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Conserved domains on  [gi|1958644571|ref|XP_038964511|]
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galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 isoform X2 [Rattus norvegicus]

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 ...
75-206 8.69e-52

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 cd00218:

Pssm-ID: 472172  Cd Length: 223  Bit Score: 167.09  E-value: 8.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571  75 PTIYVITPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPK----------AQR 144
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSdptwlkprgvEQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571 145 ------LRE----------------------------------------------------------------------- 147
Cdd:cd00218    81 nlalrwIREhlsakldgvvyfadddntydlelfeemrkikrvgvwpvglvgglrvegpvcengkvvgwhtawkperpfpi 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644571 148 ---GFAVSLPLLLAKPNAQFDATAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTEK 206
Cdd:cd00218   161 dmaGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
75-206 8.69e-52

Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan synthesis; Beta1,3-glucuronyltransferase I (GlcAT-I) domain; GlcAT-I is a Key enzyme involved in the initial steps of proteoglycan synthesis. GlcAT-I catalyzes the transfer of a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region of trisaccharide Gal-beta-(1-3)-Gal-beta-(1-4)-Xyl of proteoglycans. The enzyme has two subdomains that bind the donor and acceptor substrate separately. The active site is located at the cleft between both subdomains in which the trisaccharide molecule is oriented perpendicular to the UDP. This family has been classified as Glycosyltransferase family 43 (GT-43).


Pssm-ID: 132995  Cd Length: 223  Bit Score: 167.09  E-value: 8.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571  75 PTIYVITPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPK----------AQR 144
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSdptwlkprgvEQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571 145 ------LRE----------------------------------------------------------------------- 147
Cdd:cd00218    81 nlalrwIREhlsakldgvvyfadddntydlelfeemrkikrvgvwpvglvgglrvegpvcengkvvgwhtawkperpfpi 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644571 148 ---GFAVSLPLLLAKPNAQFDATAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTEK 206
Cdd:cd00218   161 dmaGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
96-205 1.07e-35

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 124.95  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571  96 LSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPK-----------AQR------LRE----------- 147
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKppnwtdkprgvHQRnvalrwIREnkhrldgvvyf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571 148 --------------------------------------------------------------GFAVSLPLLLAKPNAQFD 165
Cdd:pfam03360  81 adddntydlrlfdemrktkkvgvwpvglvgglrvegpvcnngkvvgwhtgwkperpfpidmaGFAVNSRLLWDPPEAVFS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958644571 166 A-TAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTE 205
Cdd:pfam03360 161 LdSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
75-206 8.69e-52

Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan synthesis; Beta1,3-glucuronyltransferase I (GlcAT-I) domain; GlcAT-I is a Key enzyme involved in the initial steps of proteoglycan synthesis. GlcAT-I catalyzes the transfer of a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region of trisaccharide Gal-beta-(1-3)-Gal-beta-(1-4)-Xyl of proteoglycans. The enzyme has two subdomains that bind the donor and acceptor substrate separately. The active site is located at the cleft between both subdomains in which the trisaccharide molecule is oriented perpendicular to the UDP. This family has been classified as Glycosyltransferase family 43 (GT-43).


Pssm-ID: 132995  Cd Length: 223  Bit Score: 167.09  E-value: 8.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571  75 PTIYVITPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPK----------AQR 144
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSdptwlkprgvEQR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571 145 ------LRE----------------------------------------------------------------------- 147
Cdd:cd00218    81 nlalrwIREhlsakldgvvyfadddntydlelfeemrkikrvgvwpvglvgglrvegpvcengkvvgwhtawkperpfpi 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958644571 148 ---GFAVSLPLLLAKPNAQFDATAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTEK 206
Cdd:cd00218   161 dmaGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
96-205 1.07e-35

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 124.95  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571  96 LSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPK-----------AQR------LRE----------- 147
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKppnwtdkprgvHQRnvalrwIREnkhrldgvvyf 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958644571 148 --------------------------------------------------------------GFAVSLPLLLAKPNAQFD 165
Cdd:pfam03360  81 adddntydlrlfdemrktkkvgvwpvglvgglrvegpvcnngkvvgwhtgwkperpfpidmaGFAVNSRLLWDPPEAVFS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958644571 166 A-TAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTE 205
Cdd:pfam03360 161 LdSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
 
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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