| Basic Information | |
|---|---|
| Species | Phaseolus vulgaris |
| Cazyme ID | Phvul.003G186600.1 |
| Family | GH79 |
| Protein Properties | Length: 547 Molecular Weight: 60884.2 Isoelectric Point: 7.0874 |
| Chromosome | Chromosome/Scaffold: 03 Start: 39857665 End: 39861944 |
| Description | glucuronidase 2 |
| View CDS | |
| External Links |
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| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GH79 | 39 | 534 | 0 |
| DDNFICATIDWWTHDKCDYKYCPWGDSSAVNLDLSHPFLAKAIQALKPLRIRVGGSLQDQVLYEVGNLKAPCHPFQKMKGGLFGFSKGCLQMKRWDELNH FFNDTGVLVTFGLNALHGRHPSHTVWGGDWDSSNAYDLINYTVSKGYKIDSWEFGNELSGKGIGASVSAAQYGKDLIKLKEVLHSLYNNSNFKPLLVAPG GFYNKDWYDKLLQVTGPGIVNVLTHHVYNLGPGSDVHLDRKILDPKQLSNVESTFSNLSETIKKYGHWSSAWVGEAGGAFNSGGRQISNTFINSFWYLDQ LGIASRYNTKVYCRQTLIGGNYGLLDTTTFVPNPDYYSALLWHQLMGKTVLAANSDVFSPSLRTYAHCSKGRDGITLLLINLSNQTRFRLMVHDRVPVSN GGNENATMIHAENSFFSHLKRAFSWIGSKGSDVTFREEYHLNAKDDYLRSQTMLLNGIPLELTNDGEIPTLDPLLNSVQSPILLAPLSIAFVVFPY | |||
| Full Sequence |
|---|
| Protein Sequence Length: 547 Download |
| MGMHLVVFLF LASLRLALSQ DVEHGLILVE GIQAIAETDD NFICATIDWW THDKCDYKYC 60 PWGDSSAVNL DLSHPFLAKA IQALKPLRIR VGGSLQDQVL YEVGNLKAPC HPFQKMKGGL 120 FGFSKGCLQM KRWDELNHFF NDTGVLVTFG LNALHGRHPS HTVWGGDWDS SNAYDLINYT 180 VSKGYKIDSW EFGNELSGKG IGASVSAAQY GKDLIKLKEV LHSLYNNSNF KPLLVAPGGF 240 YNKDWYDKLL QVTGPGIVNV LTHHVYNLGP GSDVHLDRKI LDPKQLSNVE STFSNLSETI 300 KKYGHWSSAW VGEAGGAFNS GGRQISNTFI NSFWYLDQLG IASRYNTKVY CRQTLIGGNY 360 GLLDTTTFVP NPDYYSALLW HQLMGKTVLA ANSDVFSPSL RTYAHCSKGR DGITLLLINL 420 SNQTRFRLMV HDRVPVSNGG NENATMIHAE NSFFSHLKRA FSWIGSKGSD VTFREEYHLN 480 AKDDYLRSQT MLLNGIPLEL TNDGEIPTLD PLLNSVQSPI LLAPLSIAFV VFPYFDAPAC 540 AEHRKL* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam03662 | Glyco_hydro_79n | 0 | 23 | 340 | 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 | CAB62595.1 | 0 | 18 | 541 | 1 | 521 | putative protein [Arabidopsis thaliana] |
| EMBL | CBI15157.1 | 0 | 1 | 541 | 1 | 513 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_196400.2 | 0 | 1 | 541 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
| RefSeq | XP_002284470.1 | 0 | 1 | 541 | 1 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002514696.1 | 0 | 16 | 541 | 16 | 539 | Heparanase-2, putative [Ricinus communis] |
