Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi1g70300.1 |
Family | GH79 |
Protein Properties | Length: 545 Molecular Weight: 60598.9 Isoelectric Point: 8.4394 |
Chromosome | Chromosome/Scaffold: 1 Start: 68685680 End: 68692258 |
Description | glucuronidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 43 | 538 | 0 |
DENYVCATIDWWPPEKCNYNQCPWGQSSILNLDLDHPFLAQAIQAFDNLRIRLGGSLQDRVVYDVGTNSPCSPFTNMSSGLFGFSVGCLSMDRWDKLNDL FQKTGAIITFGLNALYGRHNVQRSVWTGKWNSTNAYDFLKYTISKGYQVESWEFGNELSGHGTGARVDAKLYGKDVTELKSILRKLYRAPLSQPLLLAPG GFFDQQWYTQLLQTSGHGVVSALTHHIYNLGGGDDVHLMRKIVDPKYLDRAEDTYRDMQLTLQRHGTWASAWVSESGGVFNNGRLMVSNTFMNSIWYLDQ LGMASKYNTKVFCRQTLIGGNYGLLDTQTFIPNPDYYSALLWHRLMGKGVLSVDINAPRKVRAYAHCSKQQQGITLLLINLSNSTGYNVTLQNDINVSLE KQTNLRRHSSFTHGLRRAVSWLGRKPSSRDAAAKREEYHLAAKDGDHQSRTMLLNGVPLELADDGSIPALDPVTAAVSSPVYLAPTSIAFVVLPKF |
Full Sequence |
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Protein Sequence Length: 545 Download |
MAVRLLLLLL ALACLHAPWS ASAQQPEEAT VIVKGSNRIA ETDENYVCAT IDWWPPEKCN 60 YNQCPWGQSS ILNLDLDHPF LAQAIQAFDN LRIRLGGSLQ DRVVYDVGTN SPCSPFTNMS 120 SGLFGFSVGC LSMDRWDKLN DLFQKTGAII TFGLNALYGR HNVQRSVWTG KWNSTNAYDF 180 LKYTISKGYQ VESWEFGNEL SGHGTGARVD AKLYGKDVTE LKSILRKLYR APLSQPLLLA 240 PGGFFDQQWY TQLLQTSGHG VVSALTHHIY NLGGGDDVHL MRKIVDPKYL DRAEDTYRDM 300 QLTLQRHGTW ASAWVSESGG VFNNGRLMVS NTFMNSIWYL DQLGMASKYN TKVFCRQTLI 360 GGNYGLLDTQ TFIPNPDYYS ALLWHRLMGK GVLSVDINAP RKVRAYAHCS KQQQGITLLL 420 INLSNSTGYN VTLQNDINVS LEKQTNLRRH SSFTHGLRRA VSWLGRKPSS RDAAAKREEY 480 HLAAKDGDHQ SRTMLLNGVP LELADDGSIP ALDPVTAAVS SPVYLAPTSI AFVVLPKFEA 540 KACS* |
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 | 26 | 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 |
GenBank | ACG44916.1 | 0 | 17 | 544 | 16 | 541 | heparanase-like protein 2 precursor [Zea mays] |
GenBank | ACV84153.1 | 0 | 1 | 544 | 1 | 542 | heparanase [Oryza sativa Indica Group] |
RefSeq | NP_001049350.1 | 0 | 1 | 544 | 1 | 541 | Os03g0211700 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001145968.1 | 0 | 17 | 544 | 16 | 541 | hypothetical protein LOC100279495 [Zea mays] |
RefSeq | XP_002468296.1 | 0 | 14 | 544 | 15 | 543 | hypothetical protein SORBIDRAFT_01g043180 [Sorghum bicolor] |