y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.B00567.1 |
Family | GH79 |
Protein Properties | Length: 541 Molecular Weight: 59758.3 Isoelectric Point: 8.5086 |
Chromosome | Chromosome/Scaffold: 2 Start: 7274523 End: 7279031 |
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 | 40 | 534 | 0 |
DDNFICATLDWWPHDKCNYDQCPWGYSSVINLNLSHPVLGKAIQAFKSLRIRIGGSLQDRVLYDVGQLGLRCQPFRKIKGSLFGFSKGCLHMKRWDELNN LFSKTGAIVTFGLNALNGRHWIKDQVWGGDWNFSNAYDFIKYTVARGYSIDSWEFGNELSGSGVDASVSVEQYGKDLIFLKNIINELYKSSRSKPSVIAP GGFYDQQWYAKLLQVSGSGLINAMSHHIYNLGGGDDPHLVSKILDPSYLSQISDTFINLEETIKKHGPWASAWVGESGGAYNSGGRHISNTFINSFWYLD QLGMASKYDTKVYCRQSLVGGNYGLLNTTTLVPNPDYYSALLWHRLMGKRALAVSGDAPPSLRCYAHCLKGRAGVTLLLINLRNQTKFIITTQKSVQNLH VEEQSVNKGSILIHGLKKTVSFVGQGPSRAPLFREEYHLTPQGGHLQSQTMLLNGSPLELTRDGAIPPLKPNLVHADSLISVSPLSIAFIVLPNF |
Full Sequence |
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Protein Sequence Length: 541 Download |
MGLSCLALFI FIVSFPWGLA QDVARSTLII HGSEAIAETD DNFICATLDW WPHDKCNYDQ 60 CPWGYSSVIN LNLSHPVLGK AIQAFKSLRI RIGGSLQDRV LYDVGQLGLR CQPFRKIKGS 120 LFGFSKGCLH MKRWDELNNL FSKTGAIVTF GLNALNGRHW IKDQVWGGDW NFSNAYDFIK 180 YTVARGYSID SWEFGNELSG SGVDASVSVE QYGKDLIFLK NIINELYKSS RSKPSVIAPG 240 GFYDQQWYAK LLQVSGSGLI NAMSHHIYNL GGGDDPHLVS KILDPSYLSQ ISDTFINLEE 300 TIKKHGPWAS AWVGESGGAY NSGGRHISNT FINSFWYLDQ LGMASKYDTK VYCRQSLVGG 360 NYGLLNTTTL VPNPDYYSAL LWHRLMGKRA LAVSGDAPPS LRCYAHCLKG RAGVTLLLIN 420 LRNQTKFIIT TQKSVQNLHV EEQSVNKGSI LIHGLKKTVS FVGQGPSRAP LFREEYHLTP 480 QGGHLQSQTM LLNGSPLELT RDGAIPPLKP NLVHADSLIS VSPLSIAFIV LPNFDVQACA 540 * 600 |
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 | 24 | 342 | 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 | |
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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 | CAB62595.1 | 0 | 19 | 540 | 1 | 521 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 13 | 540 | 12 | 513 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 19 | 540 | 23 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 13 | 540 | 12 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514696.1 | 0 | 16 | 540 | 15 | 539 | Heparanase-2, putative [Ricinus communis] |