Basic Information | |
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Species | Brachypodium distachyon |
Cazyme ID | Bradi1g47760.1 |
Family | GH79 |
Protein Properties | Length: 539 Molecular Weight: 57738 Isoelectric Point: 9.2364 |
Chromosome | Chromosome/Scaffold: 1 Start: 46473055 End: 46475745 |
Description | glucuronidase 3 |
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 | 50 | 532 | 0 |
DEDFVCATLDWWPPEKCDYGTCSWGHAGLLNLDLSNKILLNAVRAFSPLKLRLGGTLQDKVVYGAGDSGQPCKPFLKGNGSELFGFTQACLPQRRWDELN AFFQKSGATIVFGLNALNGRVRLPDGSMGGDWDISNAASFIRYTVSKGYKIHGWELGNELSGTGVGVRIGSGQYAKDVVALKSEVDKIYQGNASSSKPLV IAPGGFFDRGWFKDLLVKTKPNMLNAVTHHIYNLGPGVDTHLIEKILKPSVLDGMASTFRNLQGLLKSTGTSAVAWVGEAGGAYNSGHHLVTDAFVFSFW FLDQLGMSAKYDTKTYCRQTFIGGNYGMLNTSTFEPNPDYYSALLWHRLMGTKVLATKFSGTNKIRAYAHCTKRSPGITLLLINLGGNTTNHVSVTSEGA ATKHGRKVRHVVGFAQGAGAMREEYHLTPKGGNIQSQVMVLNGKELATDAAGNIPRLEPVKVDAAQHIAVAPHSIVFAHIPHF |
Full Sequence |
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Protein Sequence Length: 539 Download |
MGGLPRRLVV GSLWLTALAL LLCADAAAAA AEGTAGVVSV DARRAIASTD EDFVCATLDW 60 WPPEKCDYGT CSWGHAGLLN LDLSNKILLN AVRAFSPLKL RLGGTLQDKV VYGAGDSGQP 120 CKPFLKGNGS ELFGFTQACL PQRRWDELNA FFQKSGATIV FGLNALNGRV RLPDGSMGGD 180 WDISNAASFI RYTVSKGYKI HGWELGNELS GTGVGVRIGS GQYAKDVVAL KSEVDKIYQG 240 NASSSKPLVI APGGFFDRGW FKDLLVKTKP NMLNAVTHHI YNLGPGVDTH LIEKILKPSV 300 LDGMASTFRN LQGLLKSTGT SAVAWVGEAG GAYNSGHHLV TDAFVFSFWF LDQLGMSAKY 360 DTKTYCRQTF IGGNYGMLNT STFEPNPDYY SALLWHRLMG TKVLATKFSG TNKIRAYAHC 420 TKRSPGITLL LINLGGNTTN HVSVTSEGAA TKHGRKVRHV VGFAQGAGAM REEYHLTPKG 480 GNIQSQVMVL NGKELATDAA GNIPRLEPVK VDAAQHIAVA PHSIVFAHIP HFHAPACS* 540 |
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 | 33 | 355 | 323 | + 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 | ACF81144.1 | 0 | 41 | 538 | 35 | 543 | unknown [Zea mays] |
GenBank | EAY99897.1 | 0 | 6 | 538 | 4 | 525 | hypothetical protein OsI_21892 [Oryza sativa Indica Group] |
GenBank | EAZ36024.1 | 0 | 6 | 538 | 4 | 525 | hypothetical protein OsJ_20330 [Oryza sativa Japonica Group] |
RefSeq | NP_001056967.1 | 0 | 6 | 538 | 4 | 526 | Os06g0179000 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001132339.1 | 0 | 41 | 538 | 35 | 543 | hypothetical protein LOC100193781 [Zea mays] |
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 | 0.002 | 146 | 458 | 122 | 420 | A Chain A, Solution Structure Of The Ph Domain Of Pleckstrin Homology Domain-Containing Family A Member 6 From Human |
PDB | 3vnz_A | 0.002 | 146 | 458 | 122 | 420 | A Chain A, Solution Structure Of The Ph Domain Of Pleckstrin Homology Domain-Containing Family A Member 6 From Human |
PDB | 3vny_A | 0.002 | 146 | 458 | 122 | 420 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |