Basic Information | |
---|---|
Species | Ricinus communis |
Cazyme ID | 30174.m009142 |
Family | GH79 |
Protein Properties | Length: 596 Molecular Weight: 66143.8 Isoelectric Point: 6.8851 |
Chromosome | Chromosome/Scaffold: 30174 Start: 3268755 End: 3272506 |
Description | glucuronidase 2 |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
GH79 | 45 | 525 | 0 |
DENFICATLDWWPDTKCDYGQCPWGQAGILNLDLENKILANAIKAFDPLRIRIGGSLQDQLVYQVGNYIKKFPHFKRRDGDDYLFGFTRGSLPMDRWDQI NALFNQTGVKLTFGLNALIGKQKSKDDGSILWVGDWDPQNARDFMKYTISKGYHIDSYELGNELCGSGVSARLDAVEYGNDVIALRKLVNELYPDPNSRP AVLGPAGFYDQQWFNTFLMTVGPNVVDGVTHHIYNLGAGVDKALINKIQDPYFLDQIAQTFKDVSDSVRQFGPWSGPWVGESGGAYNSGGKDVSHTFANG FWYLDQLGMTSTYNHKVYCRQAFIGGNYGLLNTTSFIPNPDYYGALLWHRLMGKQVLATSHNASPYLRAYSHCSKKKPGITLLLINMSNQTSYSVSVIDD DNFFASNSANQYSSAGNEQREEYHLTPKDGNIQSDVLLLNGTPLQLTDSLDIPAMKPQLVDPSSPITVAPDSFVYVTIKDF |
Full Sequence |
---|
Protein Sequence Length: 596 Download |
MANPRLCSFL LVVFSSLLSL LSSNSVNAEV VQVTVRGLTS RASTDENFIC ATLDWWPDTK 60 CDYGQCPWGQ AGILNLDLEN KILANAIKAF DPLRIRIGGS LQDQLVYQVG NYIKKFPHFK 120 RRDGDDYLFG FTRGSLPMDR WDQINALFNQ TGVKLTFGLN ALIGKQKSKD DGSILWVGDW 180 DPQNARDFMK YTISKGYHID SYELGNELCG SGVSARLDAV EYGNDVIALR KLVNELYPDP 240 NSRPAVLGPA GFYDQQWFNT FLMTVGPNVV DGVTHHIYNL GAGVDKALIN KIQDPYFLDQ 300 IAQTFKDVSD SVRQFGPWSG PWVGESGGAY NSGGKDVSHT FANGFWYLDQ LGMTSTYNHK 360 VYCRQAFIGG NYGLLNTTSF IPNPDYYGAL LWHRLMGKQV LATSHNASPY LRAYSHCSKK 420 KPGITLLLIN MSNQTSYSVS VIDDDNFFAS NSANQYSSAG NEQREEYHLT PKDGNIQSDV 480 LLLNGTPLQL TDSLDIPAMK PQLVDPSSPI TVAPDSFVYV TIKDFKAPAL DDVKVKGLAS 540 KCRYNQCPWG HSGLFTLDVK NKILWNAVKA FNPLRIRVGG SLQDQLVASP CRDAIN 600 |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03662 | Glyco_hydro_79n | 1.0e-19 | 504 | 592 | 95 | + 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. | ||
pfam03662 | Glyco_hydro_79n | 5.0e-179 | 28 | 352 | 325 | + 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 | |
---|---|
GO Term | Description |
GO:0016020 | membrane |
GO:0016798 | hydrolase activity, acting on glycosyl bonds |
Annotations - NR Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002274743.1 | 0 | 28 | 529 | 22 | 520 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002274743.1 | 0.000000000005 | 539 | 587 | 52 | 100 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002315010.1 | 0 | 6 | 529 | 1 | 516 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002315010.1 | 0.00000000000004 | 539 | 587 | 53 | 101 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002512114.1 | 0 | 1 | 596 | 1 | 596 | Heparanase precursor, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
---|---|---|---|---|---|---|---|
Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3vo0_A | 0.0000001 | 142 | 442 | 122 | 411 | A Chain A, Crystal Structure Of A Rice Os3bglu6 Beta-glucosidase |
PDB | 3vnz_A | 0.0000001 | 142 | 442 | 122 | 411 | A Chain A, Crystal Structure Of A Rice Os3bglu6 Beta-glucosidase |
PDB | 3vny_A | 0.0000001 | 142 | 442 | 122 | 411 | A Chain A, Crystal Structure Of Beta-Glucuronidase From Acidobacterium Capsulatum |