Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.198040.1 |
Family | GH79 |
Protein Properties | Length: 541 Molecular Weight: 59991 Isoelectric Point: 7.0871 |
Chromosome | Chromosome/Scaffold: 01357 Start: 1216528 End: 1220580 |
Description | glucuronidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 39 | 534 | 0 |
DDNYICATIDWWPHDKCNYNRCPWGYSSAVNLNLSHPLLIKAIQAFEHLRIRIGGSLQDQVLYDVGNLKTPCHLFQKVSWGLFGFSKGCLHMSRWDDLNQ LFKTTGAIVTFGLNALHGRHQIQRDKWGGEWDSTNARDFMNYTVSKGYVVDSWEFGNELSGHGVGASVDVATYAKDVIKLREIINDLYKNSNSKPSLVAP GGFFEPEWYAKLLQVSGSNVVNVVTHHIYNLGAGIDPHLTNNILDPHYLSRVSEVFNRLDQTIQVHGPWASAWVGESGGAYNSGGRHVSNTFINSFWYLD QLGLASKYNTKVYCRQTLIGGHYGLLNTSTLVPNPDFYSALLWHRLMGKIVLPIGTDASSYLRSYAHCSKGNTGVTVLLINLSNQTQFSIHVQNSKNMFL DVQENGVRREKSFLKGMKKTVAWIGNKVSDATVSREEYHLTPKDGYLQSQTMVLNGTPLELTADGDIPNLNPILRDVNTPIHMDPLSIAFVVFPNF |
Full Sequence |
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Protein Sequence Length: 541 Download |
MDFSISLFLV FVSLPAILAQ GATHASIIVD GAAVVAETDD NYICATIDWW PHDKCNYNRC 60 PWGYSSAVNL NLSHPLLIKA IQAFEHLRIR IGGSLQDQVL YDVGNLKTPC HLFQKVSWGL 120 FGFSKGCLHM SRWDDLNQLF KTTGAIVTFG LNALHGRHQI QRDKWGGEWD STNARDFMNY 180 TVSKGYVVDS WEFGNELSGH GVGASVDVAT YAKDVIKLRE IINDLYKNSN SKPSLVAPGG 240 FFEPEWYAKL LQVSGSNVVN VVTHHIYNLG AGIDPHLTNN ILDPHYLSRV SEVFNRLDQT 300 IQVHGPWASA WVGESGGAYN SGGRHVSNTF INSFWYLDQL GLASKYNTKV YCRQTLIGGH 360 YGLLNTSTLV PNPDFYSALL WHRLMGKIVL PIGTDASSYL RSYAHCSKGN TGVTVLLINL 420 SNQTQFSIHV QNSKNMFLDV QENGVRREKS FLKGMKKTVA WIGNKVSDAT VSREEYHLTP 480 KDGYLQSQTM VLNGTPLELT ADGDIPNLNP ILRDVNTPIH MDPLSIAFVV FPNFDAPACS 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 | 12 | 540 | 12 | 513 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 1 | 540 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 12 | 540 | 12 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002321464.1 | 0 | 1 | 540 | 1 | 541 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514696.1 | 0 | 15 | 540 | 15 | 539 | Heparanase-2, putative [Ricinus communis] |