Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10008038 |
Family | GH79 |
Protein Properties | Length: 538 Molecular Weight: 59304.1 Isoelectric Point: 6.5473 |
Chromosome | Chromosome/Scaffold: 896 Start: 100794 End: 103168 |
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 | 43 | 530 | 0 |
DEDFICATLDWWPPEKCDYGTCAWDHTSLINLDLNDQILLKAIKAFSPLKIRLGGTLQDKVLYDTPDNHQPCAQFVKNTSELFGFTQGCLPMYRWDELNS FFTKSGAKIIFGLNALMGRTIQPDGSAAGPWNYSNAQSFITYSVRHNYSIHGWELGNELSGSGVGTRVPADQYASDTISLHDIVDNVYSGIEQKPLVLAP AGFYDSNWFRTLIDKAGSSLDVVTHHIYNLGPGVDAHLVEKILNPAVLDNVVGAFRGLQSLLRISQSSATAWVGEAGGAYNSGRNLVSNAFVYSFWYLDQ LGLAAAHDTKTYCRQSLIGGNYGLLNTTTYVPNPDYYSALLWHRLMGRNSLSTSFSGSNKLRVYAHCAKYSKSFVLLLINLDNSTKFDVNVGLNTTLMLQ NKHSPHWHHNHRTEIIQLPPHRSKNGQMRDEYHLTAEGGNLPSQTMLLNGKSLKVNSDGDIPEFEPLHVNSSEPISVAPLSIVFARVP |
Full Sequence |
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Protein Sequence Length: 538 Download |
MGSQILVVGF LVVVCIIVPV SSQENVVEET VVVDGTTVIG RTDEDFICAT LDWWPPEKCD 60 YGTCAWDHTS LINLDLNDQI LLKAIKAFSP LKIRLGGTLQ DKVLYDTPDN HQPCAQFVKN 120 TSELFGFTQG CLPMYRWDEL NSFFTKSGAK IIFGLNALMG RTIQPDGSAA GPWNYSNAQS 180 FITYSVRHNY SIHGWELGNE LSGSGVGTRV PADQYASDTI SLHDIVDNVY SGIEQKPLVL 240 APAGFYDSNW FRTLIDKAGS SLDVVTHHIY NLGPGVDAHL VEKILNPAVL DNVVGAFRGL 300 QSLLRISQSS ATAWVGEAGG AYNSGRNLVS NAFVYSFWYL DQLGLAAAHD TKTYCRQSLI 360 GGNYGLLNTT TYVPNPDYYS ALLWHRLMGR NSLSTSFSGS NKLRVYAHCA KYSKSFVLLL 420 INLDNSTKFD VNVGLNTTLM LQNKHSPHWH HNHRTEIIQL PPHRSKNGQM RDEYHLTAEG 480 GNLPSQTMLL NGKSLKVNSD GDIPEFEPLH VNSSEPISVA PLSIVFARVP YILPACR* 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 | 39 | 344 | 307 | + 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 | CBI25561.1 | 0 | 27 | 537 | 28 | 533 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002263173.1 | 0 | 1 | 537 | 5 | 559 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002324603.1 | 0 | 30 | 536 | 2 | 505 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002331013.1 | 0 | 8 | 536 | 1 | 546 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533671.1 | 0 | 1 | 537 | 1 | 551 | 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 | 0.00003 | 138 | 384 | 122 | 357 | A Chain A, Crystal Structure Of The Pseudomonas Aeruginosa Murg:udp-glcnac Substrate Comp |
PDB | 3vnz_A | 0.00003 | 138 | 384 | 122 | 357 | A Chain A, Crystal Structure Of The Pseudomonas Aeruginosa Murg:udp-glcnac Substrate Comp |
PDB | 3vny_A | 0.00003 | 138 | 384 | 122 | 357 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |