| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna30784.1-v1.0-hybrid |
| Family | GH79 |
| Protein Properties | Length: 560 Molecular Weight: 62002.6 Isoelectric Point: 7.6986 |
| Chromosome | Chromosome/Scaffold: 1 Start: 2920131 End: 2922800 |
| Description | glucuronidase 3 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| GH79 | 54 | 552 | 0 |
| DEDFICATLDWWPPEKCDYGTCSWGKTSLLNLDLSNTILSNAIKAFSPLKLRLGGTLQDQIIYDTEDNKKPCPPIPFVENNTTLFGEMFGFNEACLPMKR WDELNSFFLRTGAKIVFGLNVLTGKTFKNNIPAIGDWDFTNAESFIRYTVKNNYSVAGWELGNELCGKGVGTSISASQYANDSASLRNIVQEIYKGGAGP KPLILAPGGFFDGPWFKEVADKSTTTLDALTHHVYNLGPGVDNNLIEKILDPESLDSMVDTYSKLQNILKTSATSATAWVGESGGAWNSGHHLVTDAFVF SFWYLDQLGMSAVYDTKTYCRQTLVGGNYGLLNTTTFVPNPDYYSALLWHRLMGRNVLATRFGGPKKIRAYTHCAKQSKGIVVLLINLHNTTVVQARVAF NSTWSLRHRHKSHKSYRSHMKELNGLRSRAERVRGDREREEYHLTPKDGNIQSQTMLLNGNALNLDSSGNIPTLEPVFVNSSQPIIVAPFSIVFVHIPY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 560 Download |
| MGSQNWRMGM CFWVCLIGFL SFIHCVSSEG EGIGGGSVEA LIRIDGKEAI AKVDEDFICA 60 TLDWWPPEKC DYGTCSWGKT SLLNLDLSNT ILSNAIKAFS PLKLRLGGTL QDQIIYDTED 120 NKKPCPPIPF VENNTTLFGE MFGFNEACLP MKRWDELNSF FLRTGAKIVF GLNVLTGKTF 180 KNNIPAIGDW DFTNAESFIR YTVKNNYSVA GWELGNELCG KGVGTSISAS QYANDSASLR 240 NIVQEIYKGG AGPKPLILAP GGFFDGPWFK EVADKSTTTL DALTHHVYNL GPGVDNNLIE 300 KILDPESLDS MVDTYSKLQN ILKTSATSAT AWVGESGGAW NSGHHLVTDA FVFSFWYLDQ 360 LGMSAVYDTK TYCRQTLVGG NYGLLNTTTF VPNPDYYSAL LWHRLMGRNV LATRFGGPKK 420 IRAYTHCAKQ SKGIVVLLIN LHNTTVVQAR VAFNSTWSLR HRHKSHKSYR SHMKELNGLR 480 SRAERVRGDR EREEYHLTPK DGNIQSQTML LNGNALNLDS SGNIPTLEPV FVNSSQPIIV 540 APFSIVFVHI PYVVPPACR* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 8.0e-180 | 40 | 362 | 324 | + 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 - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vo0_A | 0.0005 | 155 | 415 | 122 | 370 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3vnz_A | 0.0005 | 155 | 415 | 122 | 370 | A Chain A, Crystal Structure Of The Kifc3 Motor Domain In Complex With Adp |
| PDB | 3vny_A | 0.0005 | 155 | 415 | 122 | 370 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
