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Conserved domains on  [gi|1238885738|ref|XP_022255368|]
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galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase S-like [Limulus polyphemus]

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 ...
55-272 5.07e-105

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: 305.37  E-value: 5.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738  55 PIIYIVTPTYKRAAQMADMTRLAQTLQLVPSIHWIVVEDSENLTQPVSNLLRRTGVPFTHLCSKKPKNKTNPTSgRGVAN 134
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSDPTWLKP-RGVEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738 135 RMKAIEWLRNSSI--NDGVLYFADDDNSYDVRIFEEMRWTKKASVWPVGLASKYSISSPILKDGKVIGFHDGFKRSRLFA 212
Cdd:cd00218    80 RNLALRWIREHLSakLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWKPERPFP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238885738 213 VDMAGFAVSIRLLKQSKNPSMPYRL--GHLEDGFLKSLKIKMRDLEPKAANCTEVLVWHTKT 272
Cdd:cd00218   160 IDMAGFAFNSKLLWDPPRAVFPYSAkrGYQESSFLEQLVLDRKELEPLANNCSKVLVWHTRT 221
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
55-272 5.07e-105

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: 305.37  E-value: 5.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738  55 PIIYIVTPTYKRAAQMADMTRLAQTLQLVPSIHWIVVEDSENLTQPVSNLLRRTGVPFTHLCSKKPKNKTNPTSgRGVAN 134
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSDPTWLKP-RGVEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738 135 RMKAIEWLRNSSI--NDGVLYFADDDNSYDVRIFEEMRWTKKASVWPVGLASKYSISSPILKDGKVIGFHDGFKRSRLFA 212
Cdd:cd00218    80 RNLALRWIREHLSakLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWKPERPFP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238885738 213 VDMAGFAVSIRLLKQSKNPSMPYRL--GHLEDGFLKSLKIKMRDLEPKAANCTEVLVWHTKT 272
Cdd:cd00218   160 IDMAGFAFNSKLLWDPPRAVFPYSAkrGYQESSFLEQLVLDRKELEPLANNCSKVLVWHTRT 221
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
76-272 6.85e-103

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 299.06  E-value: 6.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738  76 LAQTLQLVPSIHWIVVEDSENLTQPVSNLLRRTGVPFTHLCSKKPKNKTNPTSGRGVANRMKAIEWLR-NSSINDGVLYF 154
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKPPNWTDKPRGVHQRNVALRWIReNKHRLDGVVYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738 155 ADDDNSYDVRIFEEMRWTKKASVWPVGLASKYSISSPILKDGKVIGFHDGFKRSRLFAVDMAGFAVSIRLLKQSKNPSMP 234
Cdd:pfam03360  81 ADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAGFAVNSRLLWDPPEAVFS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1238885738 235 YRL---GHLEDGFLKSLKIKMRDLEPKAANCTEVLVWHTKT 272
Cdd:pfam03360 161 LDSvkrGYQESSFLEQLVEDESDLEPLADNCTKVLVWHTRT 201
PLN02458 PLN02458
transferase, transferring glycosyl groups
56-202 4.41e-16

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 77.64  E-value: 4.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738  56 IIYIVTPT-YKRAAQMADMTRLAQTLQLV-PSIHWIVVEDSENlTQPVSNLLRRTGVPFTHLCSKkpKNKTNPTS----G 129
Cdd:PLN02458  113 LVIIVTPIsTKDRYQGVLLRRLANTLRLVpPPLLWIVVEGQSD-SEEVSEMLRKTGIMYRHLVFK--ENFTDPEAeldhQ 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238885738 130 RGVAnrMKAIEWLRNSsindGVLYFADDDNSYDVRIFEEMRWTKKASVWPVGLAS----KYSISSPILKDGKVIGFH 202
Cdd:PLN02458  190 RNLA--LRHIEHHKLS----GIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSanrnKVIIEGPVCDSSQVIGWH 260
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
55-272 5.07e-105

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: 305.37  E-value: 5.07e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738  55 PIIYIVTPTYKRAAQMADMTRLAQTLQLVPSIHWIVVEDSENLTQPVSNLLRRTGVPFTHLCSKKPKNKTNPTSgRGVAN 134
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSDPTWLKP-RGVEQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738 135 RMKAIEWLRNSSI--NDGVLYFADDDNSYDVRIFEEMRWTKKASVWPVGLASKYSISSPILKDGKVIGFHDGFKRSRLFA 212
Cdd:cd00218    80 RNLALRWIREHLSakLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWKPERPFP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1238885738 213 VDMAGFAVSIRLLKQSKNPSMPYRL--GHLEDGFLKSLKIKMRDLEPKAANCTEVLVWHTKT 272
Cdd:cd00218   160 IDMAGFAFNSKLLWDPPRAVFPYSAkrGYQESSFLEQLVLDRKELEPLANNCSKVLVWHTRT 221
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
76-272 6.85e-103

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 299.06  E-value: 6.85e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738  76 LAQTLQLVPSIHWIVVEDSENLTQPVSNLLRRTGVPFTHLCSKKPKNKTNPTSGRGVANRMKAIEWLR-NSSINDGVLYF 154
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKPPNWTDKPRGVHQRNVALRWIReNKHRLDGVVYF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738 155 ADDDNSYDVRIFEEMRWTKKASVWPVGLASKYSISSPILKDGKVIGFHDGFKRSRLFAVDMAGFAVSIRLLKQSKNPSMP 234
Cdd:pfam03360  81 ADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAGFAVNSRLLWDPPEAVFS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1238885738 235 YRL---GHLEDGFLKSLKIKMRDLEPKAANCTEVLVWHTKT 272
Cdd:pfam03360 161 LDSvkrGYQESSFLEQLVEDESDLEPLADNCTKVLVWHTRT 201
PLN02458 PLN02458
transferase, transferring glycosyl groups
56-202 4.41e-16

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 77.64  E-value: 4.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238885738  56 IIYIVTPT-YKRAAQMADMTRLAQTLQLV-PSIHWIVVEDSENlTQPVSNLLRRTGVPFTHLCSKkpKNKTNPTS----G 129
Cdd:PLN02458  113 LVIIVTPIsTKDRYQGVLLRRLANTLRLVpPPLLWIVVEGQSD-SEEVSEMLRKTGIMYRHLVFK--ENFTDPEAeldhQ 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1238885738 130 RGVAnrMKAIEWLRNSsindGVLYFADDDNSYDVRIFEEMRWTKKASVWPVGLAS----KYSISSPILKDGKVIGFH 202
Cdd:PLN02458  190 RNLA--LRHIEHHKLS----GIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSanrnKVIIEGPVCDSSQVIGWH 260
 
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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