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Conserved domains on  [gi|1214774834|ref|WP_088885992|]
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glycosyltransferase [Thermococcus gorgonarius]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-204 5.65e-42

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


The actual alignment was detected with superfamily member cd06433:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 202  Bit Score: 143.45  E-value: 5.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDGRIRYIPQKGRGIANARNLGVLKARGEFIA 85
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  86 FLDDDDRWREDKLERQLELFRELPESyGLIYtAFTYYYLEKNRVLGIKHPKASgnVYKYLLKDNITGTSTIIVKRDCFKK 165
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEV-DVVY-GDVLLVDENGRVIGRRRPPPF--LDKFLLYGMPICHQATFFRRSLFEK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1214774834 166 AGLFRESFVTCEDWDMWLRMSRI-CLFGAIGEPLVDYSVH 204
Cdd:cd06433   157 YGGFDESYRIAADYDLLLRLLLAgKIFKYLPEVLAAFRLG 196
 
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 ...
 6-204 5.65e-42

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: 143.45  E-value: 5.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDGRIRYIPQKGRGIANARNLGVLKARGEFIA 85
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  86 FLDDDDRWREDKLERQLELFRELPESyGLIYtAFTYYYLEKNRVLGIKHPKASgnVYKYLLKDNITGTSTIIVKRDCFKK 165
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEV-DVVY-GDVLLVDENGRVIGRRRPPPF--LDKFLLYGMPICHQATFFRRSLFEK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1214774834 166 AGLFRESFVTCEDWDMWLRMSRI-CLFGAIGEPLVDYSVH 204
Cdd:cd06433   157 YGGFDESYRIAADYDLLLRLLLAgKIFKYLPEVLAAFRLG 196
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-214 1.11e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 142.92  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   2 KPTVSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLG--DGRIRYIP-QKGRGIANARNLGVLK 78
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAakDPRIRVIRlERNRGKGAARNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  79 ARGEFIAFLDDDDRWREDKLERQLELFRELPesYGLIYTAFtyyYLEKNRVLGIKHPKASGNVYKYLLKDNITGTSTIIV 158
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP--ADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1214774834 159 KRDCFKKAGlFRESFvtCEDWDMWlrmsRICLFGA-IGEPLVDYSVHPGQFSFAKYL 214
Cdd:COG0463   156 RREVLEELG-FDEGF--LEDTELL----RALRHGFrIAEVPVRYRAGESKLNLRDLL 205
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-173 4.07e-32

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: 116.73  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSL--GDGRIRYIPQ-KGRGIANARNLGVLKARGE 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYakKDPRVRVIRLpENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  83 FIAFLDDDDRWREDKLERQLELFRELPESyglIYTAFTYYYLEKNRVLGIKHPKASGNVYKYLLKDNITGTSTIIvkrdC 162
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGAD---VVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL----I 153

                         170
                  ....*....|.
gi 1214774834 163 FKKAGLFRESF 173
Cdd:pfam00535 154 GGFALYRREAL 164
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
2-185 3.08e-21

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 90.82  E-value: 3.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   2 KPTVSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARS--ESTRELVRSLGDGRIRYIPQK-GRGIANARNLGVLK 78
Cdd:PRK10018    4 NPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTswEQLQQYVTALNDPRITYIHNDiNSGACAVRNQAIML 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  79 ARGEFIAFLDDDDRWREDKlerqLELFreLPESYGLIYTAFTYY--YLEKNRVLGIK-----HPKaSGNVYKYLLKDNIT 151
Cdd:PRK10018   84 AQGEYITGIDDDDEWTPNR----LSVF--LAHKQQLVTHAFLYAndYVCQGEVYSQPaslplYPK-SPYSRRLFYKRNII 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1214774834 152 GTSTIIVKRDCfkKAGLFRESFVTCEDWDMWLRM 185
Cdd:PRK10018  157 GNQVFTWAWRF--KECLFDTELKAAQDYDIFLRM 188
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-199 7.47e-12

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: 63.30  E-value: 7.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   5 VSVIIPTYNRDALLKRAIESVLNQSfDDFEVLVIDGARSESTRELVRSLGDGRIRyiPQKGRgiANARNLGVLKARGEFI 84
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALR-GDAEVIVVDGGSTDGTVEIARSLGAKVIH--SPKGR--ARQMNAGAALAKGDIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  85 AFLDDDDRWREDklerQLELFRELPESYGLIYTAFTYYYLEKNRVLGIkhpKASGNVYKYLLKDNITGTSTIIVKRDCFK 164
Cdd:TIGR04283  76 LFLHADTRLPKD----FLEAIRRALAKPGYVAGAFDLRFDGPGLLLRL---IEWGVNLRSRLTGIPYGDQGLFVRRSLFE 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1214774834 165 KAGLFrESFVTCEDWDMWLRMSRICLFGAIGEPLV 199
Cdd:TIGR04283 149 QIGGF-PDIPLMEDIELSRRLRRLGRLAILPAPVV 182
 
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 ...
 6-204 5.65e-42

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: 143.45  E-value: 5.65e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDGRIRYIPQKGRGIANARNLGVLKARGEFIA 85
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  86 FLDDDDRWREDKLERQLELFRELPESyGLIYtAFTYYYLEKNRVLGIKHPKASgnVYKYLLKDNITGTSTIIVKRDCFKK 165
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEV-DVVY-GDVLLVDENGRVIGRRRPPPF--LDKFLLYGMPICHQATFFRRSLFEK 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1214774834 166 AGLFRESFVTCEDWDMWLRMSRI-CLFGAIGEPLVDYSVH 204
Cdd:cd06433   157 YGGFDESYRIAADYDLLLRLLLAgKIFKYLPEVLAAFRLG 196
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 2-214 1.11e-41

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 142.92  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   2 KPTVSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLG--DGRIRYIP-QKGRGIANARNLGVLK 78
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAakDPRIRVIRlERNRGKGAARNAGLAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  79 ARGEFIAFLDDDDRWREDKLERQLELFRELPesYGLIYTAFtyyYLEKNRVLGIKHPKASGNVYKYLLKDNITGTSTIIV 158
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALEEGP--ADLVYGSR---LIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLF 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1214774834 159 KRDCFKKAGlFRESFvtCEDWDMWlrmsRICLFGA-IGEPLVDYSVHPGQFSFAKYL 214
Cdd:COG0463   156 RREVLEELG-FDEGF--LEDTELL----RALRHGFrIAEVPVRYRAGESKLNLRDLL 205
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-187 2.24e-35

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 126.26  E-value: 2.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   1 MKPTVSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDGRIRYIPQKG-RGIANARNLGVLKA 79
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFPRVRVIRNPEnLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  80 RGEFIAFLDDDDRWREDKLERQLElfrelpesygliytaftyyyleknrvlgikhpkasgnvykyllkdnitgTSTIIVK 159
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLA-------------------------------------------------AACLLIR 111

                         170       180
                  ....*....|....*....|....*....
gi 1214774834 160 RDCFKKAGLFRES-FVTCEDWDMWLRMSR 187
Cdd:COG1216   112 REVFEEVGGFDERfFLYGEDVDLCLRLRK 140
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 7-194 1.14e-33

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: 120.30  E-value: 1.14e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDG---RIRYIPQKGRGIANARNLGVLKARGEF 83
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAKKdprVIRVINEENQGLAAARNAGLKAARGEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  84 IAFLDDDDRWREDKLERQLELFRelpesygliytaftyyyleknrvlgiKHPKASGnvykyllkdnITGTSTIIVKRDCF 163
Cdd:cd00761    81 ILFLDADDLLLPDWLERLVAELL--------------------------ADPEADA----------VGGPGNLLFRRELL 124

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1214774834 164 KKAGLFRESFVTC-EDWDMWLRMSRICLFGAI 194
Cdd:cd00761   125 EEIGGFDEALLSGeEDDDFLLRLLRGGKVAFR 156
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 6-173 4.07e-32

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: 116.73  E-value: 4.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSL--GDGRIRYIPQ-KGRGIANARNLGVLKARGE 82
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYakKDPRVRVIRLpENRGKAGARNAGLRAATGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  83 FIAFLDDDDRWREDKLERQLELFRELPESyglIYTAFTYYYLEKNRVLGIKHPKASGNVYKYLLKDNITGTSTIIvkrdC 162
Cdd:pfam00535  81 YIAFLDADDEVPPDWLEKLVEALEEDGAD---VVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFL----I 153

                         170
                  ....*....|.
gi 1214774834 163 FKKAGLFRESF 173
Cdd:pfam00535 154 GGFALYRREAL 164
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 4-229 4.00e-30

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


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 113.87  E-value: 4.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   4 TVSVIIPTYNRDALLKRAIESVLNQSF--DDFEVLVIDGARSESTRELVRSLG--DGRIRYIPQKGRGIANARNLGVLKA 79
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYpkDLIEIIVVDGGSTDGTREIVQEYAakDPRIRLIDNPKRIQSAGLNIGIRNS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  80 RGEFIAFLDDDDRWREDKLERQLE-LFRELPESYGLIYTAFTYYYLEKNRVLGIKHPKASGNVYKYLLKDNITGTSTI-- 156
Cdd:cd02525    81 RGDIIIRVDAHAVYPKDYILELVEaLKRTGADNVGGPMETIGESKFQKAIAVAQSSPLGSGGSAYRGGAVKIGYVDTVhh 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834 157 -IVKRDCFKKAGLFRESFVTCEDWDMWLRMSR----ICLFGAIgepLVDYSVHPGQFSFAK----YLEGRYRMIKEHGDI 227
Cdd:cd02525   161 gAYRREVFEKVGGFDESLVRNEDAELNYRLRKagykIWLSPDI---RVYYYPRSTLKKLARqyfrYGKWRARTLRKHRKS 237


                  ....*
gi 1214774834 228 ---RH 229
Cdd:cd02525   238 lslRH 242
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-187 8.19e-29

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: 111.76  E-value: 8.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   3 PTVSVIIPTYNRDALLKRAIESVLNQSF--DDFEVLVIDGARSESTRELVRSLG--DGRIRYIPQ-KGRGIANARNLGVL 77
Cdd:COG1215    29 PRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAaeYPRVRVIERpENGGKAAALNAGLK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  78 KARGEFIAFLDDDDRWREDKLERQLELFrelpesygliytaftyyyleknrvlgiKHPKASGNvykyllkdnitgTSTII 157
Cdd:COG1215   109 AARGDIVVFLDADTVLDPDWLRRLVAAF---------------------------ADPGVGAS------------GANLA 149

                         170       180       190
                  ....*....|....*....|....*....|
gi 1214774834 158 VKRDCFKKAGLFRESFVTcEDWDMWLRMSR 187
Cdd:COG1215   150 FRREALEEVGGFDEDTLG-EDLDLSLRLLR 178
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 3-186 4.70e-24

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: 96.50  E-value: 4.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   3 PTVSVIIPTYNRD-ALLKRAIESVLNQSFDDFEVLVIDGA-RSESTRELVRSLG--DGRIRYI-PQKGRGIANARNLGVL 77
Cdd:cd04184     1 PLISIVMPVYNTPeKYLREAIESVRAQTYPNWELCIADDAsTDPEVKRVLKKYAaqDPRIKVVfREENGGISAATNSALE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  78 KARGEFIAFLDDDDRWREDKLerqLELFRELPES--YGLIYTAFTyyYLEKNRVLGIKHPKASGNvYKYLLKDNITGtST 155
Cdd:cd04184    81 LATGEFVALLDHDDELAPHAL---YEVVKALNEHpdADLIYSDED--KIDEGGKRSEPFFKPDWS-PDLLLSQNYIG-HL 153

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1214774834 156 IIVKRDCFKKAGLFRESFVTCEDWDMWLRMS 186
Cdd:cd04184   154 LVYRRSLVRQVGGFREGFEGAQDYDLVLRVS 184
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
2-185 3.08e-21

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 90.82  E-value: 3.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   2 KPTVSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARS--ESTRELVRSLGDGRIRYIPQK-GRGIANARNLGVLK 78
Cdd:PRK10018    4 NPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTswEQLQQYVTALNDPRITYIHNDiNSGACAVRNQAIML 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  79 ARGEFIAFLDDDDRWREDKlerqLELFreLPESYGLIYTAFTYY--YLEKNRVLGIK-----HPKaSGNVYKYLLKDNIT 151
Cdd:PRK10018   84 AQGEYITGIDDDDEWTPNR----LSVF--LAHKQQLVTHAFLYAndYVCQGEVYSQPaslplYPK-SPYSRRLFYKRNII 156

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1214774834 152 GTSTIIVKRDCfkKAGLFRESFVTCEDWDMWLRM 185
Cdd:PRK10018  157 GNQVFTWAWRF--KECLFDTELKAAQDYDIFLRM 188
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-185 1.50e-19

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: 83.38  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDgRIRYIPQKG-RGIANARNLGVLKARGEFIA 85
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFP-EVRLIRNGEnLGFGAGNNQGIREAKGDYVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  86 FLDDDDRWREDKLERQLELFRELPEsygliytaftyyyleknrvLGIKHPKASGnvykyllkdnitgtSTIIVKRDCFKK 165
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAEQDPD-------------------VGIVGPKVSG--------------AFLLVRREVFEE 126

                         170       180
                  ....*....|....*....|.
gi 1214774834 166 AGLFRES-FVTCEDWDMWLRM 185
Cdd:cd04186   127 VGGFDEDfFLYYEDVDLCLRA 147
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 6-209 4.73e-19

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: 84.64  E-value: 4.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDALlKRAIESVLNQSF---DDFEVLVIDGARSESTRELVRSLGDGR----IRYIPQKGRGIANARNLGVLK 78
Cdd:pfam10111   1 SVVIPVYNGEKT-HWIQERILNQTFqydPEFELIIINDGSTDKTLEEVSSIKDHNlqvyYPNAPDTTYSLAASRNRGTSH 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  79 ARGEFIAFLDDDDRWREDKLERQLEL-----FRELPESygLIYTAFTYYYLEKNRVL-GIKHPKASGNV-------YKYL 145
Cdd:pfam10111  80 AIGEYISFIDGDCLWSPDKFEKQLKIatslaLQENIQA--AVVLPVTDLNDESSNFLrRGGDLTASGDVlrdllvfYSPL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1214774834 146 LKDNITGTSTIIVKRDCFKKAGLFRESFVT--CEDWDMWLRMSRICLFGAIGEPLVDYSVHPGQFS 209
Cdd:pfam10111 158 AIFFAPNSSNALINRQAFIEVGGFDESFRGhgAEDFDIFLRLAARYPFVAVMPPQLLYRLSAKSMS 223
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-206 8.64e-19

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: 82.68  E-value: 8.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSL--GDGRIRYIPQKGRGIANARN--LGVLKARG 81
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYidKDPFIIILIRNGKNLGVARNfeSLLQAADG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  82 EFIAFLDDDDRWREDKLERQLELFrELPESYGLIYTAFTYYYlEKNRVLGIK----HPKASGNVYKYLLKDNITGTSTII 157
Cdd:cd04196    81 DYVFFCDQDDIWLPDKLERLLKAF-LKDDKPLLVYSDLELVD-ENGNPIGESffeyQKIKPGTSFNNLLFQNVVTGCTMA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1214774834 158 VKRDCFKKAGLFRESFVTCEDWDMWLrmsRICLFGAIG---EPLVDYSVHPG 206
Cdd:cd04196   159 FNRELLELALPFPDADVIMHDWWLAL---LASAFGKVVfldEPLILYRQHGN 207
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 7-178 7.38e-16

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: 73.80  E-value: 7.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDG----RIRYIPQKGRGIANARNLGVLKARGE 82
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALyirrVLVVRDKENGGKAGALNAGLRHAKGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  83 FIAFLDDDDRWREDKLERQLELFRELPE-------------SYGLIYTAFTYYYLEKNRVLgikhpKASGNVYKYLLkdN 149
Cdd:cd06423    81 IVVVLDADTILEPDALKRLVVPFFADPKvgavqgrvrvrngSENLLTRLQAIEYLSIFRLG-----RRAQSALGGVL--V 153

                         170       180
                  ....*....|....*....|....*....
gi 1214774834 150 ITGTSTIIvKRDCFKKAGLFRESFVTcED 178
Cdd:cd06423   154 LSGAFGAF-RREALREVGGWDEDTLT-ED 180
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 3-187 1.23e-15

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: 74.33  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   3 PTVSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVI----DGARSESTRELVRSLGDGRIRYIPQ--------KGRGIAN 70
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVvnpsDAETLDVAEEIAARFPDVRLRVIRNarllgptgKSRGLNH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  71 ARNLgvlkARGEFIAFLDDDDRWREDKLERQLELFRElpESYGLIYT-----------AFTY---YYLEKNRVLGIKHpk 136
Cdd:pfam13641  82 GFRA----VKSDLVVLHDDDSVLHPGTLKKYVQYFDS--PKVGAVGTpvfslnrstmlSALGaleFALRHLRMMSLRL-- 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1214774834 137 ASGNVYkyllkdnITGTSTIIvKRDCFKKAGLFRESFVTCEDWDMWLRMSR 187
Cdd:pfam13641 154 ALGVLP-------LSGAGSAI-RREVLKELGLFDPFFLLGDDKSLGRRLRR 196
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 7-90 1.63e-15

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: 73.00  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDG---RIRYIPQKGRG--IANARNLGVLKARG 81
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQfpiPIKHVWQEDEGfrKAKIRNKAIAAAKG 80


                  ....*....
gi 1214774834  82 EFIAFLDDD 90
Cdd:cd06420    81 DYLIFIDGD 89
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 6-201 1.23e-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: 70.81  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRD--ALLKRAIESVLNQSFDDFE-VLVIDGARSESTRELVRSLGDG-RIRYIP-QKGRGIANARNLGVLKAR 80
Cdd:cd04195     1 SVLMSVYIKEkpEFLREALESILKQTLPPDEvVLVKDGPVTQSLNEVLEEFKRKlPLKVVPlEKNRGLGKALNEGLKHCT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  81 GEFIAFLDDDDRWREDKLERQLELFRELPESYGLIYTA--FTYyylEKNRVLGIKHPKASGNVYKYLLKDNITGTSTIIV 158
Cdd:cd04195    81 YDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVleFDS---DGNDIGKRRLPTSHDDILKFARRRSPFNHPTVMF 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1214774834 159 KRDCFKKAGLFREsFVTCEDWDMWLRM-SRICLFGAIGEPLVDY 201
Cdd:cd04195   158 RKSKVLAVGGYQD-LPLVEDYALWARMlANGARFANLPEILVKA 200
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-199 3.17e-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: 3.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   5 VSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDGRIRyiPQKGRgiANARNLGVLKARGEFI 84
Cdd:cd02522     1 LSIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVVIS--SPKGR--ARQMNAGAAAARGDWL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  85 AFLDDDDRWREDKLERQLELFRELPESYGliytAFTYYYLEKNRVLGIKHPKAsgNVYKYLLKdNITGTSTIIVKRDCFK 164
Cdd:cd02522    77 LFLHADTRLPPDWDAAIIETLRADGAVAG----AFRLRFDDPGPRLRLLELGA--NLRSRLFG-LPYGDQGLFIRRELFE 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1214774834 165 KAGLFRESFVTcEDWDMWLRMSRICLFGAIGEPLV 199
Cdd:cd02522   150 ELGGFPELPLM-EDVELVRRLRRRGRPALLPSPVT 183
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 2-104 1.37e-13

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 69.69  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   2 KPTVSVIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGD--GRIRYIPQKGRGIANARNLGVLKA 79
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAEnyPHVRLLHQANAGVSVARNTGLAVA 84

                          90       100
                  ....*....|....*....|....*
gi 1214774834  80 RGEFIAFLDDDDRWREDKLERQLEL 104
Cdd:PRK10073   85 TGKYVAFPDADDVVYPTMYETLMTM 109
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 2-100 5.22e-12

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: 64.53  E-value: 5.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   2 KPTVSVIIPTYNRDALLKRAIESVLNQSF--DDFEVLVIDGARSESTRELVRSLGDGRIRYIPQKGR-GIANARNLGVLK 78
Cdd:cd06439    28 LPTVTIIIPAYNEEAVIEAKLENLLALDYprDRLEIIVVSDGSTDGTAEIAREYADKGVKLLRFPERrGKAAALNRALAL 107

                          90       100
                  ....*....|....*....|..
gi 1214774834  79 ARGEFIAFLDDDDRWREDKLER 100
Cdd:cd06439   108 ATGEIVVFTDANALLDPDALRL 129
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-199 7.47e-12

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: 63.30  E-value: 7.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   5 VSVIIPTYNRDALLKRAIESVLNQSfDDFEVLVIDGARSESTRELVRSLGDGRIRyiPQKGRgiANARNLGVLKARGEFI 84
Cdd:TIGR04283   1 LSIIIPVLNEAATLPELLADLQALR-GDAEVIVVDGGSTDGTVEIARSLGAKVIH--SPKGR--ARQMNAGAALAKGDIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  85 AFLDDDDRWREDklerQLELFRELPESYGLIYTAFTYYYLEKNRVLGIkhpKASGNVYKYLLKDNITGTSTIIVKRDCFK 164
Cdd:TIGR04283  76 LFLHADTRLPKD----FLEAIRRALAKPGYVAGAFDLRFDGPGLLLRL---IEWGVNLRSRLTGIPYGDQGLFVRRSLFE 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1214774834 165 KAGLFrESFVTCEDWDMWLRMSRICLFGAIGEPLV 199
Cdd:TIGR04283 149 QIGGF-PDIPLMEDIELSRRLRRLGRLAILPAPVV 182
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-107 2.21e-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: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDGR-IRYIPQ-KGRGIANARNLGVLKA--RG- 81
Cdd:cd04185     1 AVVVTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSLGDLDnIVYLRLpENLGGAGGFYEGVRRAyeLGy 80

                          90       100
                  ....*....|....*....|....*.
gi 1214774834  82 EFIAFLDDDDRWREDKLERQLELFRE 107
Cdd:cd04185    81 DWIWLMDDDAIPDPDALEKLLAYADK 106
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 2-90 1.20e-09

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 57.40  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   2 KPTVSVIIPTYNRD---ALLKRAIESVLnQSFDDFEVLVIDGARSESTRELVRSL----GDGRIRYIPQKGR-GIANARN 73
Cdd:PLN02726    8 AMKYSIIVPTYNERlniALIVYLIFKAL-QDVKDFEIIVVDDGSPDGTQDVVKQLqkvyGEDRILLRPRPGKlGLGTAYI 86

                          90
                  ....*....|....*..
gi 1214774834  74 LGVLKARGEFIAFLDDD 90
Cdd:PLN02726   87 HGLKHASGDFVVIMDAD 103
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 7-90 1.75e-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: 56.04  E-value: 1.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYN-RDALLK--RAIESVLNQSFDdFEVLVIDGARSESTRELVRSLG--DGRIRYIP-QKGRGIANARNLGVLKAR 80
Cdd:cd04179     1 VVIPAYNeEENIPElvERLLAVLEEGYD-YEIIVVDDGSTDGTAEIARELAarVPRVRVIRlSRNFGKGAAVRAGFKAAR 79

                          90
                  ....*....|
gi 1214774834  81 GEFIAFLDDD 90
Cdd:cd04179    80 GDIVVTMDAD 89
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 4-134 1.87e-09

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: 56.91  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   4 TVSVIIPTYNRDALLKRAIESVLNqsFDDfEVLVIDgarSES---TRELVRSLGDgriRYIPQKGRGIANARNLGVLKAR 80
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVKW--AVD-EIIVVD---SGStdrTVEIAKEYGA---KVYQRWWDGFGAQRNFALELAT 71

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1214774834  81 GEFIAFLDDDDRWREDKLERQLELFRELPESYgliytaftYYYLEKNRVLG--IKH 134
Cdd:cd02511    72 NDWVLSLDADERLTPELADEILALLATDDYDG--------YYVPRRNFFLGrwIRH 119
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 4-105 1.87e-09

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 56.88  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   4 TVSVIIPTYNRDA-LLKRAIESVLNQSFDDFeVLVIDGARSESTRELVRSLGDGRIRYIPQKGRGIANARNLGVLKARGE 82
Cdd:cd06434     1 DVTVIIPVYDEDPdVFRECLRSILRQKPLEI-IVVTDGDDEPYLSILSQTVKYGGIFVITVPHPGKRRALAEGIRHVTTD 79

                          90       100
                  ....*....|....*....|...
gi 1214774834  83 FIAFLDDDDRWREDKLERQLELF 105
Cdd:cd06434    80 IVVLLDSDTVWPPNALPEMLKPF 102
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 3-122 2.73e-09

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: 56.43  E-value: 2.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   3 PTVSVIIPTYNRD-ALLKRAIESVLNQSF--DDFEVLVIDGARSESTRELVRSLGDGR-IRYI-PQKGRGiANARNL--G 75
Cdd:cd06421     1 PTVDVFIPTYNEPlEIVRKTLRAALAIDYphDKLRVYVLDDGRRPELRALAAELGVEYgYRYLtRPDNRH-AKAGNLnnA 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1214774834  76 VLKARGEFIAFLDDDDRWREDKLERQLELFRELPEsYGLIYTAFTYY 122
Cdd:cd06421    80 LAHTTGDFVAILDADHVPTPDFLRRTLGYFLDDPK-VALVQTPQFFY 125
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 7-111 5.13e-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: 55.16  E-value: 5.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSFDD-FEVLVIDGARSESTRELVRS----LGDGRIRYIPQKG-----RGIANARNLGV 76
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKwrkkLEDSGVIVLVGSHnspspKGVGYAKNQAI 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1214774834  77 LKARGEFIAFLDDDDRWREDKLERQLELFRELPES 111
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQRIRLQYEAALQHPNS 115
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 7-90 8.66e-08

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: 51.41  E-value: 8.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNR----DALLKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSLGDGR---IRYIPQKG-RGIANARNLGVLK 78
Cdd:cd04188     1 VVIPAYNEekrlPPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTAEVARKLARKNpalIRVLTLPKnRGKGGAVRAGMLA 80

                          90
                  ....*....|..
gi 1214774834  79 ARGEFIAFLDDD 90
Cdd:cd04188    81 ARGDYILFADAD 92
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 7-173 2.42e-07

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: 50.75  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRD-ALLKRAIESVLNQsFDdfEVLVIDGaRSESTRELVRSLGDGRIRYIPQKG-RGIANARNLGV--LKARG- 81
Cdd:cd02526     1 AVVVTYNPDlSKLKELLAALAEQ-VD--KVVVVDN-SSGNDIELRLRLNSEKIELIHLGEnLGIAKALNIGIkaALENGa 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  82 EFIAFLDDDDRWREDKLERQLELFRELP--ESYGLIytAFTYYYLEKNRVLGIKHPKASGNVYKYLLKDNITGTSTII-- 157
Cdd:cd02526    77 DYVLLFDQDSVPPPDMVEKLLAYKILSDknSNIGAV--GPRIIDRRTGENSPGVRKSGYKLRIQKEGEEGLKEVDFLIts 154

                         170
                  ....*....|....*....
gi 1214774834 158 ---VKRDCFKKAGLFRESF 173
Cdd:cd02526   155 gslISLEALEKVGGFDEDL 173
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
 3-187 7.58e-07

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: 49.18  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   3 PTVSVIIPTYNRDALLKRAIESV--LNQSFDDFEVLVIDGARSESTRELVRSLGDGRIRYI----PQKGRGIANARNLGV 76
Cdd:cd06427     1 PVYTILVPLYKEAEVLPQLIASLsaLDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVvvvpPSQPRTKPKACNYAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  77 LKARGEFIAFLDDDDRWREDKLERQLELFRELPESYGLIYTAFTYYYLEKN---RVLGIKHpkasGNVYKYLLKD----- 148
Cdd:cd06427    81 AFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDKLACVQAPLNYYNARENwltRMFALEY----AAWFDYLLPGlarlg 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1214774834 149 ---NITGTSTiIVKRDCFKKAGLFRESFVTcEDWDMWLRMSR 187
Cdd:cd06427   157 lpiPLGGTSN-HFRTDVLRELGGWDPFNVT-EDADLGLRLAR 196
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 7-90 1.08e-06

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: 47.86  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYN-RDAL--LKRAIESVLNQSFDDFEVLVIDGARSESTRELVRSL--GDGRIRYIpqkgrgiANARNLG------ 75
Cdd:cd04187     1 IVVPVYNeEENLpeLYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRELaaRDPRVKVI-------RLSRNFGqqaall 73

                          90
                  ....*....|....*..
gi 1214774834  76 --VLKARGEFIAFLDDD 90
Cdd:cd04187    74 agLDHARGDAVITMDAD 90
glyco_TIGR04440 TIGR04440
glycosyltransferase domain; This model describes a putative glycotransferase domain, related ...
 5-91 5.81e-06

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


Pssm-ID: 275233  Cd Length: 215  Bit Score: 46.14  E-value: 5.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   5 VSVIIPTYNRDALLKRAIESVLNQSFdDFEVLVIDGAR---SESTRELVRSLGDGRIRYI--PQKGRGIANARNLGVLKA 79
Cdd:TIGR04440   2 LTIIIPTYNRPEYLKRWLRYYSDFGC-DYRIIIADSSDekfNENNLKVFKNYSNPNITYLhyPDLGVPFYEKLLDALEQV 80

                          90
                  ....*....|..
gi 1214774834  80 RGEFIAFLDDDD 91
Cdd:TIGR04440  81 ETPYVVICADDD 92
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-122 9.12e-06

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: 45.74  E-value: 9.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSF--DDFEVLVIDGARSESTRELV---RSLGDGRIRYIPQKGRGI---ANARNLGVLK 78
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILefaAAKPNFQLKILNNSRVSIsgkKNALTTAIKA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1214774834  79 ARGEFIAFLDDDDRWREDKLERQLELFRElpESYGLIYTAFTYY 122
Cdd:cd04192    81 AKGDWIVTTDADCVVPSNWLLTFVAFIQK--EQIGLVAGPVIYF 122
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 7-90 9.96e-06

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: 45.60  E-value: 9.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   7 VIIPTYNRDALLKRAIESVLNQSFD-DFEVLVIDGARSESTRELVRSL--GDGRIRYIPQKG-RGIANARNLGVLKARGE 82
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAEIVRELakEYPRVRLIVRPGkRGLGSAYIEGFKAARGD 80


                  ....*...
gi 1214774834  83 FIAFLDDD 90
Cdd:cd06442    81 VIVVMDAD 88
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 6-88 1.02e-04

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


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 42.96  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYN--RDALLkRAIESVLNQSFDDF--E-VLVIDGarseSTRELVRSLGDGRIRYIPQKGR--------GIANAR 72
Cdd:cd02510     1 SVIIIFHNeaLSTLL-RTVHSVINRTPPELlkEiILVDDF----SDKPELKLLLEEYYKKYLPKVKvlrlkkreGLIRAR 75

                          90
                  ....*....|....*.
gi 1214774834  73 NLGVLKARGEFIAFLD 88
Cdd:cd02510    76 IAGARAATGDVLVFLD 91
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
 3-107 3.07e-04

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 41.14  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   3 PTVSVIIPTYNRDALLKRAIESVLNQSF--DDFEVLVIDGARSESTRELVRSLGDGR-----IRYIPQKGRGIANARNL- 74
Cdd:cd06437     1 PMVTVQLPVFNEKYVVERLIEAACALDYpkDRLEIQVLDDSTDETVRLAREIVEEYAaqgvnIKHVRRADRTGYKAGALa 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1214774834  75 -GVLKARGEFIAFLDDDDRWREDKLERQLELFRE 107
Cdd:cd06437    81 eGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFAD 114
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
 4-90 5.93e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 40.67  E-value: 5.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   4 TVSVIIPTYNRDALLKRAIESVLNQSFDDF--EVLVID--------------GARSESTRELVRSLGdgriryiPQKGRG 67
Cdd:PRK13915   32 TVSVVLPALNEEETVGKVVDSIRPLLMEPLvdELIVIDsgstdataeraaaaGARVVSREEILPELP-------PRPGKG 104

                          90       100
                  ....*....|....*....|...
gi 1214774834  68 IANARNLGVlkARGEFIAFLDDD 90
Cdd:PRK13915  105 EALWRSLAA--TTGDIVVFVDAD 125
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
 6-111 6.58e-04

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 40.91  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   6 SVIIPTYNRDA----LLKRAIESVLNQSFDD----FEVLVIDGARSESTRELVRSLGDGRI---------RYIPQKGRGi 68
Cdd:PTZ00260   73 SIVIPAYNEEDrlpkMLKETIKYLESRSRKDpkfkYEIIIVNDGSKDKTLKVAKDFWRQNInpnidirllSLLRNKGKG- 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1214774834  69 aNARNLGVLKARGEFIAFLDDDDRWREDKLERQLELFRELPES 111
Cdd:PTZ00260  152 -GAVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQN 193
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
 3-115 1.77e-03

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 40.01  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834   3 PTVSVIIPTYNRD-ALLKRAIESVLNQSF--DDFEVLVIDGARSESTRELVRSLGdgrIRYIPQKGRGIANARNLG-VLK 78
Cdd:PRK11498  260 PTVDIFVPTYNEDlNVVKNTIYASLGIDWpkDKLNIWILDDGGREEFRQFAQEVG---VKYIARPTHEHAKAGNINnALK 336

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214774834  79 -ARGEFIAFLDDDD---R--------W--REDKL---------------ERQLELFRELPES----YGLI 115
Cdd:PRK11498  337 yAKGEFVAIFDCDHvptRsflqmtmgWflKDKKLammqtphhffspdpfERNLGRFRKTPNEgtlfYGLV 406
 
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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