y
Basic Information | |
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Species | Thellungiella halophila |
Cazyme ID | Thhalv10003960m |
Family | GH79 |
Protein Properties | Length: 541 Molecular Weight: 60054.7 Isoelectric Point: 6.6691 |
Chromosome | Chromosome/Scaffold: 6 Start: 2539761 End: 2542069 |
Description | glucuronidase 1 |
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 | 42 | 534 | 0 |
DENFVCATLDWWPPEKCNYDQCPWGYASLINLNLSSPLLAKAIQAFKTLRIRLGGSLQDQVIYDVGDLKTPCSPFKKTDDGLFGFSKGCLYMDRWNELNR FFNSTGAIVTFGLNALYGRDKLSGNSWGGDWDHINTQDFMNYTVSMGYAIDSWEFGNELSGSGIDASVSVELYGKDLIVLKDVIKNVYKNSQTKPLLLAP GGFYDEKWYSELLRLSGPGVLDVMTHHIYNLGPGNDPQLENRILDPKYLSGISGKFKNVDQTIQEHGPWAAAWVGEAGGASNSGGRQVSETFINSFWYLD QLGMSSMHNTKVYCRQALVGGFYGLLEKETFVPNPDYYSALLWHRLMGKGVLGVQTNASEYLRTYVHCSKGTAGITILLINLSKQTTFTVGVSNGVKVIL QAEPMKRKSFLETIKSKVSWVGNKASDGYLNREEYHLSPKDGNLRSKIMLLNGIPLEPTITGDIPKLEPIRHGVKSPVYINPLSISFIVLPTF |
Full Sequence |
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Protein Sequence Length: 541 Download |
MGFNVCFLVF LIRLLLLPVT FGSNMEQTTI VIDGEHRIAE IDENFVCATL DWWPPEKCNY 60 DQCPWGYASL INLNLSSPLL AKAIQAFKTL RIRLGGSLQD QVIYDVGDLK TPCSPFKKTD 120 DGLFGFSKGC LYMDRWNELN RFFNSTGAIV TFGLNALYGR DKLSGNSWGG DWDHINTQDF 180 MNYTVSMGYA IDSWEFGNEL SGSGIDASVS VELYGKDLIV LKDVIKNVYK NSQTKPLLLA 240 PGGFYDEKWY SELLRLSGPG VLDVMTHHIY NLGPGNDPQL ENRILDPKYL SGISGKFKNV 300 DQTIQEHGPW AAAWVGEAGG ASNSGGRQVS ETFINSFWYL DQLGMSSMHN TKVYCRQALV 360 GGFYGLLEKE TFVPNPDYYS ALLWHRLMGK GVLGVQTNAS EYLRTYVHCS KGTAGITILL 420 INLSKQTTFT VGVSNGVKVI LQAEPMKRKS FLETIKSKVS WVGNKASDGY LNREEYHLSP 480 KDGNLRSKIM LLNGIPLEPT ITGDIPKLEP IRHGVKSPVY INPLSISFIV LPTFDAPACS 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 | 25 | 344 | 320 | + 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 |
DDBJ | BAB08480.1 | 0 | 25 | 540 | 1 | 516 | unnamed protein product [Arabidopsis thaliana] |
EMBL | CAB62595.1 | 0 | 21 | 540 | 1 | 521 | putative protein [Arabidopsis thaliana] |
RefSeq | NP_196400.2 | 0 | 1 | 540 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | NP_200933.2 | 0 | 1 | 540 | 1 | 539 | AtGUS1 (Arabidopsis thaliana glucuronidase 1); beta-glucuronidase |
RefSeq | XP_002514696.1 | 0 | 18 | 540 | 15 | 539 | Heparanase-2, putative [Ricinus communis] |