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Conserved domains on  [gi|1835592138|ref|XP_033812818|]
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galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3 [Geotrypetes seraphini]

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 ...
76-304 4.63e-131

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: 372.40  E-value: 4.63e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138  76 PTIYAITPTYSRLVQKAELLRLSQTFLHVKNFHWIVVEDSVTKTRLVGDLLTQSGLKFTHLNVETSSDyklkqndPSWLK 155
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSD-------PTWLK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 156 PRGVEQRNLGLQWLRENRELSEEGVVYFADDDNTYSLQLFEEMRFTHQVSVWPVGLVGGLRFERPLVEKGKVVGFYTAWK 235
Cdd:cd00218    74 PRGVEQRNLALRWIREHLSAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 236 PNRPFPMDMAGFAIALQLLLANREAKFDLLVERGYLESSLLQSLVS-IEELEPKADNCSKILVWHTRTEK 304
Cdd:cd00218   154 PERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVLdRKELEPLANNCSKVLVWHTRTEK 223
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
76-304 4.63e-131

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: 372.40  E-value: 4.63e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138  76 PTIYAITPTYSRLVQKAELLRLSQTFLHVKNFHWIVVEDSVTKTRLVGDLLTQSGLKFTHLNVETSSDyklkqndPSWLK 155
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSD-------PTWLK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 156 PRGVEQRNLGLQWLRENRELSEEGVVYFADDDNTYSLQLFEEMRFTHQVSVWPVGLVGGLRFERPLVEKGKVVGFYTAWK 235
Cdd:cd00218    74 PRGVEQRNLALRWIREHLSAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 236 PNRPFPMDMAGFAIALQLLLANREAKFDLLVERGYLESSLLQSLVS-IEELEPKADNCSKILVWHTRTEK 304
Cdd:cd00218   154 PERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVLdRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
97-303 1.79e-114

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 329.49  E-value: 1.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138  97 LSQTFLHVKNFHWIVVEDSVTKTRLVGDLLTQSGLKFTHLNVETSSDyklkqndPSWL-KPRGVEQRNLGLQWLRENREl 175
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKP-------PNWTdKPRGVHQRNVALRWIRENKH- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 176 SEEGVVYFADDDNTYSLQLFEEMRFTHQVSVWPVGLVGGLRFERPLVEKGKVVGFYTAWKPNRPFPMDMAGFAIALQLLL 255
Cdd:pfam03360  73 RLDGVVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAGFAVNSRLLW 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835592138 256 ANREAKFDL-LVERGYLESSLLQSLV-SIEELEPKADNCSKILVWHTRTE 303
Cdd:pfam03360 153 DPPEAVFSLdSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
34-298 1.96e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 54.92  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138  34 THHLKSTSDLIRAKDKKISQLQN-ELKRLEAAGKSEKQPtSTLPTIYAI--TPTYSRL-VQKAELLRLSQTFLHVKN-FH 108
Cdd:PLN02458   68 PHHSNLNRTLINAQTPVPAPARSaESETASLLEKEEEEP-KLAPRRLVIivTPISTKDrYQGVLLRRLANTLRLVPPpLL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 109 WIVVEDSvTKTRLVGDLLTQSGLKFTHLnvetssdyKLKQNdpsWLKPRGV--EQRNLGLQWLRENReLSeeGVVYFADD 186
Cdd:PLN02458  147 WIVVEGQ-SDSEEVSEMLRKTGIMYRHL--------VFKEN---FTDPEAEldHQRNLALRHIEHHK-LS--GIVHFAGL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 187 DNTYSLQLFEEMRFTHQVSVWPVGLVGGLR----FERPLVEKGKVVGFYTAWKPN----RPfPMDMAGFAIALQLLLANR 258
Cdd:PLN02458  212 SNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIEGPVCDSSQVIGWHLKKMNNetetRP-PIHISSFAFNSSILWDPE 290
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1835592138 259 EAKFDLLVERGYLESSLLQSLVSIEElEPK-----ADNCSKILVW 298
Cdd:PLN02458  291 RWGRPSSVQGTSQNSIKFVKQVALED-ETKlkgipPEDCSKIMLW 334
 
Name Accession Description Interval E-value
GlcAT-I cd00218
Beta1,3-glucuronyltransferase I (GlcAT-I) is involved in the initial steps of proteoglycan ...
76-304 4.63e-131

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: 372.40  E-value: 4.63e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138  76 PTIYAITPTYSRLVQKAELLRLSQTFLHVKNFHWIVVEDSVTKTRLVGDLLTQSGLKFTHLNVETSSDyklkqndPSWLK 155
Cdd:cd00218     1 PTIYVVTPTYARPVQKAELTRLAHTLRLVPPLHWIVVEDSEEKTPLVAELLRRSGLMYTHLNAKTPSD-------PTWLK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 156 PRGVEQRNLGLQWLRENRELSEEGVVYFADDDNTYSLQLFEEMRFTHQVSVWPVGLVGGLRFERPLVEKGKVVGFYTAWK 235
Cdd:cd00218    74 PRGVEQRNLALRWIREHLSAKLDGVVYFADDDNTYDLELFEEMRKIKRVGVWPVGLVGGLRVEGPVCENGKVVGWHTAWK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 236 PNRPFPMDMAGFAIALQLLLANREAKFDLLVERGYLESSLLQSLVS-IEELEPKADNCSKILVWHTRTEK 304
Cdd:cd00218   154 PERPFPIDMAGFAFNSKLLWDPPRAVFPYSAKRGYQESSFLEQLVLdRKELEPLANNCSKVLVWHTRTEK 223
Glyco_transf_43 pfam03360
Glycosyltransferase family 43;
97-303 1.79e-114

Glycosyltransferase family 43;


Pssm-ID: 460898  Cd Length: 202  Bit Score: 329.49  E-value: 1.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138  97 LSQTFLHVKNFHWIVVEDSVTKTRLVGDLLTQSGLKFTHLNVETSSDyklkqndPSWL-KPRGVEQRNLGLQWLRENREl 175
Cdd:pfam03360   1 LAHTLRLVPPLHWIVVEDSESKTPLVANLLRRSGLPYTHLNAKKYKP-------PNWTdKPRGVHQRNVALRWIRENKH- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 176 SEEGVVYFADDDNTYSLQLFEEMRFTHQVSVWPVGLVGGLRFERPLVEKGKVVGFYTAWKPNRPFPMDMAGFAIALQLLL 255
Cdd:pfam03360  73 RLDGVVYFADDDNTYDLRLFDEMRKTKKVGVWPVGLVGGLRVEGPVCNNGKVVGWHTGWKPERPFPIDMAGFAVNSRLLW 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835592138 256 ANREAKFDL-LVERGYLESSLLQSLV-SIEELEPKADNCSKILVWHTRTE 303
Cdd:pfam03360 153 DPPEAVFSLdSVKRGYQESSFLEQLVeDESDLEPLADNCTKVLVWHTRTE 202
PLN02458 PLN02458
transferase, transferring glycosyl groups
34-298 1.96e-08

transferase, transferring glycosyl groups


Pssm-ID: 215252  Cd Length: 346  Bit Score: 54.92  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138  34 THHLKSTSDLIRAKDKKISQLQN-ELKRLEAAGKSEKQPtSTLPTIYAI--TPTYSRL-VQKAELLRLSQTFLHVKN-FH 108
Cdd:PLN02458   68 PHHSNLNRTLINAQTPVPAPARSaESETASLLEKEEEEP-KLAPRRLVIivTPISTKDrYQGVLLRRLANTLRLVPPpLL 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 109 WIVVEDSvTKTRLVGDLLTQSGLKFTHLnvetssdyKLKQNdpsWLKPRGV--EQRNLGLQWLRENReLSeeGVVYFADD 186
Cdd:PLN02458  147 WIVVEGQ-SDSEEVSEMLRKTGIMYRHL--------VFKEN---FTDPEAEldHQRNLALRHIEHHK-LS--GIVHFAGL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835592138 187 DNTYSLQLFEEMRFTHQVSVWPVGLVGGLR----FERPLVEKGKVVGFYTAWKPN----RPfPMDMAGFAIALQLLLANR 258
Cdd:PLN02458  212 SNVYDLDFFDEIRDIEVFGTWPMALLSANRnkviIEGPVCDSSQVIGWHLKKMNNetetRP-PIHISSFAFNSSILWDPE 290
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1835592138 259 EAKFDLLVERGYLESSLLQSLVSIEElEPK-----ADNCSKILVW 298
Cdd:PLN02458  291 RWGRPSSVQGTSQNSIKFVKQVALED-ETKlkgipPEDCSKIMLW 334
 
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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