Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.C02741.1 |
Family | GH79 |
Protein Properties | Length: 491 Molecular Weight: 53517.3 Isoelectric Point: 6.5695 |
Chromosome | Chromosome/Scaffold: 3 Start: 52488334 End: 52491268 |
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 | 118 | 483 | 0 |
AVTFGLNALYGRTIGSDGSVNGPWNSSNAESLIRYTVNKGYSILGWELGNELSGDGVEARVSAHQYASDITTLQHLVEDIYAGFEVKPLVLAPGGFFKPD WFADFVNQTSKTLQVVTHHIYNLGPGVDDHLIQKILDPSYLDGELQIFSSLQSLLKNSGTSAVAWVGEAGGAYNSGRNLVTNTFVFSFWYLDQLGMAATY NTKTYCRQTLIGGNYGLLNTQNFLPNPDYYSALLWHKLMGSKVLLTSFLGTDKIRAYAHCSKNSVIHVSTENATSNGTLTLKQESQNHRTKFARMSRGSS NDGNIREEYHLTAKEGNIQSQVLLLNGKVLNTDSSGNIPSFDPINVSHSDPITVAPFSVVFAQIPN |
Full Sequence |
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Protein Sequence Length: 491 Download |
MGSLLVLVGL GFLVFWIHHN SSSALSQSTG ISGDVLSGTV FINGTASIAK TDDDYICATL 60 DWWPPEKCDY NTCSWGRATL LTLDLTNTIL INAVKAFSPL RIRMGGTLQD KVVYEKQAVT 120 FGLNALYGRT IGSDGSVNGP WNSSNAESLI RYTVNKGYSI LGWELGNELS GDGVEARVSA 180 HQYASDITTL QHLVEDIYAG FEVKPLVLAP GGFFKPDWFA DFVNQTSKTL QVVTHHIYNL 240 GPGVDDHLIQ KILDPSYLDG ELQIFSSLQS LLKNSGTSAV AWVGEAGGAY NSGRNLVTNT 300 FVFSFWYLDQ LGMAATYNTK TYCRQTLIGG NYGLLNTQNF LPNPDYYSAL LWHKLMGSKV 360 LLTSFLGTDK IRAYAHCSKN SVIHVSTENA TSNGTLTLKQ ESQNHRTKFA RMSRGSSNDG 420 NIREEYHLTA KEGNIQSQVL LLNGKVLNTD SSGNIPSFDP INVSHSDPIT VAPFSVVFAQ 480 IPNMNVTACK * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 2.0e-141 | 38 | 312 | 317 | + 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 | 26 | 490 | 434 | 885 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002283254.1 | 0 | 1 | 489 | 1 | 536 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002283260.1 | 0 | 1 | 490 | 1 | 546 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324878.1 | 0 | 38 | 489 | 1 | 504 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002515478.1 | 0 | 31 | 489 | 8 | 522 | 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 | 0.00004 | 122 | 402 | 132 | 423 | A Chain A, Solution Structure Of Tm1509 From Thermotoga Maritima: Vt1, A Nesgc Target Prot |
PDB | 3vnz_A | 0.00004 | 122 | 402 | 132 | 423 | A Chain A, Solution Structure Of Tm1509 From Thermotoga Maritima: Vt1, A Nesgc Target Prot |
PDB | 3vny_A | 0.00004 | 122 | 402 | 132 | 423 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |