| Basic Information | |
|---|---|
| Species | Linum usitatissimum |
| Cazyme ID | Lus10015737 |
| Family | GH79 |
| Protein Properties | Length: 540 Molecular Weight: 59679.7 Isoelectric Point: 7.0833 |
| Chromosome | Chromosome/Scaffold: 430 Start: 158022 End: 160752 |
| Description | glucuronidase 2 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| GH79 | 39 | 533 | 0 |
| DDNYVCATLDWWPHDKCDYHHCPWGNTSVENLDLSHPLLAKAIQAFKSLRIRIGGSLQDQVLYDVGNLGSPCQSFFKKKGGLFDFSKGCLHMDRWDALND LFNTTGALVTFGLNALRGRHKIKGRLWGGPWNSTNAYDFISYTISKGYKIYAWEYGNELSGTGIGASVTADTYAKDVIKLKEIVDELYTNSSVRPSIMAP GGFYDKDWYGKLLKITGPGRLDIVTHHIYNLGAGVDPHLIHNILDPSLLNTALVTFRDLSQTLQRNGPWASAWVGEAGGAYNSGGFHISDTFVNSFWYLD QLGMAATYNTKVYCRQTLVGGHYSLLNTTTFVPNPDYYSALLWHRLMGKSVLGVTSTASRYLRHYAHCSKGREGITLLLINLSNNTDYEVNIRSSSDSEL TLQETVGRSNSFANRLKRSILWIGSEASDESLLREEYHLSPKDGNLQSQEMVLNGVPVQLTEKGDVPKLEPLRSRLSSRLFVGSLSISFVVLPNF | |||
| Full Sequence |
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| Protein Sequence Length: 540 Download |
| MGLLFSSFVL LAFLRVIVAQ EIIPATIAVD GAVAVAETDD NYVCATLDWW PHDKCDYHHC 60 PWGNTSVENL DLSHPLLAKA IQAFKSLRIR IGGSLQDQVL YDVGNLGSPC QSFFKKKGGL 120 FDFSKGCLHM DRWDALNDLF NTTGALVTFG LNALRGRHKI KGRLWGGPWN STNAYDFISY 180 TISKGYKIYA WEYGNELSGT GIGASVTADT YAKDVIKLKE IVDELYTNSS VRPSIMAPGG 240 FYDKDWYGKL LKITGPGRLD IVTHHIYNLG AGVDPHLIHN ILDPSLLNTA LVTFRDLSQT 300 LQRNGPWASA WVGEAGGAYN SGGFHISDTF VNSFWYLDQL GMAATYNTKV YCRQTLVGGH 360 YSLLNTTTFV PNPDYYSALL WHRLMGKSVL GVTSTASRYL RHYAHCSKGR EGITLLLINL 420 SNNTDYEVNI RSSSDSELTL QETVGRSNSF ANRLKRSILW IGSEASDESL LREEYHLSPK 480 DGNLQSQEMV LNGVPVQLTE KGDVPKLEPL RSRLSSRLFV GSLSISFVVL PNFDAPACA* 540 |
| 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 | 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 - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CAB62595.1 | 0 | 18 | 539 | 1 | 521 | putative protein [Arabidopsis thaliana] |
| EMBL | CBI15157.1 | 0 | 1 | 539 | 1 | 513 | unnamed protein product [Vitis vinifera] |
| RefSeq | XP_002284470.1 | 0 | 1 | 539 | 1 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002321464.1 | 0 | 1 | 539 | 1 | 541 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002514696.1 | 0 | 16 | 539 | 16 | 539 | Heparanase-2, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vo0_A | 0.003 | 136 | 430 | 124 | 408 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
| PDB | 3vnz_A | 0.003 | 136 | 430 | 124 | 408 | A Chain A, Crystal Structure Of A Glycosyltransferase Involved In The Glycosylation Of The Major Capsid Of Pbcv-1 |
| PDB | 3vny_A | 0.003 | 136 | 430 | 124 | 408 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
