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Conserved domains on  [gi|332192731|gb|AEE30852|]
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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 ...
141-372 2.15e-117

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: 340.43  E-value: 2.15e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 141 KLLIVVTPTYNRAMQAYYLNRVAQTLRLVEsPVLWIVVE-GNVASFETSEILRKTGVMYRHLVCKRN--MTSIKDRGVHQ 217
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVP-PLHWIVVEdSEEKTPLVAELLRRSGLMYTHLNAKTPsdPTWLKPRGVEQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 218 RNTALEHIELH---KLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAqsknKAILEGPVCNGSQVIGWHTNEKSk 294
Cdd:cd00218   80 RNLALRWIREHlsaKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVG----GLRVEGPVCENGKVVGWHTAWKP- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332192731 295 rLRRFHVDMSGFAFNSTILWDPKRWRRPFShptrqldtVKEGFQETSFIEQVVADESEMEGVPPACSSILNWHLHLDA 372
Cdd:cd00218  155 -ERPFPIDMAGFAFNSKLLWDPPRAVFPYS--------AKRGYQESSFLEQLVLDRKELEPLANNCSKVLVWHTRTEK 223
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
141-372 2.15e-117

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: 340.43  E-value: 2.15e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 141 KLLIVVTPTYNRAMQAYYLNRVAQTLRLVEsPVLWIVVE-GNVASFETSEILRKTGVMYRHLVCKRN--MTSIKDRGVHQ 217
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVP-PLHWIVVEdSEEKTPLVAELLRRSGLMYTHLNAKTPsdPTWLKPRGVEQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 218 RNTALEHIELH---KLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAqsknKAILEGPVCNGSQVIGWHTNEKSk 294
Cdd:cd00218   80 RNLALRWIREHlsaKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVG----GLRVEGPVCENGKVVGWHTAWKP- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332192731 295 rLRRFHVDMSGFAFNSTILWDPKRWRRPFShptrqldtVKEGFQETSFIEQVVADESEMEGVPPACSSILNWHLHLDA 372
Cdd:cd00218  155 -ERPFPIDMAGFAFNSKLLWDPPRAVFPYS--------AKRGYQESSFLEQLVLDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
162-370 5.05e-101

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 297.91  E-value: 5.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731  162 VAQTLRLVeSPVLWIVVE-GNVASFETSEILRKTGVMYRHLVCKRNM---TSIKDRGVHQRNTALEHIEL--HKLDGIVY 235
Cdd:pfam03360   1 LAHTLRLV-PPLHWIVVEdSESKTPLVANLLRRSGLPYTHLNAKKYKppnWTDKPRGVHQRNVALRWIREnkHRLDGVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731  236 FADDDNIYSLELFQSLRQISRFGTWPVAMLAQSknkaILEGPVCNGSQVIGWHTNEKSKrlRRFHVDMSGFAFNSTILWD 315
Cdd:pfam03360  80 FADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGL----RVEGPVCNNGKVVGWHTGWKPE--RPFPIDMAGFAVNSRLLWD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332192731  316 PKRWRRPfshptrqLDTVKEGFQETSFIEQVVADESEMEGVPPACSSILNWHLHL 370
Cdd:pfam03360 154 PPEAVFS-------LDSVKRGYQESSFLEQLVEDESDLEPLADNCTKVLVWHTRT 201
PLN02458 PLN02458
transferase, transferring glycosyl groups
62-370 2.57e-90

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 276.02  E-value: 2.57e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731  62 WRRPFYQFLVFFLLGFVLGLTPFGKME----DVNGSDRFSFEIK-------QPYVEERLENRK--REEAAVDAVSFVAET 128
Cdd:PLN02458  14 WKKAVVHFSLCFVMGFFTGFAPAGKASffssHEAASNKSQFSPQpvemlhvATTPHHSNLNRTliNAQTPVPAPARSAES 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 129 E------NGKKEVNFVPKKLLIVVTPTYNR-AMQAYYLNRVAQTLRLVESPVLWIVVEGNVASFETSEILRKTGVMYRHL 201
Cdd:PLN02458  94 EtaslleKEEEEPKLAPRRLVIIVTPISTKdRYQGVLLRRLANTLRLVPPPLLWIVVEGQSDSEEVSEMLRKTGIMYRHL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 202 VCKRNMTSIKDRGVHQRNTALEHIELHKLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAQSKNKAILEGPVCNG 281
Cdd:PLN02458 174 VFKENFTDPEAELDHQRNLALRHIEHHKLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRNKVIIEGPVCDS 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 282 SQVIGWH----TNEKSKRLRrfhVDMSGFAFNSTILWDPKRWRRPFSHPTRQLDTVKegfqetsFIEQVV-ADESEMEGV 356
Cdd:PLN02458 254 SQVIGWHlkkmNNETETRPP---IHISSFAFNSSILWDPERWGRPSSVQGTSQNSIK-------FVKQVAlEDETKLKGI 323
                        330
                 ....*....|....*
gi 332192731 357 PPA-CSSILNWHLHL 370
Cdd:PLN02458 324 PPEdCSKIMLWRLNF 338
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
141-372 2.15e-117

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: 340.43  E-value: 2.15e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 141 KLLIVVTPTYNRAMQAYYLNRVAQTLRLVEsPVLWIVVE-GNVASFETSEILRKTGVMYRHLVCKRN--MTSIKDRGVHQ 217
Cdd:cd00218    1 PTIYVVTPTYARPVQKAELTRLAHTLRLVP-PLHWIVVEdSEEKTPLVAELLRRSGLMYTHLNAKTPsdPTWLKPRGVEQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 218 RNTALEHIELH---KLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAqsknKAILEGPVCNGSQVIGWHTNEKSk 294
Cdd:cd00218   80 RNLALRWIREHlsaKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVG----GLRVEGPVCENGKVVGWHTAWKP- 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332192731 295 rLRRFHVDMSGFAFNSTILWDPKRWRRPFShptrqldtVKEGFQETSFIEQVVADESEMEGVPPACSSILNWHLHLDA 372
Cdd:cd00218  155 -ERPFPIDMAGFAFNSKLLWDPPRAVFPYS--------AKRGYQESSFLEQLVLDRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
162-370 5.05e-101

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 297.91  E-value: 5.05e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731  162 VAQTLRLVeSPVLWIVVE-GNVASFETSEILRKTGVMYRHLVCKRNM---TSIKDRGVHQRNTALEHIEL--HKLDGIVY 235
Cdd:pfam03360   1 LAHTLRLV-PPLHWIVVEdSESKTPLVANLLRRSGLPYTHLNAKKYKppnWTDKPRGVHQRNVALRWIREnkHRLDGVVY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731  236 FADDDNIYSLELFQSLRQISRFGTWPVAMLAQSknkaILEGPVCNGSQVIGWHTNEKSKrlRRFHVDMSGFAFNSTILWD 315
Cdd:pfam03360  80 FADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGL----RVEGPVCNNGKVVGWHTGWKPE--RPFPIDMAGFAVNSRLLWD 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 332192731  316 PKRWRRPfshptrqLDTVKEGFQETSFIEQVVADESEMEGVPPACSSILNWHLHL 370
Cdd:pfam03360 154 PPEAVFS-------LDSVKRGYQESSFLEQLVEDESDLEPLADNCTKVLVWHTRT 201
PLN02458 PLN02458
transferase, transferring glycosyl groups
62-370 2.57e-90

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 276.02  E-value: 2.57e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731  62 WRRPFYQFLVFFLLGFVLGLTPFGKME----DVNGSDRFSFEIK-------QPYVEERLENRK--REEAAVDAVSFVAET 128
Cdd:PLN02458  14 WKKAVVHFSLCFVMGFFTGFAPAGKASffssHEAASNKSQFSPQpvemlhvATTPHHSNLNRTliNAQTPVPAPARSAES 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 129 E------NGKKEVNFVPKKLLIVVTPTYNR-AMQAYYLNRVAQTLRLVESPVLWIVVEGNVASFETSEILRKTGVMYRHL 201
Cdd:PLN02458  94 EtaslleKEEEEPKLAPRRLVIIVTPISTKdRYQGVLLRRLANTLRLVPPPLLWIVVEGQSDSEEVSEMLRKTGIMYRHL 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 202 VCKRNMTSIKDRGVHQRNTALEHIELHKLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAQSKNKAILEGPVCNG 281
Cdd:PLN02458 174 VFKENFTDPEAELDHQRNLALRHIEHHKLSGIVHFAGLSNVYDLDFFDEIRDIEVFGTWPMALLSANRNKVIIEGPVCDS 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332192731 282 SQVIGWH----TNEKSKRLRrfhVDMSGFAFNSTILWDPKRWRRPFSHPTRQLDTVKegfqetsFIEQVV-ADESEMEGV 356
Cdd:PLN02458 254 SQVIGWHlkkmNNETETRPP---IHISSFAFNSSILWDPERWGRPSSVQGTSQNSIK-------FVKQVAlEDETKLKGI 323
                        330
                 ....*....|....*
gi 332192731 357 PPA-CSSILNWHLHL 370
Cdd:PLN02458 324 PPEdCSKIMLWRLNF 338
 
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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