y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.008G196400.1 |
Family | GH79 |
Protein Properties | Length: 540 Molecular Weight: 60404.9 Isoelectric Point: 8.4527 |
Chromosome | Chromosome/Scaffold: 08 Start: 48109104 End: 48113206 |
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 | 533 | 0 |
DDNFVCATIDWWPHDKCNYDQCPWHYTSVMNLNLSHPFLAKAIQAFNRLRIRVGGSLQDQVLYDVGNLKSPCHPFQKMKDGLFGFSKGCLHMERWDELNR FFKETSAMVTFGLNALHGRHKIKRSLWGGDWDSSNAQDFMKYTISKGYQIDSWEFGNELSGNGIGAHVHADQYGKDLVNLRKIINELYKGSQSKPSLIAP GGFYDEEWFVKLLQTSGFGVIDVMSHHMYNLGAGVDPKLVSKILNPDHLNKAAYTFGNLTHIIRRHGPWTSAWVGESGGAYNSGGAHVSNTFINSFWYLD QLGMASKYHTKVYCRQTLIGGNYGLLNATTFVPNPDYYSGLLWHRLMGKVVLNVESHASPFLRSYAHCSKGRAGVTLLVINLSNQTNFIMNAQNSINLKL AAIEQNISRDSFTHNLKKTFSWVGTKASDDALLREEYHLTPKDGYLRSQTMVLNGIPLELTRTGDIPSLNPVRVNVKSPITISPLSIAFIVFPNF |
Full Sequence |
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Protein Sequence Length: 540 Download |
MELCFGWFLL VASIPAIFAQ DISHGSIVVD GTMTVAQTDD NFVCATIDWW PHDKCNYDQC 60 PWHYTSVMNL NLSHPFLAKA IQAFNRLRIR VGGSLQDQVL YDVGNLKSPC HPFQKMKDGL 120 FGFSKGCLHM ERWDELNRFF KETSAMVTFG LNALHGRHKI KRSLWGGDWD SSNAQDFMKY 180 TISKGYQIDS WEFGNELSGN GIGAHVHADQ YGKDLVNLRK IINELYKGSQ SKPSLIAPGG 240 FYDEEWFVKL LQTSGFGVID VMSHHMYNLG AGVDPKLVSK ILNPDHLNKA AYTFGNLTHI 300 IRRHGPWTSA WVGESGGAYN SGGAHVSNTF INSFWYLDQL GMASKYHTKV YCRQTLIGGN 360 YGLLNATTFV PNPDYYSGLL WHRLMGKVVL NVESHASPFL RSYAHCSKGR AGVTLLVINL 420 SNQTNFIMNA QNSINLKLAA IEQNISRDSF THNLKKTFSW VGTKASDDAL LREEYHLTPK 480 DGYLRSQTMV LNGIPLELTR TGDIPSLNPV RVNVKSPITI SPLSIAFIVF PNFEAPACR* 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 | 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 | CAB62595.1 | 0 | 18 | 538 | 1 | 520 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 12 | 538 | 12 | 512 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 5 | 538 | 12 | 542 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 12 | 538 | 12 | 538 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514696.1 | 0 | 15 | 538 | 15 | 538 | Heparanase-2, putative [Ricinus communis] |