y
Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_004963m |
Family | GH79 |
Protein Properties | Length: 548 Molecular Weight: 60830.4 Isoelectric Point: 8.8387 |
Chromosome | Chromosome/Scaffold: 12794 Start: 2189349 End: 2194586 |
Description | glucuronidase 2 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 48 | 541 | 0 |
DDNFICATLDWWPHDKCDYNQCPWHYSSVINLNLSRPLLAKAIQAFRYLRMRIGGSLQDQVFYDVGNLNSTCHPFRKMKDGLFGFSKGCLHMNRWDELNH LFSRTGAIVTFSLNALHGRHQIRKGVWGGAWDSSNAYDFMNYTVSKGYKIDSWEFGNELSGSGIGASVSAELYGKDVIKLKEIIKDLYKNSDSKPSLVAP GGFYNQQWYAKLLQVSGSGIVNIMTHHIYNLGAGVDPNLVNKILDPRHLSKVSETFSGIVQTIQHNGPWASAWVGESGGAFNSGGHRVSNTFVNSFWYLD QLGMAAKYHTKVYCRQTLIGGNYGLLNATTFIPNPDYYSALLWHRLMGKGVLAVGSDASPYLRAYAHCSKGRAGITLLLINLSNQTDYIISVRNSMTMRL HTKKKMQTESSLIHGLKRSVSWVGHDTLNGATREEYHLTPKDGYLRSETMVLNGIPLQLTESGDIPRMDPVHNNVNSPIYISSLSISFIVFPNF |
Full Sequence |
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Protein Sequence Length: 548 Download |
MKSSIIICPM GYCLSLLFFL ASLPGIFAQD VKHATVVVDG TLTTATTDDN FICATLDWWP 60 HDKCDYNQCP WHYSSVINLN LSRPLLAKAI QAFRYLRMRI GGSLQDQVFY DVGNLNSTCH 120 PFRKMKDGLF GFSKGCLHMN RWDELNHLFS RTGAIVTFSL NALHGRHQIR KGVWGGAWDS 180 SNAYDFMNYT VSKGYKIDSW EFGNELSGSG IGASVSAELY GKDVIKLKEI IKDLYKNSDS 240 KPSLVAPGGF YNQQWYAKLL QVSGSGIVNI MTHHIYNLGA GVDPNLVNKI LDPRHLSKVS 300 ETFSGIVQTI QHNGPWASAW VGESGGAFNS GGHRVSNTFV NSFWYLDQLG MAAKYHTKVY 360 CRQTLIGGNY GLLNATTFIP NPDYYSALLW HRLMGKGVLA VGSDASPYLR AYAHCSKGRA 420 GITLLLINLS NQTDYIISVR NSMTMRLHTK KKMQTESSLI HGLKRSVSWV GHDTLNGATR 480 EEYHLTPKDG YLRSETMVLN GIPLQLTESG DIPRMDPVHN NVNSPIYISS LSISFIVFPN 540 FDAPSCA* 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 | 34 | 350 | 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 | CAB62595.1 | 0 | 27 | 547 | 1 | 521 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 10 | 547 | 1 | 513 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002284470.1 | 0 | 10 | 547 | 1 | 539 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002321464.1 | 0 | 10 | 547 | 1 | 541 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002514696.1 | 0 | 24 | 547 | 15 | 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 | 0.0005 | 98 | 438 | 75 | 409 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3vnz_A | 0.0005 | 98 | 438 | 75 | 409 | A Chain A, Catalytic Function And Substrate Recognition Of The Pectate Lyase From Thermotoga Maritima |
PDB | 3vny_A | 0.0005 | 98 | 438 | 75 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |