| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.010G059600.2 |
| Family | GH79 |
| Protein Properties | Length: 452 Molecular Weight: 49590.8 Isoelectric Point: 8.074 |
| Chromosome | Chromosome/Scaffold: 10 Start: 7116045 End: 7119260 |
| Description | glucuronidase 3 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH79 | 46 | 417 | 0 |
| DDDFVCATLDWWPPEKCDYGTCSWGLAGLLNLDLNNNIFLNAVKAFSPLKIRLGGSLQDKVIYGTDDNQEPCTSFVKDPSEMFGFTKGCLPMKRWDELNA FFAKAGAKIIVGLNALAGKSIKPGGSAVGAWNYTNAESFIRYTVEKNYKIHGWELGNELSGNGVGTRIAVNQYAADTAALQRIVQKIYKDVDLKPLIIAP GGFYESKWFKEFIDKTTTSLDVVTHHIYNLGPGVDTHLIEKILNPSVLDGISGTFSGLHNVIKSSATKAIAWVGEAGGAYNSGRNLVTNAFVFSFWYLDQ LGMASKYDTKTYCRQSLIGGNYGLLDTSTFVPNPDYYSALLWHRLMGRNVLSTSFDGTKKIRSYTHCAKQSV | |||
| Full Sequence |
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| Protein Sequence Length: 452 Download |
| MGFCFWVCFG YSLLFVSLQA VAAAEGDAIV EGTVYIDGKA PIGIIDDDFV CATLDWWPPE 60 KCDYGTCSWG LAGLLNLDLN NNIFLNAVKA FSPLKIRLGG SLQDKVIYGT DDNQEPCTSF 120 VKDPSEMFGF TKGCLPMKRW DELNAFFAKA GAKIIVGLNA LAGKSIKPGG SAVGAWNYTN 180 AESFIRYTVE KNYKIHGWEL GNELSGNGVG TRIAVNQYAA DTAALQRIVQ KIYKDVDLKP 240 LIIAPGGFYE SKWFKEFIDK TTTSLDVVTH HIYNLGPGVD THLIEKILNP SVLDGISGTF 300 SGLHNVIKSS ATKAIAWVGE AGGAYNSGRN LVTNAFVFSF WYLDQLGMAS KYDTKTYCRQ 360 SLIGGNYGLL DTSTFVPNPD YYSALLWHRL MGRNVLSTSF DGTKKIRSYT HCAKQSVSLI 420 PQLCSRKASW YYLSTLTKAL LSKLNLHSIV Q* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 0 | 30 | 347 | 319 | + 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 synthesised 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. | ||
| Gene Ontology | |
|---|---|
| GO Term | Description |
| GO:0016020 | membrane |
| GO:0016798 | hydrolase activity, acting on glycosyl bonds |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAN81917.1 | 0 | 1 | 416 | 8 | 421 | hypothetical protein [Vitis vinifera] |
| EMBL | CBI25561.1 | 0 | 1 | 416 | 1 | 414 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002263173.1 | 0 | 1 | 416 | 12 | 425 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002324603.1 | 0 | 32 | 416 | 1 | 385 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002331013.1 | 0 | 1 | 416 | 1 | 411 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vo0_A | 0.000000008 | 141 | 387 | 122 | 357 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
| PDB | 3vnz_A | 0.000000008 | 141 | 387 | 122 | 357 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
| PDB | 3vny_A | 0.000000008 | 141 | 387 | 122 | 357 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
