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Conserved domains on  [gi|15240245|ref|NP_201524|]
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Nucleotide-diphospho-sugar transferases superfamily protein [Arabidopsis thaliana]

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 ...
152-418 6.04e-84

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: 258.38  E-value: 6.04e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 152 RTVIVVTPTYVRTFQALHLTGVMHSLMLVPyDLVWIVVE-AGGITNETASFIAKSGLKTIHLGFD------QKMPNTWED 224
Cdd:cd00218   1 PTIYVVTPTYARPVQKAELTRLAHTLRLVP-PLHWIVVEdSEEKTPLVAELLRRSGLMYTHLNAKtpsdptWLKPRGVEQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 225 RHKLETKMRLHAlrvvrEKKLDGIVMFADDSNMHSMELFDEIQTVKWFGALSVGILAHsgnadelssilkneqgknkekp 304
Cdd:cd00218  80 RNLALRWIREHL-----SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGG---------------------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 305 sMPIQGPSCNSSeKLVGWHIFNTqpyakktavyidekaPVMPSKMEWSGFVLNSRLLWkesldDKPAWVKDLSlLDDGYA 384
Cdd:cd00218 133 -LRVEGPVCENG-KVVGWHTAWK---------------PERPFPIDMAGFAFNSKLLW-----DPPRAVFPYS-AKRGYQ 189
                       250       260       270
                ....*....|....*....|....*....|....
gi 15240245 385 EIESPLSLVKDPSMVEPLGSCGRRVLLWWLRVEA 418
Cdd:cd00218 190 ESSFLEQLVLDRKELEPLANNCSKVLVWHTRTEK 223
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
152-418 6.04e-84

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: 258.38  E-value: 6.04e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 152 RTVIVVTPTYVRTFQALHLTGVMHSLMLVPyDLVWIVVE-AGGITNETASFIAKSGLKTIHLGFD------QKMPNTWED 224
Cdd:cd00218   1 PTIYVVTPTYARPVQKAELTRLAHTLRLVP-PLHWIVVEdSEEKTPLVAELLRRSGLMYTHLNAKtpsdptWLKPRGVEQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 225 RHKLETKMRLHAlrvvrEKKLDGIVMFADDSNMHSMELFDEIQTVKWFGALSVGILAHsgnadelssilkneqgknkekp 304
Cdd:cd00218  80 RNLALRWIREHL-----SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGG---------------------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 305 sMPIQGPSCNSSeKLVGWHIFNTqpyakktavyidekaPVMPSKMEWSGFVLNSRLLWkesldDKPAWVKDLSlLDDGYA 384
Cdd:cd00218 133 -LRVEGPVCENG-KVVGWHTAWK---------------PERPFPIDMAGFAFNSKLLW-----DPPRAVFPYS-AKRGYQ 189
                       250       260       270
                ....*....|....*....|....*....|....
gi 15240245 385 EIESPLSLVKDPSMVEPLGSCGRRVLLWWLRVEA 418
Cdd:cd00218 190 ESSFLEQLVLDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
173-417 1.86e-71

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 225.49  E-value: 1.86e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245   173 VMHSLMLVPyDLVWIVVEAG-GITNETASFIAKSGLKTIHLGFDQKMPNTWEDRHKlETKMRLHALRVVRE--KKLDGIV 249
Cdd:pfam03360   1 LAHTLRLVP-PLHWIVVEDSeSKTPLVANLLRRSGLPYTHLNAKKYKPPNWTDKPR-GVHQRNVALRWIREnkHRLDGVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245   250 MFADDSNMHSMELFDEIQTVKWFGALSVGILAHSgnadelssilkneqgknkekpsmPIQGPSCNSSeKLVGWHifntqp 329
Cdd:pfam03360  79 YFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGL-----------------------RVEGPVCNNG-KVVGWH------ 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245   330 yakktavyiDEKAPVMPSKMEWSGFVLNSRLLWkesldDKPAWVKDLSLLDDGYAEIESPLSLVKDPSMVEPLGSCGRRV 409
Cdd:pfam03360 129 ---------TGWKPERPFPIDMAGFAVNSRLLW-----DPPEAVFSLDSVKRGYQESSFLEQLVEDESDLEPLADNCTKV 194

                  ....*...
gi 15240245   410 LLWWLRVE 417
Cdd:pfam03360 195 LVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
152-377 2.64e-19

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 89.20  E-value: 2.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245  152 RTVIVVTPTYVRT-FQALHLTGVMHSLMLVPYDLVWIVVEAGGITNETASFIAKSGLKTIHLGFDQkmpNTWEDRHKLET 230
Cdd:PLN02458 112 RLVIIVTPISTKDrYQGVLLRRLANTLRLVPPPLLWIVVEGQSDSEEVSEMLRKTGIMYRHLVFKE---NFTDPEAELDH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245  231 KMRLhALRVVREKKLDGIVMFADDSNMHSMELFDEIQTVKWFGALSVGILAhsgnadelssilkneqgKNKEKpsMPIQG 310
Cdd:PLN02458 189 QRNL-ALRHIEHHKLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLS-----------------ANRNK--VIIEG 248
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240245  311 PSCNSSEkLVGWHIfntqpyaKKTAVYIDEKAPVmpskmEWSGFVLNSRLLWKESLDDKPAWVKDLS 377
Cdd:PLN02458 249 PVCDSSQ-VIGWHL-------KKMNNETETRPPI-----HISSFAFNSSILWDPERWGRPSSVQGTS 302
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
152-418 6.04e-84

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: 258.38  E-value: 6.04e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 152 RTVIVVTPTYVRTFQALHLTGVMHSLMLVPyDLVWIVVE-AGGITNETASFIAKSGLKTIHLGFD------QKMPNTWED 224
Cdd:cd00218   1 PTIYVVTPTYARPVQKAELTRLAHTLRLVP-PLHWIVVEdSEEKTPLVAELLRRSGLMYTHLNAKtpsdptWLKPRGVEQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 225 RHKLETKMRLHAlrvvrEKKLDGIVMFADDSNMHSMELFDEIQTVKWFGALSVGILAHsgnadelssilkneqgknkekp 304
Cdd:cd00218  80 RNLALRWIREHL-----SAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGG---------------------- 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245 305 sMPIQGPSCNSSeKLVGWHIFNTqpyakktavyidekaPVMPSKMEWSGFVLNSRLLWkesldDKPAWVKDLSlLDDGYA 384
Cdd:cd00218 133 -LRVEGPVCENG-KVVGWHTAWK---------------PERPFPIDMAGFAFNSKLLW-----DPPRAVFPYS-AKRGYQ 189
                       250       260       270
                ....*....|....*....|....*....|....
gi 15240245 385 EIESPLSLVKDPSMVEPLGSCGRRVLLWWLRVEA 418
Cdd:cd00218 190 ESSFLEQLVLDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
173-417 1.86e-71

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 225.49  E-value: 1.86e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245   173 VMHSLMLVPyDLVWIVVEAG-GITNETASFIAKSGLKTIHLGFDQKMPNTWEDRHKlETKMRLHALRVVRE--KKLDGIV 249
Cdd:pfam03360   1 LAHTLRLVP-PLHWIVVEDSeSKTPLVANLLRRSGLPYTHLNAKKYKPPNWTDKPR-GVHQRNVALRWIREnkHRLDGVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245   250 MFADDSNMHSMELFDEIQTVKWFGALSVGILAHSgnadelssilkneqgknkekpsmPIQGPSCNSSeKLVGWHifntqp 329
Cdd:pfam03360  79 YFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGL-----------------------RVEGPVCNNG-KVVGWH------ 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245   330 yakktavyiDEKAPVMPSKMEWSGFVLNSRLLWkesldDKPAWVKDLSLLDDGYAEIESPLSLVKDPSMVEPLGSCGRRV 409
Cdd:pfam03360 129 ---------TGWKPERPFPIDMAGFAVNSRLLW-----DPPEAVFSLDSVKRGYQESSFLEQLVEDESDLEPLADNCTKV 194

                  ....*...
gi 15240245   410 LLWWLRVE 417
Cdd:pfam03360 195 LVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
152-377 2.64e-19

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 89.20  E-value: 2.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245  152 RTVIVVTPTYVRT-FQALHLTGVMHSLMLVPYDLVWIVVEAGGITNETASFIAKSGLKTIHLGFDQkmpNTWEDRHKLET 230
Cdd:PLN02458 112 RLVIIVTPISTKDrYQGVLLRRLANTLRLVPPPLLWIVVEGQSDSEEVSEMLRKTGIMYRHLVFKE---NFTDPEAELDH 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15240245  231 KMRLhALRVVREKKLDGIVMFADDSNMHSMELFDEIQTVKWFGALSVGILAhsgnadelssilkneqgKNKEKpsMPIQG 310
Cdd:PLN02458 189 QRNL-ALRHIEHHKLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLS-----------------ANRNK--VIIEG 248
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15240245  311 PSCNSSEkLVGWHIfntqpyaKKTAVYIDEKAPVmpskmEWSGFVLNSRLLWKESLDDKPAWVKDLS 377
Cdd:PLN02458 249 PVCDSSQ-VIGWHL-------KKMNNETETRPPI-----HISSFAFNSSILWDPERWGRPSSVQGTS 302
 
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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