Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna11598.1-v1.0-hybrid |
Family | GH79 |
Protein Properties | Length: 570 Molecular Weight: 62151.3 Isoelectric Point: 6.0993 |
Chromosome | Chromosome/Scaffold: Start: 9132312 End: 9137543 |
Description | glucuronidase 3 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 113 | 562 | 0 |
DDDFVCATLDWWPPEKCDYGTCSWGNASLLNLDLGNDILLNAIKAFSPLKLRLGGTLQDKVIYQTEDGPKHTSFVKDSSQLFGFSDGYLPMPRWDELNIF FKNAGAVIIFGLNALQGRTIDSHGVAVGDWNASNAESFIRYTVNKGYTIHGWELGNELCGSGVGTRVTAVQYASDINSLQNKILFYKAPQSVQVLTHHIY NLGPGSATDLVDKILNPSVLDGISKTFSDLQMLVKSSHTSAVAWVGESGGAYNSGHNLVTNAFVFSFWYLDQLGMSASYDTKTHCRQTLIGGNYGLLDIN TFKPNPDYYSALLWHRLMGNNVLSTSFSGTKKLRTYAHCSKKTQGITVLLINLGNTTVQVDVSTKNGGSSSTLNFEEGLKDSKATKNDVREEYHITAKDG DLHSRVMLLNEKELTVNSAGQIPSLEPMIVGISDPTSVAPFSIVFVHIPN |
Full Sequence |
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Protein Sequence Length: 570 Download |
MCLVLIVWEH QLSNVLGPGF SWHDRMSVEA KTGHAGFGGE VEVFPVIVMV HGQSGGIDQD 60 HREIPTNEIR LAHPDPTYKI PLTPALVDLE QIRKSTEADT VFVNGTAAIG SIDDDFVCAT 120 LDWWPPEKCD YGTCSWGNAS LLNLDLGNDI LLNAIKAFSP LKLRLGGTLQ DKVIYQTEDG 180 PKHTSFVKDS SQLFGFSDGY LPMPRWDELN IFFKNAGAVI IFGLNALQGR TIDSHGVAVG 240 DWNASNAESF IRYTVNKGYT IHGWELGNEL CGSGVGTRVT AVQYASDINS LQNKILFYKA 300 PQSVQVLTHH IYNLGPGSAT DLVDKILNPS VLDGISKTFS DLQMLVKSSH TSAVAWVGES 360 GGAYNSGHNL VTNAFVFSFW YLDQLGMSAS YDTKTHCRQT LIGGNYGLLD INTFKPNPDY 420 YSALLWHRLM GNNVLSTSFS GTKKLRTYAH CSKKTQGITV LLINLGNTTV QVDVSTKNGG 480 SSSTLNFEEG LKDSKATKND VREEYHITAK DGDLHSRVML LNEKELTVNS AGQIPSLEPM 540 IVGISDPTSV APFSIVFVHI PNITVPACK* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 5.0e-150 | 97 | 386 | 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 |
Sequence Alignments (This image is cropped. Click for full image.) |
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