y
Basic Information | |
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Species | Cucumis sativus |
Cazyme ID | Cucsa.034470.1 |
Family | GH79 |
Protein Properties | Length: 529 Molecular Weight: 59224.4 Isoelectric Point: 7.374 |
Chromosome | Chromosome/Scaffold: 00444 Start: 220355 End: 223216 |
Description | glucuronidase 2 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH79 | 41 | 522 | 0 |
DENFICFTLDIWPHDECSQPNLCVWDGHASMLNMDLSLPILNKAVQAFKTLRIRVGGTLQDRLIYNIGDGFKGNCNPFEAHKGLLFDFTEGCLYMERWDD LNNFFNNTGAIVTFGLNALLGKYNTKGIQWEGNWNYSNAEALIKYTVEKKYNINSWEFGNELAGANSIGASVSASQYAKDLLKLRQIIDRLYKNSQQKPL IVAPGAFFDDKWYDELVTKTGSNVVSALTHHIYNMGAGDDPKLIYRFVNPTYLSQVSNTFRQLKNIIEKHAPWASAWVGEAGGAYHGGGLHISDTFINSF WYLDQLGMAASYNTKVYCRQTLVGGYYGVLRTKTFIPTPDYYGALLFHRLMGSSVLKVDNNVSSYLRTYAHCSRGRSGVTMLFINLSNTTEFTINIENHM NLSLHKSKPKHSSSKNVGTQREEYHLTPQNGLLRSSTVLLNGKALELTNEGEVPDLTPVYRDSNSSISIPNWSIAFIVIPDF |
Full Sequence |
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Protein Sequence Length: 529 Download |
MEYQIFLLIL VFAFIPRTIL GLNVTTGKIV VDGTTKIAET DENFICFTLD IWPHDECSQP 60 NLCVWDGHAS MLNMDLSLPI LNKAVQAFKT LRIRVGGTLQ DRLIYNIGDG FKGNCNPFEA 120 HKGLLFDFTE GCLYMERWDD LNNFFNNTGA IVTFGLNALL GKYNTKGIQW EGNWNYSNAE 180 ALIKYTVEKK YNINSWEFGN ELAGANSIGA SVSASQYAKD LLKLRQIIDR LYKNSQQKPL 240 IVAPGAFFDD KWYDELVTKT GSNVVSALTH HIYNMGAGDD PKLIYRFVNP TYLSQVSNTF 300 RQLKNIIEKH APWASAWVGE AGGAYHGGGL HISDTFINSF WYLDQLGMAA SYNTKVYCRQ 360 TLVGGYYGVL RTKTFIPTPD YYGALLFHRL MGSSVLKVDN NVSSYLRTYA HCSRGRSGVT 420 MLFINLSNTT EFTINIENHM NLSLHKSKPK HSSSKNVGTQ REEYHLTPQN GLLRSSTVLL 480 NGKALELTNE GEVPDLTPVY RDSNSSISIP NWSIAFIVIP DFVAIGCN* 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 | 8.0e-155 | 27 | 347 | 321 | + 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 | CAB62595.1 | 0 | 29 | 528 | 10 | 521 | putative protein [Arabidopsis thaliana] |
EMBL | CBI15157.1 | 0 | 29 | 527 | 27 | 512 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_196400.2 | 0 | 1 | 528 | 1 | 543 | AtGUS2 (Arabidopsis thaliana glucuronidase 2); beta-glucuronidase |
RefSeq | XP_002284470.1 | 0 | 29 | 527 | 27 | 538 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002514696.1 | 0 | 18 | 527 | 16 | 538 | Heparanase-2, 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 | 0.00000001 | 136 | 457 | 119 | 432 | A Chain A, Metallo-Beta-Lactamase (C181s Mutant) |
PDB | 3vnz_A | 0.00000001 | 136 | 457 | 119 | 432 | A Chain A, Metallo-Beta-Lactamase (C181s Mutant) |
PDB | 3vny_A | 0.00000001 | 136 | 457 | 119 | 432 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |