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Conserved domains on  [gi|1820302111|ref|XP_032597447|]
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galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase P isoform X1 [Drosophila grimshawi]

Protein Classification

glycosyltransferase family 43 protein( domain architecture ID 10083049)

glycosyltransferase family 43 protein similar to Arabidopsis thaliana beta-1,4-xylosyltransferase IRX9H and human galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferases

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
60-281 1.91e-108

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: 314.23  E-value: 1.91e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111  60 PPLYIITPTYRRPEQLAELTRLGYTLKHVLNLLWLVIEDANRTNPLVAHTLDRIGVPYEYLVAPMPEQyklTKRAKPRGV 139
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSD---PTWLKPRGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111 140 SNRNRGLDYLRANA---TEGVLYFADDDNTYDINIFEQMRYTKKVAMWPVGLVTKTGVSSPIIRAGKLDGYYDGWIGGRK 216
Cdd:cd00218    78 EQRNLALRWIREHLsakLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWKPERP 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820302111 217 YPVDMAGFAVSVKFLHERPKAKMPF--KPGYEEDGFLRSLApLQNNEIELLADECRDILTWHTQTKK 281
Cdd:cd00218   158 FPIDMAGFAFNSKLLWDPPRAVFPYsaKRGYQESSFLEQLV-LDRKELEPLANNCSKVLVWHTRTEK 223
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
60-281 1.91e-108

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: 314.23  E-value: 1.91e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111  60 PPLYIITPTYRRPEQLAELTRLGYTLKHVLNLLWLVIEDANRTNPLVAHTLDRIGVPYEYLVAPMPEQyklTKRAKPRGV 139
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSD---PTWLKPRGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111 140 SNRNRGLDYLRANA---TEGVLYFADDDNTYDINIFEQMRYTKKVAMWPVGLVTKTGVSSPIIRAGKLDGYYDGWIGGRK 216
Cdd:cd00218    78 EQRNLALRWIREHLsakLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWKPERP 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820302111 217 YPVDMAGFAVSVKFLHERPKAKMPF--KPGYEEDGFLRSLApLQNNEIELLADECRDILTWHTQTKK 281
Cdd:cd00218   158 FPIDMAGFAFNSKLLWDPPRAVFPYsaKRGYQESSFLEQLV-LDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
81-280 1.33e-95

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 280.96  E-value: 1.33e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111  81 LGYTLKHVLNLLWLVIEDANRTNPLVAHTLDRIGVPYEYLVAPMPEQYKLTkrAKPRGVSNRNRGLDYLRANATE--GVL 158
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKPPNWT--DKPRGVHQRNVALRWIRENKHRldGVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111 159 YFADDDNTYDINIFEQMRYTKKVAMWPVGLVTKTGVSSPIIRAGKLDGYYDGWIGGRKYPVDMAGFAVSVKFLHERPKAK 238
Cdd:pfam03360  79 YFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAGFAVNSRLLWDPPEAV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1820302111 239 MPF---KPGYEEDGFLRSLApLQNNEIELLADECRDILTWHTQTK 280
Cdd:pfam03360 159 FSLdsvKRGYQESSFLEQLV-EDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
64-275 1.69e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 54.92  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111  64 IITPTYRR-PEQLAELTRLGYTLKHVLN-LLWLVIEDANRTNPlVAHTLDRIGVPYEYLVapMPEQYkltkrAKPRGV-- 139
Cdd:PLN02458  116 IVTPISTKdRYQGVLLRRLANTLRLVPPpLLWIVVEGQSDSEE-VSEMLRKTGIMYRHLV--FKENF-----TDPEAEld 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111 140 SNRNRGLDYLRANATEGVLYFADDDNTYDINIFEQMRYTKKVAMWPVGLVT----KTGVSSPIIRAGKLDGYYDGWIGG- 214
Cdd:PLN02458  188 HQRNLALRHIEHHKLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSanrnKVIIEGPVCDSSQVIGWHLKKMNNe 267
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820302111 215 --RKYPVDMAGFAVSVKFLHERPKAKMPFK-PGYEEDG--FLRSLAPLQNNEIE-LLADECRDILTW 275
Cdd:PLN02458  268 teTRPPIHISSFAFNSSILWDPERWGRPSSvQGTSQNSikFVKQVALEDETKLKgIPPEDCSKIMLW 334
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
60-281 1.91e-108

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: 314.23  E-value: 1.91e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111  60 PPLYIITPTYRRPEQLAELTRLGYTLKHVLNLLWLVIEDANRTNPLVAHTLDRIGVPYEYLVAPMPEQyklTKRAKPRGV 139
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSD---PTWLKPRGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111 140 SNRNRGLDYLRANA---TEGVLYFADDDNTYDINIFEQMRYTKKVAMWPVGLVTKTGVSSPIIRAGKLDGYYDGWIGGRK 216
Cdd:cd00218    78 EQRNLALRWIREHLsakLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWKPERP 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820302111 217 YPVDMAGFAVSVKFLHERPKAKMPF--KPGYEEDGFLRSLApLQNNEIELLADECRDILTWHTQTKK 281
Cdd:cd00218   158 FPIDMAGFAFNSKLLWDPPRAVFPYsaKRGYQESSFLEQLV-LDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
81-280 1.33e-95

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 280.96  E-value: 1.33e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111  81 LGYTLKHVLNLLWLVIEDANRTNPLVAHTLDRIGVPYEYLVAPMPEQYKLTkrAKPRGVSNRNRGLDYLRANATE--GVL 158
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKPPNWT--DKPRGVHQRNVALRWIRENKHRldGVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111 159 YFADDDNTYDINIFEQMRYTKKVAMWPVGLVTKTGVSSPIIRAGKLDGYYDGWIGGRKYPVDMAGFAVSVKFLHERPKAK 238
Cdd:pfam03360  79 YFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAGFAVNSRLLWDPPEAV 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1820302111 239 MPF---KPGYEEDGFLRSLApLQNNEIELLADECRDILTWHTQTK 280
Cdd:pfam03360 159 FSLdsvKRGYQESSFLEQLV-EDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
64-275 1.69e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 54.92  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111  64 IITPTYRR-PEQLAELTRLGYTLKHVLN-LLWLVIEDANRTNPlVAHTLDRIGVPYEYLVapMPEQYkltkrAKPRGV-- 139
Cdd:PLN02458  116 IVTPISTKdRYQGVLLRRLANTLRLVPPpLLWIVVEGQSDSEE-VSEMLRKTGIMYRHLV--FKENF-----TDPEAEld 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820302111 140 SNRNRGLDYLRANATEGVLYFADDDNTYDINIFEQMRYTKKVAMWPVGLVT----KTGVSSPIIRAGKLDGYYDGWIGG- 214
Cdd:PLN02458  188 HQRNLALRHIEHHKLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSanrnKVIIEGPVCDSSQVIGWHLKKMNNe 267
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1820302111 215 --RKYPVDMAGFAVSVKFLHERPKAKMPFK-PGYEEDG--FLRSLAPLQNNEIE-LLADECRDILTW 275
Cdd:PLN02458  268 teTRPPIHISSFAFNSSILWDPERWGRPSSvQGTSQNSikFVKQVALEDETKLKgIPPEDCSKIMLW 334
 
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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