Basic Information | |
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Species | Glycine max |
Cazyme ID | Glyma13g23190.1 |
Family | GH79 |
Protein Properties | Length: 525 Molecular Weight: 57593 Isoelectric Point: 8.5476 |
Chromosome | Chromosome/Scaffold: 13 Start: 26640141 End: 26643792 |
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 | 52 | 518 | 0 |
DDSVCATLDWWPPQKCDYGKCSWGHASLLNLDLNNKILLNAVKAFSPLKIRLGGTLQDKVMYGTEDCRQPCTPFVLNANEMFGFTQGCLPMYRWDELNSF FQKAGAKVVFGLNALAGKSMKSGSAVGPWNYTNAESLIRYTVRKKYTIHGWELGNELCGSGIGASVAADQYASDVAALRNIVENAYRGIEPKPLVIAPGG FFDSDWFKEFISKSGKSADVITHHIYNLGPGVDDHLTEKILDPSYLDGEANTFSSLKGILQSSSTSVKSWVGEAGGAYNSGHHLVSDAFVYSFWYLDQLG MSAVYDTRTYCRQSLIGGNYGLLNTSTFVPNPDYYSALLWHRLMGGRVLLTTFYGTKKIRTYAHCAKESKGITILVLNLDNSTTVQVNVALKFNKLPYRR VGEPARREYHLTAPDRNLHSQTMLLNGKMLSVNSAGEIPPLEPLYVNSRKPIIVGPLSIVFAHIPNV |
Full Sequence |
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Protein Sequence Length: 525 Download |
MGSQIRLLGL CLWMYLSSLS FIGAGAVYGR EGEVVKGIVL VHGKTAIGRI DDDSVCATLD 60 WWPPQKCDYG KCSWGHASLL NLDLNNKILL NAVKAFSPLK IRLGGTLQDK VMYGTEDCRQ 120 PCTPFVLNAN EMFGFTQGCL PMYRWDELNS FFQKAGAKVV FGLNALAGKS MKSGSAVGPW 180 NYTNAESLIR YTVRKKYTIH GWELGNELCG SGIGASVAAD QYASDVAALR NIVENAYRGI 240 EPKPLVIAPG GFFDSDWFKE FISKSGKSAD VITHHIYNLG PGVDDHLTEK ILDPSYLDGE 300 ANTFSSLKGI LQSSSTSVKS WVGEAGGAYN SGHHLVSDAF VYSFWYLDQL GMSAVYDTRT 360 YCRQSLIGGN YGLLNTSTFV PNPDYYSALL WHRLMGGRVL LTTFYGTKKI RTYAHCAKES 420 KGITILVLNL DNSTTVQVNV ALKFNKLPYR RVGEPARREY HLTAPDRNLH SQTMLLNGKM 480 LSVNSAGEIP PLEPLYVNSR KPIIVGPLSI VFAHIPNVLL SACS* |
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 | 35 | 351 | 319 | + 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 | ACU20377.1 | 0 | 1 | 524 | 1 | 525 | unknown [Glycine max] |
EMBL | CAN81917.1 | 0 | 1 | 523 | 1 | 554 | hypothetical protein [Vitis vinifera] |
EMBL | CBI25561.1 | 0 | 8 | 523 | 1 | 532 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 1 | 523 | 5 | 558 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 37 | 524 | 1 | 506 | predicted protein [Populus trichocarpa] |
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 | 0.0000001 | 146 | 439 | 122 | 409 | A Chain A, Crystal Structure Of Tryptophan Synthase Alpha-subunit From The Psychrophile Shewanella Frigidimarina K14-2 |
PDB | 3vnz_A | 0.0000001 | 146 | 439 | 122 | 409 | A Chain A, Crystal Structure Of Tryptophan Synthase Alpha-subunit From The Psychrophile Shewanella Frigidimarina K14-2 |
PDB | 3vny_A | 0.0000001 | 146 | 439 | 122 | 409 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |