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Conserved domains on  [gi|189491871|ref|NP_001121656|]
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galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 [Rattus norvegicus]

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 ...
75-313 2.89e-125

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: 358.15  E-value: 2.89e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871  75 PTIYVITPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPKaqrlregEPGWVR 154
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 155 PRGVEQRNKALDWLRGKGgavggekdspPPGTQGVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLRFEGPRVQDG 234
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 235 RVVGFHTAWEPNRPFPLDMAGFAVSLPLLLAKPNAQFDATAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTEK 313
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 ...
75-313 2.89e-125

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: 358.15  E-value: 2.89e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871  75 PTIYVITPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPKaqrlregEPGWVR 154
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 155 PRGVEQRNKALDWLRGKGgavggekdspPPGTQGVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLRFEGPRVQDG 234
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 235 RVVGFHTAWEPNRPFPLDMAGFAVSLPLLLAKPNAQFDATAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTEK 313
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
96-312 1.59e-107

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 312.16  E-value: 1.59e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871   96 LSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPKaqrlreGEPGWVRPRGVEQRNKALDWLRgkggav 175
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYK------PPNWTDKPRGVHQRNVALRWIR------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871  176 ggEKDSPPPGtqgVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLRFEGPRVQDGRVVGFHTAWEPNRPFPLDMAG 255
Cdd:pfam03360  69 --ENKHRLDG---VVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 189491871  256 FAVSLPLLLAKPNAQFDA-TAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTE 312
Cdd:pfam03360 144 FAVNSRLLWDPPEAVFSLdSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
77-263 3.00e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 54.53  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871  77 IYVITPTYARL-VQKAELVRLSQTLSLVPR-LHWLLVEdAESPTPLVSGLLAASGLLFTHLAV---LTPKAQRLREgepg 151
Cdd:PLN02458 114 VIIVTPISTKDrYQGVLLRRLANTLRLVPPpLLWIVVE-GQSDSEEVSEMLRKTGIMYRHLVFkenFTDPEAELDH---- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 152 wvrprgveQRNKALDWLrgkggavggEKDSpppgTQGVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLR----FE 227
Cdd:PLN02458 189 --------QRNLALRHI---------EHHK----LSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIE 247
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 189491871 228 GPRVQDGRVVGFHTAWEPN----RPfPLDMAGFAVSLPLL 263
Cdd:PLN02458 248 GPVCDSSQVIGWHLKKMNNetetRP-PIHISSFAFNSSIL 286
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
75-313 2.89e-125

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: 358.15  E-value: 2.89e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871  75 PTIYVITPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPKaqrlregEPGWVR 154
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPS-------DPTWLK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 155 PRGVEQRNKALDWLRGKGgavggekdspPPGTQGVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLRFEGPRVQDG 234
Cdd:cd00218   74 PRGVEQRNLALRWIREHL----------SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 235 RVVGFHTAWEPNRPFPLDMAGFAVSLPLLLAKPNAQFDATAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTEK 313
Cdd:cd00218  144 KVVGWHTAWKPERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVlDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
96-312 1.59e-107

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 312.16  E-value: 1.59e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871   96 LSQTLSLVPRLHWLLVEDAESPTPLVSGLLAASGLLFTHLAVLTPKaqrlreGEPGWVRPRGVEQRNKALDWLRgkggav 175
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYK------PPNWTDKPRGVHQRNVALRWIR------ 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871  176 ggEKDSPPPGtqgVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLRFEGPRVQDGRVVGFHTAWEPNRPFPLDMAG 255
Cdd:pfam03360  69 --ENKHRLDG---VVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAG 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 189491871  256 FAVSLPLLLAKPNAQFDA-TAPRGHLESSLLSHLV-DPKDLEPRAANCTQVLVWHTRTE 312
Cdd:pfam03360 144 FAVNSRLLWDPPEAVFSLdSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
77-263 3.00e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 54.53  E-value: 3.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871  77 IYVITPTYARL-VQKAELVRLSQTLSLVPR-LHWLLVEdAESPTPLVSGLLAASGLLFTHLAV---LTPKAQRLREgepg 151
Cdd:PLN02458 114 VIIVTPISTKDrYQGVLLRRLANTLRLVPPpLLWIVVE-GQSDSEEVSEMLRKTGIMYRHLVFkenFTDPEAELDH---- 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 189491871 152 wvrprgveQRNKALDWLrgkggavggEKDSpppgTQGVVYFADDDNTYSRELFKEMRWTRGVSVWPVGLVGGLR----FE 227
Cdd:PLN02458 189 --------QRNLALRHI---------EHHK----LSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIE 247
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 189491871 228 GPRVQDGRVVGFHTAWEPN----RPfPLDMAGFAVSLPLL 263
Cdd:PLN02458 248 GPVCDSSQVIGWHLKKMNNetetRP-PIHISSFAFNSSIL 286
 
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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