y
Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.C04395.2 |
Family | GH79 |
Protein Properties | Length: 462 Molecular Weight: 50527.8 Isoelectric Point: 8.0864 |
Chromosome | Chromosome/Scaffold: 3 Start: 79823874 End: 79827557 |
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 | 51 | 424 | 0 |
DDDFVCATLDWWPPEKCDYGVCSWHRASLLNLDLSNKILLNAVKAFSPLKIRLGGTLQDKVLYNTPDLKQPCTSFVKNSSALFGFTQGCLPMARWDRLNA FFKESGAKIIFGLNALNGRTISPQGPAVGAWDSTNAESFIRYTVSKNYTIFGWELGNELSGSGVGTRVTASQYVSDTISLKNLILDIYKDVEPKPLILAP GGFVDSSWFKEFLDNTPKSLDVITHHIYNLGSGADQHLVEKILDPTVLDGELATFSNLQSIIKSSASATSAVAWVGEAGGAYNSGRDHVSNTFLYSFWYL DQMAMASTFDTKTYCRQAFIGGNYGLLDATSFIPNPDYYSALLWHRLMGRKVLGASLSRSDKIRAYAHCAKASV |
Full Sequence |
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Protein Sequence Length: 462 Download |
MGRRVSFLGL CFWVCMFCCG AASADSRGSS GEEGTVQVTV SVGKSAIAEI DDDFVCATLD 60 WWPPEKCDYG VCSWHRASLL NLDLSNKILL NAVKAFSPLK IRLGGTLQDK VLYNTPDLKQ 120 PCTSFVKNSS ALFGFTQGCL PMARWDRLNA FFKESGAKII FGLNALNGRT ISPQGPAVGA 180 WDSTNAESFI RYTVSKNYTI FGWELGNELS GSGVGTRVTA SQYVSDTISL KNLILDIYKD 240 VEPKPLILAP GGFVDSSWFK EFLDNTPKSL DVITHHIYNL GSGADQHLVE KILDPTVLDG 300 ELATFSNLQS IIKSSASATS AVAWVGEAGG AYNSGRDHVS NTFLYSFWYL DQMAMASTFD 360 TKTYCRQAFI GGNYGLLDAT SFIPNPDYYS ALLWHRLMGR KVLGASLSRS DKIRAYAHCA 420 KASVSLFCIL TSISFYFLCI RKKRNTLILG IYCRKGSCCC S* 480 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 4.0e-179 | 36 | 353 | 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 |
EMBL | CAN81917.1 | 0 | 1 | 433 | 1 | 431 | hypothetical protein [Vitis vinifera] |
EMBL | CBI25561.1 | 0 | 8 | 433 | 1 | 424 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 1 | 433 | 5 | 435 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 43 | 433 | 7 | 395 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331013.1 | 0 | 8 | 433 | 1 | 421 | 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 | 0.00000009 | 146 | 408 | 122 | 371 | A Chain A, The Structure Of Fcp1, An Essential Rna Polymerase Ii Ctd Phosphatase |
PDB | 3vnz_A | 0.00000009 | 146 | 408 | 122 | 371 | A Chain A, The Structure Of Fcp1, An Essential Rna Polymerase Ii Ctd Phosphatase |
PDB | 3vny_A | 0.00000009 | 146 | 408 | 122 | 371 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |