y
Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000252327 |
Family | GH79 |
Protein Properties | Length: 506 Molecular Weight: 56335.1 Isoelectric Point: 6.1406 |
Chromosome | Chromosome/Scaffold: 01529096 Start: 6247 End: 8726 |
Description | glucuronidase 1 |
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 | 38 | 499 | 0 |
DDNFICATLDWWPADKCDYDQCPWGKAGTFNLDLSNKILHNAVKAFNPMRIRVGGSLQDQVXYGVGFGDKSCNRFKKNDSGLFGFSEACLHXKRWDELNQ FFNKTKAKVTFGLNALHGKKVSSEDKSLRIGDWNAQNSRDLMEYTIAKGYEIDSYELGNELSGSGVSARIESEQYAKDMXKLKEVVTELYPDASNRPKVL GPAGFYDKKWFENFLQATGPGVVDGVTHHLYNLGAEIAQTXYDLSNTIQQFGPWSEAWVGEAGGAYNSGGKDVSHTFADGFWYLDQLGMTSTYNHKVYCX QALIGGNYALLNTTTFIPNPDYYGALLWHRLMGTRVLSTMNFGSPYLRAYCHCTKNQKGVTLLLINMSNATTFDVAVLPDYNLYPRQILTTRKYGANDEP EREEYHLTPEGGNIQSDVVLLNGTPLKLTNSSDIPEMKPKLVDPTSTISVAADSIVFVSIKN |
Full Sequence |
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Protein Sequence Length: 506 Download |
MEVRGGAIFF ICVSWFSLGL AEYVEVRVKG VTFIATTDDN FICATLDWWP ADKCDYDQCP 60 WGKAGTFNLD LSNKILHNAV KAFNPMRIRV GGSLQDQVXY GVGFGDKSCN RFKKNDSGLF 120 GFSEACLHXK RWDELNQFFN KTKAKVTFGL NALHGKKVSS EDKSLRIGDW NAQNSRDLME 180 YTIAKGYEID SYELGNELSG SGVSARIESE QYAKDMXKLK EVVTELYPDA SNRPKVLGPA 240 GFYDKKWFEN FLQATGPGVV DGVTHHLYNL GAEIAQTXYD LSNTIQQFGP WSEAWVGEAG 300 GAYNSGGKDV SHTFADGFWY LDQLGMTSTY NHKVYCXQAL IGGNYALLNT TTFIPNPDYY 360 GALLWHRLMG TRVLSTMNFG SPYLRAYCHC TKNQKGVTLL LINMSNATTF DVAVLPDYNL 420 YPRQILTTRK YGANDEPERE EYHLTPEGGN IQSDVVLLNG TPLKLTNSSD IPEMKPKLVD 480 PTSTISVAAD SIVFVSIKNX HAPACA 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 | 5.0e-164 | 21 | 325 | 322 | + 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 | CBI27258.1 | 0 | 1 | 505 | 3 | 523 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0 | 1 | 505 | 1 | 521 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 11 | 506 | 6 | 518 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 21 | 504 | 28 | 529 | Heparanase precursor, putative [Ricinus communis] |
RefSeq | XP_002512114.1 | 0.00000000000004 | 26 | 98 | 510 | 586 | Heparanase precursor, 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 | 0.001 | 116 | 388 | 105 | 383 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 3vnz_A | 0.001 | 116 | 388 | 105 | 383 | B Chain B, Crystal Structure Of The Complex Between Pectin Methylesterase And Its Inhibitor Protein |
PDB | 3vny_A | 0.001 | 116 | 388 | 105 | 383 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |