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Conserved domains on  [gi|767948454|ref|XP_011514771|]
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polypeptide N-acetylgalactosaminyltransferase 17 isoform X3 [Homo sapiens]

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 ...
 155-320 9.54e-82

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 cd02510:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 299  Bit Score: 249.81  E-value: 9.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 155 SIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKVPLEEYvHKRYPGLVKVVRNQKREGLIRARIEGW 234
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEY-YKKYLPKVKVLRLKKREGLIRARIAGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 235 KVATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSA-HGYSWELWCMYISPPKDWWDA 313
Cdd:cd02510   80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDArGGFDWSLHFKWLPLPEEERRR 159


                 ....*..
gi 767948454 314 GDPSLPI 320
Cdd:cd02510  160 ESPTAPI 166
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 155-320 9.54e-82

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: 249.81  E-value: 9.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 155 SIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKVPLEEYvHKRYPGLVKVVRNQKREGLIRARIEGW 234
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEY-YKKYLPKVKVLRLKKREGLIRARIAGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 235 KVATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSA-HGYSWELWCMYISPPKDWWDA 313
Cdd:cd02510   80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDArGGFDWSLHFKWLPLPEEERRR 159


                 ....*..
gi 767948454 314 GDPSLPI 320
Cdd:cd02510  160 ESPTAPI 166
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 155-290 1.07e-24

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: 97.85  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454  155 SIIFIFVNEAlSVILRSVHSAVNHTptHLLKEIILVDDNSdEEELKVPLEEYVHKryPGLVKVVRNQKREGLIRARIEGW 234
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGS-TDGTVEIAEEYAKK--DPRVRVIRLPENRGKAGARNAGL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767948454  235 KVATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYEN 290
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR 130
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 152-271 2.84e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 64.72  E-value: 2.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 152 PQISIIFIFVNEAlSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELKVpLEEYVhKRYPGlVKVVRNQKREGLIRARI 231
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTAEI-LRELA-AKDPR-IRVIRLERNRGKGAARN 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767948454 232 EGWKVATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVI 271
Cdd:COG0463   76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
 
Name Accession Description Interval E-value
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 155-320 9.54e-82

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: 249.81  E-value: 9.54e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 155 SIIFIFVNEALSVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKVPLEEYvHKRYPGLVKVVRNQKREGLIRARIEGW 234
Cdd:cd02510    1 SVIIIFHNEALSTLLRTVHSVINRTPPELLKEIILVDDFSDKPELKLLLEEY-YKKYLPKVKVLRLKKREGLIRARIAGA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 235 KVATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYENSA-HGYSWELWCMYISPPKDWWDA 313
Cdd:cd02510   80 RAATGDVLVFLDSHCEVNVGWLEPLLARIAENRKTVVCPIIDVIDADTFEYRGSSGDArGGFDWSLHFKWLPLPEEERRR 159


                 ....*..
gi 767948454 314 GDPSLPI 320
Cdd:cd02510  160 ESPTAPI 166
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 155-290 1.07e-24

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: 97.85  E-value: 1.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454  155 SIIFIFVNEAlSVILRSVHSAVNHTptHLLKEIILVDDNSdEEELKVPLEEYVHKryPGLVKVVRNQKREGLIRARIEGW 234
Cdd:pfam00535   1 SVIIPTYNEE-KYLLETLESLLNQT--YPNFEIIVVDDGS-TDGTVEIAEEYAKK--DPRVRVIRLPENRGKAGARNAGL 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767948454  235 KVATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVILPSIDNIKQDNFEVQRYEN 290
Cdd:pfam00535  75 RAATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASR 130
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 152-271 2.84e-12

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 64.72  E-value: 2.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 152 PQISIIFIFVNEAlSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELKVpLEEYVhKRYPGlVKVVRNQKREGLIRARI 231
Cdd:COG0463    2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDF--EIIVVDDGSTDGTAEI-LRELA-AKDPR-IRVIRLERNRGKGAARN 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767948454 232 EGWKVATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVI 271
Cdd:COG0463   76 AGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLV 115
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 156-271 1.03e-11

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: 62.14  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 156 IIFIFVNEAlSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELKVpLEEYVHKRYPglVKVVRNQKREGLIRARIEGWK 235
Cdd:cd00761    1 VIIPAYNEE-PYLERCLESLLAQTYPNF--EVIVVDDGSTDGTLEI-LEEYAKKDPR--VIRVINEENQGLAAARNAGLK 74

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 767948454 236 VATGQVTGFFDAHVEFTAGWAEPVLSRIQENRKRVI 271
Cdd:cd00761   75 AARGEYILFLDADDLLLPDWLERLVAELLADPEADA 110
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 148-267 2.63e-11

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: 63.22  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 148 SKDLPQISIIFIFVNEALsVILRSVHSAVNHTPTHLLKEIILVDDNSDEEELKVpLEEYVHKRYPglVKVVRNQKREGLI 227
Cdd:COG1215   25 PADLPRVSVIIPAYNEEA-VIEETLRSLLAQDYPKEKLEVIVVDDGSTDETAEI-ARELAAEYPR--VRVIERPENGGKA 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767948454 228 RARIEGWKVATGQVTGFFDAHVEFTAGWAEPVLSRIQENR 267
Cdd:COG1215  101 AALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFADPG 140
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
152-261 8.69e-08

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 51.53  E-value: 8.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 152 PQISIIFIFVNEAlSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELkvpleEYVHKRYPGLVKVVRNQKREGLIRARI 231
Cdd:COG1216    3 PKVSVVIPTYNRP-ELLRRCLESLLAQTYPPF--EVIVVDNGSTDGTA-----ELLAALAFPRVRVIRNPENLGFAAARN 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 767948454 232 EGWKVATGQVTGFFDAHVEFTAGWAEPVLS 261
Cdd:COG1216   75 LGLRAAGGDYLLFLDDDTVVEPDWLERLLA 104
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 162-247 1.98e-06

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: 47.57  E-value: 1.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 162 NEA--LSVILRSVHSAVNHTPTHllkEIILVDDNSDEEELKVpLEEYvHKRYPGlVKVVRNQKREGLIRARIEGWKVATG 239
Cdd:cd04179    7 NEEenIPELVERLLAVLEEGYDY---EIIVVDDGSTDGTAEI-AREL-AARVPR-VRVIRLSRNFGKGAAVRAGFKAARG 80


                 ....*...
gi 767948454 240 QVTGFFDA 247
Cdd:cd04179   81 DIVVTMDA 88
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 162-247 6.25e-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: 46.37  E-value: 6.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 162 NEA--LSVILRSVHSAVNHTPThllkEIILVDDNSDEEELKVpLEEYVhKRYPGLVKVVRNQKReGLIRARIEGWKVATG 239
Cdd:cd06442    7 NERenIPELIERLDAALKGIDY----EIIVVDDNSPDGTAEI-VRELA-KEYPRVRLIVRPGKR-GLGSAYIEGFKAARG 79


                 ....*...
gi 767948454 240 QVTGFFDA 247
Cdd:cd06442   80 DVIVVMDA 87
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 186-247 2.48e-05

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: 44.48  E-value: 2.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767948454 186 EIILVDDNSDEEELKVpLEEYVHKrYPGLVKVVRNQKREGLIRARIEGWKVATGQVTGFFDA 247
Cdd:cd04188   32 EIIVVDDGSKDGTAEV-ARKLARK-NPALIRVLTLPKNRGKGGAVRAGMLAARGDYILFADA 91
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 162-247 6.05e-05

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: 42.98  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 162 NEAlSVILRSVHSAVNHTptHLLKEIILVDDNSDEEELKVPLEEYVhkRYPGLVKVVRNQKREGLIRARIEGWKVATGQV 241
Cdd:cd06423    7 NEE-AVIERTIESLLALD--YPKLEVIVVDDGSTDDTLEILEELAA--LYIRRVLVVRDKENGGKAGALNAGLRHAKGDI 81


                 ....*.
gi 767948454 242 TGFFDA 247
Cdd:cd06423   82 VVVLDA 87
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 152-246 1.97e-04

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: 41.80  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 152 PQISIIFIFVNEALSVILRSVHSAVNHTPTHLlkEIILVDDNSDEEELKVPLEEYV--HKRypglVKVVRNQKREGLIRA 229
Cdd:cd04184    1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNW--ELCIADDASTDPEVKRVLKKYAaqDPR----IKVVFREENGGISAA 74

                         90
                 ....*....|....*..
gi 767948454 230 RIEGWKVATGQVTGFFD 246
Cdd:cd04184   75 TNSALELATGEFVALLD 91
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 154-324 1.21e-03

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: 39.54  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 154 ISIIFIFVNEALSVILRSVHSAVNHTPthllKEIILVDDNSDEEELKVPLEEYVHKRypglvKVVRNQKREGLIRARIEG 233
Cdd:cd06434    2 VTVIIPVYDEDPDVFRECLRSILRQKP----LEIIVVTDGDDEPYLSILSQTVKYGG-----IFVITVPHPGKRRALAEG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767948454 234 WKVATGQVTGFFDAHVEFTAGWAEPVLS--------------RIQENRKRVIL-PSIDNIKQDNFEvqryENSAHGYSWE 298
Cdd:cd06434   73 IRHVTTDIVVLLDSDTVWPPNALPEMLKpfedpkvggvgtnqRILRPRDSKWSfLAAEYLERRNEE----IRAAMSYDGG 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767948454 299 LWCM----------YISPPK------DWWDAGDPSLPISDRF 324
Cdd:cd06434  149 VPCLsgrtaayrteILKDFLfleeftNETFMGRRLNAGDDRF 190
 
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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