| Basic Information | |
|---|---|
| Species | Fragaria vesca |
| Cazyme ID | mrna26075.1-v1.0-hybrid |
| Family | GH79 |
| Protein Properties | Length: 541 Molecular Weight: 59463.9 Isoelectric Point: 8.3971 |
| Chromosome | Chromosome/Scaffold: 5 Start: 7450784 End: 7453625 |
| Description | glucuronidase 2 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH79 | 39 | 534 | 0 |
| DNNFVCATLDWWNHEKCDYNHCPWGSASVLNLNLSHPLLAKSIQAFNQLRIRIGGSLQDQVLYGVGDLKYPCHPFRKQKGGLFGFSTGCLPMSRWDELNH FFSKTRPLVTFSLNALSGRHHKGAGVWVGDWDSRNAYDFINYTVSKGYQINSWELGNELCGKGVGASVGAEQYGKDLIKLKHIVNQLYNDSHIKPALVGP GGFFDQKWFTTLLQVSGSGVVDVVTQHIYNLGPGVDPNLMQKILNPSYLDQISGTFDSLAATVRHHGPWASIWVGESGGAYNSGGFNVSNTFVNSFWYLD QLGMSAMYNSAVYCRQSLVGGHYGLLNRTSFVPNPDYYSALLWHRLMGESVLKVDRNGAPHLRVYAHCSKGSAGITVLLINLSNQTDFIVNVKNVLELDR ADRSRSTGKGSKFSHGLKRTVSWVGLKASDGTLHRKEYHLTPKDGNLRSKIMVLNGVPLEITKDGNIPELEPVIVPVNDPISITSFSIKFVVLPHF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 541 Download |
| MELCVSLILF LVSLPAFLAK EVGHASVVVD GTVAIAHIDN NFVCATLDWW NHEKCDYNHC 60 PWGSASVLNL NLSHPLLAKS IQAFNQLRIR IGGSLQDQVL YGVGDLKYPC HPFRKQKGGL 120 FGFSTGCLPM SRWDELNHFF SKTRPLVTFS LNALSGRHHK GAGVWVGDWD SRNAYDFINY 180 TVSKGYQINS WELGNELCGK GVGASVGAEQ YGKDLIKLKH IVNQLYNDSH IKPALVGPGG 240 FFDQKWFTTL LQVSGSGVVD VVTQHIYNLG PGVDPNLMQK ILNPSYLDQI SGTFDSLAAT 300 VRHHGPWASI WVGESGGAYN SGGFNVSNTF VNSFWYLDQL GMSAMYNSAV YCRQSLVGGH 360 YGLLNRTSFV PNPDYYSALL WHRLMGESVL KVDRNGAPHL RVYAHCSKGS AGITVLLINL 420 SNQTDFIVNV KNVLELDRAD RSRSTGKGSK FSHGLKRTVS WVGLKASDGT LHRKEYHLTP 480 KDGNLRSKIM VLNGVPLEIT KDGNIPELEP VIVPVNDPIS ITSFSIKFVV LPHFEAPACG 540 * |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam03662 | Glyco_hydro_79n | 0 | 25 | 341 | 317 | + 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 | 0.00008 | 235 | 440 | 212 | 427 | A Chain A, Crystal Structure Of A Response Regulator From Myxococcus Xanthus |
| PDB | 3vnz_A | 0.00008 | 235 | 440 | 212 | 427 | A Chain A, Crystal Structure Of A Response Regulator From Myxococcus Xanthus |
| PDB | 3vny_A | 0.00008 | 235 | 440 | 212 | 427 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
