional
6-128 4.13e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.43  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGS----KEYVKSLG-VRLISlDKNYGPAYARNIVLKTFKSKF 80
Cdd:PRK10073   10 IIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSveiaKHYAENYPhVRLLH-QANAGVSVARNTGLAVATGKY 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVETIILDD-KIAAVQSLYTDWPYGEQPRLIP 128
Cdd:PRK10073   89 VAFPDADDVVYPTMYETLMTMALEDDlDVAQCNADWCFRDTGETWQSIP 137
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
11-95 6.02e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 44.01  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  11 YNGlellKKYLPSILE-------TRYPYKEVVIVDNGSNDGSKEYVK------SLGVRLI-SLDKNYGPAYARNIVLKTF 76
Cdd:NF038302   10 YNG----ANRLPEVLErlrsqigTESLSWEIIVVDNNSTDNTAQVVQeyqknwPSPYPLRyCFEPQQGAAFARQRAIQEA 85
                          90
                  ....*....|....*....
gi 2205656907  77 KSKFIAFLDNDVRTPPDWL 95
Cdd:NF038302   86 KGELIGFLDDDNLPAPNWV 104
 
Name Accession Description Interval E-value
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-184 3.85e-57

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: 181.60  E-value: 3.85e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG--VRLISLDKNYGPAYARNIVLKTFKSKFIAF 83
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFpeVRLIRNGENLGFGAGNNQGIREAKGDYVLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  84 LDNDVRTPPDWLDPLVETIILDDKIAAVQslytdwpygeqPRLipwfSTASALVRREEILKIGGFDEHYFFYWEDAELSW 163
Cdd:cd04186    81 LNPDTVVEPGALLELLDAAEQDPDVGIVG-----------PKV----SGAFLLVRREVFEEVGGFDEDFFLYYEDVDLCL 145
                         170       180
                  ....*....|....*....|.
gi 2205656907 164 RLYRAGYKILMVPKSKVYHEA 184
Cdd:cd04186   146 RARLAGYRVLYVPQAVIYHHG 166
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
6-218 9.23e-57

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 181.73  E-value: 9.23e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSL---GVRLISLDKNYGPAYARNIVLKTFKSKFIA 82
Cdd:COG1216     7 VVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALafpRVRVIRNPENLGFAAARNLGLRAAGGDYLL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  83 FLDNDVRTPPDWLDPLVETiilddkiaavqslytdwpygeqprlipwfstASALVRREEILKIGGFDEHYFFYWEDAELS 162
Cdd:COG1216    87 FLDDDTVVEPDWLERLLAA-------------------------------ACLLIRREVFEEVGGFDERFFLYGEDVDLC 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2205656907 163 WRLYRAGYKILMVPKSKVYHEAHGTFKKLpspFTSYLTLRNQMLLLLTYYHLSQLL 218
Cdd:COG1216   136 LRLRKAGYRIVYVPDAVVYHLGGASSGPL---LRAYYLGRNRLLFLRKHGPRPLLR 188
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
6-191 8.92e-30

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: 114.45  E-value: 8.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYK--EVVIVDNGSNDGSKEYVKSLG-----VRLISLDKNYGPAYARNIVLKTFKS 78
Cdd:COG1215    33 VIIPAYNEEAVIEETLRSLLAQDYPKEklEVIVVDDGSTDETAEIARELAaeyprVRVIERPENGGKAAALNAGLKAARG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  79 KFIAFLDNDVRTPPDWLDPLVETIiLDDKIAAvqslytdwpygeqprlipwfSTASALVRREEILKIGGFDEHYFFywED 158
Cdd:COG1215   113 DIVVFLDADTVLDPDWLRRLVAAF-ADPGVGA--------------------SGANLAFRREALEEVGGFDEDTLG--ED 169
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2205656907 159 AELSWRLYRAGYKILMVPKSKVYHEAHGTFKKL 191
Cdd:COG1215   170 LDLSLRLLRAGYRIVYVPDAVVYEEAPETLRAL 202
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-172 1.99e-28

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: 106.82  E-value: 1.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG-----VRLISLDKNYGPAYARNIVLKTFKSKF 80
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAkkdprVIRVINEENQGLAAARNAGLKAARGEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVETIILDDKIAAVqslytdwpygeqprlipwFSTASALVRREEILKIGGFDEHYFFYWEDAE 160
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELLADPEADAV------------------GGPGNLLFRRELLEEIGGFDEALLSGEEDDD 142
                         170
                  ....*....|..
gi 2205656907 161 LSWRLYRAGYKI 172
Cdd:cd00761   143 FLLRLLRGGKVA 154
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-191 2.36e-24

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 97.85  E-value: 2.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   1 MEEIPIVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG-----VRLISLDKNYGPAYARNIVLKT 75
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAakdprIRVIRLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  76 FKSKFIAFLDNDVRTPPDWLDPLVETIILDDKIAAVQSLYTDWPYGEQPRL-------------IPWFSTASALVRREEI 142
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYGSRLIREGESDLRRLgsrlfnlvrlltnLPDSTSGFRLFRREVL 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2205656907 143 LKIgGFDEHYFfywEDAELsWRLYRAGYKILMVPkskVYHEAHGTFKKL 191
Cdd:COG0463   161 EEL-GFDEGFL---EDTEL-LRALRHGFRIAEVP---VRYRAGESKLNL 201
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-207 3.73e-24

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: 96.94  E-value: 3.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   7 VVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG----VRLISLDKNYGPAYARNIVLKTF---KSK 79
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGdldnIVYLRLPENLGGAGGFYEGVRRAyelGYD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  80 FIAFLDNDVRTPPDWLDPLVETIILDDkIAAVQSLytdwpygeqpRLIPWFSTASALVRREEILKIGGFDEHYFFYWEDA 159
Cdd:cd04185    82 WIWLMDDDAIPDPDALEKLLAYADKDN-PQFLAPL----------VLDPDGSFVGVLISRRVVEKIGLPDKEFFIWGDDT 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2205656907 160 ELSWRLYRAGYKILmVPKSKVYHE-----AHGTFKKLPSPFTSYLTLRNQMLL 207
Cdd:cd04185   151 EYTLRASKAGPGIY-VPDAVVVHKtainkGSSAVVNIDPPWKLYYGVRNRIYL 202
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
6-155 6.29e-23

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: 92.84  E-value: 6.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSL-----GVRLISLDKNYGPAYARNIVLKTFKSKF 80
Cdd:pfam00535   2 VIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYakkdpRVRVIRLPENRGKAGARNAGLRAATGDY 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVETIILDDKIAAVQSLY---TDWPYGEQPRLIPWFSTASALVRREEILKIGGFDEHYFFY 155
Cdd:pfam00535  82 IAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYvifGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFALY 159
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
3-183 4.19e-21

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: 92.90  E-value: 4.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   3 EIPIVVLNYNGLELLKKYLPSILETRYP--YKEVVIVDNGSNDG---SKEYVKSLGVRLISLDKNYGPAYARNIVLKTFK 77
Cdd:TIGR03965  75 SVTVVVPVRNRPAGLARLLAALLALDYPrdRLEVIVVDDGSEDPvptRAARGARLPVRVIRHPRRQGPAAARNAGARAAR 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  78 SKFIAFLDNDVRTPPDWLDPLVETI-----------IL-----DDKIAAVQSLYTDWPYGEQPRLI------PWFSTASA 135
Cdd:TIGR03965 155 TEFVAFTDSDVVPRPGWLRALLAHFddpgvalvaprVValpaaDTRLARYEAVRSSLDLGPEEAVVrprgpvSYVPSAAL 234
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2205656907 136 LVRREEILKIGGFDEHYFFyWEDAELSWRLYRAGYKILMVPKSKVYHE 183
Cdd:TIGR03965 235 LVRRRALLEVGGFDERLEV-GEDVDLCWRLCEAGGRVRYEPAAVVAHD 281
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
4-191 6.12e-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: 89.60  E-value: 6.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   4 IPIVVLNYNGLELLKKYLPSILETRYPYK--EVVIVDNGSNDGSKEYVKSLG-----VRLISLDKNYGPAyARNIVLKTF 76
Cdd:cd02525     2 VSIIIPVRNEEKYIEELLESLLNQSYPKDliEIIVVDGGSTDGTREIVQEYAakdprIRLIDNPKRIQSA-GLNIGIRNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  77 KSKFIAFLDNDVRTPPDWLDPLVETIILDDKIAAVQSLYTDwPYGEQPRLIPWF-----------------------STA 133
Cdd:cd02525    81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETI-GESKFQKAIAVAqssplgsggsayrggavkigyvdTVH 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656907 134 SALVRREEILKIGGFDEHyFFYWEDAELSWRLYRAGYKILMVPKSKVYHEAHGTFKKL 191
Cdd:cd02525   160 HGAYRREVFEKVGGFDES-LVRNEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKL 216
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
6-208 2.15e-19

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: 85.03  E-value: 2.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLnYNGLelLKKYLPSILETRYPYKEVVIVDNGSN--DGSKEYVKSLGVRLISLDKNYGPAYARNIVLKTFKSK---F 80
Cdd:cd02526     2 VVVT-YNPD--LSKLKELLAALAEQVDKVVVVDNSSGndIELRLRLNSEKIELIHLGENLGIAKALNIGIKAALENgadY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVETIIL---DDKIAAVQSLYTD--------------------WPYGEQPRLIPWFSTASALV 137
Cdd:cd02526    79 VLLFDQDSVPPPDMVEKLLAYKILsdkNSNIGAVGPRIIDrrtgenspgvrksgyklriqKEGEEGLKEVDFLITSGSLI 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2205656907 138 RREEILKIGGFDEHYFFYWEDAELSWRLYRAGYKILMVPKSKVYHE-AHGTFKKLP-------SPFTSYLTLRNQMLLL 208
Cdd:cd02526   159 SLEALEKVGGFDEDLFIDYVDTEWCLRARSKGYKIYVVPDAVLKHElGDKRVKRLGgvsvplhSPLRRYYLFRNAIYLL 237
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
4-209 2.32e-18

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: 81.85  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   4 IPIVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLGVRLISLDK------NYGPAYAR-NIVLktf 76
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVVISSPKgrarqmNAGAAAARgDWLL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  77 kskfiaFLDNDVRTPPDWLDPLVETIILDDKIAAVQSLYTD---------------------WPYGEQprlipwfstaSA 135
Cdd:cd02522    78 ------FLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDdpgprlrllelganlrsrlfgLPYGDQ----------GL 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2205656907 136 LVRREEILKIGGFDEHYFFywEDAELSWRLYRAGykILMVPKSKVY-----HEAHGTFKklpspftsyLTLRNQMLLLL 209
Cdd:cd02522   142 FIRRELFEELGGFPELPLM--EDVELVRRLRRRG--RPALLPSPVTtsarrWERNGWLR---------TTLLNWLLLLL 207
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
11-151 2.18e-12

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: 64.17  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  11 YNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG------VRLISLDKNYGPAYARNIVLKTFKSKFIAFL 84
Cdd:cd06423     6 YNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAalyirrVLVVRDKENGGKAGALNAGLRHAKGDIVVVL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  85 DNDVRTPPDWLDPLVETIILDDKIAAVQSLYtdWPYGEQPRLIPWFST-------------------------ASALVRR 139
Cdd:cd06423    86 DADTILEPDALKRLVVPFFADPKVGAVQGRV--RVRNGSENLLTRLQAieylsifrlgrraqsalggvlvlsgAFGAFRR 163
                         170
                  ....*....|..
gi 2205656907 140 EEILKIGGFDEH 151
Cdd:cd06423   164 EALREVGGWDED 175
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
6-186 5.64e-12

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: 63.72  E-value: 5.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLGVRLISL----DKnyGPAYARNIVLKTFKSKFI 81
Cdd:cd06433     2 IITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWisepDK--GIYDAMNKGIALATGDII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  82 AFLDNDvrtppDWLDPlveTIILDDKIAAVQSLYTDWPYGE-----------QPRLIPWFSTA-----------SALVRR 139
Cdd:cd06433    80 GFLNSD-----DTLLP---GALLAVVAAFAEHPEVDVVYGDvllvdengrviGRRRPPPFLDKfllygmpichqATFFRR 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2205656907 140 EEILKIGGFDEHYFFYwEDAELSWRLYRAGYKILMVPKSKVYHEAHG 186
Cdd:cd06433   152 SLFEKYGGFDESYRIA-ADYDLLLRLLLAGKIFKYLPEVLAAFRLGG 197
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
15-198 1.78e-11

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: 62.80  E-value: 1.78e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  15 ELLKKYLPSILETRYPYKEVVIVDNGSNDGS-----KEYVKSLGVRLISLDKNYGPAY---ARNIVLK--TFKSKFIAFL 84
Cdd:cd06435    12 EMVKETLDSLAALDYPNFEVIVIDNNTKDEAlwkpvEAHCAQLGERFRFFHVEPLPGAkagALNYALErtAPDAEIIAVI 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  85 DNDVRTPPDWLDPLVEtIILDDKIAAVQSL--YTDWPYGEQPRLIPWFST--------------------ASALVRREEI 142
Cdd:cd06435    92 DADYQVEPDWLKRLVP-IFDDPRVGFVQAPqdYRDGEESLFKRMCYAEYKgffdigmvsrnernaiiqhgTMCLIRRSAL 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2205656907 143 LKIGGFDEhyffyW---EDAELSWRLYRAGYKILMVPKSKvyheAHGTfkkLPSPFTSY 198
Cdd:cd06435   171 DDVGGWDE-----WcitEDSELGLRMHEAGYIGVYVAQSY----GHGL---IPDTFEAF 217
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
6-204 1.88e-11

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


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 62.59  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYN-GLELLKKYLPSILETRYPY--KEVVIVDNGSNDGSKEYVKSLGV----RLISLDKNYGpAYARNI--VLKTF 76
Cdd:cd06421     5 VFIPTYNePLEIVRKTLRAALAIDYPHdkLRVYVLDDGRRPELRALAAELGVeygyRYLTRPDNRH-AKAGNLnnALAHT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  77 KSKFIAFLDNDVRTPPDWLDPLVETIILDDKIAAVQS----------LYTDWPYGEQPRLI-------------PWFSTA 133
Cdd:cd06421    84 TGDFVAILDADHVPTPDFLRRTLGYFLDDPKVALVQTpqffynpdpfDWLADGAPNEQELFygviqpgrdrwgaAFCCGS 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205656907 134 SALVRREEILKIGGFDEhyFFYWEDAELSWRLYRAGYKILMVPKSKVYHEAhgtfkklPSPFTSYLTLRNQ 204
Cdd:cd06421   164 GAVVRREALDEIGGFPT--DSVTEDLATSLRLHAKGWRSVYVPEPLAAGLA-------PETLAAYIKQRLR 225
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
25-178 2.11e-11

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: 62.20  E-value: 2.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  25 LETRYPYK-EVVIVDNGSNDGSKEYVKSLG------VRLISLDKNYGPAYARNIVLKTFKSKFIAFLDNDVRTPPDWLDP 97
Cdd:cd04188    23 LEERPSFSyEIIVVDDGSKDGTAEVARKLArknpalIRVLTLPKNRGKGGAVRAGMLAARGDYILFADADLATPFEELEK 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  98 LVETII-------------LDDKIAAVQSLYtdwpygeqpR--------LIPWFSTASA---------LVRREEILKIGG 147
Cdd:cd04188   103 LEEALKtsgydiaigsrahLASAAVVKRSWL---------RnllgrgfnFLVRLLLGLGikdtqcgfkLFTRDAARRLFP 173
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2205656907 148 --FDEHYFFyweDAELSWRLYRAGYKILMVPKS 178
Cdd:cd04188   174 rlHLERWAF---DVELLVLARRLGYPIEEVPVR 203
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
6-205 2.30e-11

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: 63.38  E-value: 2.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYN-GLELLKKYLPSILET--RYPYKEVVIVDNGSND------GSKEYVKSLG-VRLISLDKNYGPAYARNIVLKT 75
Cdd:cd02510     2 VIIIFHNeALSTLLRTVHSVINRtpPELLKEIILVDDFSDKpelkllLEEYYKKYLPkVKVLRLKKREGLIRARIAGARA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  76 FKSKFIAFLDNDVRTPPDWLDPLVETIILDDKIAAVQSLYT-------------------DWP--YGEQPRLIPWFSTAS 134
Cdd:cd02510    82 ATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVidadtfeyrgssgdarggfDWSlhFKWLPLPEEERRRES 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907 135 AL--------------VRREEILKIGGFDEhYFFYW--EDAELSWRLYRAGYKILMVPKSKVYHEAHGTFKKLPSPFTSY 198
Cdd:cd02510   162 PTapirsptmagglfaIDREWFLELGGYDE-GMDIWggENLELSFKVWQCGGSIEIVPCSRVGHIFRRKRKPYTFPGGSG 240

                  ....*..
gi 2205656907 199 LTLRNQM 205
Cdd:cd02510   241 TVLRNYK 247
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
6-191 1.61e-10

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: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVKSLG-------VRLISLDKNYGP---AYARNIVLKT 75
Cdd:pfam13641   6 VVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAarfpdvrLRVIRNARLLGPtgkSRGLNHGFRA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  76 FKSKFIAFLDNDVRTPPDWLDPLVeTIILDDKIAAVQ------------SLYTDWPYGE--QPRLIPW-------FSTAS 134
Cdd:pfam13641  86 VKSDLVVLHDDDSVLHPGTLKKYV-QYFDSPKVGAVGtpvfslnrstmlSALGALEFALrhLRMMSLRlalgvlpLSGAG 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2205656907 135 ALVRREEILKIGGFDEhyFFY-WEDAELSWRLYRAGYKILMVPKSKVYHEAHGTFKKL 191
Cdd:pfam13641 165 SAIRREVLKELGLFDP--FFLlGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAAS 220
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
21-106 1.32e-09

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: 56.43  E-value: 1.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  21 LPSILETRYPYkEVVIVDNGSNDGSKEYVKSLG-----VRLISLDKNYGPAYARNIVLKTFKSKFIAFLDNDVRTPPDWL 95
Cdd:cd04179    19 LLAVLEEGYDY-EIIVVDDGSTDGTAEIARELAarvprVRVIRLSRNFGKGAAVRAGFKAARGDIVVTMDADLQHPPEDI 97
                          90
                  ....*....|.
gi 2205656907  96 DPLVETIILDD 106
Cdd:cd04179    98 PKLLEKLLEGG 108
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
6-171 1.27e-08

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: 53.74  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILE-TRYPYkEVVIVDNGSNDGSKEYVKSLG----VRLISL---DKNYGPAYARNIVLKTFK 77
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNqSILPF-EVIIADDGSTEETKELIEEFKsqfpIPIKHVwqeDEGFRKAKIRNKAIAAAK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  78 SKFIAFLDNDVRTPPDWldplVET-IILDDKIAAVQslytdwpyGEQPRLIPWFSTASAL-----VRREEILKIGGFDEh 151
Cdd:cd06420    80 GDYLIFIDGDCIPHPDF----IADhIELAEPGVFLS--------GSRVLLNEKLTERGIRgcnmsFWKKDLLAVNGFDE- 146
                         170       180
                  ....*....|....*....|..
gi 2205656907 152 YFFYW--EDAELSWRLYRAGYK 171
Cdd:cd06420   147 EFTGWggEDSELVARLLNSGIK 168
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-191 2.00e-08

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: 53.83  E-value: 2.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYK--EVVIVDNGSNDGSKEYVKSL----GVRLISLDKNYGPAYARNIVLKTF--- 76
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYPKEkfEVILVDDHSTDGTVQILEFAaakpNFQLKILNNSRVSISGKKNALTTAika 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  77 -KSKFIAFLDNDVRTPPDWLDPLVETiILDDKIAAVQSLYTdwpyGEQPR-------LIPWFSTASA------------- 135
Cdd:cd04192    81 aKGDWIVTTDADCVVPSNWLLTFVAF-IQKEQIGLVAGPVI----YFKGKsllakfqRLDWLSLLGLiagsfglgkpfmc 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2205656907 136 -----LVRREEILKIGGFDEHYFFYWEDAELSWRLYRAGYKILMVPKSK---VYHEAHGTFKKL 191
Cdd:cd04192   156 nganmAYRKEAFFEVGGFEGNDHIASGDDELLLAKVASKYPKVAYLKNPealVTTQPVTSWKEL 219
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-143 2.54e-07

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: 50.32  E-value: 2.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGSKEYVK------SLGVRLISLDKNYGPAYA-RNIVLKTfKS 78
Cdd:cd04196     2 VLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKeyidkdPFIIILIRNGKNLGVARNfESLLQAA-DG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2205656907  79 KFIAFLDNDvrtppD-WLDPLVETIIL----DDKIAAVQS-LYTDWPYGEQPRLIPWFSTASALVRREEIL 143
Cdd:cd04196    81 DYVFFCDQD-----DiWLPDKLERLLKaflkDDKPLLVYSdLELVDENGNPIGESFFEYQKIKPGTSFNNL 146
PRK10073 PRK10073
putative glycosyl transferase; Provisional
6-128 4.13e-07

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 50.43  E-value: 4.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYKEVVIVDNGSNDGS----KEYVKSLG-VRLISlDKNYGPAYARNIVLKTFKSKF 80
Cdd:PRK10073   10 IIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSveiaKHYAENYPhVRLLH-QANAGVSVARNTGLAVATGKY 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVETIILDD-KIAAVQSLYTDWPYGEQPRLIP 128
Cdd:PRK10073   89 VAFPDADDVVYPTMYETLMTMALEDDlDVAQCNADWCFRDTGETWQSIP 137
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
4-182 4.37e-07

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: 49.51  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   4 IPIVVLNYNG-LELLKKYLPSILETRYPYKEVVIVDNGSNDGS-KEYVKSLG-----VRLISLDKNYGPAYARNIVLKTF 76
Cdd:cd04184     3 ISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDASTDPEvKRVLKKYAaqdprIKVVFREENGGISAATNSALELA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  77 KSKFIAFLDNDVRTPPDWLDPLVETIILDDKIAAvqsLYTDwpygE----------QPRLIPWFS----------TASAL 136
Cdd:cd04184    83 TGEFVALLDHDDELAPHALYEVVKALNEHPDADL---IYSD----EdkideggkrsEPFFKPDWSpdlllsqnyiGHLLV 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2205656907 137 VRREEILKIGGFDEHYffywE---DAELSWRLYRAGYKILMVPKSkVYH 182
Cdd:cd04184   156 YRRSLVRQVGGFREGF----EgaqDYDLVLRVSEHTDRIAHIPRV-LYH 199
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
80-230 5.23e-07

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


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 49.26  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  80 FIAFLDNDVRTPPDWLDPLVETIiLDDKIAAVQSLYTDWPYGEQP-------------RLIPW---------FSTASALV 137
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEM-ASPEVAIIQGPILPMNVGNYLeelaalffaddhgKSIPVrmalgrvlpFVGSGAFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907 138 RREEILKIGGFDEhyFFYWEDAELSWRLYRAGYKILMVPKSKVYHEAHGTFKK-----------------------LPSP 194
Cdd:pfam13632  80 RRSALQEVGGWDD--GSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDflrqrrrwaygcllillirllgyLGTL 157
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2205656907 195 FTSYLTLRnqMLLLLTYYHLSQLLTMFPILYIIRFV 230
Cdd:pfam13632 158 LWSGLPLA--LLLLLLFSISSLALVLLLLALLAGLL 191
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
77-176 9.41e-06

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


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 44.97  E-value: 9.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  77 KSKFIAFLDNDVRTPPDWLDPLVETIiLDDKIAAVQSLY------TDWPYGEQ------PRLI------PWFST-ASALV 137
Cdd:pfam13506  30 KYDLLVISDSDIRVPPDYLRDLLAPL-ADPKVGLVTSPPvgsdpkGLAAALEAaffntlAGVLqaalsgIGFAVgMSMAF 108
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2205656907 138 RREEILKIGGFDEhyFFYW--EDAELSWRLYRAGYKILMVP 176
Cdd:pfam13506 109 RRADLERIGGFEA--LADYlaEDYALGKLLRAAGLKVVLSP 147
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
6-100 2.32e-05

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: 44.01  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNG----LELLKKYLPSILETRYPYkEVVIVDNGSNDGSKEYVKSL-----GVRLISLDKNYGPAYARNIVLKTF 76
Cdd:cd04187     1 IVVPVYNEeenlPELYERLKAVLESLGYDY-EIIFVDDGSTDRTLEILRELaardpRVKVIRLSRNFGQQAALLAGLDHA 79
                          90       100
                  ....*....|....*....|....
gi 2205656907  77 KSKFIAFLDNDVRTPPDWLDPLVE 100
Cdd:cd04187    80 RGDAVITMDADLQDPPELIPEMLA 103
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
33-120 2.52e-05

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


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 44.59  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  33 EVVIVDNGSNDGSKEYVKSLGVRLISLD-KNYGPayARNIVLKTFKSKFIAFLDNDvrtppDWLDPlvetiildDKIAAV 111
Cdd:cd02511    28 EIIVVDSGSTDRTVEIAKEYGAKVYQRWwDGFGA--QRNFALELATNDWVLSLDAD-----ERLTP--------ELADEI 92

                  ....*....
gi 2205656907 112 QSLYTDWPY 120
Cdd:cd02511    93 LALLATDDY 101
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
11-95 6.02e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 44.01  E-value: 6.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  11 YNGlellKKYLPSILE-------TRYPYKEVVIVDNGSNDGSKEYVK------SLGVRLI-SLDKNYGPAYARNIVLKTF 76
Cdd:NF038302   10 YNG----ANRLPEVLErlrsqigTESLSWEIIVVDNNSTDNTAQVVQeyqknwPSPYPLRyCFEPQQGAAFARQRAIQEA 85
                          90
                  ....*....|....*....
gi 2205656907  77 KSKFIAFLDNDVRTPPDWL 95
Cdd:NF038302   86 KGELIGFLDDDNLPAPNWV 104
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
15-181 1.62e-04

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: 41.92  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  15 ELLKKYLPSILETRYPYKEVVIVDNGSNDGS-----KEYVKSLGVRLISLDKNYGPAYARNIVLKTFKSKFIAFLDNDVR 89
Cdd:cd04195    13 EFLREALESILKQTLPPDEVVLVKDGPVTQSlnevlEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCTYDWVARMDTDDI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  90 TPPDWLDPLVETIILDDKIAAVQSLYTDWPYGEQP---RLIPW--------------FSTASALVRREEILKIGGFDEHY 152
Cdd:cd04195    93 SLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDigkRRLPTshddilkfarrrspFNHPTVMFRKSKVLAVGGYQDLP 172
                         170       180
                  ....*....|....*....|....*....
gi 2205656907 153 ffYWEDAELSWRLYRAGYKILMVPKSKVY 181
Cdd:cd04195   173 --LVEDYALWARMLANGARFANLPEILVK 199
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
62-189 9.03e-04

CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, Glucan Biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of glucan.


Pssm-ID: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 39.93  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  62 NYGPAYARnivlktfkSKFIAFLDNDVRTPPDWLDPLVETI-ILDDKIAAVQSL--YTDWPYGEQPR------------L 126
Cdd:cd06427    77 NYALAFAR--------GEYVVIYDAEDAPDPDQLKKAVAAFaRLDDKLACVQAPlnYYNARENWLTRmfaleyaawfdyL 148
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2205656907 127 IPWFSTASALV---------RREEILKIGGFDEHYFFywEDAELSWRLYRAGYKILMVPkSKVYHEAHGTFK 189
Cdd:cd06427   149 LPGLARLGLPIplggtsnhfRTDVLRELGGWDPFNVT--EDADLGLRLARAGYRTGVLN-STTLEEANNALG 217
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
6-111 1.73e-03

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: 39.10  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907   6 IVVLNYNGLELLKKYLPSILETRYPYK--EVVIVDNGSNDGSKEYVKSL---GVRLISLDKNYGPAYARNIVLKTFKSKF 80
Cdd:cd06439    33 IIIPAYNEEAVIEAKLENLLALDYPRDrlEIIVVSDGSTDGTAEIAREYadkGVKLLRFPERRGKAAALNRALALATGEI 112
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVEtIILDDKIAAV 111
Cdd:cd06439   113 VVFTDANALLDPDALRLLVR-HFADPSVGAV 142
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
13-176 4.90e-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: 37.58  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  13 GLEL-LKKYLPSILETRYPYKEVVI-VDNGSnDGSKEYVKSLGVR--------LISLDKNYGPAYARNIV--LKTFKSKF 80
Cdd:cd02520    11 GVDPnLYENLESFFQQDYPKYEILFcVQDED-DPAIPVVRKLIAKypnvdarlLIGGEKVGINPKVNNLIkgYEEARYDI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2205656907  81 IAFLDNDVRTPPDWLDPLVETIiLDDKIAAVQSLYTdwpygeqprlipwfSTASALVRREEILKIGGFDEHYFFYWEDAE 160
Cdd:cd02520    90 LVISDSDISVPPDYLRRMVAPL-MDPGVGLVTCLCA--------------FGKSMALRREVLDAIGGFEAFADYLAEDYF 154
                         170
                  ....*....|....*.
gi 2205656907 161 LSWRLYRAGYKILMVP 176
Cdd:cd02520   155 LGKLIWRLGYRVVLSP 170
 
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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