Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.C02742.2 |
Family | GH79 |
Protein Properties | Length: 436 Molecular Weight: 47913.5 Isoelectric Point: 6.9673 |
Chromosome | Chromosome/Scaffold: 3 Start: 52494508 End: 52497659 |
Description | glucuronidase 3 |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 48 | 418 | 0 |
DDDYICATLDWWPPEKCDYGTCSWGRATLQTLDLKNTLLLNAVKAFSPLRIRIGGTLQDKVVYETQGDDRPCGIFTKNSSEFLGFSQGCLPLARWDELNS FFKQTGSAVTFGLNALYGRIIGSDSFVNGPWNSSNTESLIRYTVNKGYSILGWELGNELSGHGVGARVSAHQYASDIKTLQHLVEEIYAGFEVKPLVLAP GGFFDVDWFAHFIDQTSKTLQVVTHHIYNLGPGVDDHLIYKILNPSYLDGAVRTFSSLQTLLKNSGTSAVAWVGEAGGAYNSGRNLVTNSFVFSFWYLDQ LGMAATYDTKTYCRQTLIGGNYGLLNTQTFLPNPDYYSALLWHKLMGSEVLLTSFSGTDKIRAYAHCSKNP |
Full Sequence |
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Protein Sequence Length: 436 Download |
MYCRAASLLV LVGSGVLVLW VCYNSSLPVS QSAGILFING TASVAKTDDD YICATLDWWP 60 PEKCDYGTCS WGRATLQTLD LKNTLLLNAV KAFSPLRIRI GGTLQDKVVY ETQGDDRPCG 120 IFTKNSSEFL GFSQGCLPLA RWDELNSFFK QTGSAVTFGL NALYGRIIGS DSFVNGPWNS 180 SNTESLIRYT VNKGYSILGW ELGNELSGHG VGARVSAHQY ASDIKTLQHL VEEIYAGFEV 240 KPLVLAPGGF FDVDWFAHFI DQTSKTLQVV THHIYNLGPG VDDHLIYKIL NPSYLDGAVR 300 TFSSLQTLLK NSGTSAVAWV GEAGGAYNSG RNLVTNSFVF SFWYLDQLGM AATYDTKTYC 360 RQTLIGGNYG LLNTQTFLPN PDYYSALLWH KLMGSEVLLT SFSGTDKIRA YAHCSKNPVK 420 CLLLLKQEDK PRVFG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 1.0e-177 | 33 | 349 | 318 | + 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 | CBI21126.1 | 0 | 25 | 429 | 4 | 417 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283254.1 | 0 | 8 | 429 | 4 | 433 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283260.1 | 0 | 8 | 429 | 4 | 433 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324878.1 | 0 | 34 | 429 | 1 | 394 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515478.1 | 0 | 29 | 434 | 9 | 413 | heparanase, 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 | 0.000005 | 143 | 412 | 122 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vnz_A | 0.000005 | 143 | 412 | 122 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |
PDB | 3vny_A | 0.000005 | 143 | 412 | 122 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |