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Conserved domains on  [gi|586597883|ref|NP_001275651|]
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galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 isoform 3 [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 ...
75-312 3.81e-120

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: 344.28  E-value: 3.81e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883  75 PTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlregEPGWVH 154
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883 155 PRGVEQRNKALDWLRGRGgavggekdppPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDG 234
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586597883 235 RVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLV-DPKDLEPRAANCTRSLAVSPRLE 312
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTE 222
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
75-312 3.81e-120

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: 344.28  E-value: 3.81e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883  75 PTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlregEPGWVH 154
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883 155 PRGVEQRNKALDWLRGRGgavggekdppPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDG 234
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586597883 235 RVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLV-DPKDLEPRAANCTRSLAVSPRLE 312
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTE 222
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
96-312 6.95e-99

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 289.82  E-value: 6.95e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883   96 LSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlreGEPGWVHPRGVEQRNKALDWLRgrggav 175
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYK------PPNWTDKPRGVHQRNVALRWIR------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883  176 ggEKDPPPPGtqgVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPSRPFPVDMAG 255
Cdd:pfam03360  69 --ENKHRLDG---VVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 586597883  256 FAVALPLLLDKPNAQFD-STAPRGHLESSLLSHLV-DPKDLEPRAANCTRSLAVSPRLE 312
Cdd:pfam03360 144 FAVNSRLLWDPPEAVFSlDSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
77-265 4.54e-09

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 56.84  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883  77 IYVVTPTYARL-VQKAELVRLSQTLSLV-PRLHWLLVEdAEGPTPLVSGLLAASGLLFTHLVVltpkAQRLREGEPGWVH 154
Cdd:PLN02458 114 VIIVTPISTKDrYQGVLLRRLANTLRLVpPPLLWIVVE-GQSDSEEVSEMLRKTGIMYRHLVF----KENFTDPEAELDH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883 155 prgveQRNKALDWLRGRggavggekdppppGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLR----FEGPQ 230
Cdd:PLN02458 189 -----QRNLALRHIEHH-------------KLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIEGPV 250
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 586597883 231 VQDGRVVGFH----TAWEPSRPfPVDMAGFAVALPLLLD 265
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 ...
75-312 3.81e-120

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: 344.28  E-value: 3.81e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883  75 PTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlregEPGWVH 154
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883 155 PRGVEQRNKALDWLRGRGgavggekdppPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDG 234
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586597883 235 RVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLV-DPKDLEPRAANCTRSLAVSPRLE 312
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTE 222
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
96-312 6.95e-99

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 289.82  E-value: 6.95e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883   96 LSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKaqrlreGEPGWVHPRGVEQRNKALDWLRgrggav 175
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYK------PPNWTDKPRGVHQRNVALRWIR------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883  176 ggEKDPPPPGtqgVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPSRPFPVDMAG 255
Cdd:pfam03360  69 --ENKHRLDG---VVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 586597883  256 FAVALPLLLDKPNAQFD-STAPRGHLESSLLSHLV-DPKDLEPRAANCTRSLAVSPRLE 312
Cdd:pfam03360 144 FAVNSRLLWDPPEAVFSlDSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
77-265 4.54e-09

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 56.84  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883  77 IYVVTPTYARL-VQKAELVRLSQTLSLV-PRLHWLLVEdAEGPTPLVSGLLAASGLLFTHLVVltpkAQRLREGEPGWVH 154
Cdd:PLN02458 114 VIIVTPISTKDrYQGVLLRRLANTLRLVpPPLLWIVVE-GQSDSEEVSEMLRKTGIMYRHLVF----KENFTDPEAELDH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586597883 155 prgveQRNKALDWLRGRggavggekdppppGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLR----FEGPQ 230
Cdd:PLN02458 189 -----QRNLALRHIEHH-------------KLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIEGPV 250
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 586597883 231 VQDGRVVGFH----TAWEPSRPfPVDMAGFAVALPLLLD 265
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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