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Conserved domains on  [gi|585420401|ref|NP_001275650|]
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galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 isoform 2 [Homo sapiens]

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 ...
68-306 7.06e-128

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: 364.31  E-value: 7.06e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401  68 PTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlregEPGWVH 147
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 148 PRGVEQRNKALDWLRGRGgavggekdppPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDG 227
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 228 RVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLV-DPKDLEPRAANCTRVLVWHTRTEK 306
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
68-306 7.06e-128

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: 364.31  E-value: 7.06e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401  68 PTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlregEPGWVH 147
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 148 PRGVEQRNKALDWLRGRGgavggekdppPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDG 227
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 228 RVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLV-DPKDLEPRAANCTRVLVWHTRTEK 306
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
89-305 3.10e-107

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 311.00  E-value: 3.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401   89 LSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlreGEPGWVHPRGVEQRNKALDWLRgrggav 168
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYK------PPNWTDKPRGVHQRNVALRWIR------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401  169 ggEKDPPPPGtqgVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPSRPFPVDMAG 248
Cdd:pfam03360  69 --ENKHRLDG---VVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 585420401  249 FAVALPLLLDKPNAQFD-STAPRGHLESSLLSHLV-DPKDLEPRAANCTRVLVWHTRTE 305
Cdd:pfam03360 144 FAVNSRLLWDPPEAVFSlDSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
70-258 1.38e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 55.30  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401  70 IYVVTPTYARL-VQKAELVRLSQTLSLV-PRLHWLLVEdAEGPTPLVSGLLAASGLLFTHLVVltpkAQRLREGEPGWVH 147
Cdd:PLN02458 114 VIIVTPISTKDrYQGVLLRRLANTLRLVpPPLLWIVVE-GQSDSEEVSEMLRKTGIMYRHLVF----KENFTDPEAELDH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 148 prgveQRNKALDWLRGRggavggekdppppGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLR----FEGPQ 223
Cdd:PLN02458 189 -----QRNLALRHIEHH-------------KLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIEGPV 250
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 585420401 224 VQDGRVVGFH----TAWEPSRPfPVDMAGFAVALPLLLD 258
Cdd:PLN02458 251 CDSSQVIGWHlkkmNNETETRP-PIHISSFAFNSSILWD 288
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
68-306 7.06e-128

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: 364.31  E-value: 7.06e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401  68 PTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlregEPGWVH 147
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 148 PRGVEQRNKALDWLRGRGgavggekdppPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDG 227
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 228 RVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLV-DPKDLEPRAANCTRVLVWHTRTEK 306
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
89-305 3.10e-107

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 311.00  E-value: 3.10e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401   89 LSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlreGEPGWVHPRGVEQRNKALDWLRgrggav 168
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYK------PPNWTDKPRGVHQRNVALRWIR------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401  169 ggEKDPPPPGtqgVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPSRPFPVDMAG 248
Cdd:pfam03360  69 --ENKHRLDG---VVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 585420401  249 FAVALPLLLDKPNAQFD-STAPRGHLESSLLSHLV-DPKDLEPRAANCTRVLVWHTRTE 305
Cdd:pfam03360 144 FAVNSRLLWDPPEAVFSlDSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
70-258 1.38e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 55.30  E-value: 1.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401  70 IYVVTPTYARL-VQKAELVRLSQTLSLV-PRLHWLLVEdAEGPTPLVSGLLAASGLLFTHLVVltpkAQRLREGEPGWVH 147
Cdd:PLN02458 114 VIIVTPISTKDrYQGVLLRRLANTLRLVpPPLLWIVVE-GQSDSEEVSEMLRKTGIMYRHLVF----KENFTDPEAELDH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585420401 148 prgveQRNKALDWLRGRggavggekdppppGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLR----FEGPQ 223
Cdd:PLN02458 189 -----QRNLALRHIEHH-------------KLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIEGPV 250
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 585420401 224 VQDGRVVGFH----TAWEPSRPfPVDMAGFAVALPLLLD 258
Cdd:PLN02458 251 CDSSQVIGWHlkkmNNETETRP-PIHISSFAFNSSILWD 288
 
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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