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Conserved domains on  [gi|42567736|ref|NP_196400|]
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glucuronidase 2 [Arabidopsis thaliana]

Protein Classification

glycosyl hydrolase family 79 N-terminal domain-containing protein( domain architecture ID 10508437)

glycosyl hydrolase family 79 N-terminal domain-containing protein similar to Arabidopsis thaliana heparanase-like protein 1-3, which are endoglycosidases that cleave heparan sulfate proteoglycans (HSPGs) into heparan sulfate side chains and core proteoglycans

EC:  3.2.-.-
Gene Ontology:  GO:0016798
SCOP:  4004076|4003957

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_79n pfam03662
Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or ...
29-347 0e+00

Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular micro-environment. Heparanase degrades HS at specific intra-chain sites. The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity.


:

Pssm-ID: 461010  Cd Length: 318  Bit Score: 636.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736    29 RASIVIQGARRVCETDENFVCATLDWWPHDKCNYDQCPWGYSSVINMDLTRPLLTKAIKAFKPLRIRIGGSLQDQVIYDV 108
Cdd:pfam03662   1 EGTVFVDGSTAIAETDENFICATLDWWPPEKCDYGTCSWGHASILNLDLNNPILANAIKAFSPLRIRLGGSLQDQVIYDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736   109 GNLKTPCRPFQKMNSGLFGFSKGCLHMKRWDELNSFLTATGAVVTFGLNALRGRHKLRGKAWGGAWDHINTQDFLNYTVS 188
Cdd:pfam03662  81 GDLKQPCPPFVKNSDGLFGFSQGCLPMSRWDELNAFFNKTGALVTFGLNALYGRSKDSDGVWGGPWDSSNARDFIRYTVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736   189 KGYVIDSWEFGNELSGSGVGASVSAELYGKDLIVLKDVINKVYKNSwLHKPILVAPGGFYEQQWYTKLLEISGPSVVDVV 268
Cdd:pfam03662 161 KGYKIDSWELGNELSGSGVGASVDADQYAKDVIALKNIVDDLYKNS-EPKPLVLAPGGFFDADWFTELLQKSGPGVVDVV 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42567736   269 THHIYNLGSGNDPALVKKIMDPSYLSQVSKTFKDVNQTIQEHGPWASPWVGESGGAYNSGGRHVSDTFIDSFWYLDQLG 347
Cdd:pfam03662 240 THHIYNLGPGVDPHLINKILDPSYLDQEAQTFSDLQGTIKSSGPWASAWVGEAGGAYNSGGHLVSNAFVNSFWYLDQLG 318
 
Name Accession Description Interval E-value
Glyco_hydro_79n pfam03662
Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or ...
29-347 0e+00

Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular micro-environment. Heparanase degrades HS at specific intra-chain sites. The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity.


Pssm-ID: 461010  Cd Length: 318  Bit Score: 636.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736    29 RASIVIQGARRVCETDENFVCATLDWWPHDKCNYDQCPWGYSSVINMDLTRPLLTKAIKAFKPLRIRIGGSLQDQVIYDV 108
Cdd:pfam03662   1 EGTVFVDGSTAIAETDENFICATLDWWPPEKCDYGTCSWGHASILNLDLNNPILANAIKAFSPLRIRLGGSLQDQVIYDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736   109 GNLKTPCRPFQKMNSGLFGFSKGCLHMKRWDELNSFLTATGAVVTFGLNALRGRHKLRGKAWGGAWDHINTQDFLNYTVS 188
Cdd:pfam03662  81 GDLKQPCPPFVKNSDGLFGFSQGCLPMSRWDELNAFFNKTGALVTFGLNALYGRSKDSDGVWGGPWDSSNARDFIRYTVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736   189 KGYVIDSWEFGNELSGSGVGASVSAELYGKDLIVLKDVINKVYKNSwLHKPILVAPGGFYEQQWYTKLLEISGPSVVDVV 268
Cdd:pfam03662 161 KGYKIDSWELGNELSGSGVGASVDADQYAKDVIALKNIVDDLYKNS-EPKPLVLAPGGFFDADWFTELLQKSGPGVVDVV 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42567736   269 THHIYNLGSGNDPALVKKIMDPSYLSQVSKTFKDVNQTIQEHGPWASPWVGESGGAYNSGGRHVSDTFIDSFWYLDQLG 347
Cdd:pfam03662 240 THHIYNLGPGVDPHLINKILDPSYLDQEAQTFSDLQGTIKSSGPWASAWVGEAGGAYNSGGHLVSNAFVNSFWYLDQLG 318
 
Name Accession Description Interval E-value
Glyco_hydro_79n pfam03662
Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or ...
29-347 0e+00

Glycosyl hydrolase family 79, N-terminal domain; Family of endo-beta-N-glucuronidase, or heparanase. Heparan sulfate proteoglycans (HSPGs) play a key role in the self- assembly, insolubility and barrier properties of basement membranes and extracellular matrices. Hence, cleavage of heparan sulfate (HS) affects the integrity and functional state of tissues and thereby fundamental normal and pathological phenomena involving cell migration and response to changes in the extracellular micro-environment. Heparanase degrades HS at specific intra-chain sites. The enzyme is synthesized as a latent approximately 65 kDa protein that is processed at the N-terminus into a highly active approximately 50 kDa form. Experimental evidence suggests that heparanase may facilitate both tumour cell invasion and neovascularization, both critical steps in cancer progression. The enzyme is also involved in cell migration associated with inflammation and autoimmunity.


Pssm-ID: 461010  Cd Length: 318  Bit Score: 636.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736    29 RASIVIQGARRVCETDENFVCATLDWWPHDKCNYDQCPWGYSSVINMDLTRPLLTKAIKAFKPLRIRIGGSLQDQVIYDV 108
Cdd:pfam03662   1 EGTVFVDGSTAIAETDENFICATLDWWPPEKCDYGTCSWGHASILNLDLNNPILANAIKAFSPLRIRLGGSLQDQVIYDV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736   109 GNLKTPCRPFQKMNSGLFGFSKGCLHMKRWDELNSFLTATGAVVTFGLNALRGRHKLRGKAWGGAWDHINTQDFLNYTVS 188
Cdd:pfam03662  81 GDLKQPCPPFVKNSDGLFGFSQGCLPMSRWDELNAFFNKTGALVTFGLNALYGRSKDSDGVWGGPWDSSNARDFIRYTVS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42567736   189 KGYVIDSWEFGNELSGSGVGASVSAELYGKDLIVLKDVINKVYKNSwLHKPILVAPGGFYEQQWYTKLLEISGPSVVDVV 268
Cdd:pfam03662 161 KGYKIDSWELGNELSGSGVGASVDADQYAKDVIALKNIVDDLYKNS-EPKPLVLAPGGFFDADWFTELLQKSGPGVVDVV 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42567736   269 THHIYNLGSGNDPALVKKIMDPSYLSQVSKTFKDVNQTIQEHGPWASPWVGESGGAYNSGGRHVSDTFIDSFWYLDQLG 347
Cdd:pfam03662 240 THHIYNLGPGVDPHLINKILDPSYLDQEAQTFSDLQGTIKSSGPWASAWVGEAGGAYNSGGHLVSNAFVNSFWYLDQLG 318
 
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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