Basic Information | |
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Species | Ricinus communis |
Cazyme ID | 30138.m004015 |
Family | GH79 |
Protein Properties | Length: 539 Molecular Weight: 59927.3 Isoelectric Point: 8.3672 |
Chromosome | Chromosome/Scaffold: 30138 Start: 1297442 End: 1302939 |
Description | glucuronidase 1 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 39 | 533 | 0 |
DDNFICATLDWWPHDKCDYNQCPWGYSSVLNLNLSHPLLAKAMQAFRHLRIRIGGSLQDRVLYDVGDLKFPCHPFRKMKDGLFGFSKGCLHMNRWDELNL LFSKTGAIVTFSLNALHGRHQIRRGVWGGAWDSSNAYDFMNYTVSKGHKIDSWEFGNELSGSGVGASVNAELYGKDVINLKNIINELYKNSGFKPSLIAP GGFFNQQWYAEFLKVSGSGIINILTHHIYNLGAGIDPNLVSKILDPHYLSKITETFSGLAQTIQQHGPWSSAWVGESGGAYNSGGRHVSNTFVNSFWYLD QLGLASKYNTKAYCRQTLIGGNYGLLNTTTLVPNPDYYSALLWHRLMGKGVLAVGSDASPYLRAYAHCSRGRAGVTLLLINLSNQTDFIISVQNSMAMKL HVKENIQRESRIVRGLKRSVSWVGNRASDESLTREEYHLTSKDGYLRSQTMVLNGIPLELTEDGEIPRLDPVHNNVKSPIYISPLSIAFIVFPNF |
Full Sequence |
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Protein Sequence Length: 539 Download |
MGFSLSLLFL LASLPVIFAQ DVKHATIVVD GTVTVAETDD NFICATLDWW PHDKCDYNQC 60 PWGYSSVLNL NLSHPLLAKA MQAFRHLRIR IGGSLQDRVL YDVGDLKFPC HPFRKMKDGL 120 FGFSKGCLHM NRWDELNLLF SKTGAIVTFS LNALHGRHQI RRGVWGGAWD SSNAYDFMNY 180 TVSKGHKIDS WEFGNELSGS GVGASVNAEL YGKDVINLKN IINELYKNSG FKPSLIAPGG 240 FFNQQWYAEF LKVSGSGIIN ILTHHIYNLG AGIDPNLVSK ILDPHYLSKI TETFSGLAQT 300 IQQHGPWSSA WVGESGGAYN SGGRHVSNTF VNSFWYLDQL GLASKYNTKA YCRQTLIGGN 360 YGLLNTTTLV PNPDYYSALL WHRLMGKGVL AVGSDASPYL RAYAHCSRGR AGVTLLLINL 420 SNQTDFIISV QNSMAMKLHV KENIQRESRI VRGLKRSVSW VGNRASDESL TREEYHLTSK 480 DGYLRSQTMV LNGIPLELTE DGEIPRLDPV HNNVKSPIYI SPLSIAFIVF PNFDAPSCA 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 | |
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GO Term | Description |
GO:0016020 | membrane |
GO:0016798 | hydrolase activity, acting on glycosyl bonds |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI15157.1 | 0 | 1 | 539 | 1 | 513 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_200933.2 | 0 | 1 | 539 | 1 | 539 | AtGUS1 (Arabidopsis thaliana glucuronidase 1); beta-glucuronidase |
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 | 1 | 539 | 1 | 539 | Heparanase-2, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vo0_A | 0.0006 | 167 | 429 | 142 | 409 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3vnz_A | 0.0006 | 167 | 429 | 142 | 409 | A Chain A, Crystal Structure Of Medicago Truncatula Ugt71g1 |
PDB | 3vny_A | 0.0006 | 167 | 429 | 142 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |